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IEPA.d0 | 1645753 | [
{
"id": "IEPA.d0.s0",
"type": "",
"text": [
"Oxytocin stimulates IP3 production in dose-dependent fashion as well"
],
"offsets": [
[
0,
68
]
]
}
] | [
{
"id": "IEPA.d0.s0.e0",
"type": "",
"text": [
"Oxytocin"
],
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[
0,
8
]
],
"normalized": []
},
{
"id": "IEPA.d0.s0.e1",
"type": "",
"text": [
"IP3"
],
"offsets": [
[
20,
23
]
],
"normalized": []
}
] | [] | [] | [
{
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"normalized": []
}
] |
IEPA.d1 | 1936930 | [
{
"id": "IEPA.d1.s1",
"type": "",
"text": [
"Phosphoinositide hydrolysis, resulting in inositol trisphosphate (IP3) and diacylglycerol (DG) formation, has been implicated in oxytocin-stimulated pulsatile secretion of prostaglandin F2 alpha (PGF2 alpha) from uterine endometrium of sheep and other mammals"
],
"offsets": [
[
0,
259
]
]
}
] | [
{
"id": "IEPA.d1.s1.e0",
"type": "",
"text": [
"inositol trisphosphate"
],
"offsets": [
[
42,
64
]
],
"normalized": []
},
{
"id": "IEPA.d1.s1.e1",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
129,
137
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d1.s1.i0",
"type": "PPI",
"arg1_id": "IEPA.d1.s1.e0",
"arg2_id": "IEPA.d1.s1.e1",
"normalized": []
}
] |
IEPA.d2 | 1963324 | [
{
"id": "IEPA.d2.s2",
"type": "",
"text": [
"SP ewes also had greater incorporation of [3H]inositol into inositol trisphosphate (IP3) (+3449%, p less than 0.01) and total inositol phosphate (IP) (+760%, p less than 0.08), in response to oxytocin, than did oCSP ewes (+553 and +168% for IP3 and total IP, respectively) in endometrium collected at ovariectomy/hysterectomy on Day 16"
],
"offsets": [
[
0,
335
]
]
},
{
"id": "IEPA.d2.s3",
"type": "",
"text": [
"These results indicate that oTP-1 may prevent luteolysis by inhibiting development of endometrial responsiveness to oxytocin and, therefore, reduce oxytocin-induced synthesis of IP3 and PGF2 alpha"
],
"offsets": [
[
336,
532
]
]
}
] | [
{
"id": "IEPA.d2.s2.e0",
"type": "",
"text": [
"inositol trisphosphate"
],
"offsets": [
[
60,
82
]
],
"normalized": []
},
{
"id": "IEPA.d2.s2.e1",
"type": "",
"text": [
"inositol phosphate"
],
"offsets": [
[
126,
144
]
],
"normalized": []
},
{
"id": "IEPA.d2.s2.e2",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
192,
200
]
],
"normalized": []
},
{
"id": "IEPA.d2.s2.e3",
"type": "",
"text": [
"IP3"
],
"offsets": [
[
241,
244
]
],
"normalized": []
},
{
"id": "IEPA.d2.s2.e4",
"type": "",
"text": [
"IP"
],
"offsets": [
[
255,
257
]
],
"normalized": []
},
{
"id": "IEPA.d2.s3.e0",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
452,
460
]
],
"normalized": []
},
{
"id": "IEPA.d2.s3.e1",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
484,
492
]
],
"normalized": []
},
{
"id": "IEPA.d2.s3.e2",
"type": "",
"text": [
"IP3"
],
"offsets": [
[
514,
517
]
],
"normalized": []
}
] | [] | [] | [
{
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{
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"arg2_id": "IEPA.d2.s2.e2",
"normalized": []
},
{
"id": "IEPA.d2.s2.i2",
"type": "PPI",
"arg1_id": "IEPA.d2.s2.e2",
"arg2_id": "IEPA.d2.s2.e3",
"normalized": []
},
{
"id": "IEPA.d2.s2.i3",
"type": "PPI",
"arg1_id": "IEPA.d2.s2.e2",
"arg2_id": "IEPA.d2.s2.e4",
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},
{
"id": "IEPA.d2.s3.i0",
"type": "PPI",
"arg1_id": "IEPA.d2.s3.e1",
"arg2_id": "IEPA.d2.s3.e2",
"normalized": []
}
] |
IEPA.d3 | 2163308 | [
{
"id": "IEPA.d3.s4",
"type": "",
"text": [
"Inositol 1,4,5-trisphosphate and oxytocin binding in human myometrium"
],
"offsets": [
[
0,
69
]
]
}
] | [
{
"id": "IEPA.d3.s4.e0",
"type": "",
"text": [
"Inositol 1,4,5-trisphosphate"
],
"offsets": [
[
0,
28
]
],
"normalized": []
},
{
"id": "IEPA.d3.s4.e1",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
33,
41
]
],
"normalized": []
}
] | [] | [] | [] |
IEPA.d4 | 2229283 | [
{
"id": "IEPA.d4.s5",
"type": "",
"text": [
"The effects of prostaglandin F2 alpha (PGF2 alpha) on intracellular Ca2+ concentration ([Ca2+]i) and inositol phosphate (IP) generation in human myometrial cells were evaluated and compared to the effects of oxytocin"
],
"offsets": [
[
0,
216
]
]
},
{
"id": "IEPA.d4.s6",
"type": "",
"text": [
"In contrast, the potencies of oxytocin to raise IP and [Ca2+]i were similar and independent of extracellular Ca2+, and could be suppressed by pertussis toxin and phorbol ester, but not by verapamil"
],
"offsets": [
[
217,
414
]
]
},
{
"id": "IEPA.d4.s7",
"type": "",
"text": [
"The action of PGF2 alpha depends on extracellular Ca2+, whereas oxytocin activates the G-protein-dependent phospholipase-C-IP3-Ca2+ signal-transducing pathway, complemented by the influx of extracellular Ca2+"
],
"offsets": [
[
415,
623
]
]
}
] | [
{
"id": "IEPA.d4.s5.e0",
"type": "",
"text": [
"inositol phosphate"
],
"offsets": [
[
101,
119
]
],
"normalized": []
},
{
"id": "IEPA.d4.s5.e1",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
208,
216
]
],
"normalized": []
},
{
"id": "IEPA.d4.s6.e0",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
247,
255
]
],
"normalized": []
},
{
"id": "IEPA.d4.s6.e1",
"type": "",
"text": [
"IP"
],
"offsets": [
[
265,
267
]
],
"normalized": []
},
{
"id": "IEPA.d4.s7.e0",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
479,
487
]
],
"normalized": []
},
{
"id": "IEPA.d4.s7.e1",
"type": "",
"text": [
"IP3"
],
"offsets": [
[
538,
541
]
],
"normalized": []
}
] | [] | [] | [
{
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},
{
"id": "IEPA.d4.s7.i0",
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"arg1_id": "IEPA.d4.s7.e0",
"arg2_id": "IEPA.d4.s7.e1",
"normalized": []
}
] |
IEPA.d8 | 7581972 | [
{
"id": "IEPA.d8.s14",
"type": "",
"text": [
"The objectives of this study were to evaluate and compare the actions of endothelin-1 (ET-1), oxytocin, prostaglandin F2 alpha (PGF2 alpha) and inositol 1,4,5-trisphosphate (IP3) on 45Ca2+ mobilization in permeabilized rat myometrial cells and to examine the activation of the inositol lipid cycle in intact myocytes"
],
"offsets": [
[
0,
316
]
]
},
{
"id": "IEPA.d8.s15",
"type": "",
"text": [
"All four agonists caused a biphasic release of 45Ca2+ from non-mitochondrial pool(s), with the rank order of potency: oxytocin > PGF2 alpha > ET-1 > IP3"
],
"offsets": [
[
317,
469
]
]
},
{
"id": "IEPA.d8.s16",
"type": "",
"text": [
"Endothelin-1 and oxytocin stimulated inositol phosphate accumulation at concentrations similar to those that promoted 45Ca2+ efflux, whereas about 100 times higher concentrations of PGF2 alpha were needed to activate this signaling pathway in intact cells"
],
"offsets": [
[
470,
725
]
]
},
{
"id": "IEPA.d8.s17",
"type": "",
"text": [
"It is concluded that the primary action of PGF2 alpha in myometrial cells is to enhance Ca2+ influx, whereas oxytocin and ET-1 receptors are coupled to phospholipase C, generating IP3 and raising the intracellular concentration of free Ca2+ from intracellular as well as extracellular sources"
],
"offsets": [
[
726,
1018
]
]
}
] | [
{
"id": "IEPA.d8.s14.e0",
"type": "",
"text": [
"oxytocin"
],
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[
94,
102
]
],
"normalized": []
},
{
"id": "IEPA.d8.s14.e1",
"type": "",
"text": [
"inositol 1,4,5-trisphosphate"
],
"offsets": [
[
144,
172
]
],
"normalized": []
},
{
"id": "IEPA.d8.s15.e0",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
435,
443
]
],
"normalized": []
},
{
"id": "IEPA.d8.s15.e1",
"type": "",
"text": [
"IP3"
],
"offsets": [
[
466,
469
]
],
"normalized": []
},
{
"id": "IEPA.d8.s16.e0",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
487,
495
]
],
"normalized": []
},
{
"id": "IEPA.d8.s16.e1",
"type": "",
"text": [
"inositol phosphate"
],
"offsets": [
[
507,
525
]
],
"normalized": []
},
{
"id": "IEPA.d8.s17.e0",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
835,
843
]
],
"normalized": []
},
{
"id": "IEPA.d8.s17.e1",
"type": "",
"text": [
"IP3"
],
"offsets": [
[
906,
909
]
],
"normalized": []
}
] | [] | [] | [
{
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},
{
"id": "IEPA.d8.s17.i0",
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"arg1_id": "IEPA.d8.s17.e0",
"arg2_id": "IEPA.d8.s17.e1",
"normalized": []
}
] |
IEPA.d9 | 7619502 | [
{
"id": "IEPA.d9.s18",
"type": "",
"text": [
"Oxytocin induced a biphasic increase in the intracellular Ca2+ concentration of porcine myometrial cells: participation of a pertussis toxin-insensitive G-protein, inositol 1,4,5-trisphosphate-sensitive Ca2+ pool, and Ca2+ channels"
],
"offsets": [
[
0,
231
]
]
},
{
"id": "IEPA.d9.s19",
"type": "",
"text": [
"Administration of OT (1 microM) for 15 sec increased inositol 1,4,5-trisphosphate (IP3) formation by 61%"
],
"offsets": [
[
232,
336
]
]
},
{
"id": "IEPA.d9.s20",
"type": "",
"text": [
"Pretreatment with pertussis toxin (PTX, 1 microgram/ml) for 2 hr failed to alter the OT-induced increase in [Ca2+]i and IP3 formation"
],
"offsets": [
[
337,
470
]
]
},
{
"id": "IEPA.d9.s21",
"type": "",
"text": [
"U-73122 (3 microM) also abolished the OT-induced IP3 formation"
],
"offsets": [
[
471,
533
]
]
}
] | [
{
"id": "IEPA.d9.s18.e0",
"type": "",
"text": [
"Oxytocin"
],
"offsets": [
[
0,
8
]
],
"normalized": []
},
{
"id": "IEPA.d9.s18.e1",
"type": "",
"text": [
"inositol 1,4,5-trisphosphate"
],
"offsets": [
[
164,
192
]
],
"normalized": []
},
{
"id": "IEPA.d9.s19.e0",
"type": "",
"text": [
"OT"
],
"offsets": [
[
250,
252
]
],
"normalized": []
},
{
"id": "IEPA.d9.s19.e1",
"type": "",
"text": [
"inositol 1,4,5-trisphosphate"
],
"offsets": [
[
285,
313
]
],
"normalized": []
},
{
"id": "IEPA.d9.s20.e0",
"type": "",
"text": [
"OT"
],
"offsets": [
[
422,
424
]
],
"normalized": []
},
{
"id": "IEPA.d9.s20.e1",
"type": "",
"text": [
"IP3"
],
"offsets": [
[
457,
460
]
],
"normalized": []
},
{
"id": "IEPA.d9.s21.e0",
"type": "",
"text": [
"OT"
],
"offsets": [
[
509,
511
]
],
"normalized": []
},
{
"id": "IEPA.d9.s21.e1",
"type": "",
"text": [
"IP3"
],
"offsets": [
[
520,
523
]
],
"normalized": []
}
] | [] | [] | [
{
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{
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},
{
"id": "IEPA.d9.s21.i0",
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"arg1_id": "IEPA.d9.s21.e0",
"arg2_id": "IEPA.d9.s21.e1",
"normalized": []
}
] |
IEPA.d10 | 7700473 | [
{
"id": "IEPA.d10.s22",
"type": "",
"text": [
"Amyloid beta protein disruption of cholinergic and growth factor phospholipase C signals could underlie cognitive and neurodegerative aspects of Alzheimer's disease"
],
"offsets": [
[
0,
164
]
]
}
] | [
{
"id": "IEPA.d10.s22.e0",
"type": "",
"text": [
"Amyloid"
],
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[
0,
7
]
],
"normalized": []
},
{
"id": "IEPA.d10.s22.e1",
"type": "",
"text": [
"phospholipase C"
],
"offsets": [
[
65,
80
]
],
"normalized": []
}
] | [] | [] | [
{
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"normalized": []
}
] |
IEPA.d11 | 7781763 | [
{
"id": "IEPA.d11.s23",
"type": "",
"text": [
"Amyloid beta protein (25-35) stimulation of phospholipases A, C and D activities of LA-N-2 cells"
],
"offsets": [
[
0,
96
]
]
},
{
"id": "IEPA.d11.s24",
"type": "",
"text": [
"[3H]Inositol prelabeled LA-N-2 cells were exposed to varying concentrations of A beta P, from 20 to 125 micrograms/ml, and phospholipase C activation was measured"
],
"offsets": [
[
97,
259
]
]
},
{
"id": "IEPA.d11.s25",
"type": "",
"text": [
"The effects of adrenergic, metabotropic amino acid and bombesin antagonists on the A beta P mediated stimulation of phospholipase C activity was investigated"
],
"offsets": [
[
260,
417
]
]
},
{
"id": "IEPA.d11.s26",
"type": "",
"text": [
"Propranolol, a beta adrenergic antagonist, 7-chloro-kynurenic acid, a metabotropic amino acid antagonist, and [Tyr4-D-Phe12]bombesin, a bombesin antagonist, blunted the A beta P stimulation of phospholipase C activity in [3H]inositol prelabeled LA-N-2 cells"
],
"offsets": [
[
418,
675
]
]
},
{
"id": "IEPA.d11.s27",
"type": "",
"text": [
"This suggests that amyloid beta protein activation of phospholipase C may be receptor mediated"
],
"offsets": [
[
676,
770
]
]
},
{
"id": "IEPA.d11.s28",
"type": "",
"text": [
"The phospholipase C inhibitor U 71322 prevented the activation of phospholipase C by A beta P"
],
"offsets": [
[
771,
864
]
]
}
] | [
{
"id": "IEPA.d11.s23.e0",
"type": "",
"text": [
"Amyloid"
],
"offsets": [
[
0,
7
]
],
"normalized": []
},
{
"id": "IEPA.d11.s23.e1",
"type": "",
"text": [
"phospholipases"
],
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[
44,
58
]
],
"normalized": []
},
{
"id": "IEPA.d11.s24.e0",
"type": "",
"text": [
"A beta P"
],
"offsets": [
[
176,
184
]
],
"normalized": []
},
{
"id": "IEPA.d11.s24.e1",
"type": "",
"text": [
"phospholipase C"
],
"offsets": [
[
220,
235
]
],
"normalized": []
},
{
"id": "IEPA.d11.s25.e0",
"type": "",
"text": [
"A beta P"
],
"offsets": [
[
343,
351
]
],
"normalized": []
},
{
"id": "IEPA.d11.s25.e1",
"type": "",
"text": [
"phospholipase C"
],
"offsets": [
[
376,
391
]
],
"normalized": []
},
{
"id": "IEPA.d11.s26.e0",
"type": "",
"text": [
"A beta P"
],
"offsets": [
[
587,
595
]
],
"normalized": []
},
{
"id": "IEPA.d11.s26.e1",
"type": "",
"text": [
"phospholipase C"
],
"offsets": [
[
611,
626
]
],
"normalized": []
},
{
"id": "IEPA.d11.s27.e0",
"type": "",
"text": [
"amyloid"
],
"offsets": [
[
695,
702
]
],
"normalized": []
},
{
"id": "IEPA.d11.s27.e1",
"type": "",
"text": [
"phospholipase C"
],
"offsets": [
[
730,
745
]
],
"normalized": []
},
{
"id": "IEPA.d11.s28.e0",
"type": "",
"text": [
"phospholipase C"
],
"offsets": [
[
775,
790
]
],
"normalized": []
},
{
"id": "IEPA.d11.s28.e1",
"type": "",
"text": [
"phospholipase C"
],
"offsets": [
[
837,
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]
],
"normalized": []
},
{
"id": "IEPA.d11.s28.e2",
"type": "",
"text": [
"A beta P"
],
"offsets": [
[
856,
864
]
],
"normalized": []
}
] | [] | [] | [
{
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"arg2_id": "IEPA.d11.s26.e1",
"normalized": []
},
{
"id": "IEPA.d11.s27.i0",
"type": "PPI",
"arg1_id": "IEPA.d11.s27.e0",
"arg2_id": "IEPA.d11.s27.e1",
"normalized": []
},
{
"id": "IEPA.d11.s28.i0",
"type": "PPI",
"arg1_id": "IEPA.d11.s28.e1",
"arg2_id": "IEPA.d11.s28.e2",
"normalized": []
}
] |
IEPA.d12 | 7876266 | [
{
"id": "IEPA.d12.s29",
"type": "",
"text": [
"These results suggest that APP-S secretion and A beta production in NT2N neurons are regulated by the muscarinic/phospholipase C signal transduction pathway"
],
"offsets": [
[
0,
156
]
]
}
] | [
{
"id": "IEPA.d12.s29.e0",
"type": "",
"text": [
"APP-S"
],
"offsets": [
[
27,
32
]
],
"normalized": []
},
{
"id": "IEPA.d12.s29.e1",
"type": "",
"text": [
"A beta"
],
"offsets": [
[
47,
53
]
],
"normalized": []
},
{
"id": "IEPA.d12.s29.e2",
"type": "",
"text": [
"phospholipase C"
],
"offsets": [
[
113,
128
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d12.s29.i0",
"type": "PPI",
"arg1_id": "IEPA.d12.s29.e0",
"arg2_id": "IEPA.d12.s29.e2",
"normalized": []
},
{
"id": "IEPA.d12.s29.i1",
"type": "PPI",
"arg1_id": "IEPA.d12.s29.e1",
"arg2_id": "IEPA.d12.s29.e2",
"normalized": []
}
] |
IEPA.d13 | 7884548 | [
{
"id": "IEPA.d13.s30",
"type": "",
"text": [
"Current interest in reducing heart disease risks by diet involves attention to total fat; saturated, monounsaturated, polyunsaturated and trans fatty acids, as well as dietary cholesterol, soluble fiber, salt, alcohol, antioxidants, dietary alterations causing homocysteinemia and other dietary constituents, such as flavonoid compounds in some soy products"
],
"offsets": [
[
0,
357
]
]
}
] | [
{
"id": "IEPA.d13.s30.e0",
"type": "",
"text": [
"cholesterol"
],
"offsets": [
[
176,
187
]
],
"normalized": []
},
{
"id": "IEPA.d13.s30.e1",
"type": "",
"text": [
"flavonoid"
],
"offsets": [
[
317,
326
]
],
"normalized": []
}
] | [] | [] | [] |
IEPA.d14 | 7960031 | [
{
"id": "IEPA.d14.s31",
"type": "",
"text": [
"This indicates that the calcium response to OT application was principally associated with activation of the IP3-sensitive calcium stores"
],
"offsets": [
[
0,
137
]
]
}
] | [
{
"id": "IEPA.d14.s31.e0",
"type": "",
"text": [
"OT"
],
"offsets": [
[
44,
46
]
],
"normalized": []
},
{
"id": "IEPA.d14.s31.e1",
"type": "",
"text": [
"IP3"
],
"offsets": [
[
109,
112
]
],
"normalized": []
}
] | [] | [] | [] |
IEPA.d15 | 7986826 | [
{
"id": "IEPA.d15.s32",
"type": "",
"text": [
"The beta amyloid protein fragments had diverse effects on phosphoinositide-specific phospholipase C (PI-PLC) as assayed in rat cortical membranes"
],
"offsets": [
[
0,
145
]
]
}
] | [
{
"id": "IEPA.d15.s32.e0",
"type": "",
"text": [
"amyloid"
],
"offsets": [
[
9,
16
]
],
"normalized": []
},
{
"id": "IEPA.d15.s32.e1",
"type": "",
"text": [
"phospholipase C"
],
"offsets": [
[
84,
99
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d15.s32.i0",
"type": "PPI",
"arg1_id": "IEPA.d15.s32.e0",
"arg2_id": "IEPA.d15.s32.e1",
"normalized": []
}
] |
IEPA.d16 | 8324162 | [
{
"id": "IEPA.d16.s33",
"type": "",
"text": [
"They are needed for the catabolism of cholesterol, bile acids, and steroid hormones; they hydrolyze a number of flavonoid glycosides to anticarcinogens; and they detoxify certain carcinogens"
],
"offsets": [
[
0,
190
]
]
}
] | [
{
"id": "IEPA.d16.s33.e0",
"type": "",
"text": [
"cholesterol"
],
"offsets": [
[
38,
49
]
],
"normalized": []
},
{
"id": "IEPA.d16.s33.e1",
"type": "",
"text": [
"flavonoid"
],
"offsets": [
[
112,
121
]
],
"normalized": []
}
] | [] | [] | [] |
IEPA.d17 | 8527814 | [
{
"id": "IEPA.d17.s34",
"type": "",
"text": [
"The aim of this study was to investigate the effects of hCG, hCG plus oxytocin and oxytocin on [3H] inositol phosphate (IP) formations in porcine myometrial cells obtained from ovariectomized and cyclic gilts"
],
"offsets": [
[
0,
208
]
]
},
{
"id": "IEPA.d17.s35",
"type": "",
"text": [
"The highest production of total inositol phosphates (d.p.m.) was found in cells from ovariectomized gilts given in vivo estradiol benzoate and progesterone for five consecutive days and treated with 1000 mU hCG and 100 mU hCG plus 1 microM oxytocin (984 +/- 84 and 1063 +/- 131 vs 314 +/- 36, respectively)"
],
"offsets": [
[
209,
515
]
]
},
{
"id": "IEPA.d17.s36",
"type": "",
"text": [
"There was also a very significant increase of IP1 after the addition of 1000 mU hCG (p < 0.001) and IP1 and IP3 when 1000 mU hCG plus oxytocin were added (p < 0.001 and p < 0.01, respectively)"
],
"offsets": [
[
516,
708
]
]
},
{
"id": "IEPA.d17.s37",
"type": "",
"text": [
"Only oxytocin alone increased the formation of IPs in cells from ovariectomized pigs treated with estradiol in vivo (p < 0.01)"
],
"offsets": [
[
709,
835
]
]
},
{
"id": "IEPA.d17.s38",
"type": "",
"text": [
"The highest dose of hCG plus The highest dose of hCG plus oxytocin provoked accumulation of total [3H]inositol phosphate (p < 0.05) 53% over the basal level on days 21/1 of the estrous cycle"
],
"offsets": [
[
836,
1026
]
]
},
{
"id": "IEPA.d17.s39",
"type": "",
"text": [
"The present study demonstrates that hCG and oxytocin can increase the accumulation of inositol phosphates in porcine myometrial cells"
],
"offsets": [
[
1027,
1160
]
]
}
] | [
{
"id": "IEPA.d17.s34.e0",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
70,
78
]
],
"normalized": []
},
{
"id": "IEPA.d17.s34.e1",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
83,
91
]
],
"normalized": []
},
{
"id": "IEPA.d17.s34.e2",
"type": "",
"text": [
"inositol phosphate"
],
"offsets": [
[
100,
118
]
],
"normalized": []
},
{
"id": "IEPA.d17.s35.e0",
"type": "",
"text": [
"inositol phosphates"
],
"offsets": [
[
241,
260
]
],
"normalized": []
},
{
"id": "IEPA.d17.s35.e1",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
449,
457
]
],
"normalized": []
},
{
"id": "IEPA.d17.s36.e0",
"type": "",
"text": [
"IP1"
],
"offsets": [
[
562,
565
]
],
"normalized": []
},
{
"id": "IEPA.d17.s36.e1",
"type": "",
"text": [
"IP1"
],
"offsets": [
[
616,
619
]
],
"normalized": []
},
{
"id": "IEPA.d17.s36.e2",
"type": "",
"text": [
"IP3"
],
"offsets": [
[
624,
627
]
],
"normalized": []
},
{
"id": "IEPA.d17.s36.e3",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
650,
658
]
],
"normalized": []
},
{
"id": "IEPA.d17.s37.e0",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
714,
722
]
],
"normalized": []
},
{
"id": "IEPA.d17.s37.e1",
"type": "",
"text": [
"IPs"
],
"offsets": [
[
756,
759
]
],
"normalized": []
},
{
"id": "IEPA.d17.s38.e0",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
894,
902
]
],
"normalized": []
},
{
"id": "IEPA.d17.s38.e1",
"type": "",
"text": [
"inositol phosphate"
],
"offsets": [
[
938,
956
]
],
"normalized": []
},
{
"id": "IEPA.d17.s39.e0",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
1071,
1079
]
],
"normalized": []
},
{
"id": "IEPA.d17.s39.e1",
"type": "",
"text": [
"inositol phosphates"
],
"offsets": [
[
1113,
1132
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d17.s34.i0",
"type": "PPI",
"arg1_id": "IEPA.d17.s34.e0",
"arg2_id": "IEPA.d17.s34.e2",
"normalized": []
},
{
"id": "IEPA.d17.s34.i1",
"type": "PPI",
"arg1_id": "IEPA.d17.s34.e1",
"arg2_id": "IEPA.d17.s34.e2",
"normalized": []
},
{
"id": "IEPA.d17.s35.i0",
"type": "PPI",
"arg1_id": "IEPA.d17.s35.e0",
"arg2_id": "IEPA.d17.s35.e1",
"normalized": []
},
{
"id": "IEPA.d17.s36.i0",
"type": "PPI",
"arg1_id": "IEPA.d17.s36.e0",
"arg2_id": "IEPA.d17.s36.e3",
"normalized": []
},
{
"id": "IEPA.d17.s36.i1",
"type": "PPI",
"arg1_id": "IEPA.d17.s36.e1",
"arg2_id": "IEPA.d17.s36.e3",
"normalized": []
},
{
"id": "IEPA.d17.s36.i2",
"type": "PPI",
"arg1_id": "IEPA.d17.s36.e2",
"arg2_id": "IEPA.d17.s36.e3",
"normalized": []
},
{
"id": "IEPA.d17.s37.i0",
"type": "PPI",
"arg1_id": "IEPA.d17.s37.e0",
"arg2_id": "IEPA.d17.s37.e1",
"normalized": []
},
{
"id": "IEPA.d17.s38.i0",
"type": "PPI",
"arg1_id": "IEPA.d17.s38.e0",
"arg2_id": "IEPA.d17.s38.e1",
"normalized": []
},
{
"id": "IEPA.d17.s39.i0",
"type": "PPI",
"arg1_id": "IEPA.d17.s39.e0",
"arg2_id": "IEPA.d17.s39.e1",
"normalized": []
}
] |
IEPA.d18 | 8597679 | [
{
"id": "IEPA.d18.s40",
"type": "",
"text": [
"The relative risks between highest and lowest quarters of flavonoid intake adjusted for age, smoking, serum cholesterol concentration, blood pressure, and body mass index were 0.69 (95% confidence interval 0.53 to 0.90) and 0.54 (0.33 to 0.87) for total and coronary mortality, respectively"
],
"offsets": [
[
0,
290
]
]
}
] | [
{
"id": "IEPA.d18.s40.e0",
"type": "",
"text": [
"flavonoid"
],
"offsets": [
[
58,
67
]
],
"normalized": []
},
{
"id": "IEPA.d18.s40.e1",
"type": "",
"text": [
"cholesterol"
],
"offsets": [
[
108,
119
]
],
"normalized": []
}
] | [] | [] | [] |
IEPA.d19 | 8647319 | [
{
"id": "IEPA.d19.s41",
"type": "",
"text": [
"Granulosa cells were isolated from bovine preovulatory follicles and cultured for 3 days with or without OT in medium supplemented with either insulin (1 microgram/ml) + 1% fetal calf serum (FCS), which maintains basal estradiol secretion, or low doses of FSH (1 and 2 ng/ml) + 1% FCS, a culture condition that maximizes effects of FSH on estradiol secretion"
],
"offsets": [
[
0,
358
]
]
}
] | [
{
"id": "IEPA.d19.s41.e0",
"type": "",
"text": [
"OT"
],
"offsets": [
[
105,
107
]
],
"normalized": []
},
{
"id": "IEPA.d19.s41.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
143,
150
]
],
"normalized": []
}
] | [] | [] | [] |
IEPA.d20 | 8713996 | [
{
"id": "IEPA.d20.s42",
"type": "",
"text": [
"We propose that OT binds to specific OT receptors (OTR) on the endometrium to stimulate phosphoinositide (PI) hydrolysis, thereby activating the inositol trisphosphate (IP3)-diacylglycerol (DAG) second-messenger system to promote pulsatile PGF2 alpha secretion"
],
"offsets": [
[
0,
260
]
]
},
{
"id": "IEPA.d20.s43",
"type": "",
"text": [
"Endometrial IP3 was increased within 30 seconds after OT treatment and preceded the increase in PGF2 alpha release stimulated by OT"
],
"offsets": [
[
261,
392
]
]
},
{
"id": "IEPA.d20.s44",
"type": "",
"text": [
"These results support the hypothesis that OT stimulates phospholipase C to hydrolyze PI, yielding IP3 and DAG second-messengers which promote endometrial PGF2 alpha release during CL regression in pigs"
],
"offsets": [
[
393,
594
]
]
}
] | [
{
"id": "IEPA.d20.s42.e0",
"type": "",
"text": [
"OT"
],
"offsets": [
[
16,
18
]
],
"normalized": []
},
{
"id": "IEPA.d20.s42.e1",
"type": "",
"text": [
"IP3"
],
"offsets": [
[
169,
172
]
],
"normalized": []
},
{
"id": "IEPA.d20.s43.e0",
"type": "",
"text": [
"IP3"
],
"offsets": [
[
273,
276
]
],
"normalized": []
},
{
"id": "IEPA.d20.s43.e1",
"type": "",
"text": [
"OT"
],
"offsets": [
[
315,
317
]
],
"normalized": []
},
{
"id": "IEPA.d20.s43.e2",
"type": "",
"text": [
"OT"
],
"offsets": [
[
390,
392
]
],
"normalized": []
},
{
"id": "IEPA.d20.s44.e0",
"type": "",
"text": [
"OT"
],
"offsets": [
[
435,
437
]
],
"normalized": []
},
{
"id": "IEPA.d20.s44.e1",
"type": "",
"text": [
"IP3"
],
"offsets": [
[
491,
494
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d20.s42.i0",
"type": "PPI",
"arg1_id": "IEPA.d20.s42.e0",
"arg2_id": "IEPA.d20.s42.e1",
"normalized": []
},
{
"id": "IEPA.d20.s43.i0",
"type": "PPI",
"arg1_id": "IEPA.d20.s43.e0",
"arg2_id": "IEPA.d20.s43.e1",
"normalized": []
},
{
"id": "IEPA.d20.s44.i0",
"type": "PPI",
"arg1_id": "IEPA.d20.s44.e0",
"arg2_id": "IEPA.d20.s44.e1",
"normalized": []
}
] |
IEPA.d21 | 8713999 | [
{
"id": "IEPA.d21.s45",
"type": "",
"text": [
"These data suggest that cAMP-dependent phosphorylation at a step involving GTP-binding protein/PLC coupling can exert a negative effect on the stimulation of IP3 formation by oxytocin and thereby affect contraction/relaxation in the myometrium"
],
"offsets": [
[
0,
243
]
]
}
] | [
{
"id": "IEPA.d21.s45.e0",
"type": "",
"text": [
"IP3"
],
"offsets": [
[
158,
161
]
],
"normalized": []
},
{
"id": "IEPA.d21.s45.e1",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
175,
183
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d21.s45.i0",
"type": "PPI",
"arg1_id": "IEPA.d21.s45.e0",
"arg2_id": "IEPA.d21.s45.e1",
"normalized": []
}
] |
IEPA.d22 | 8735881 | [
{
"id": "IEPA.d22.s46",
"type": "",
"text": [
"Once the abnormally phosphorylated abnormal prion protein isoform agent is initiated, any stress event ensuing in adult life induces a nerve growth factor-mediated synthesis of normal cellular prion protein isoform that aggregates to abnormally phosphorylated abnormal prion protein isoform, thereby becoming 'infected'/transformed into the same; due to the vicious circle of positive feedback invoked by the blocking of a prion protein-specific kinase"
],
"offsets": [
[
0,
452
]
]
}
] | [
{
"id": "IEPA.d22.s46.e0",
"type": "",
"text": [
"prion protein"
],
"offsets": [
[
44,
57
]
],
"normalized": []
},
{
"id": "IEPA.d22.s46.e1",
"type": "",
"text": [
"prion protein"
],
"offsets": [
[
193,
206
]
],
"normalized": []
},
{
"id": "IEPA.d22.s46.e2",
"type": "",
"text": [
"prion protein"
],
"offsets": [
[
269,
282
]
],
"normalized": []
},
{
"id": "IEPA.d22.s46.e3",
"type": "",
"text": [
"prion protein"
],
"offsets": [
[
423,
436
]
],
"normalized": []
},
{
"id": "IEPA.d22.s46.e4",
"type": "",
"text": [
"kinase"
],
"offsets": [
[
446,
452
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d22.s46.i0",
"type": "PPI",
"arg1_id": "IEPA.d22.s46.e3",
"arg2_id": "IEPA.d22.s46.e4",
"normalized": []
}
] |
IEPA.d23 | 8735882 | [
{
"id": "IEPA.d23.s47",
"type": "",
"text": [
"The resulting abnormally phosphorylated PrPsc aggregates to freshly synthesized PrPc, transforming it into same; due to a system of positive feedback invoked by the organophosphate-induced blockage of a prion protein-specific protein kinase."
],
"offsets": [
[
0,
241
]
]
}
] | [
{
"id": "IEPA.d23.s47.e0",
"type": "",
"text": [
"PrPsc"
],
"offsets": [
[
40,
45
]
],
"normalized": []
},
{
"id": "IEPA.d23.s47.e1",
"type": "",
"text": [
"PrPc"
],
"offsets": [
[
80,
84
]
],
"normalized": []
},
{
"id": "IEPA.d23.s47.e2",
"type": "",
"text": [
"prion protein"
],
"offsets": [
[
203,
216
]
],
"normalized": []
},
{
"id": "IEPA.d23.s47.e3",
"type": "",
"text": [
"protein kinase"
],
"offsets": [
[
226,
240
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d23.s47.i0",
"type": "PPI",
"arg1_id": "IEPA.d23.s47.e2",
"arg2_id": "IEPA.d23.s47.e3",
"normalized": []
}
] |
IEPA.d24 | 8739893 | [
{
"id": "IEPA.d24.s48",
"type": "",
"text": [
"The aim of the present study was to investigate how oxytocin given subcutaneously (SC) and intracerebroventricularly (ICV) influences the secretion of insulin, glucagon and glucose and to investigate whether the effect on these variables of suckling in lactating rats is mediated by oxytocinergic mechanisms"
],
"offsets": [
[
0,
307
]
]
},
{
"id": "IEPA.d24.s49",
"type": "",
"text": [
"Subcutaneous injections of oxytocin increased insulin, glucagon and glucose levels significantly"
],
"offsets": [
[
308,
404
]
]
},
{
"id": "IEPA.d24.s50",
"type": "",
"text": [
"Two nanograms oxytocin given ICV had no effect on glucagon and glucose levels but caused a significant rise in insulin levels at this time point"
],
"offsets": [
[
405,
549
]
]
},
{
"id": "IEPA.d24.s51",
"type": "",
"text": [
"The oxytocin antagonist 1-deamino-2-D-Tyr-(OEt)-4-Thr-8-Orn-oxytocin administered ICV increased insulin levels itself and therefore the effect on oxytocin-induced insulin secretion was difficult to evaluate"
],
"offsets": [
[
550,
756
]
]
},
{
"id": "IEPA.d24.s52",
"type": "",
"text": [
"Intracerebroventricular injections of 200 ng oxytocin caused a significant rise not only of insulin but also of glucagon and glucose levels"
],
"offsets": [
[
757,
896
]
]
},
{
"id": "IEPA.d24.s53",
"type": "",
"text": [
"In contrast, nanogram amounts of oxytocin administered ICV cause a rise of insulin levels"
],
"offsets": [
[
897,
986
]
]
}
] | [
{
"id": "IEPA.d24.s48.e0",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
52,
60
]
],
"normalized": []
},
{
"id": "IEPA.d24.s48.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
151,
158
]
],
"normalized": []
},
{
"id": "IEPA.d24.s49.e0",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
335,
343
]
],
"normalized": []
},
{
"id": "IEPA.d24.s49.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
354,
361
]
],
"normalized": []
},
{
"id": "IEPA.d24.s50.e0",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
419,
427
]
],
"normalized": []
},
{
"id": "IEPA.d24.s50.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
516,
523
]
],
"normalized": []
},
{
"id": "IEPA.d24.s51.e0",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
554,
562
]
],
"normalized": []
},
{
"id": "IEPA.d24.s51.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
646,
653
]
],
"normalized": []
},
{
"id": "IEPA.d24.s51.e2",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
696,
704
]
],
"normalized": []
},
{
"id": "IEPA.d24.s51.e3",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
713,
720
]
],
"normalized": []
},
{
"id": "IEPA.d24.s52.e0",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
802,
810
]
],
"normalized": []
},
{
"id": "IEPA.d24.s52.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
849,
856
]
],
"normalized": []
},
{
"id": "IEPA.d24.s53.e0",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
930,
938
]
],
"normalized": []
},
{
"id": "IEPA.d24.s53.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
972,
979
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d24.s48.i0",
"type": "PPI",
"arg1_id": "IEPA.d24.s48.e0",
"arg2_id": "IEPA.d24.s48.e1",
"normalized": []
},
{
"id": "IEPA.d24.s49.i0",
"type": "PPI",
"arg1_id": "IEPA.d24.s49.e0",
"arg2_id": "IEPA.d24.s49.e1",
"normalized": []
},
{
"id": "IEPA.d24.s50.i0",
"type": "PPI",
"arg1_id": "IEPA.d24.s50.e0",
"arg2_id": "IEPA.d24.s50.e1",
"normalized": []
},
{
"id": "IEPA.d24.s51.i0",
"type": "PPI",
"arg1_id": "IEPA.d24.s51.e2",
"arg2_id": "IEPA.d24.s51.e3",
"normalized": []
},
{
"id": "IEPA.d24.s52.i0",
"type": "PPI",
"arg1_id": "IEPA.d24.s52.e0",
"arg2_id": "IEPA.d24.s52.e1",
"normalized": []
},
{
"id": "IEPA.d24.s53.i0",
"type": "PPI",
"arg1_id": "IEPA.d24.s53.e0",
"arg2_id": "IEPA.d24.s53.e1",
"normalized": []
}
] |
IEPA.d25 | 8771561 | [
{
"id": "IEPA.d25.s54",
"type": "",
"text": [
"The responses of serum oxytocin (OT) and vasopressin (AVP) to the serotonergic HT1A agonist buspirone (15 mg p.o.) or the HTD1 agonist sumatriptan (6 mg injected subcutaneously) were evaluated in 7 normal men either in basal conditions or during an insulin (0.15 iu/kg as an i.v. bolus) tolerance test (ITT)"
],
"offsets": [
[
0,
307
]
]
},
{
"id": "IEPA.d25.s55",
"type": "",
"text": [
"Stimulation of 5HT-1D receptors with sumatriptan was unable to change neither AVP nor OT response to insulin-induced hypoglycemia"
],
"offsets": [
[
308,
437
]
]
}
] | [
{
"id": "IEPA.d25.s54.e0",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
23,
31
]
],
"normalized": []
},
{
"id": "IEPA.d25.s54.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
249,
256
]
],
"normalized": []
},
{
"id": "IEPA.d25.s55.e0",
"type": "",
"text": [
"OT"
],
"offsets": [
[
394,
396
]
],
"normalized": []
},
{
"id": "IEPA.d25.s55.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
409,
416
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d25.s55.i0",
"type": "PPI",
"arg1_id": "IEPA.d25.s55.e0",
"arg2_id": "IEPA.d25.s55.e1",
"normalized": []
}
] |
IEPA.d26 | 8777160 | [
{
"id": "IEPA.d26.s56",
"type": "",
"text": [
"The SGR and RGR also had different endocrine profiles with, for example, twice as high oxytocin (p < 0.01) and insulin levels (p < 0.01) in RGR compared to the SGR"
],
"offsets": [
[
0,
163
]
]
}
] | [
{
"id": "IEPA.d26.s56.e0",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
87,
95
]
],
"normalized": []
},
{
"id": "IEPA.d26.s56.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
111,
118
]
],
"normalized": []
}
] | [] | [] | [] |
IEPA.d27 | 8795088 | [
{
"id": "IEPA.d27.s57",
"type": "",
"text": [
"8-OH-DPAT also increased insulin and decreased CCK and somatostatin levels, effects that were blocked by pretreatment with the oxytocin antagonist"
],
"offsets": [
[
0,
146
]
]
},
{
"id": "IEPA.d27.s58",
"type": "",
"text": [
"Taken together, these data suggest that the effect of 8-OH-DPAT on plasma levels of insulin, somatostatin and CCK may be mediated by oxytocin"
],
"offsets": [
[
147,
288
]
]
},
{
"id": "IEPA.d27.s59",
"type": "",
"text": [
"In previous experiments, we have shown that following i.c.v. application of oxytocin, plasma levels of insulin are increased through a cholinergic mechanism"
],
"offsets": [
[
289,
445
]
]
}
] | [
{
"id": "IEPA.d27.s57.e0",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
25,
32
]
],
"normalized": []
},
{
"id": "IEPA.d27.s57.e1",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
127,
135
]
],
"normalized": []
},
{
"id": "IEPA.d27.s58.e0",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
231,
238
]
],
"normalized": []
},
{
"id": "IEPA.d27.s58.e1",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
280,
288
]
],
"normalized": []
},
{
"id": "IEPA.d27.s59.e0",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
365,
373
]
],
"normalized": []
},
{
"id": "IEPA.d27.s59.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
392,
399
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d27.s57.i0",
"type": "PPI",
"arg1_id": "IEPA.d27.s57.e0",
"arg2_id": "IEPA.d27.s57.e1",
"normalized": []
},
{
"id": "IEPA.d27.s58.i0",
"type": "PPI",
"arg1_id": "IEPA.d27.s58.e0",
"arg2_id": "IEPA.d27.s58.e1",
"normalized": []
},
{
"id": "IEPA.d27.s59.i0",
"type": "PPI",
"arg1_id": "IEPA.d27.s59.e0",
"arg2_id": "IEPA.d27.s59.e1",
"normalized": []
}
] |
IEPA.d28 | 8851493 | [
{
"id": "IEPA.d28.s60",
"type": "",
"text": [
"In HVSMC both oxytocin and AVP increased inositol 1,4,5-trisphosphate (IP3) production and [Ca2+]i response, but the efficacy of the responses was greater for oxytocin than AVP"
],
"offsets": [
[
0,
176
]
]
}
] | [
{
"id": "IEPA.d28.s60.e0",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
14,
22
]
],
"normalized": []
},
{
"id": "IEPA.d28.s60.e1",
"type": "",
"text": [
"inositol 1,4,5-trisphosphate"
],
"offsets": [
[
41,
69
]
],
"normalized": []
},
{
"id": "IEPA.d28.s60.e2",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
159,
167
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d28.s60.i0",
"type": "PPI",
"arg1_id": "IEPA.d28.s60.e0",
"arg2_id": "IEPA.d28.s60.e1",
"normalized": []
}
] |
IEPA.d31 | 8886594 | [
{
"id": "IEPA.d31.s63",
"type": "",
"text": [
"OT may rapidly stimulate inositol (1,4,5)-trisphosphate (IP3) and diacylglycerol (DAG) formation, consistent with the concept of rapid activation of a second-messenger system"
],
"offsets": [
[
0,
174
]
]
},
{
"id": "IEPA.d31.s64",
"type": "",
"text": [
"In support of this hypothesis, endometrial IP3 levels were increased (P < 0.05) within 0.5 min after treatment with 0.1 microM OT"
],
"offsets": [
[
175,
304
]
]
},
{
"id": "IEPA.d31.s65",
"type": "",
"text": [
"These results indicate that OT induces endometrial IP3 production in a rapid manner indicative of a second-messenger system"
],
"offsets": [
[
305,
428
]
]
}
] | [
{
"id": "IEPA.d31.s63.e0",
"type": "",
"text": [
"OT"
],
"offsets": [
[
0,
2
]
],
"normalized": []
},
{
"id": "IEPA.d31.s63.e1",
"type": "",
"text": [
"inositol (1,4,5)-trisphosphate"
],
"offsets": [
[
25,
55
]
],
"normalized": []
},
{
"id": "IEPA.d31.s64.e0",
"type": "",
"text": [
"IP3"
],
"offsets": [
[
218,
221
]
],
"normalized": []
},
{
"id": "IEPA.d31.s64.e1",
"type": "",
"text": [
"OT"
],
"offsets": [
[
302,
304
]
],
"normalized": []
},
{
"id": "IEPA.d31.s65.e0",
"type": "",
"text": [
"OT"
],
"offsets": [
[
333,
335
]
],
"normalized": []
},
{
"id": "IEPA.d31.s65.e1",
"type": "",
"text": [
"IP3"
],
"offsets": [
[
356,
359
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d31.s63.i0",
"type": "PPI",
"arg1_id": "IEPA.d31.s63.e0",
"arg2_id": "IEPA.d31.s63.e1",
"normalized": []
},
{
"id": "IEPA.d31.s64.i0",
"type": "PPI",
"arg1_id": "IEPA.d31.s64.e0",
"arg2_id": "IEPA.d31.s64.e1",
"normalized": []
},
{
"id": "IEPA.d31.s65.i0",
"type": "PPI",
"arg1_id": "IEPA.d31.s65.e0",
"arg2_id": "IEPA.d31.s65.e1",
"normalized": []
}
] |
IEPA.d32 | 8952001 | [
{
"id": "IEPA.d32.s66",
"type": "",
"text": [
"Gamma-aminobutyric acid mediation of the inhibitory effect of nitric oxide on the arginine vasopressin and oxytocin responses to insulin-induced hypoglycemia"
],
"offsets": [
[
0,
157
]
]
},
{
"id": "IEPA.d32.s67",
"type": "",
"text": [
"Previous studies have demonstrated that the nitric oxide (NO) synthase inhibitor L-NAME exerts positive effects on the arginine vasopressin (AVP) and oxytocin (OT) responses to insulin-induced hypoglycemia, suggesting inhibitory actions of NO"
],
"offsets": [
[
158,
400
]
]
},
{
"id": "IEPA.d32.s68",
"type": "",
"text": [
"AVP and OT secretory patterns during insulin (0.15 IU/kg, i.v.)-tolerance tests (ITT) were examined in seven normal male subjects with (experimental tests) and without (control test) concomitant treatment with L-NAME (40 micrograms/kg injected plus 50 micrograms/kg infused, i.v.), the GABAergic agent sodium valproate (600 mg in three divided doses orally) or the combination of L-NAME and sodium valproate"
],
"offsets": [
[
401,
808
]
]
},
{
"id": "IEPA.d32.s69",
"type": "",
"text": [
"Insulin-induced hypoglycemia increased by 2-fold (peak vs. baseline) plasma AVP and OT levels"
],
"offsets": [
[
809,
902
]
]
},
{
"id": "IEPA.d32.s70",
"type": "",
"text": [
"These data indicate a GABAergic mediation of the inhibitory modulation by NO of the AVP and OT responses to insulin-induced hypoglycemia"
],
"offsets": [
[
903,
1039
]
]
}
] | [
{
"id": "IEPA.d32.s66.e0",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
107,
115
]
],
"normalized": []
},
{
"id": "IEPA.d32.s66.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
129,
136
]
],
"normalized": []
},
{
"id": "IEPA.d32.s67.e0",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
308,
316
]
],
"normalized": []
},
{
"id": "IEPA.d32.s67.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
335,
342
]
],
"normalized": []
},
{
"id": "IEPA.d32.s68.e0",
"type": "",
"text": [
"OT"
],
"offsets": [
[
409,
411
]
],
"normalized": []
},
{
"id": "IEPA.d32.s68.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
438,
445
]
],
"normalized": []
},
{
"id": "IEPA.d32.s69.e0",
"type": "",
"text": [
"Insulin"
],
"offsets": [
[
809,
816
]
],
"normalized": []
},
{
"id": "IEPA.d32.s69.e1",
"type": "",
"text": [
"OT"
],
"offsets": [
[
893,
895
]
],
"normalized": []
},
{
"id": "IEPA.d32.s70.e0",
"type": "",
"text": [
"OT"
],
"offsets": [
[
995,
997
]
],
"normalized": []
},
{
"id": "IEPA.d32.s70.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
1011,
1018
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d32.s66.i0",
"type": "PPI",
"arg1_id": "IEPA.d32.s66.e0",
"arg2_id": "IEPA.d32.s66.e1",
"normalized": []
},
{
"id": "IEPA.d32.s67.i0",
"type": "PPI",
"arg1_id": "IEPA.d32.s67.e0",
"arg2_id": "IEPA.d32.s67.e1",
"normalized": []
},
{
"id": "IEPA.d32.s69.i0",
"type": "PPI",
"arg1_id": "IEPA.d32.s69.e0",
"arg2_id": "IEPA.d32.s69.e1",
"normalized": []
},
{
"id": "IEPA.d32.s70.i0",
"type": "PPI",
"arg1_id": "IEPA.d32.s70.e0",
"arg2_id": "IEPA.d32.s70.e1",
"normalized": []
}
] |
IEPA.d33 | 8987334 | [
{
"id": "IEPA.d33.s71",
"type": "",
"text": [
"Correlation between the stimulatory effect of oxytocin on the formation of inositol phosphates and the oxytocin receptor level in the pregnant rabbit myometrium"
],
"offsets": [
[
0,
160
]
]
},
{
"id": "IEPA.d33.s72",
"type": "",
"text": [
"OBJECTIVE: In order to elucidate the roles of inositol trisphosphate (IP3) and oxytocin (OT) receptors in rabbit parturition, the concentration of IP3 induced by OT and the OT receptor levels were determined in rabbit myometria before and after parturition"
],
"offsets": [
[
161,
417
]
]
},
{
"id": "IEPA.d33.s73",
"type": "",
"text": [
"METHODS: The effects of OT on IP3 formation and OT receptor levels were determined in the myometria of non-pregnant rabbits, Days 26, 28 and 30 of pregnancy rabbits, postpartum rabbits within 12 hours and steroid-treated ovariectomized rabbits"
],
"offsets": [
[
418,
661
]
]
},
{
"id": "IEPA.d33.s74",
"type": "",
"text": [
"RESULTS: OT receptors were not detectable in the myometria of non-pregnant rabbits, and OT had no effect on the formation of inositol phosphates (IPs)"
],
"offsets": [
[
662,
812
]
]
},
{
"id": "IEPA.d33.s75",
"type": "",
"text": [
"On Day 28 of pregnancy, OT receptors became detectable, and then OT could induce the formation of IPs"
],
"offsets": [
[
813,
914
]
]
},
{
"id": "IEPA.d33.s76",
"type": "",
"text": [
"Thereafter, the stimulatory effects of OT on IPs formation and the OT receptor levels dramatically increased toward the end of pregnancy and reduced rapidly after parturition"
],
"offsets": [
[
915,
1089
]
]
},
{
"id": "IEPA.d33.s77",
"type": "",
"text": [
"When the ovariectomized pregnant rabbits were treated with estrogen, OT receptors in the myometrium were induced, and OT acquired the ability to stimulate IP3 formation"
],
"offsets": [
[
1090,
1258
]
]
},
{
"id": "IEPA.d33.s78",
"type": "",
"text": [
"In addition, an OT receptor antagonist inhibited the stimulatory effects of OT on IP3 formation"
],
"offsets": [
[
1259,
1354
]
]
},
{
"id": "IEPA.d33.s79",
"type": "",
"text": [
"CONCLUSIONS: These results suggest that the formation of IPs by OT, the OT receptor levels in the myometrium, and the production of PGF2 in the decidua might play crucial roles in parturition"
],
"offsets": [
[
1355,
1546
]
]
}
] | [
{
"id": "IEPA.d33.s71.e0",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
46,
54
]
],
"normalized": []
},
{
"id": "IEPA.d33.s71.e1",
"type": "",
"text": [
"inositol phosphates"
],
"offsets": [
[
75,
94
]
],
"normalized": []
},
{
"id": "IEPA.d33.s72.e0",
"type": "",
"text": [
"inositol trisphosphate"
],
"offsets": [
[
207,
229
]
],
"normalized": []
},
{
"id": "IEPA.d33.s72.e1",
"type": "",
"text": [
"IP3"
],
"offsets": [
[
308,
311
]
],
"normalized": []
},
{
"id": "IEPA.d33.s72.e2",
"type": "",
"text": [
"OT"
],
"offsets": [
[
323,
325
]
],
"normalized": []
},
{
"id": "IEPA.d33.s73.e0",
"type": "",
"text": [
"OT"
],
"offsets": [
[
442,
444
]
],
"normalized": []
},
{
"id": "IEPA.d33.s73.e1",
"type": "",
"text": [
"IP3"
],
"offsets": [
[
448,
451
]
],
"normalized": []
},
{
"id": "IEPA.d33.s74.e0",
"type": "",
"text": [
"OT"
],
"offsets": [
[
750,
752
]
],
"normalized": []
},
{
"id": "IEPA.d33.s74.e1",
"type": "",
"text": [
"inositol phosphates"
],
"offsets": [
[
787,
806
]
],
"normalized": []
},
{
"id": "IEPA.d33.s75.e0",
"type": "",
"text": [
"OT"
],
"offsets": [
[
878,
880
]
],
"normalized": []
},
{
"id": "IEPA.d33.s75.e1",
"type": "",
"text": [
"IPs"
],
"offsets": [
[
911,
914
]
],
"normalized": []
},
{
"id": "IEPA.d33.s76.e0",
"type": "",
"text": [
"OT"
],
"offsets": [
[
954,
956
]
],
"normalized": []
},
{
"id": "IEPA.d33.s76.e1",
"type": "",
"text": [
"IPs"
],
"offsets": [
[
960,
963
]
],
"normalized": []
},
{
"id": "IEPA.d33.s77.e0",
"type": "",
"text": [
"OT"
],
"offsets": [
[
1208,
1210
]
],
"normalized": []
},
{
"id": "IEPA.d33.s77.e1",
"type": "",
"text": [
"IP3"
],
"offsets": [
[
1245,
1248
]
],
"normalized": []
},
{
"id": "IEPA.d33.s78.e0",
"type": "",
"text": [
"OT"
],
"offsets": [
[
1335,
1337
]
],
"normalized": []
},
{
"id": "IEPA.d33.s78.e1",
"type": "",
"text": [
"IP3"
],
"offsets": [
[
1341,
1344
]
],
"normalized": []
},
{
"id": "IEPA.d33.s79.e0",
"type": "",
"text": [
"IPs"
],
"offsets": [
[
1412,
1415
]
],
"normalized": []
},
{
"id": "IEPA.d33.s79.e1",
"type": "",
"text": [
"OT"
],
"offsets": [
[
1419,
1421
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d33.s71.i0",
"type": "PPI",
"arg1_id": "IEPA.d33.s71.e0",
"arg2_id": "IEPA.d33.s71.e1",
"normalized": []
},
{
"id": "IEPA.d33.s72.i0",
"type": "PPI",
"arg1_id": "IEPA.d33.s72.e1",
"arg2_id": "IEPA.d33.s72.e2",
"normalized": []
},
{
"id": "IEPA.d33.s74.i0",
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"arg2_id": "IEPA.d33.s74.e1",
"normalized": []
},
{
"id": "IEPA.d33.s75.i0",
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"arg2_id": "IEPA.d33.s75.e1",
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},
{
"id": "IEPA.d33.s76.i0",
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"normalized": []
},
{
"id": "IEPA.d33.s77.i0",
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"arg1_id": "IEPA.d33.s77.e0",
"arg2_id": "IEPA.d33.s77.e1",
"normalized": []
},
{
"id": "IEPA.d33.s78.i0",
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"arg2_id": "IEPA.d33.s78.e1",
"normalized": []
},
{
"id": "IEPA.d33.s79.i0",
"type": "PPI",
"arg1_id": "IEPA.d33.s79.e0",
"arg2_id": "IEPA.d33.s79.e1",
"normalized": []
}
] |
IEPA.d34 | 9003017 | [
{
"id": "IEPA.d34.s80",
"type": "",
"text": [
"Immunohistochemical localization of leptin and uncoupling protein in white and brown adipose tissue"
],
"offsets": [
[
0,
99
]
]
},
{
"id": "IEPA.d34.s81",
"type": "",
"text": [
"To establish the cell type expressing leptin, we also assessed the size and organization of lipid droplets, the ultrastructural features of mitochondria, and the presence or absence of uncoupling protein, a brown fat-specific marker"
],
"offsets": [
[
100,
332
]
]
},
{
"id": "IEPA.d34.s82",
"type": "",
"text": [
"In brown adipose tissue of lean animals, multilocular uncoupling protein (UCP)-positive brown adipocytes had typical brown mitochondria and were leptin-negative, both in fed and fasted conditions"
],
"offsets": [
[
333,
528
]
]
},
{
"id": "IEPA.d34.s83",
"type": "",
"text": [
"At the periphery of the interscapular brown adipose tissue depot, unilocular, UCP-negative adipocytes (mean diameter: 41.55 microns) with white-type mitochondria were observed, and these cells were leptin-positive"
],
"offsets": [
[
529,
742
]
]
},
{
"id": "IEPA.d34.s84",
"type": "",
"text": [
"In obese (db/db) animals, brown fat was composed mainly of small unilocular, UCP-positive adipocytes (mean diameter: 40.08 microns), which were also leptin-positive"
],
"offsets": [
[
743,
907
]
]
},
{
"id": "IEPA.d34.s85",
"type": "",
"text": [
"In summary, classical brown adipocytes differ from white adipocytes, not only by their morphology and UCP expression, but also by their apparent lack of detectable leptin expression"
],
"offsets": [
[
908,
1089
]
]
}
] | [
{
"id": "IEPA.d34.s80.e0",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
36,
42
]
],
"normalized": []
},
{
"id": "IEPA.d34.s80.e1",
"type": "",
"text": [
"uncoupling protein"
],
"offsets": [
[
47,
65
]
],
"normalized": []
},
{
"id": "IEPA.d34.s81.e0",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
138,
144
]
],
"normalized": []
},
{
"id": "IEPA.d34.s81.e1",
"type": "",
"text": [
"uncoupling protein"
],
"offsets": [
[
285,
303
]
],
"normalized": []
},
{
"id": "IEPA.d34.s82.e0",
"type": "",
"text": [
"uncoupling protein"
],
"offsets": [
[
387,
405
]
],
"normalized": []
},
{
"id": "IEPA.d34.s82.e1",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
478,
484
]
],
"normalized": []
},
{
"id": "IEPA.d34.s83.e0",
"type": "",
"text": [
"UCP"
],
"offsets": [
[
607,
610
]
],
"normalized": []
},
{
"id": "IEPA.d34.s83.e1",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
727,
733
]
],
"normalized": []
},
{
"id": "IEPA.d34.s84.e0",
"type": "",
"text": [
"UCP"
],
"offsets": [
[
820,
823
]
],
"normalized": []
},
{
"id": "IEPA.d34.s84.e1",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
892,
898
]
],
"normalized": []
},
{
"id": "IEPA.d34.s85.e0",
"type": "",
"text": [
"UCP"
],
"offsets": [
[
1010,
1013
]
],
"normalized": []
},
{
"id": "IEPA.d34.s85.e1",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
1072,
1078
]
],
"normalized": []
}
] | [] | [] | [] |
IEPA.d36 | 9005971 | [
{
"id": "IEPA.d36.s87",
"type": "",
"text": [
"Wortmannin converts insulin but not oxytocin from an antilipolytic to a lipolytic agent in the presence of forskolin"
],
"offsets": [
[
0,
116
]
]
},
{
"id": "IEPA.d36.s88",
"type": "",
"text": [
"The present studies compared the effects of insulin in rat adipocytes with the effects of oxytocin and peroxovanadate, which mimic some effects of insulin"
],
"offsets": [
[
117,
271
]
]
},
{
"id": "IEPA.d36.s89",
"type": "",
"text": [
"The antilipolytic effects of peroxovanadate and oxytocin were unaffected by 500 nmol/L wortmannin, which blocked the antilipolytic action of insulin"
],
"offsets": [
[
272,
420
]
]
},
{
"id": "IEPA.d36.s90",
"type": "",
"text": [
"The data provide additional support for the hypothesis that oxytocin and peroxovanadate affect adipose tissue metabolism by mechanisms distinctly different from those involved in insulin action"
],
"offsets": [
[
421,
614
]
]
}
] | [
{
"id": "IEPA.d36.s87.e0",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
20,
27
]
],
"normalized": []
},
{
"id": "IEPA.d36.s87.e1",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
36,
44
]
],
"normalized": []
},
{
"id": "IEPA.d36.s88.e0",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
161,
168
]
],
"normalized": []
},
{
"id": "IEPA.d36.s88.e1",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
207,
215
]
],
"normalized": []
},
{
"id": "IEPA.d36.s88.e2",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
264,
271
]
],
"normalized": []
},
{
"id": "IEPA.d36.s89.e0",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
320,
328
]
],
"normalized": []
},
{
"id": "IEPA.d36.s89.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
413,
420
]
],
"normalized": []
},
{
"id": "IEPA.d36.s90.e0",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
481,
489
]
],
"normalized": []
},
{
"id": "IEPA.d36.s90.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
600,
607
]
],
"normalized": []
}
] | [] | [] | [] |
IEPA.d37 | 9013600 | [
{
"id": "IEPA.d37.s91",
"type": "",
"text": [
"These findings support the concept that the mitochondrial metabolism of nutrient molecules is an event sufficient to acutely augment insulin release from the beta cell, to increase phospholipase C-mediated phosphoinositide hydrolysis, and to induce time-dependent potentiation of insulin secretion"
],
"offsets": [
[
0,
297
]
]
}
] | [
{
"id": "IEPA.d37.s91.e0",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
133,
140
]
],
"normalized": []
},
{
"id": "IEPA.d37.s91.e1",
"type": "",
"text": [
"phospholipase C"
],
"offsets": [
[
181,
196
]
],
"normalized": []
},
{
"id": "IEPA.d37.s91.e2",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
280,
287
]
],
"normalized": []
}
] | [] | [] | [] |
IEPA.d38 | 9057099 | [
{
"id": "IEPA.d38.s92",
"type": "",
"text": [
"2) IGF-1, IGF-2, and insulin also induced a Ca2+ mobilization from the endoplasmic reticulum: phospholipase C (PLC) inhibitors, neomycin, or U-73122 partially blocked the intracellular [Ca2+]i increase induced by IGF-1 and insulin and totally inhibited the effect of IGF-2"
],
"offsets": [
[
0,
272
]
]
}
] | [
{
"id": "IEPA.d38.s92.e0",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
21,
28
]
],
"normalized": []
},
{
"id": "IEPA.d38.s92.e1",
"type": "",
"text": [
"phospholipase C"
],
"offsets": [
[
94,
109
]
],
"normalized": []
},
{
"id": "IEPA.d38.s92.e2",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
223,
230
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d38.s92.i0",
"type": "PPI",
"arg1_id": "IEPA.d38.s92.e1",
"arg2_id": "IEPA.d38.s92.e2",
"normalized": []
}
] |
IEPA.d39 | 9126376 | [
{
"id": "IEPA.d39.s93",
"type": "",
"text": [
"Homogeneous liposome immunoassay for insulin using phospholipase C from Clostridium perfringens"
],
"offsets": [
[
0,
95
]
]
},
{
"id": "IEPA.d39.s94",
"type": "",
"text": [
"Insulin was conjugated to phospholipase C by a three-step procedure with hetero-bifunctional crosslinking reagents, succinimidyl 4-(N-maleimidomethyl)cyclohexane-1-carboxylate and 3-(2-pyridyldithio)propionic acid N-hydroxysuccinimide ester"
],
"offsets": [
[
96,
336
]
]
},
{
"id": "IEPA.d39.s95",
"type": "",
"text": [
"Both p-nitrophenylphosphatidylcholine hydrolytic activity and liposome lytic activity of insulin-phospholipase C conjugate were inhibited in the presence of insulin antiserum"
],
"offsets": [
[
337,
511
]
]
}
] | [
{
"id": "IEPA.d39.s93.e0",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
37,
44
]
],
"normalized": []
},
{
"id": "IEPA.d39.s93.e1",
"type": "",
"text": [
"phospholipase C"
],
"offsets": [
[
51,
66
]
],
"normalized": []
},
{
"id": "IEPA.d39.s94.e0",
"type": "",
"text": [
"Insulin"
],
"offsets": [
[
96,
103
]
],
"normalized": []
},
{
"id": "IEPA.d39.s94.e1",
"type": "",
"text": [
"phospholipase C"
],
"offsets": [
[
122,
137
]
],
"normalized": []
},
{
"id": "IEPA.d39.s95.e0",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
426,
433
]
],
"normalized": []
},
{
"id": "IEPA.d39.s95.e1",
"type": "",
"text": [
"phospholipase C"
],
"offsets": [
[
434,
449
]
],
"normalized": []
},
{
"id": "IEPA.d39.s95.e2",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
494,
501
]
],
"normalized": []
}
] | [] | [] | [] |
IEPA.d40 | 9135570 | [
{
"id": "IEPA.d40.s96",
"type": "",
"text": [
"Roles of GTP and phospholipase C in the potentiation of Ca(2+)-induced insulin secretion by glucose in rat pancreatic islets"
],
"offsets": [
[
0,
124
]
]
},
{
"id": "IEPA.d40.s97",
"type": "",
"text": [
"There was a 98% greater augmentation of insulin secretion by 16.7 mM glucose (in the presence of diazoxide and 40 mM K+) in primed islets; however, the ability of high glucose to augment PLC activity bore no relationship to the secretory response"
],
"offsets": [
[
125,
371
]
]
},
{
"id": "IEPA.d40.s98",
"type": "",
"text": [
"MPA markedly inhibited PLC in both conditions; however, insulin secretion was only inhibited (by 46%) in primed islets"
],
"offsets": [
[
372,
490
]
]
},
{
"id": "IEPA.d40.s99",
"type": "",
"text": [
"These data indicate that an adequate level of GTP is critical for glucose's potentiation of Ca(2+)-induced insulin secretion in primed islets but that PLC activation can clearly be dissociated from insulin secretion and therefore cannot be the major cause of glucose's augmentation of Ca(2+)-induced insulin secretion"
],
"offsets": [
[
491,
808
]
]
}
] | [
{
"id": "IEPA.d40.s96.e0",
"type": "",
"text": [
"phospholipase C"
],
"offsets": [
[
17,
32
]
],
"normalized": []
},
{
"id": "IEPA.d40.s96.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
71,
78
]
],
"normalized": []
},
{
"id": "IEPA.d40.s97.e0",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
165,
172
]
],
"normalized": []
},
{
"id": "IEPA.d40.s97.e1",
"type": "",
"text": [
"PLC"
],
"offsets": [
[
312,
315
]
],
"normalized": []
},
{
"id": "IEPA.d40.s98.e0",
"type": "",
"text": [
"PLC"
],
"offsets": [
[
395,
398
]
],
"normalized": []
},
{
"id": "IEPA.d40.s98.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
428,
435
]
],
"normalized": []
},
{
"id": "IEPA.d40.s99.e0",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
598,
605
]
],
"normalized": []
},
{
"id": "IEPA.d40.s99.e1",
"type": "",
"text": [
"PLC"
],
"offsets": [
[
642,
645
]
],
"normalized": []
},
{
"id": "IEPA.d40.s99.e2",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
689,
696
]
],
"normalized": []
},
{
"id": "IEPA.d40.s99.e3",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
791,
798
]
],
"normalized": []
}
] | [] | [] | [] |
IEPA.d41 | 9142890 | [
{
"id": "IEPA.d41.s100",
"type": "",
"text": [
"Regulation of insulin secretion via ATP-sensitive K+ channel independent mechanisms: role of phospholipase C"
],
"offsets": [
[
0,
108
]
]
},
{
"id": "IEPA.d41.s101",
"type": "",
"text": [
"The further addition of carbachol, an agonist that activates an isozyme of phospholipase C distinct from that activated by glucose, together with K+, 20 mM glucose, plus diazoxide resulted in a sustained amplification of insulin secretion from mouse but not rat islets"
],
"offsets": [
[
109,
377
]
]
},
{
"id": "IEPA.d41.s102",
"type": "",
"text": [
"The inability to activate a nutrient- and calcium-regulated phospholipase C isozyme in mouse islets to the same extent as in rat islets appears to account, at least in part, for these different insulin secretory responses under these unique conditions"
],
"offsets": [
[
378,
629
]
]
}
] | [
{
"id": "IEPA.d41.s100.e0",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
14,
21
]
],
"normalized": []
},
{
"id": "IEPA.d41.s100.e1",
"type": "",
"text": [
"phospholipase C"
],
"offsets": [
[
93,
108
]
],
"normalized": []
},
{
"id": "IEPA.d41.s101.e0",
"type": "",
"text": [
"phospholipase C"
],
"offsets": [
[
184,
199
]
],
"normalized": []
},
{
"id": "IEPA.d41.s101.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
330,
337
]
],
"normalized": []
},
{
"id": "IEPA.d41.s102.e0",
"type": "",
"text": [
"phospholipase C"
],
"offsets": [
[
438,
453
]
],
"normalized": []
},
{
"id": "IEPA.d41.s102.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
572,
579
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d41.s100.i0",
"type": "PPI",
"arg1_id": "IEPA.d41.s100.e0",
"arg2_id": "IEPA.d41.s100.e1",
"normalized": []
},
{
"id": "IEPA.d41.s101.i0",
"type": "PPI",
"arg1_id": "IEPA.d41.s101.e0",
"arg2_id": "IEPA.d41.s101.e1",
"normalized": []
},
{
"id": "IEPA.d41.s102.i0",
"type": "PPI",
"arg1_id": "IEPA.d41.s102.e0",
"arg2_id": "IEPA.d41.s102.e1",
"normalized": []
}
] |
IEPA.d43 | 9177227 | [
{
"id": "IEPA.d43.s108",
"type": "",
"text": [
"Induction by leptin of uncoupling protein-2 and enzymes of fatty acid oxidation"
],
"offsets": [
[
0,
79
]
]
},
{
"id": "IEPA.d43.s109",
"type": "",
"text": [
"Here we show that leptin alters in pancreatic islets the mRNA of the genes encoding enzymes of free fatty acid metabolism and uncoupling protein-2 (UCP-2)"
],
"offsets": [
[
80,
234
]
]
},
{
"id": "IEPA.d43.s110",
"type": "",
"text": [
"Leptin overexpression increased UCP-2 mRNA by more than 10-fold in epididymal, retroperitoneal, and subcutaneous fat tissue of normal, but not of leptin-receptor-defective obese rats"
],
"offsets": [
[
235,
417
]
]
},
{
"id": "IEPA.d43.s111",
"type": "",
"text": [
"By directly regulating the expression of enzymes of free fatty acid metabolism and of UCP-2, leptin controls intracellular triglyceride content of certain nonadipocytes, as well as adipocytes"
],
"offsets": [
[
418,
609
]
]
}
] | [
{
"id": "IEPA.d43.s108.e0",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
13,
19
]
],
"normalized": []
},
{
"id": "IEPA.d43.s108.e1",
"type": "",
"text": [
"uncoupling protein-2"
],
"offsets": [
[
23,
43
]
],
"normalized": []
},
{
"id": "IEPA.d43.s109.e0",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
98,
104
]
],
"normalized": []
},
{
"id": "IEPA.d43.s109.e1",
"type": "",
"text": [
"uncoupling protein-2"
],
"offsets": [
[
206,
226
]
],
"normalized": []
},
{
"id": "IEPA.d43.s110.e0",
"type": "",
"text": [
"Leptin"
],
"offsets": [
[
235,
241
]
],
"normalized": []
},
{
"id": "IEPA.d43.s110.e1",
"type": "",
"text": [
"UCP-2"
],
"offsets": [
[
267,
272
]
],
"normalized": []
},
{
"id": "IEPA.d43.s111.e0",
"type": "",
"text": [
"UCP-2"
],
"offsets": [
[
504,
509
]
],
"normalized": []
},
{
"id": "IEPA.d43.s111.e1",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
511,
517
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d43.s108.i0",
"type": "PPI",
"arg1_id": "IEPA.d43.s108.e0",
"arg2_id": "IEPA.d43.s108.e1",
"normalized": []
},
{
"id": "IEPA.d43.s109.i0",
"type": "PPI",
"arg1_id": "IEPA.d43.s109.e0",
"arg2_id": "IEPA.d43.s109.e1",
"normalized": []
},
{
"id": "IEPA.d43.s110.i0",
"type": "PPI",
"arg1_id": "IEPA.d43.s110.e0",
"arg2_id": "IEPA.d43.s110.e1",
"normalized": []
},
{
"id": "IEPA.d43.s111.i0",
"type": "PPI",
"arg1_id": "IEPA.d43.s111.e0",
"arg2_id": "IEPA.d43.s111.e1",
"normalized": []
}
] |
IEPA.d44 | 9186274 | [
{
"id": "IEPA.d44.s112",
"type": "",
"text": [
"Further, the oxytocin-induced activation of IK(sl) was effectively antagonized by 5 x 10(-8) mol/l U-73122 or 5 x 10(-6) mol/l 2-nitro-4-carboxyphenyl N,N-diphenylcarbamate (inhibitors of the cell membrane phospholipase C), as well as by intracellularly applied heparin (selective inhibitor of inositol-1,4,5-trisphosphate (IP3)-induced Ca2+ release channels)"
],
"offsets": [
[
0,
359
]
]
},
{
"id": "IEPA.d44.s113",
"type": "",
"text": [
"The data obtained suggest (i) that selective oxytocin receptors are present on the membranes of guinea-pig antral smooth muscle cells, (ii) that the oxytocin-related relaxation may result from the activation of Ca(2+)-sensitive K+ conductivity via activation of IP3-induced release of Ca2+ from the submembrane located cisternae of the sarcoplasmic reticulum Ca2+ stores and (iii) in turn, this evokes a non-inactivating component of IK, hyperpolarizing the cell membrane"
],
"offsets": [
[
360,
831
]
]
}
] | [
{
"id": "IEPA.d44.s112.e0",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
13,
21
]
],
"normalized": []
},
{
"id": "IEPA.d44.s112.e1",
"type": "",
"text": [
"inositol-1,4,5-trisphosphate"
],
"offsets": [
[
294,
322
]
],
"normalized": []
},
{
"id": "IEPA.d44.s113.e0",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
405,
413
]
],
"normalized": []
},
{
"id": "IEPA.d44.s113.e1",
"type": "",
"text": [
"IP3"
],
"offsets": [
[
622,
625
]
],
"normalized": []
}
] | [] | [] | [] |
IEPA.d45 | 9187302 | [
{
"id": "IEPA.d45.s114",
"type": "",
"text": [
"Cellular preincubation with 200 microg/ml antibodies against the inositolphosphoglycan (IPG) moiety of the GPI-anchor (Ab(IPG)), or depletion in GPI-anchored proteins by cellular pretreatment with 0.5 U/ml PI-PLC, 1 mM insulin and 2 HU/ml streptolysin-O, or depletion in membrane cholesterol content by filipin (5 microg/ml), digitonin (5 microg/ml) and cholesterol oxidase (0.5 U/ml) decreases the HDL3-signal, suggesting the involvement of a lipolytic cleavage of GPI-anchored proteins"
],
"offsets": [
[
0,
487
]
]
}
] | [
{
"id": "IEPA.d45.s114.e0",
"type": "",
"text": [
"PLC"
],
"offsets": [
[
209,
212
]
],
"normalized": []
},
{
"id": "IEPA.d45.s114.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
219,
226
]
],
"normalized": []
}
] | [] | [] | [] |
IEPA.d48 | 9252501 | [
{
"id": "IEPA.d48.s123",
"type": "",
"text": [
"Leptin increases uncoupling protein expression and energy expenditure"
],
"offsets": [
[
0,
69
]
]
},
{
"id": "IEPA.d48.s124",
"type": "",
"text": [
"Leptin increased BAT UCP mRNA levels greater than twofold in both ad libitum-fed and food-restricted rats"
],
"offsets": [
[
70,
175
]
]
},
{
"id": "IEPA.d48.s125",
"type": "",
"text": [
"These data demonstrate a leptin-induced increase in energy expenditure in nonmutant rodents and suggest that one mechanism by which leptin increases energy expenditure is through increased thermogenesis in BAT, including increased expression of UCP"
],
"offsets": [
[
176,
424
]
]
}
] | [
{
"id": "IEPA.d48.s123.e0",
"type": "",
"text": [
"Leptin"
],
"offsets": [
[
0,
6
]
],
"normalized": []
},
{
"id": "IEPA.d48.s123.e1",
"type": "",
"text": [
"uncoupling protein"
],
"offsets": [
[
17,
35
]
],
"normalized": []
},
{
"id": "IEPA.d48.s124.e0",
"type": "",
"text": [
"Leptin"
],
"offsets": [
[
70,
76
]
],
"normalized": []
},
{
"id": "IEPA.d48.s124.e1",
"type": "",
"text": [
"UCP"
],
"offsets": [
[
91,
94
]
],
"normalized": []
},
{
"id": "IEPA.d48.s125.e0",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
201,
207
]
],
"normalized": []
},
{
"id": "IEPA.d48.s125.e1",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
308,
314
]
],
"normalized": []
},
{
"id": "IEPA.d48.s125.e2",
"type": "",
"text": [
"UCP"
],
"offsets": [
[
421,
424
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d48.s123.i0",
"type": "PPI",
"arg1_id": "IEPA.d48.s123.e0",
"arg2_id": "IEPA.d48.s123.e1",
"normalized": []
},
{
"id": "IEPA.d48.s124.i0",
"type": "PPI",
"arg1_id": "IEPA.d48.s124.e0",
"arg2_id": "IEPA.d48.s124.e1",
"normalized": []
},
{
"id": "IEPA.d48.s125.i0",
"type": "PPI",
"arg1_id": "IEPA.d48.s125.e1",
"arg2_id": "IEPA.d48.s125.e2",
"normalized": []
}
] |
IEPA.d52 | 9305858 | [
{
"id": "IEPA.d52.s135",
"type": "",
"text": [
"Uncoupling protein-3 is a mediator of thermogenesis regulated by thyroid hormone, beta3-adrenergic agonists, and leptin"
],
"offsets": [
[
0,
119
]
]
},
{
"id": "IEPA.d52.s136",
"type": "",
"text": [
"UCP3 mRNA levels were also regulated by dexamethasone, leptin, and starvation, albeit differently in muscle and brown adipose tissue"
],
"offsets": [
[
120,
252
]
]
}
] | [
{
"id": "IEPA.d52.s135.e0",
"type": "",
"text": [
"Uncoupling protein-3"
],
"offsets": [
[
0,
20
]
],
"normalized": []
},
{
"id": "IEPA.d52.s135.e1",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
113,
119
]
],
"normalized": []
},
{
"id": "IEPA.d52.s136.e0",
"type": "",
"text": [
"UCP3"
],
"offsets": [
[
120,
124
]
],
"normalized": []
},
{
"id": "IEPA.d52.s136.e1",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
175,
181
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d52.s135.i0",
"type": "PPI",
"arg1_id": "IEPA.d52.s135.e0",
"arg2_id": "IEPA.d52.s135.e1",
"normalized": []
},
{
"id": "IEPA.d52.s136.i0",
"type": "PPI",
"arg1_id": "IEPA.d52.s136.e0",
"arg2_id": "IEPA.d52.s136.e1",
"normalized": []
}
] |
IEPA.d54 | 9366557 | [
{
"id": "IEPA.d54.s138",
"type": "",
"text": [
"This effect is maximal at 10(-8) M AVP (a concentration clearly above the normal physiological range of AVP concentrations) and involves the V2 receptor pathway, while activation of protein kinase C or changes in intracellular calcium are ineffective"
],
"offsets": [
[
0,
250
]
]
}
] | [
{
"id": "IEPA.d54.s138.e0",
"type": "",
"text": [
"AVP"
],
"offsets": [
[
104,
107
]
],
"normalized": []
},
{
"id": "IEPA.d54.s138.e1",
"type": "",
"text": [
"AVP"
],
"offsets": [
[
35,
38
]
],
"normalized": []
},
{
"id": "IEPA.d54.s138.e2",
"type": "",
"text": [
"protein kinase C"
],
"offsets": [
[
182,
198
]
],
"normalized": []
}
] | [] | [] | [] |
IEPA.d55 | 9369264 | [
{
"id": "IEPA.d55.s139",
"type": "",
"text": [
"After protein kinase C activity was functionally depleted by treating cells with phorbol 12-myristate 13-acetate for 24 hours, AVP did not augment IL-1beta-induced NO production"
],
"offsets": [
[
0,
177
]
]
},
{
"id": "IEPA.d55.s140",
"type": "",
"text": [
"The effect of AVP was also inhibited in the presence of the protein kinase C inhibitor calphostin C"
],
"offsets": [
[
178,
277
]
]
},
{
"id": "IEPA.d55.s141",
"type": "",
"text": [
"The addition of AVP increased protein kinase C activity in cardiac myocytes, and its effect was significantly inhibited in the presence of calphostin C"
],
"offsets": [
[
278,
429
]
]
},
{
"id": "IEPA.d55.s142",
"type": "",
"text": [
"These results support the hypothesis that the heart may be a target organ for AVP and that AVP modulates IL-1beta-induced iNOS expression in myocytes through the V1a receptor, which is mediated at least partially via activation of protein kinase C"
],
"offsets": [
[
430,
677
]
]
}
] | [
{
"id": "IEPA.d55.s139.e0",
"type": "",
"text": [
"protein kinase C"
],
"offsets": [
[
6,
22
]
],
"normalized": []
},
{
"id": "IEPA.d55.s139.e1",
"type": "",
"text": [
"AVP"
],
"offsets": [
[
127,
130
]
],
"normalized": []
},
{
"id": "IEPA.d55.s140.e0",
"type": "",
"text": [
"AVP"
],
"offsets": [
[
192,
195
]
],
"normalized": []
},
{
"id": "IEPA.d55.s140.e1",
"type": "",
"text": [
"protein kinase C"
],
"offsets": [
[
238,
254
]
],
"normalized": []
},
{
"id": "IEPA.d55.s141.e0",
"type": "",
"text": [
"AVP"
],
"offsets": [
[
294,
297
]
],
"normalized": []
},
{
"id": "IEPA.d55.s141.e1",
"type": "",
"text": [
"protein kinase C"
],
"offsets": [
[
308,
324
]
],
"normalized": []
},
{
"id": "IEPA.d55.s142.e0",
"type": "",
"text": [
"AVP"
],
"offsets": [
[
508,
511
]
],
"normalized": []
},
{
"id": "IEPA.d55.s142.e1",
"type": "",
"text": [
"AVP"
],
"offsets": [
[
521,
524
]
],
"normalized": []
},
{
"id": "IEPA.d55.s142.e2",
"type": "",
"text": [
"protein kinase C"
],
"offsets": [
[
661,
677
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d55.s140.i0",
"type": "PPI",
"arg1_id": "IEPA.d55.s140.e0",
"arg2_id": "IEPA.d55.s140.e1",
"normalized": []
},
{
"id": "IEPA.d55.s141.i0",
"type": "PPI",
"arg1_id": "IEPA.d55.s141.e0",
"arg2_id": "IEPA.d55.s141.e1",
"normalized": []
},
{
"id": "IEPA.d55.s142.i0",
"type": "PPI",
"arg1_id": "IEPA.d55.s142.e1",
"arg2_id": "IEPA.d55.s142.e2",
"normalized": []
}
] |
IEPA.d57 | 9389497 | [
{
"id": "IEPA.d57.s146",
"type": "",
"text": [
"Activation of EGFR overexpressing 3T3-L1 adipocytes leads to a 3.4 +/- 1.2-fold stimulation of PLC activity over basal levels vs. only 1.06 +/- 0.01-fold stimulation by insulin."
],
"offsets": [
[
0,
177
]
]
},
{
"id": "IEPA.d57.s147",
"type": "",
"text": [
"Despite the low levels of insulin-induced PLC activity, insulin-stimulated glucose transport activity was similarly inhibited by U73122 (55.9 +/- 13.1% inhibition)"
],
"offsets": [
[
178,
341
]
]
},
{
"id": "IEPA.d57.s148",
"type": "",
"text": [
"Inhibition of PLC activation did not impair either EGF- or insulin-induced activation of glycogen synthase or incorporation of glucose into lipid, supporting the hypothesis that both EGF- and insulin-induced glucose disposal can be independent of GLUT4-mediated glucose transport."
],
"offsets": [
[
342,
622
]
]
},
{
"id": "IEPA.d57.s149",
"type": "",
"text": [
"The diminution of glucose transport secondary to inhibition of PLC activity was reflected by a decrease in GLUT4 translocation to the plasma membrane upon either EGF or insulin stimulation"
],
"offsets": [
[
623,
811
]
]
}
] | [
{
"id": "IEPA.d57.s146.e0",
"type": "",
"text": [
"PLC"
],
"offsets": [
[
95,
98
]
],
"normalized": []
},
{
"id": "IEPA.d57.s146.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
169,
176
]
],
"normalized": []
},
{
"id": "IEPA.d57.s147.e0",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
204,
211
]
],
"normalized": []
},
{
"id": "IEPA.d57.s147.e1",
"type": "",
"text": [
"PLC"
],
"offsets": [
[
220,
223
]
],
"normalized": []
},
{
"id": "IEPA.d57.s147.e2",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
234,
241
]
],
"normalized": []
},
{
"id": "IEPA.d57.s148.e0",
"type": "",
"text": [
"PLC"
],
"offsets": [
[
356,
359
]
],
"normalized": []
},
{
"id": "IEPA.d57.s148.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
401,
408
]
],
"normalized": []
},
{
"id": "IEPA.d57.s148.e2",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
534,
541
]
],
"normalized": []
},
{
"id": "IEPA.d57.s149.e0",
"type": "",
"text": [
"PLC"
],
"offsets": [
[
686,
689
]
],
"normalized": []
},
{
"id": "IEPA.d57.s149.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
792,
799
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d57.s146.i0",
"type": "PPI",
"arg1_id": "IEPA.d57.s146.e0",
"arg2_id": "IEPA.d57.s146.e1",
"normalized": []
},
{
"id": "IEPA.d57.s147.i0",
"type": "PPI",
"arg1_id": "IEPA.d57.s147.e0",
"arg2_id": "IEPA.d57.s147.e1",
"normalized": []
}
] |
IEPA.d58 | 9397959 | [
{
"id": "IEPA.d58.s150",
"type": "",
"text": [
"We have recently shown that AVP causes a protein kinase C (PKC)-dependent increase in ACTH release and biosynthesis in ovine anterior pituitary cells"
],
"offsets": [
[
0,
149
]
]
},
{
"id": "IEPA.d58.s151",
"type": "",
"text": [
"In these cells, AVP also causes the translocation of PKC from the cytosol to the cell membrane which is maximal at 5 min, but the intracellular events distal to protein kinase C activation that underlie ACTH secretion have not been well characterized to date"
],
"offsets": [
[
150,
408
]
]
},
{
"id": "IEPA.d58.s152",
"type": "",
"text": [
"Since the MARCKS protein has been implicated in neurosecretion and is phosphorylated by PKC in synaptosomes, studies were carried out to determine whether AVP might cause MARCKS phosphorylation in the ovine anterior pituitary, and to determine whether this phenomenon might be temporally correlated with PKC translocation and the release of ACTH"
],
"offsets": [
[
409,
754
]
]
},
{
"id": "IEPA.d58.s153",
"type": "",
"text": [
"We conclude that: (1) AVP causes a rapid, and reversible, phosphorylation of the MARCKS protein in the ovine anterior pituitary; (2) since the AVP-induced increase in MARCKS phosphorylation occurs much earlier in these cells than does PKC trans-location, MARCKS phosphorylation may provide a more sensitive index of the onset of PKC activation than the translocation assay; (3) the close temporal association between MARCKS phosphorylation and the rapid early release of ACTH suggests that MARCKS phosphorylation may be involved in the initial intracellular events that underly exocytosis of the hormone."
],
"offsets": [
[
755,
1359
]
]
}
] | [
{
"id": "IEPA.d58.s150.e0",
"type": "",
"text": [
"AVP"
],
"offsets": [
[
28,
31
]
],
"normalized": []
},
{
"id": "IEPA.d58.s150.e1",
"type": "",
"text": [
"protein kinase C"
],
"offsets": [
[
41,
57
]
],
"normalized": []
},
{
"id": "IEPA.d58.s151.e0",
"type": "",
"text": [
"AVP"
],
"offsets": [
[
166,
169
]
],
"normalized": []
},
{
"id": "IEPA.d58.s151.e1",
"type": "",
"text": [
"PKC"
],
"offsets": [
[
203,
206
]
],
"normalized": []
},
{
"id": "IEPA.d58.s151.e2",
"type": "",
"text": [
"protein kinase C"
],
"offsets": [
[
311,
327
]
],
"normalized": []
},
{
"id": "IEPA.d58.s152.e0",
"type": "",
"text": [
"PKC"
],
"offsets": [
[
497,
500
]
],
"normalized": []
},
{
"id": "IEPA.d58.s152.e1",
"type": "",
"text": [
"AVP"
],
"offsets": [
[
564,
567
]
],
"normalized": []
},
{
"id": "IEPA.d58.s152.e2",
"type": "",
"text": [
"PKC"
],
"offsets": [
[
713,
716
]
],
"normalized": []
},
{
"id": "IEPA.d58.s153.e0",
"type": "",
"text": [
"AVP"
],
"offsets": [
[
777,
780
]
],
"normalized": []
},
{
"id": "IEPA.d58.s153.e1",
"type": "",
"text": [
"AVP"
],
"offsets": [
[
898,
901
]
],
"normalized": []
},
{
"id": "IEPA.d58.s153.e2",
"type": "",
"text": [
"PKC"
],
"offsets": [
[
990,
993
]
],
"normalized": []
},
{
"id": "IEPA.d58.s153.e3",
"type": "",
"text": [
"PKC"
],
"offsets": [
[
1084,
1087
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d58.s150.i0",
"type": "PPI",
"arg1_id": "IEPA.d58.s150.e0",
"arg2_id": "IEPA.d58.s150.e1",
"normalized": []
},
{
"id": "IEPA.d58.s151.i0",
"type": "PPI",
"arg1_id": "IEPA.d58.s151.e0",
"arg2_id": "IEPA.d58.s151.e1",
"normalized": []
}
] |
IEPA.d60 | 9459490 | [
{
"id": "IEPA.d60.s155",
"type": "",
"text": [
"The activity of the MAPKs, induced by AVP or PMA was inhibited by downregulation of protein kinase C (PKC), by the tyrosine kinase inhibitor genistein and by MAPK kinase (MEK) inhibitor, PD98059"
],
"offsets": [
[
0,
194
]
]
},
{
"id": "IEPA.d60.s156",
"type": "",
"text": [
"We suggest that AVP activates the 42/44kDa MAPKs through a signal transduction pathway that involves stimulation of AVP-V1 receptor, tyrosine kinase, PKC and MEK"
],
"offsets": [
[
195,
356
]
]
}
] | [
{
"id": "IEPA.d60.s155.e0",
"type": "",
"text": [
"AVP"
],
"offsets": [
[
38,
41
]
],
"normalized": []
},
{
"id": "IEPA.d60.s155.e1",
"type": "",
"text": [
"protein kinase C"
],
"offsets": [
[
84,
100
]
],
"normalized": []
},
{
"id": "IEPA.d60.s156.e0",
"type": "",
"text": [
"AVP"
],
"offsets": [
[
211,
214
]
],
"normalized": []
},
{
"id": "IEPA.d60.s156.e1",
"type": "",
"text": [
"PKC"
],
"offsets": [
[
345,
348
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d60.s155.i0",
"type": "PPI",
"arg1_id": "IEPA.d60.s155.e0",
"arg2_id": "IEPA.d60.s155.e1",
"normalized": []
},
{
"id": "IEPA.d60.s156.i0",
"type": "PPI",
"arg1_id": "IEPA.d60.s156.e0",
"arg2_id": "IEPA.d60.s156.e1",
"normalized": []
}
] |
IEPA.d61 | 9473570 | [
{
"id": "IEPA.d61.s157",
"type": "",
"text": [
"Secreted form of beta-amyloid precursor protein activates protein kinase C and phospholipase Cgamma1 in cultured embryonic rat neocortical cells"
],
"offsets": [
[
0,
144
]
]
},
{
"id": "IEPA.d61.s158",
"type": "",
"text": [
"Furthermore, we demonstrate that tyrosine phosphorylation of phospholipase Cgamma1 and formation of inositol 1,4,5-trisphosphate were increased by sAPP695-stimulation"
],
"offsets": [
[
145,
311
]
]
}
] | [
{
"id": "IEPA.d61.s157.e0",
"type": "",
"text": [
"beta-amyloid"
],
"offsets": [
[
17,
29
]
],
"normalized": []
},
{
"id": "IEPA.d61.s157.e1",
"type": "",
"text": [
"phospholipase Cgamma1"
],
"offsets": [
[
79,
100
]
],
"normalized": []
},
{
"id": "IEPA.d61.s158.e0",
"type": "",
"text": [
"phospholipase Cgamma1"
],
"offsets": [
[
206,
227
]
],
"normalized": []
},
{
"id": "IEPA.d61.s158.e1",
"type": "",
"text": [
"sAPP695"
],
"offsets": [
[
292,
299
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d61.s157.i0",
"type": "PPI",
"arg1_id": "IEPA.d61.s157.e0",
"arg2_id": "IEPA.d61.s157.e1",
"normalized": []
},
{
"id": "IEPA.d61.s158.i0",
"type": "PPI",
"arg1_id": "IEPA.d61.s158.e0",
"arg2_id": "IEPA.d61.s158.e1",
"normalized": []
}
] |
IEPA.d62 | 9505272 | [
{
"id": "IEPA.d62.s159",
"type": "",
"text": [
"Oxytocin-treated male rats had increased circulating levels of cholecystokinin, a tendency to increased plasma levels of insulin (p = 0.066), and relatively more adipose tissue in the thigh and interscapular region, compared with controls"
],
"offsets": [
[
0,
238
]
]
}
] | [
{
"id": "IEPA.d62.s159.e0",
"type": "",
"text": [
"Oxytocin"
],
"offsets": [
[
0,
8
]
],
"normalized": []
},
{
"id": "IEPA.d62.s159.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
121,
128
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d62.s159.i0",
"type": "PPI",
"arg1_id": "IEPA.d62.s159.e0",
"arg2_id": "IEPA.d62.s159.e1",
"normalized": []
}
] |
IEPA.d63 | 9520493 | [
{
"id": "IEPA.d63.s160",
"type": "",
"text": [
"However, in brown fat, we observed a 2-3-fold increase in the expression of UCP1 in response to dietary fat challenge, which may be related to diet-induced elevations in plasma leptin levels"
],
"offsets": [
[
0,
190
]
]
}
] | [
{
"id": "IEPA.d63.s160.e0",
"type": "",
"text": [
"UCP1"
],
"offsets": [
[
76,
80
]
],
"normalized": []
},
{
"id": "IEPA.d63.s160.e1",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
177,
183
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d63.s160.i0",
"type": "PPI",
"arg1_id": "IEPA.d63.s160.e0",
"arg2_id": "IEPA.d63.s160.e1",
"normalized": []
}
] |
IEPA.d65 | 9561804 | [
{
"id": "IEPA.d65.s163",
"type": "",
"text": [
"Vasopressin-induced activation of protein kinase C in renal epithelial cells"
],
"offsets": [
[
0,
76
]
]
},
{
"id": "IEPA.d65.s164",
"type": "",
"text": [
"AVP induced a biphasic increase in diacylglycerol generation, characterized by an initial rapid rise and then a sustained elevation, and PKC activation, reflected by phosphorylation of a specific 80 kDa myristoylated alanine-rich PKC substrate (MARCKS)"
],
"offsets": [
[
77,
329
]
]
},
{
"id": "IEPA.d65.s165",
"type": "",
"text": [
"These results argue that Ca(2+)-dependent PKC is involved in the action of AVP, and that of other agonists, which stimulate sodium transport"
],
"offsets": [
[
330,
470
]
]
}
] | [
{
"id": "IEPA.d65.s163.e0",
"type": "",
"text": [
"Vasopressin"
],
"offsets": [
[
0,
11
]
],
"normalized": []
},
{
"id": "IEPA.d65.s163.e1",
"type": "",
"text": [
"protein kinase C"
],
"offsets": [
[
34,
50
]
],
"normalized": []
},
{
"id": "IEPA.d65.s164.e0",
"type": "",
"text": [
"AVP"
],
"offsets": [
[
77,
80
]
],
"normalized": []
},
{
"id": "IEPA.d65.s164.e1",
"type": "",
"text": [
"PKC"
],
"offsets": [
[
214,
217
]
],
"normalized": []
},
{
"id": "IEPA.d65.s165.e0",
"type": "",
"text": [
"PKC"
],
"offsets": [
[
372,
375
]
],
"normalized": []
},
{
"id": "IEPA.d65.s165.e1",
"type": "",
"text": [
"AVP"
],
"offsets": [
[
405,
408
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d65.s163.i0",
"type": "PPI",
"arg1_id": "IEPA.d65.s163.e0",
"arg2_id": "IEPA.d65.s163.e1",
"normalized": []
},
{
"id": "IEPA.d65.s164.i0",
"type": "PPI",
"arg1_id": "IEPA.d65.s164.e0",
"arg2_id": "IEPA.d65.s164.e1",
"normalized": []
},
{
"id": "IEPA.d65.s165.i0",
"type": "PPI",
"arg1_id": "IEPA.d65.s165.e0",
"arg2_id": "IEPA.d65.s165.e1",
"normalized": []
}
] |
IEPA.d66 | 9575789 | [
{
"id": "IEPA.d66.s166",
"type": "",
"text": [
"However, the AVP-dependent stimulation required activation of protein kinase C (PKC), whereas the inhibition was PKC independent, indicating that the NGF-induced signaling pathways leading to inhibition and stimulation of HCO3- absorption are distinct"
],
"offsets": [
[
0,
251
]
]
}
] | [
{
"id": "IEPA.d66.s166.e0",
"type": "",
"text": [
"AVP"
],
"offsets": [
[
13,
16
]
],
"normalized": []
},
{
"id": "IEPA.d66.s166.e1",
"type": "",
"text": [
"protein kinase C"
],
"offsets": [
[
62,
78
]
],
"normalized": []
},
{
"id": "IEPA.d66.s166.e2",
"type": "",
"text": [
"PKC"
],
"offsets": [
[
113,
116
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d66.s166.i0",
"type": "PPI",
"arg1_id": "IEPA.d66.s166.e0",
"arg2_id": "IEPA.d66.s166.e1",
"normalized": []
}
] |
IEPA.d67 | 9593725 | [
{
"id": "IEPA.d67.s167",
"type": "",
"text": [
"Association of the insulin receptor with phospholipase C-gamma (PLCgamma) in 3T3-L1 adipocytes suggests a role for PLCgamma in metabolic signaling by insulin"
],
"offsets": [
[
0,
157
]
]
},
{
"id": "IEPA.d67.s168",
"type": "",
"text": [
"To determine the functional significance of the interaction of PLCgamma and the IR, we used a specific inhibitor of PLC, U73122, or microinjection of SH2 domain glutathione S-transferase fusion proteins derived from PLCgamma to block insulin-stimulated GLUT4 translocation"
],
"offsets": [
[
158,
430
]
]
}
] | [
{
"id": "IEPA.d67.s167.e0",
"type": "",
"text": [
"phospholipase C-gamma"
],
"offsets": [
[
41,
62
]
],
"normalized": []
},
{
"id": "IEPA.d67.s167.e1",
"type": "",
"text": [
"PLCgamma"
],
"offsets": [
[
115,
123
]
],
"normalized": []
},
{
"id": "IEPA.d67.s167.e2",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
150,
157
]
],
"normalized": []
},
{
"id": "IEPA.d67.s168.e0",
"type": "",
"text": [
"PLCgamma"
],
"offsets": [
[
221,
229
]
],
"normalized": []
},
{
"id": "IEPA.d67.s168.e1",
"type": "",
"text": [
"PLC"
],
"offsets": [
[
274,
277
]
],
"normalized": []
},
{
"id": "IEPA.d67.s168.e2",
"type": "",
"text": [
"PLCgamma"
],
"offsets": [
[
374,
382
]
],
"normalized": []
},
{
"id": "IEPA.d67.s168.e3",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
392,
399
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d67.s167.i0",
"type": "PPI",
"arg1_id": "IEPA.d67.s167.e1",
"arg2_id": "IEPA.d67.s167.e2",
"normalized": []
}
] |
IEPA.d70 | 9633016 | [
{
"id": "IEPA.d70.s171",
"type": "",
"text": [
"Inhibition of 5-HT3 serotonergic receptors with ondansetron (4 or 8 mg) did not modify the basal secretion of AVP and OT and the OT response to insulin-induced hypoglycemia"
],
"offsets": [
[
0,
172
]
]
}
] | [
{
"id": "IEPA.d70.s171.e0",
"type": "",
"text": [
"OT"
],
"offsets": [
[
118,
120
]
],
"normalized": []
},
{
"id": "IEPA.d70.s171.e1",
"type": "",
"text": [
"OT"
],
"offsets": [
[
129,
131
]
],
"normalized": []
},
{
"id": "IEPA.d70.s171.e2",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
144,
151
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d70.s171.i0",
"type": "PPI",
"arg1_id": "IEPA.d70.s171.e1",
"arg2_id": "IEPA.d70.s171.e2",
"normalized": []
}
] |
IEPA.d71 | 9634587 | [
{
"id": "IEPA.d71.s172",
"type": "",
"text": [
"HvSPY coexpression largely abolished GA3-induced activity of an alpha-amylase promoter."
],
"offsets": [
[
0,
87
]
]
}
] | [
{
"id": "IEPA.d71.s172.e0",
"type": "",
"text": [
"GA3"
],
"offsets": [
[
37,
40
]
],
"normalized": []
},
{
"id": "IEPA.d71.s172.e1",
"type": "",
"text": [
"alpha-amylase"
],
"offsets": [
[
64,
77
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d71.s172.i0",
"type": "PPI",
"arg1_id": "IEPA.d71.s172.e0",
"arg2_id": "IEPA.d71.s172.e1",
"normalized": []
}
] |
IEPA.d72 | 9640660 | [
{
"id": "IEPA.d72.s173",
"type": "",
"text": [
"Treatment with (+)-trifluoro-ABA strongly inhibited the gibberellic acid-inducible expression of alpha-amylase I-1 encoded by RAmy1A in the aleurone layers of embryoless half-seeds at the levels of transcription, protein synthesis, and enzyme activity"
],
"offsets": [
[
0,
251
]
]
}
] | [
{
"id": "IEPA.d72.s173.e0",
"type": "",
"text": [
"gibberellic acid"
],
"offsets": [
[
56,
72
]
],
"normalized": []
},
{
"id": "IEPA.d72.s173.e1",
"type": "",
"text": [
"alpha-amylase"
],
"offsets": [
[
97,
110
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d72.s173.i0",
"type": "PPI",
"arg1_id": "IEPA.d72.s173.e0",
"arg2_id": "IEPA.d72.s173.e1",
"normalized": []
}
] |
IEPA.d73 | 9642681 | [
{
"id": "IEPA.d73.s174",
"type": "",
"text": [
"Furthermore, treatment of isolated rat diaphragms and adipocytes with PIG-P as well as with other agents exerting partially insulin-mimetic activity, such as PI-specific phospholipase C (PLC) and the sulfonylurea glimepiride, triggered tyrosine phosphorylation of the caveolar marker protein caveolin, which was apparently correlated with stimulation of lipogenesis"
],
"offsets": [
[
0,
365
]
]
},
{
"id": "IEPA.d73.s175",
"type": "",
"text": [
"Strikingly, in adipocytes subjected to combined trypsin/salt treatment, PIG-P, PI-specific PLC, and glimepiride failed completely to provoke insulin-mimetic effects"
],
"offsets": [
[
366,
530
]
]
}
] | [
{
"id": "IEPA.d73.s174.e0",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
124,
131
]
],
"normalized": []
},
{
"id": "IEPA.d73.s174.e1",
"type": "",
"text": [
"phospholipase C"
],
"offsets": [
[
170,
185
]
],
"normalized": []
},
{
"id": "IEPA.d73.s175.e0",
"type": "",
"text": [
"PLC"
],
"offsets": [
[
457,
460
]
],
"normalized": []
},
{
"id": "IEPA.d73.s175.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
507,
514
]
],
"normalized": []
}
] | [] | [] | [] |
IEPA.d74 | 9648822 | [
{
"id": "IEPA.d74.s176",
"type": "",
"text": [
"Chronic central leptin infusion enhances insulin-stimulated glucose metabolism and favors the expression of uncoupling proteins"
],
"offsets": [
[
0,
127
]
]
},
{
"id": "IEPA.d74.s177",
"type": "",
"text": [
"In marked contrast, intracerebroventricular leptin administration was accompanied by the maintenance of high UCP1, UCP2, and UCP3 expression in all these tissues"
],
"offsets": [
[
128,
289
]
]
},
{
"id": "IEPA.d74.s178",
"type": "",
"text": [
"While leptin maintains or favors energy-dissipating mechanisms (UCP1, UCP2, and UCP3), the latter are markedly depressed in pair-fed rats"
],
"offsets": [
[
290,
427
]
]
}
] | [
{
"id": "IEPA.d74.s176.e0",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
16,
22
]
],
"normalized": []
},
{
"id": "IEPA.d74.s176.e1",
"type": "",
"text": [
"uncoupling proteins"
],
"offsets": [
[
108,
127
]
],
"normalized": []
},
{
"id": "IEPA.d74.s177.e0",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
172,
178
]
],
"normalized": []
},
{
"id": "IEPA.d74.s177.e1",
"type": "",
"text": [
"UCP1"
],
"offsets": [
[
237,
241
]
],
"normalized": []
},
{
"id": "IEPA.d74.s177.e2",
"type": "",
"text": [
"UCP2"
],
"offsets": [
[
243,
247
]
],
"normalized": []
},
{
"id": "IEPA.d74.s177.e3",
"type": "",
"text": [
"UCP3"
],
"offsets": [
[
253,
257
]
],
"normalized": []
},
{
"id": "IEPA.d74.s178.e0",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
296,
302
]
],
"normalized": []
},
{
"id": "IEPA.d74.s178.e1",
"type": "",
"text": [
"UCP1"
],
"offsets": [
[
354,
358
]
],
"normalized": []
},
{
"id": "IEPA.d74.s178.e2",
"type": "",
"text": [
"UCP2"
],
"offsets": [
[
360,
364
]
],
"normalized": []
},
{
"id": "IEPA.d74.s178.e3",
"type": "",
"text": [
"UCP3"
],
"offsets": [
[
370,
374
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d74.s176.i0",
"type": "PPI",
"arg1_id": "IEPA.d74.s176.e0",
"arg2_id": "IEPA.d74.s176.e1",
"normalized": []
},
{
"id": "IEPA.d74.s177.i0",
"type": "PPI",
"arg1_id": "IEPA.d74.s177.e0",
"arg2_id": "IEPA.d74.s177.e1",
"normalized": []
},
{
"id": "IEPA.d74.s177.i1",
"type": "PPI",
"arg1_id": "IEPA.d74.s177.e0",
"arg2_id": "IEPA.d74.s177.e2",
"normalized": []
},
{
"id": "IEPA.d74.s177.i2",
"type": "PPI",
"arg1_id": "IEPA.d74.s177.e0",
"arg2_id": "IEPA.d74.s177.e3",
"normalized": []
},
{
"id": "IEPA.d74.s178.i0",
"type": "PPI",
"arg1_id": "IEPA.d74.s178.e0",
"arg2_id": "IEPA.d74.s178.e1",
"normalized": []
},
{
"id": "IEPA.d74.s178.i1",
"type": "PPI",
"arg1_id": "IEPA.d74.s178.e0",
"arg2_id": "IEPA.d74.s178.e2",
"normalized": []
},
{
"id": "IEPA.d74.s178.i2",
"type": "PPI",
"arg1_id": "IEPA.d74.s178.e0",
"arg2_id": "IEPA.d74.s178.e3",
"normalized": []
}
] |
IEPA.d76 | 9660095 | [
{
"id": "IEPA.d76.s182",
"type": "",
"text": [
"Melatonin inhibits oxytocin response to insulin-induced hypoglycemia, but not to angiotensin II in normal men"
],
"offsets": [
[
0,
109
]
]
},
{
"id": "IEPA.d76.s183",
"type": "",
"text": [
"In order to establish whether melatonin alters basal and/or stimulated oxytocin secretion, 18 normal men were treated (p.o.) with 6 or 12 mg melatonin or placebo in basal conditions (N-6 subjects) or concomitantly to the administration of insulin (O.15 IU/kg body weight in an i.v. bolus) (N-6 subjects) or angiotensin II (increasing doses of 4, 8 and 16 ng/kg/min, at intervals of 20 min)"
],
"offsets": [
[
110,
499
]
]
},
{
"id": "IEPA.d76.s184",
"type": "",
"text": [
"In contrast, the oxytocin response to insulin-induced hypoglycemia was significantly reduced by melatonin treatment"
],
"offsets": [
[
500,
615
]
]
}
] | [
{
"id": "IEPA.d76.s182.e0",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
19,
27
]
],
"normalized": []
},
{
"id": "IEPA.d76.s182.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
40,
47
]
],
"normalized": []
},
{
"id": "IEPA.d76.s183.e0",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
181,
189
]
],
"normalized": []
},
{
"id": "IEPA.d76.s183.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
349,
356
]
],
"normalized": []
},
{
"id": "IEPA.d76.s184.e0",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
517,
525
]
],
"normalized": []
},
{
"id": "IEPA.d76.s184.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
538,
545
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d76.s182.i0",
"type": "PPI",
"arg1_id": "IEPA.d76.s182.e0",
"arg2_id": "IEPA.d76.s182.e1",
"normalized": []
},
{
"id": "IEPA.d76.s184.i0",
"type": "PPI",
"arg1_id": "IEPA.d76.s184.e0",
"arg2_id": "IEPA.d76.s184.e1",
"normalized": []
}
] |
IEPA.d77 | 9662044 | [
{
"id": "IEPA.d77.s185",
"type": "",
"text": [
"Although osmotic stimuli cause an increase in nitric oxide synthase (NOS) activity as well as synthesis of AVP and oxytocin in the paraventricular (PVN) and supraoptic nuclei (SON), it is not known whether NOS activity in the hypothalamus changes in the diabetic patients who have plasma hyperosmolality with hyperglycaemia caused by insulin deficiency"
],
"offsets": [
[
0,
352
]
]
},
{
"id": "IEPA.d77.s186",
"type": "",
"text": [
"Three weeks after administration of STZ, the diabetic rats were subcutaneously treated with insulin for 1 week, which resulted in significant suppression of the induction of nNOS, AVP and oxytocin gene expression in the PVN and SON"
],
"offsets": [
[
353,
584
]
]
}
] | [
{
"id": "IEPA.d77.s185.e0",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
115,
123
]
],
"normalized": []
},
{
"id": "IEPA.d77.s185.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
334,
341
]
],
"normalized": []
},
{
"id": "IEPA.d77.s186.e0",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
445,
452
]
],
"normalized": []
},
{
"id": "IEPA.d77.s186.e1",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
541,
549
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d77.s186.i0",
"type": "PPI",
"arg1_id": "IEPA.d77.s186.e0",
"arg2_id": "IEPA.d77.s186.e1",
"normalized": []
}
] |
IEPA.d79 | 9673007 | [
{
"id": "IEPA.d79.s189",
"type": "",
"text": [
"OT evokes the release of Ca2+ from IP3-sensitive intracellular stores"
],
"offsets": [
[
0,
69
]
]
}
] | [
{
"id": "IEPA.d79.s189.e0",
"type": "",
"text": [
"OT"
],
"offsets": [
[
0,
2
]
],
"normalized": []
},
{
"id": "IEPA.d79.s189.e1",
"type": "",
"text": [
"IP3"
],
"offsets": [
[
35,
38
]
],
"normalized": []
}
] | [] | [] | [] |
IEPA.d80 | 9682828 | [
{
"id": "IEPA.d80.s190",
"type": "",
"text": [
"To explore the possible roles of the hypothalamic melanocortin system in leptin action, we examined the effects of intracerebroventricular (i.c.v.) injection of leptin with or without SHU9119, a potent antagonist of alpha-melanocyte stimulating hormone, on food intake, body weight, and mitochondrial uncoupling protein-1 (UCP-1) mRNA expression in the brown adipose tissue (BAT) in rats"
],
"offsets": [
[
0,
387
]
]
},
{
"id": "IEPA.d80.s191",
"type": "",
"text": [
"A single i.c.v. injection of leptin decreased cumulative food intake and body weight gain, and increased UCP-1 mRNA expression during 3 h at the onset of the dark phase"
],
"offsets": [
[
388,
556
]
]
},
{
"id": "IEPA.d80.s192",
"type": "",
"text": [
"Co-injection of SHU9119 also inhibited completely the leptin-induced increase in UCP-1 mRNA expression in the BAT"
],
"offsets": [
[
557,
670
]
]
}
] | [
{
"id": "IEPA.d80.s190.e0",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
73,
79
]
],
"normalized": []
},
{
"id": "IEPA.d80.s190.e1",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
161,
167
]
],
"normalized": []
},
{
"id": "IEPA.d80.s190.e2",
"type": "",
"text": [
"uncoupling protein-1"
],
"offsets": [
[
301,
321
]
],
"normalized": []
},
{
"id": "IEPA.d80.s191.e0",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
417,
423
]
],
"normalized": []
},
{
"id": "IEPA.d80.s191.e1",
"type": "",
"text": [
"UCP-1"
],
"offsets": [
[
493,
498
]
],
"normalized": []
},
{
"id": "IEPA.d80.s192.e0",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
611,
617
]
],
"normalized": []
},
{
"id": "IEPA.d80.s192.e1",
"type": "",
"text": [
"UCP-1"
],
"offsets": [
[
638,
643
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d80.s191.i0",
"type": "PPI",
"arg1_id": "IEPA.d80.s191.e0",
"arg2_id": "IEPA.d80.s191.e1",
"normalized": []
},
{
"id": "IEPA.d80.s192.i0",
"type": "PPI",
"arg1_id": "IEPA.d80.s192.e0",
"arg2_id": "IEPA.d80.s192.e1",
"normalized": []
}
] |
IEPA.d81 | 9685679 | [
{
"id": "IEPA.d81.s193",
"type": "",
"text": [
"It has been established that amyloid beta peptide (AbetaP) activates phospholipase A2, phospholipase C and phospholipase D of LA-N-2 cells and other cell types"
],
"offsets": [
[
0,
159
]
]
},
{
"id": "IEPA.d81.s194",
"type": "",
"text": [
"(-)Nicotine did not blunt the AbetaP activation of phospholipase C"
],
"offsets": [
[
160,
226
]
]
}
] | [
{
"id": "IEPA.d81.s193.e0",
"type": "",
"text": [
"amyloid"
],
"offsets": [
[
29,
36
]
],
"normalized": []
},
{
"id": "IEPA.d81.s193.e1",
"type": "",
"text": [
"phospholipase C"
],
"offsets": [
[
87,
102
]
],
"normalized": []
},
{
"id": "IEPA.d81.s194.e0",
"type": "",
"text": [
"AbetaP"
],
"offsets": [
[
190,
196
]
],
"normalized": []
},
{
"id": "IEPA.d81.s194.e1",
"type": "",
"text": [
"phospholipase C"
],
"offsets": [
[
211,
226
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d81.s193.i0",
"type": "PPI",
"arg1_id": "IEPA.d81.s193.e0",
"arg2_id": "IEPA.d81.s193.e1",
"normalized": []
},
{
"id": "IEPA.d81.s194.i0",
"type": "PPI",
"arg1_id": "IEPA.d81.s194.e0",
"arg2_id": "IEPA.d81.s194.e1",
"normalized": []
}
] |
IEPA.d82 | 9688683 | [
{
"id": "IEPA.d82.s195",
"type": "",
"text": [
"Neural site of leptin influence on neuropeptide Y signaling pathways altering feeding and uncoupling protein"
],
"offsets": [
[
0,
108
]
]
},
{
"id": "IEPA.d82.s196",
"type": "",
"text": [
"NPY in the PVN increases feeding and decreases uncoupling protein (UCP) activity in brown fat, whereas leptin decreases NPY biosynthesis in the Arc, which presumably decreases PVN NPY"
],
"offsets": [
[
109,
292
]
]
},
{
"id": "IEPA.d82.s197",
"type": "",
"text": [
"Next, we determined that leptin decreases NPY and increases UCP gene expression"
],
"offsets": [
[
293,
372
]
]
}
] | [
{
"id": "IEPA.d82.s195.e0",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
15,
21
]
],
"normalized": []
},
{
"id": "IEPA.d82.s195.e1",
"type": "",
"text": [
"uncoupling protein"
],
"offsets": [
[
90,
108
]
],
"normalized": []
},
{
"id": "IEPA.d82.s196.e0",
"type": "",
"text": [
"uncoupling protein"
],
"offsets": [
[
156,
174
]
],
"normalized": []
},
{
"id": "IEPA.d82.s196.e1",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
212,
218
]
],
"normalized": []
},
{
"id": "IEPA.d82.s197.e0",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
318,
324
]
],
"normalized": []
},
{
"id": "IEPA.d82.s197.e1",
"type": "",
"text": [
"UCP"
],
"offsets": [
[
353,
356
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d82.s195.i0",
"type": "PPI",
"arg1_id": "IEPA.d82.s195.e0",
"arg2_id": "IEPA.d82.s195.e1",
"normalized": []
},
{
"id": "IEPA.d82.s197.i0",
"type": "PPI",
"arg1_id": "IEPA.d82.s197.e0",
"arg2_id": "IEPA.d82.s197.e1",
"normalized": []
}
] |
IEPA.d83 | 9689469 | [
{
"id": "IEPA.d83.s198",
"type": "",
"text": [
"Furthermore, immunocytochemical studies showed the A beta-induced neuronal MAC expression on the SH-SY5Y cells after CD59 was removed by PIPLC or blocked by anti-CD59 antibody"
],
"offsets": [
[
0,
175
]
]
}
] | [
{
"id": "IEPA.d83.s198.e0",
"type": "",
"text": [
"A beta"
],
"offsets": [
[
51,
57
]
],
"normalized": []
},
{
"id": "IEPA.d83.s198.e1",
"type": "",
"text": [
"PIPLC"
],
"offsets": [
[
137,
142
]
],
"normalized": []
}
] | [] | [] | [] |
IEPA.d84 | 9698023 | [
{
"id": "IEPA.d84.s199",
"type": "",
"text": [
"Effect of residual endogenous insulin secretion on the abnormal oxytocin response to hypoglycaemia in insulin-dependent diabetics"
],
"offsets": [
[
0,
129
]
]
},
{
"id": "IEPA.d84.s200",
"type": "",
"text": [
"Since previous studies showed that AVP secretion is influenced by the persistence of residual endogenous insulin secretion, we wondered whether this factor also regulates OT secretion"
],
"offsets": [
[
130,
313
]
]
},
{
"id": "IEPA.d84.s201",
"type": "",
"text": [
"DESIGN: Case-control study: the OT response to insulin-induced hypoglycaemia was measured in normal and diabetic patients with or without residual endogenous insulin secretion"
],
"offsets": [
[
314,
489
]
]
},
{
"id": "IEPA.d84.s202",
"type": "",
"text": [
"Blood samples for OT assay were taken just before the rapid injection of insulin (time 0) and at time 15, 30, 45 and 60 min"
],
"offsets": [
[
490,
613
]
]
},
{
"id": "IEPA.d84.s203",
"type": "",
"text": [
"CONCLUSIONS: These data indicate that a residual endogenous insulin secretion exerts a partial protective action against the hypothalamic-pituitary disorder affecting the OT secretory system in IDDM"
],
"offsets": [
[
614,
812
]
]
}
] | [
{
"id": "IEPA.d84.s199.e0",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
30,
37
]
],
"normalized": []
},
{
"id": "IEPA.d84.s199.e1",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
64,
72
]
],
"normalized": []
},
{
"id": "IEPA.d84.s199.e2",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
102,
109
]
],
"normalized": []
},
{
"id": "IEPA.d84.s200.e0",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
235,
242
]
],
"normalized": []
},
{
"id": "IEPA.d84.s200.e1",
"type": "",
"text": [
"OT"
],
"offsets": [
[
301,
303
]
],
"normalized": []
},
{
"id": "IEPA.d84.s201.e0",
"type": "",
"text": [
"OT"
],
"offsets": [
[
346,
348
]
],
"normalized": []
},
{
"id": "IEPA.d84.s201.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
361,
368
]
],
"normalized": []
},
{
"id": "IEPA.d84.s201.e2",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
472,
479
]
],
"normalized": []
},
{
"id": "IEPA.d84.s202.e0",
"type": "",
"text": [
"OT"
],
"offsets": [
[
508,
510
]
],
"normalized": []
},
{
"id": "IEPA.d84.s202.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
563,
570
]
],
"normalized": []
},
{
"id": "IEPA.d84.s203.e0",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
674,
681
]
],
"normalized": []
},
{
"id": "IEPA.d84.s203.e1",
"type": "",
"text": [
"OT"
],
"offsets": [
[
785,
787
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d84.s199.i0",
"type": "PPI",
"arg1_id": "IEPA.d84.s199.e0",
"arg2_id": "IEPA.d84.s199.e1",
"normalized": []
},
{
"id": "IEPA.d84.s200.i0",
"type": "PPI",
"arg1_id": "IEPA.d84.s200.e0",
"arg2_id": "IEPA.d84.s200.e1",
"normalized": []
},
{
"id": "IEPA.d84.s201.i0",
"type": "PPI",
"arg1_id": "IEPA.d84.s201.e0",
"arg2_id": "IEPA.d84.s201.e1",
"normalized": []
},
{
"id": "IEPA.d84.s203.i0",
"type": "PPI",
"arg1_id": "IEPA.d84.s203.e0",
"arg2_id": "IEPA.d84.s203.e1",
"normalized": []
}
] |
IEPA.d85 | 9722564 | [
{
"id": "IEPA.d85.s204",
"type": "",
"text": [
"A barley gene encoding a novel DNA-binding protein (HRT) was identified by southwestern screening with baits containing a gibberellin phytohormone response element from an alpha-amylase promoter"
],
"offsets": [
[
0,
194
]
]
}
] | [
{
"id": "IEPA.d85.s204.e0",
"type": "",
"text": [
"gibberellin"
],
"offsets": [
[
122,
133
]
],
"normalized": []
},
{
"id": "IEPA.d85.s204.e1",
"type": "",
"text": [
"alpha-amylase"
],
"offsets": [
[
172,
185
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d85.s204.i0",
"type": "PPI",
"arg1_id": "IEPA.d85.s204.e0",
"arg2_id": "IEPA.d85.s204.e1",
"normalized": []
}
] |
IEPA.d86 | 9777024 | [
{
"id": "IEPA.d86.s205",
"type": "",
"text": [
"These observations suggest that bradykinin, like oxytocin, activates phospholipase C which generates IP3 with a subsequent release of Ca2+ from intracellular stores followed by store-operated Ca2+ influx"
],
"offsets": [
[
0,
203
]
]
}
] | [
{
"id": "IEPA.d86.s205.e0",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
49,
57
]
],
"normalized": []
},
{
"id": "IEPA.d86.s205.e1",
"type": "",
"text": [
"IP3"
],
"offsets": [
[
101,
104
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d86.s205.i0",
"type": "PPI",
"arg1_id": "IEPA.d86.s205.e0",
"arg2_id": "IEPA.d86.s205.e1",
"normalized": []
}
] |
IEPA.d87 | 9792538 | [
{
"id": "IEPA.d87.s206",
"type": "",
"text": [
"These findings led us to conclude that inositol trisphosphate [corrected] causes Ca2+ mobilization by muscarinic activation of PLC, leading to intracellular translocation of insulin granules to the ready-releasable pool in pancreatic beta-cells via Ca2+/calmodulin-dependent phosphorylation of myosin light chains"
],
"offsets": [
[
0,
313
]
]
}
] | [
{
"id": "IEPA.d87.s206.e0",
"type": "",
"text": [
"PLC"
],
"offsets": [
[
127,
130
]
],
"normalized": []
},
{
"id": "IEPA.d87.s206.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
174,
181
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d87.s206.i0",
"type": "PPI",
"arg1_id": "IEPA.d87.s206.e0",
"arg2_id": "IEPA.d87.s206.e1",
"normalized": []
}
] |
IEPA.d88 | 9792555 | [
{
"id": "IEPA.d88.s207",
"type": "",
"text": [
"To elucidate the pathophysiologic significance of UCP3 and UCP2 in the effect of TZDs on glucose metabolism and energy expenditure, we examined their basal mRNA levels in the WAT, brown adipose tissue (BAT), and skeletal muscle from Wistar fatty rats, a rat model of NIDDM and obesity with leptin receptor defect, and investigated expression of the genes encoding UCP3 and UCP2 in Wistar fatty rats and in Wistar lean rats with 2-week oral administration of 3 mg x kg(-1) x day(-1) pioglitazone, a TZD derivative"
],
"offsets": [
[
0,
512
]
]
},
{
"id": "IEPA.d88.s208",
"type": "",
"text": [
"These results clearly demonstrate that UCP3 gene expression is upregulated by TZDs in the WAT and BAT in Wistar fatty rats, an obese model with leptin receptor defect, and that adipose UCP3 gene expression is increased in response to TZDs in vitro"
],
"offsets": [
[
513,
760
]
]
}
] | [
{
"id": "IEPA.d88.s207.e0",
"type": "",
"text": [
"UCP3"
],
"offsets": [
[
50,
54
]
],
"normalized": []
},
{
"id": "IEPA.d88.s207.e1",
"type": "",
"text": [
"UCP2"
],
"offsets": [
[
59,
63
]
],
"normalized": []
},
{
"id": "IEPA.d88.s207.e2",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
290,
296
]
],
"normalized": []
},
{
"id": "IEPA.d88.s207.e3",
"type": "",
"text": [
"UCP3"
],
"offsets": [
[
364,
368
]
],
"normalized": []
},
{
"id": "IEPA.d88.s207.e4",
"type": "",
"text": [
"UCP2"
],
"offsets": [
[
373,
377
]
],
"normalized": []
},
{
"id": "IEPA.d88.s208.e0",
"type": "",
"text": [
"UCP3"
],
"offsets": [
[
552,
556
]
],
"normalized": []
},
{
"id": "IEPA.d88.s208.e1",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
657,
663
]
],
"normalized": []
},
{
"id": "IEPA.d88.s208.e2",
"type": "",
"text": [
"UCP3"
],
"offsets": [
[
698,
702
]
],
"normalized": []
}
] | [] | [] | [] |
IEPA.d89 | 9795377 | [
{
"id": "IEPA.d89.s209",
"type": "",
"text": [
"UCP2, UCP3 and leptin gene expression: modulation by food restriction and leptin"
],
"offsets": [
[
0,
80
]
]
},
{
"id": "IEPA.d89.s210",
"type": "",
"text": [
"To determine the effects of food restriction and leptin administration on several transcripts involved in energy homeostasis, we examined leptin, uncoupling proteins (UCP) 1, 2 and 3, lipoprotein lipase (LPL), beta3-adrenergic receptors (beta3AR) and hormone-sensitive lipase (HSL) mRNA levels in brown adipose tissue (BAT) and epididymal (EWAT) and perirenal (PWAT) white adipose tissue in three groups of rats"
],
"offsets": [
[
81,
492
]
]
},
{
"id": "IEPA.d89.s211",
"type": "",
"text": [
"Leptin increased LPL mRNA by 80%, UCP1 mRNA twofold, and UCP3 mRNA levels by 62% in BAT, and increased UCP2 mRNA levels twofold in EWAT"
],
"offsets": [
[
493,
628
]
]
},
{
"id": "IEPA.d89.s212",
"type": "",
"text": [
"The present study indicates that leptin increases the gene expression of UCP2 in EWAT and that of UCP1, UCP3 and LPL in BAT, whereas reduced food consumption but not leptin, decreases LPL expression in WAT"
],
"offsets": [
[
629,
834
]
]
}
] | [
{
"id": "IEPA.d89.s209.e0",
"type": "",
"text": [
"UCP2"
],
"offsets": [
[
0,
4
]
],
"normalized": []
},
{
"id": "IEPA.d89.s209.e1",
"type": "",
"text": [
"UCP3"
],
"offsets": [
[
6,
10
]
],
"normalized": []
},
{
"id": "IEPA.d89.s209.e2",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
15,
21
]
],
"normalized": []
},
{
"id": "IEPA.d89.s209.e3",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
74,
80
]
],
"normalized": []
},
{
"id": "IEPA.d89.s210.e0",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
130,
136
]
],
"normalized": []
},
{
"id": "IEPA.d89.s210.e1",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
219,
225
]
],
"normalized": []
},
{
"id": "IEPA.d89.s210.e2",
"type": "",
"text": [
"uncoupling proteins"
],
"offsets": [
[
227,
246
]
],
"normalized": []
},
{
"id": "IEPA.d89.s211.e0",
"type": "",
"text": [
"Leptin"
],
"offsets": [
[
493,
499
]
],
"normalized": []
},
{
"id": "IEPA.d89.s211.e1",
"type": "",
"text": [
"UCP1"
],
"offsets": [
[
527,
531
]
],
"normalized": []
},
{
"id": "IEPA.d89.s211.e2",
"type": "",
"text": [
"UCP3"
],
"offsets": [
[
550,
554
]
],
"normalized": []
},
{
"id": "IEPA.d89.s211.e3",
"type": "",
"text": [
"UCP2"
],
"offsets": [
[
596,
600
]
],
"normalized": []
},
{
"id": "IEPA.d89.s212.e0",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
662,
668
]
],
"normalized": []
},
{
"id": "IEPA.d89.s212.e1",
"type": "",
"text": [
"UCP2"
],
"offsets": [
[
702,
706
]
],
"normalized": []
},
{
"id": "IEPA.d89.s212.e2",
"type": "",
"text": [
"UCP1"
],
"offsets": [
[
727,
731
]
],
"normalized": []
},
{
"id": "IEPA.d89.s212.e3",
"type": "",
"text": [
"UCP3"
],
"offsets": [
[
733,
737
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d89.s209.i0",
"type": "PPI",
"arg1_id": "IEPA.d89.s209.e0",
"arg2_id": "IEPA.d89.s209.e3",
"normalized": []
},
{
"id": "IEPA.d89.s209.i1",
"type": "PPI",
"arg1_id": "IEPA.d89.s209.e1",
"arg2_id": "IEPA.d89.s209.e3",
"normalized": []
},
{
"id": "IEPA.d89.s211.i0",
"type": "PPI",
"arg1_id": "IEPA.d89.s211.e0",
"arg2_id": "IEPA.d89.s211.e1",
"normalized": []
},
{
"id": "IEPA.d89.s211.i1",
"type": "PPI",
"arg1_id": "IEPA.d89.s211.e0",
"arg2_id": "IEPA.d89.s211.e2",
"normalized": []
},
{
"id": "IEPA.d89.s211.i2",
"type": "PPI",
"arg1_id": "IEPA.d89.s211.e0",
"arg2_id": "IEPA.d89.s211.e3",
"normalized": []
},
{
"id": "IEPA.d89.s212.i0",
"type": "PPI",
"arg1_id": "IEPA.d89.s212.e0",
"arg2_id": "IEPA.d89.s212.e1",
"normalized": []
},
{
"id": "IEPA.d89.s212.i1",
"type": "PPI",
"arg1_id": "IEPA.d89.s212.e0",
"arg2_id": "IEPA.d89.s212.e2",
"normalized": []
},
{
"id": "IEPA.d89.s212.i2",
"type": "PPI",
"arg1_id": "IEPA.d89.s212.e0",
"arg2_id": "IEPA.d89.s212.e3",
"normalized": []
}
] |
IEPA.d90 | 9862499 | [
{
"id": "IEPA.d90.s213",
"type": "",
"text": [
"DNase1 footprints suggest the involvement of at least three types of transcription factors in the regulation of alpha-Amy2/A by gibberellin"
],
"offsets": [
[
0,
139
]
]
},
{
"id": "IEPA.d90.s214",
"type": "",
"text": [
"The regulation of alpha-Amy2 genes by GA therefore involves an interplay of at least three different types of transcription factor"
],
"offsets": [
[
140,
270
]
]
}
] | [
{
"id": "IEPA.d90.s213.e0",
"type": "",
"text": [
"alpha-Amy2/A"
],
"offsets": [
[
112,
124
]
],
"normalized": []
},
{
"id": "IEPA.d90.s213.e1",
"type": "",
"text": [
"gibberellin"
],
"offsets": [
[
128,
139
]
],
"normalized": []
},
{
"id": "IEPA.d90.s214.e0",
"type": "",
"text": [
"alpha-Amy2"
],
"offsets": [
[
158,
168
]
],
"normalized": []
},
{
"id": "IEPA.d90.s214.e1",
"type": "",
"text": [
"GA"
],
"offsets": [
[
178,
180
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d90.s213.i0",
"type": "PPI",
"arg1_id": "IEPA.d90.s213.e0",
"arg2_id": "IEPA.d90.s213.e1",
"normalized": []
},
{
"id": "IEPA.d90.s214.i0",
"type": "PPI",
"arg1_id": "IEPA.d90.s214.e0",
"arg2_id": "IEPA.d90.s214.e1",
"normalized": []
}
] |
IEPA.d91 | 9863156 | [
{
"id": "IEPA.d91.s215",
"type": "",
"text": [
"Oxytocin-stimulated insulin release in a clonal beta-cell line RINm5F: involvement of phospholipase C-dependent and -independent pathways."
],
"offsets": [
[
0,
138
]
]
},
{
"id": "IEPA.d91.s216",
"type": "",
"text": [
"CONCLUSION: Oxy increases insulin release through both PLC and non-PLC mediated signal transduction mechanisms."
],
"offsets": [
[
139,
250
]
]
},
{
"id": "IEPA.d91.s217",
"type": "",
"text": [
"In addition, U-73122 diminished the Oxy-induced increase in intracellular concentration of inositol 1, 4, 5-triphosphate (IP3)"
],
"offsets": [
[
251,
377
]
]
},
{
"id": "IEPA.d91.s218",
"type": "",
"text": [
"U-73122 at 8 mumol.L-1 totally abolished the Oxy-induced increases in [Ca2+]i and IP3; however it reduced the Oxy-induced increase in insulin release only by 36% and 63% in the monolayer and suspended cell preparations, respectively"
],
"offsets": [
[
378,
610
]
]
},
{
"id": "IEPA.d91.s219",
"type": "",
"text": [
"Oxytocin-stimulated insulin release in a clonal beta-cell line RINm5F: involvement of phospholipase C-dependent and -independent pathways"
],
"offsets": [
[
611,
748
]
]
},
{
"id": "IEPA.d91.s220",
"type": "",
"text": [
"AIM: To study the mechanisms underlying oxytocin (Oxy)-induced insulin release"
],
"offsets": [
[
749,
827
]
]
},
{
"id": "IEPA.d91.s221",
"type": "",
"text": [
"RESULTS: Oxy increased insulin release and [Ca2+]i in a concentration-dependent manner"
],
"offsets": [
[
828,
914
]
]
},
{
"id": "IEPA.d91.s222",
"type": "",
"text": [
"Oxy-induced insulin release was not altered by pretreatment with pertussis toxin (PT)"
],
"offsets": [
[
915,
1000
]
]
},
{
"id": "IEPA.d91.s223",
"type": "",
"text": [
"U-73122 at 8 mumol.L-1 totally abolished the Oxy-induced increases in [Ca2+]i and IP3; however it reduced the Oxy-induced increase in insulin release only by 36% and 63% in the monolayer and suspended cell preparations, respectively"
],
"offsets": [
[
1001,
1233
]
]
},
{
"id": "IEPA.d91.s224",
"type": "",
"text": [
"CONCLUSION: Oxy increases insulin release through both PLC and non-PLC mediated signal transduction mechanisms"
],
"offsets": [
[
1234,
1344
]
]
}
] | [
{
"id": "IEPA.d91.s215.e0",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
20,
27
]
],
"normalized": []
},
{
"id": "IEPA.d91.s215.e1",
"type": "",
"text": [
"phospholipase C"
],
"offsets": [
[
86,
101
]
],
"normalized": []
},
{
"id": "IEPA.d91.s216.e0",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
165,
172
]
],
"normalized": []
},
{
"id": "IEPA.d91.s216.e1",
"type": "",
"text": [
"PLC"
],
"offsets": [
[
194,
197
]
],
"normalized": []
},
{
"id": "IEPA.d91.s217.e0",
"type": "",
"text": [
"Oxy"
],
"offsets": [
[
287,
290
]
],
"normalized": []
},
{
"id": "IEPA.d91.s217.e1",
"type": "",
"text": [
"inositol 1, 4, 5-triphosphate"
],
"offsets": [
[
342,
371
]
],
"normalized": []
},
{
"id": "IEPA.d91.s218.e0",
"type": "",
"text": [
"Oxy"
],
"offsets": [
[
423,
426
]
],
"normalized": []
},
{
"id": "IEPA.d91.s218.e1",
"type": "",
"text": [
"IP3"
],
"offsets": [
[
460,
463
]
],
"normalized": []
},
{
"id": "IEPA.d91.s218.e2",
"type": "",
"text": [
"Oxy"
],
"offsets": [
[
488,
491
]
],
"normalized": []
},
{
"id": "IEPA.d91.s219.e0",
"type": "",
"text": [
"Oxytocin"
],
"offsets": [
[
611,
619
]
],
"normalized": []
},
{
"id": "IEPA.d91.s219.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
631,
638
]
],
"normalized": []
},
{
"id": "IEPA.d91.s220.e0",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
789,
797
]
],
"normalized": []
},
{
"id": "IEPA.d91.s220.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
812,
819
]
],
"normalized": []
},
{
"id": "IEPA.d91.s221.e0",
"type": "",
"text": [
"Oxy"
],
"offsets": [
[
837,
840
]
],
"normalized": []
},
{
"id": "IEPA.d91.s221.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
851,
858
]
],
"normalized": []
},
{
"id": "IEPA.d91.s222.e0",
"type": "",
"text": [
"Oxy"
],
"offsets": [
[
915,
918
]
],
"normalized": []
},
{
"id": "IEPA.d91.s222.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
927,
934
]
],
"normalized": []
},
{
"id": "IEPA.d91.s223.e0",
"type": "",
"text": [
"Oxy"
],
"offsets": [
[
1046,
1049
]
],
"normalized": []
},
{
"id": "IEPA.d91.s223.e1",
"type": "",
"text": [
"Oxy"
],
"offsets": [
[
1111,
1114
]
],
"normalized": []
},
{
"id": "IEPA.d91.s223.e2",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
1135,
1142
]
],
"normalized": []
},
{
"id": "IEPA.d91.s224.e0",
"type": "",
"text": [
"Oxy"
],
"offsets": [
[
1246,
1249
]
],
"normalized": []
},
{
"id": "IEPA.d91.s224.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
1260,
1267
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d91.s215.i0",
"type": "PPI",
"arg1_id": "IEPA.d91.s215.e0",
"arg2_id": "IEPA.d91.s215.e1",
"normalized": []
},
{
"id": "IEPA.d91.s216.i0",
"type": "PPI",
"arg1_id": "IEPA.d91.s216.e0",
"arg2_id": "IEPA.d91.s216.e1",
"normalized": []
},
{
"id": "IEPA.d91.s217.i0",
"type": "PPI",
"arg1_id": "IEPA.d91.s217.e0",
"arg2_id": "IEPA.d91.s217.e1",
"normalized": []
},
{
"id": "IEPA.d91.s218.i0",
"type": "PPI",
"arg1_id": "IEPA.d91.s218.e0",
"arg2_id": "IEPA.d91.s218.e1",
"normalized": []
},
{
"id": "IEPA.d91.s219.i0",
"type": "PPI",
"arg1_id": "IEPA.d91.s219.e0",
"arg2_id": "IEPA.d91.s219.e1",
"normalized": []
},
{
"id": "IEPA.d91.s220.i0",
"type": "PPI",
"arg1_id": "IEPA.d91.s220.e0",
"arg2_id": "IEPA.d91.s220.e1",
"normalized": []
},
{
"id": "IEPA.d91.s221.i0",
"type": "PPI",
"arg1_id": "IEPA.d91.s221.e0",
"arg2_id": "IEPA.d91.s221.e1",
"normalized": []
},
{
"id": "IEPA.d91.s222.i0",
"type": "PPI",
"arg1_id": "IEPA.d91.s222.e0",
"arg2_id": "IEPA.d91.s222.e1",
"normalized": []
},
{
"id": "IEPA.d91.s223.i0",
"type": "PPI",
"arg1_id": "IEPA.d91.s223.e1",
"arg2_id": "IEPA.d91.s223.e2",
"normalized": []
},
{
"id": "IEPA.d91.s224.i0",
"type": "PPI",
"arg1_id": "IEPA.d91.s224.e0",
"arg2_id": "IEPA.d91.s224.e1",
"normalized": []
}
] |
IEPA.d92 | 9867073 | [
{
"id": "IEPA.d92.s225",
"type": "",
"text": [
"In isolated adipocytes, the loss of almost half the 18S RNA content over a 24-hour incubation was prevented in the presence of insulin but not oxytocin or epidermal growth factor (EGF)"
],
"offsets": [
[
0,
184
]
]
}
] | [
{
"id": "IEPA.d92.s225.e0",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
127,
134
]
],
"normalized": []
},
{
"id": "IEPA.d92.s225.e1",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
143,
151
]
],
"normalized": []
}
] | [] | [] | [] |
IEPA.d93 | 9870709 | [
{
"id": "IEPA.d93.s226",
"type": "",
"text": [
"Further investigation suggested that activation of protein kinase C (PKC), which is part of the AVP-induced intracellular signalling pathway, is necessary and sufficient for the generation of the synergistic response, although it is not obligatory for AVP-induced ACTH release"
],
"offsets": [
[
0,
276
]
]
}
] | [
{
"id": "IEPA.d93.s226.e0",
"type": "",
"text": [
"protein kinase C"
],
"offsets": [
[
51,
67
]
],
"normalized": []
},
{
"id": "IEPA.d93.s226.e1",
"type": "",
"text": [
"AVP"
],
"offsets": [
[
96,
99
]
],
"normalized": []
},
{
"id": "IEPA.d93.s226.e2",
"type": "",
"text": [
"AVP"
],
"offsets": [
[
252,
255
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d93.s226.i0",
"type": "PPI",
"arg1_id": "IEPA.d93.s226.e0",
"arg2_id": "IEPA.d93.s226.e1",
"normalized": []
}
] |
IEPA.d94 | 9876242 | [
{
"id": "IEPA.d94.s227",
"type": "",
"text": [
"Oxytocin (OT) is more expressed in the TEC/TNC than vasopressin (VP); insulin-like growth factor 2 (IGF-2) thymic expression predominates over IGF-1, and much more over (pro)insulin"
],
"offsets": [
[
0,
181
]
]
},
{
"id": "IEPA.d94.s228",
"type": "",
"text": [
"Thus, OT was proposed to be the self antigen of the neurohypophysial family, and IGF-2 the self antigen precursor of the insulin family"
],
"offsets": [
[
182,
317
]
]
}
] | [
{
"id": "IEPA.d94.s227.e0",
"type": "",
"text": [
"Oxytocin"
],
"offsets": [
[
0,
8
]
],
"normalized": []
},
{
"id": "IEPA.d94.s227.e1",
"type": "",
"text": [
"(pro)insulin"
],
"offsets": [
[
169,
181
]
],
"normalized": []
},
{
"id": "IEPA.d94.s228.e0",
"type": "",
"text": [
"OT"
],
"offsets": [
[
188,
190
]
],
"normalized": []
},
{
"id": "IEPA.d94.s228.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
303,
310
]
],
"normalized": []
}
] | [] | [] | [] |
IEPA.d96 | 9892233 | [
{
"id": "IEPA.d96.s231",
"type": "",
"text": [
"Downregulation of uncoupling protein 2 mRNA in white adipose tissue and uncoupling protein 3 mRNA in skeletal muscle during the early stages of leptin treatment"
],
"offsets": [
[
0,
160
]
]
},
{
"id": "IEPA.d96.s232",
"type": "",
"text": [
"Leptin by intravenous or intracerebroventricular infusion for 5 h was associated with a decrease in UCP-2 mRNA in WAT (47-52%) and UCP-3 mRNA in SM (33-37%)"
],
"offsets": [
[
161,
317
]
]
},
{
"id": "IEPA.d96.s233",
"type": "",
"text": [
"Denervation suppressed mRNA levels for UCP-2 (49%), UCP-3 (36%), and COX-IV (59%) and eliminated the acute response to leptin in SM"
],
"offsets": [
[
318,
449
]
]
}
] | [
{
"id": "IEPA.d96.s231.e0",
"type": "",
"text": [
"uncoupling protein 2"
],
"offsets": [
[
18,
38
]
],
"normalized": []
},
{
"id": "IEPA.d96.s231.e1",
"type": "",
"text": [
"uncoupling protein 3"
],
"offsets": [
[
72,
92
]
],
"normalized": []
},
{
"id": "IEPA.d96.s231.e2",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
144,
150
]
],
"normalized": []
},
{
"id": "IEPA.d96.s232.e0",
"type": "",
"text": [
"Leptin"
],
"offsets": [
[
161,
167
]
],
"normalized": []
},
{
"id": "IEPA.d96.s232.e1",
"type": "",
"text": [
"UCP-2"
],
"offsets": [
[
261,
266
]
],
"normalized": []
},
{
"id": "IEPA.d96.s232.e2",
"type": "",
"text": [
"UCP-3"
],
"offsets": [
[
292,
297
]
],
"normalized": []
},
{
"id": "IEPA.d96.s233.e0",
"type": "",
"text": [
"UCP-2"
],
"offsets": [
[
357,
362
]
],
"normalized": []
},
{
"id": "IEPA.d96.s233.e1",
"type": "",
"text": [
"UCP-3"
],
"offsets": [
[
370,
375
]
],
"normalized": []
},
{
"id": "IEPA.d96.s233.e2",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
437,
443
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d96.s231.i0",
"type": "PPI",
"arg1_id": "IEPA.d96.s231.e0",
"arg2_id": "IEPA.d96.s231.e2",
"normalized": []
},
{
"id": "IEPA.d96.s231.i1",
"type": "PPI",
"arg1_id": "IEPA.d96.s231.e1",
"arg2_id": "IEPA.d96.s231.e2",
"normalized": []
},
{
"id": "IEPA.d96.s232.i0",
"type": "PPI",
"arg1_id": "IEPA.d96.s232.e0",
"arg2_id": "IEPA.d96.s232.e1",
"normalized": []
},
{
"id": "IEPA.d96.s232.i1",
"type": "PPI",
"arg1_id": "IEPA.d96.s232.e0",
"arg2_id": "IEPA.d96.s232.e2",
"normalized": []
}
] |
IEPA.d97 | 9893131 | [
{
"id": "IEPA.d97.s234",
"type": "",
"text": [
"The specific protein kinase C (PKC) inhibitor chelerythrine (5 micrometers) inhibited PTH-, AVP-, PGE2-, and adenosine-stimulated Ca2+ reabsorption by 77%, 67%, 79%, and 100%, respectively"
],
"offsets": [
[
0,
188
]
]
},
{
"id": "IEPA.d97.s235",
"type": "",
"text": [
"CONCLUSION: PTH, AVP, PGE2, and adenosine stimulate Ca2+ reabsorption via a pathway that is independent of cAMP and that involves a phorbol ester-insensitive PKC isotype"
],
"offsets": [
[
189,
358
]
]
}
] | [
{
"id": "IEPA.d97.s234.e0",
"type": "",
"text": [
"protein kinase C"
],
"offsets": [
[
13,
29
]
],
"normalized": []
},
{
"id": "IEPA.d97.s234.e1",
"type": "",
"text": [
"AVP"
],
"offsets": [
[
92,
95
]
],
"normalized": []
},
{
"id": "IEPA.d97.s235.e0",
"type": "",
"text": [
"AVP"
],
"offsets": [
[
206,
209
]
],
"normalized": []
},
{
"id": "IEPA.d97.s235.e1",
"type": "",
"text": [
"PKC"
],
"offsets": [
[
347,
350
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d97.s234.i0",
"type": "PPI",
"arg1_id": "IEPA.d97.s234.e0",
"arg2_id": "IEPA.d97.s234.e1",
"normalized": []
},
{
"id": "IEPA.d97.s235.i0",
"type": "PPI",
"arg1_id": "IEPA.d97.s235.e0",
"arg2_id": "IEPA.d97.s235.e1",
"normalized": []
}
] |
IEPA.d98 | 9920656 | [
{
"id": "IEPA.d98.s236",
"type": "",
"text": [
"We observed that primary microglial cultures and the THP-1 monocytic cell line are stimulated by fibrillar beta-amyloid and prion peptides to activate identical tyrosine kinase-dependent inflammatory signal transduction cascades"
],
"offsets": [
[
0,
228
]
]
}
] | [
{
"id": "IEPA.d98.s236.e0",
"type": "",
"text": [
"prion"
],
"offsets": [
[
124,
129
]
],
"normalized": []
},
{
"id": "IEPA.d98.s236.e1",
"type": "",
"text": [
"tyrosine kinase"
],
"offsets": [
[
161,
176
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d98.s236.i0",
"type": "PPI",
"arg1_id": "IEPA.d98.s236.e0",
"arg2_id": "IEPA.d98.s236.e1",
"normalized": []
}
] |
IEPA.d99 | 9920735 | [
{
"id": "IEPA.d99.s237",
"type": "",
"text": [
"Enhanced phosphoinositide hydrolysis via overexpression of phospholipase C beta1 or delta1 inhibits stimulus-induced insulin release in insulinoma MIN6 cells."
],
"offsets": [
[
0,
158
]
]
},
{
"id": "IEPA.d99.s238",
"type": "",
"text": [
"To study the effects of enhanced phosphoinositide hydrolysis on insulin secretion, phosphoinositide-specific phospholipase Cbeta1 (PLCbeta1) or PLCdelta1 was overexpressed in insulinoma MIN6 cells via adenoviral vectors."
],
"offsets": [
[
159,
379
]
]
}
] | [
{
"id": "IEPA.d99.s237.e0",
"type": "",
"text": [
"phospholipase C"
],
"offsets": [
[
59,
74
]
],
"normalized": []
},
{
"id": "IEPA.d99.s237.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
117,
124
]
],
"normalized": []
},
{
"id": "IEPA.d99.s238.e0",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
223,
230
]
],
"normalized": []
},
{
"id": "IEPA.d99.s238.e1",
"type": "",
"text": [
"phospholipase Cbeta1"
],
"offsets": [
[
268,
288
]
],
"normalized": []
},
{
"id": "IEPA.d99.s238.e2",
"type": "",
"text": [
"PLCdelta1"
],
"offsets": [
[
303,
312
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d99.s237.i0",
"type": "PPI",
"arg1_id": "IEPA.d99.s237.e0",
"arg2_id": "IEPA.d99.s237.e1",
"normalized": []
}
] |
IEPA.d100 | 9924739 | [
{
"id": "IEPA.d100.s239",
"type": "",
"text": [
"If daily oxytocin injections are repeated over a 5-day period, blood pressure is decreased by 10-20 mmHg, the withdrawal latency to heat stimuli is prolonged, cortisol levels are decreased and insulin and cholecystokinin levels are increased"
],
"offsets": [
[
0,
241
]
]
}
] | [
{
"id": "IEPA.d100.s239.e0",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
9,
17
]
],
"normalized": []
},
{
"id": "IEPA.d100.s239.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
193,
200
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d100.s239.i0",
"type": "PPI",
"arg1_id": "IEPA.d100.s239.e0",
"arg2_id": "IEPA.d100.s239.e1",
"normalized": []
}
] |
IEPA.d104 | 10066625 | [
{
"id": "IEPA.d104.s243",
"type": "",
"text": [
"In addition, abscisic acid-mediated inhibition of gibberellin-stimulated responses seems to depend on the activation of a phospholipase D during induction of alpha-amylase in barley aleurone cells as well as on a putative acetyltransferase involved in elongation growth."
],
"offsets": [
[
0,
270
]
]
}
] | [
{
"id": "IEPA.d104.s243.e0",
"type": "",
"text": [
"gibberellin"
],
"offsets": [
[
50,
61
]
],
"normalized": []
},
{
"id": "IEPA.d104.s243.e1",
"type": "",
"text": [
"alpha-amylase"
],
"offsets": [
[
158,
171
]
],
"normalized": []
}
] | [] | [] | [] |
IEPA.d106 | 10070167 | [
{
"id": "IEPA.d106.s245",
"type": "",
"text": [
"Protein kinase C (PKC) inhibitors reversed AVP inhibition, whereas PKC activator inhibited nitrite production"
],
"offsets": [
[
0,
109
]
]
},
{
"id": "IEPA.d106.s246",
"type": "",
"text": [
"The inhibitory action of AVP involves both the activation of PKC and the transcription of iNOS mRNA in cultured rat GMC"
],
"offsets": [
[
110,
229
]
]
}
] | [
{
"id": "IEPA.d106.s245.e0",
"type": "",
"text": [
"Protein kinase C"
],
"offsets": [
[
0,
16
]
],
"normalized": []
},
{
"id": "IEPA.d106.s245.e1",
"type": "",
"text": [
"AVP"
],
"offsets": [
[
43,
46
]
],
"normalized": []
},
{
"id": "IEPA.d106.s245.e2",
"type": "",
"text": [
"PKC"
],
"offsets": [
[
67,
70
]
],
"normalized": []
},
{
"id": "IEPA.d106.s246.e0",
"type": "",
"text": [
"AVP"
],
"offsets": [
[
135,
138
]
],
"normalized": []
},
{
"id": "IEPA.d106.s246.e1",
"type": "",
"text": [
"PKC"
],
"offsets": [
[
171,
174
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d106.s245.i0",
"type": "PPI",
"arg1_id": "IEPA.d106.s245.e0",
"arg2_id": "IEPA.d106.s245.e1",
"normalized": []
},
{
"id": "IEPA.d106.s246.i0",
"type": "PPI",
"arg1_id": "IEPA.d106.s246.e0",
"arg2_id": "IEPA.d106.s246.e1",
"normalized": []
}
] |
IEPA.d107 | 10080713 | [
{
"id": "IEPA.d107.s247",
"type": "",
"text": [
"Molecular characterization of catalytic-subunit cDNA sequences encoding protein phosphatases 1 and 2A and study of their roles in the gibberellin-dependent Osamy-c expression in rice"
],
"offsets": [
[
0,
182
]
]
},
{
"id": "IEPA.d107.s248",
"type": "",
"text": [
"To understand the molecular mechanism of gibberellin-dependent gene regulation, the effect of three phosphatase inhibitors on the germination of rice seeds and the expression of a target gene, the alpha-amylase gene, Osamy-c, were measured"
],
"offsets": [
[
183,
422
]
]
},
{
"id": "IEPA.d107.s249",
"type": "",
"text": [
"To further understand the possible role of protein phosphatases 1 and 2A in the GA-dependent expression of Osamy-c, we isolated cDNA clones encoding protein phosphatase 1 and protein phosphatase 2A from a rice aleurone cDNA library"
],
"offsets": [
[
423,
654
]
]
},
{
"id": "IEPA.d107.s250",
"type": "",
"text": [
"Taken together, our results suggest that protein phosphatases PP1 or PP2A are involved in the GA-dependent expression of the rice Osamy-c gene, though the PP1 or/and PP2A enzymatic activities as well as mRNA levels do not increase upon GA3 treatment"
],
"offsets": [
[
655,
904
]
]
}
] | [
{
"id": "IEPA.d107.s247.e0",
"type": "",
"text": [
"gibberellin"
],
"offsets": [
[
134,
145
]
],
"normalized": []
},
{
"id": "IEPA.d107.s247.e1",
"type": "",
"text": [
"Osamy-c"
],
"offsets": [
[
156,
163
]
],
"normalized": []
},
{
"id": "IEPA.d107.s248.e0",
"type": "",
"text": [
"gibberellin"
],
"offsets": [
[
224,
235
]
],
"normalized": []
},
{
"id": "IEPA.d107.s248.e1",
"type": "",
"text": [
"alpha-amylase"
],
"offsets": [
[
380,
393
]
],
"normalized": []
},
{
"id": "IEPA.d107.s249.e0",
"type": "",
"text": [
"GA"
],
"offsets": [
[
503,
505
]
],
"normalized": []
},
{
"id": "IEPA.d107.s249.e1",
"type": "",
"text": [
"Osamy-c"
],
"offsets": [
[
530,
537
]
],
"normalized": []
},
{
"id": "IEPA.d107.s250.e0",
"type": "",
"text": [
"GA"
],
"offsets": [
[
749,
751
]
],
"normalized": []
},
{
"id": "IEPA.d107.s250.e1",
"type": "",
"text": [
"Osamy-c"
],
"offsets": [
[
785,
792
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d107.s247.i0",
"type": "PPI",
"arg1_id": "IEPA.d107.s247.e0",
"arg2_id": "IEPA.d107.s247.e1",
"normalized": []
},
{
"id": "IEPA.d107.s248.i0",
"type": "PPI",
"arg1_id": "IEPA.d107.s248.e0",
"arg2_id": "IEPA.d107.s248.e1",
"normalized": []
},
{
"id": "IEPA.d107.s249.i0",
"type": "PPI",
"arg1_id": "IEPA.d107.s249.e0",
"arg2_id": "IEPA.d107.s249.e1",
"normalized": []
},
{
"id": "IEPA.d107.s250.i0",
"type": "PPI",
"arg1_id": "IEPA.d107.s250.e0",
"arg2_id": "IEPA.d107.s250.e1",
"normalized": []
}
] |
IEPA.d109 | 10098482 | [
{
"id": "IEPA.d109.s256",
"type": "",
"text": [
"Fasting and leptin modulate adipose and muscle uncoupling protein: divergent effects between messenger ribonucleic acid and protein expression"
],
"offsets": [
[
0,
142
]
]
},
{
"id": "IEPA.d109.s257",
"type": "",
"text": [
"In this study, we examined the effects of fasting for 2 days and exogenous s.c. leptin, 200 microg every 8 h for 2 days, on the regulation of uncoupling protein (UCP) subtypes in brown adipose tissue (BAT) and gastrocnemius muscle"
],
"offsets": [
[
143,
373
]
]
},
{
"id": "IEPA.d109.s258",
"type": "",
"text": [
"Leptin, compared with vehicle, did not alter BAT UCP-1 or UCP-3 mRNA or protein expression when administered to normal ad libitum fed rats"
],
"offsets": [
[
374,
512
]
]
},
{
"id": "IEPA.d109.s259",
"type": "",
"text": [
"Fasting significantly decreased BAT UCP-1 and UCP-3 mRNA expression, to 31% and 30% of ad libitum fed controls, respectively, effects which were prevented by administration of leptin to fasted rats"
],
"offsets": [
[
513,
710
]
]
},
{
"id": "IEPA.d109.s260",
"type": "",
"text": [
"Fasting also significantly decreased BAT UCP-1 protein expression, to 67% of control; however, that effect was not prevented by leptin treatment"
],
"offsets": [
[
711,
855
]
]
},
{
"id": "IEPA.d109.s261",
"type": "",
"text": [
"Fasting, with or without leptin administration, did not affect BAT UCP-2 mRNA; however, leptin administration to ad libitum fed rats significantly increased BAT UCP-2 mRNA, to 138% of control"
],
"offsets": [
[
856,
1047
]
]
},
{
"id": "IEPA.d109.s262",
"type": "",
"text": [
"Fasting significantly enhanced gastrocnemius muscle UCP-3 mRNA (411% of control) and protein expression (168% of control), whereas leptin administration to fasted rats did not alter either of these effects"
],
"offsets": [
[
1048,
1253
]
]
},
{
"id": "IEPA.d109.s263",
"type": "",
"text": [
"In summary, UCP subtype mRNA and protein are regulated in tissue- and subtype-specific fashion by leptin and food restriction"
],
"offsets": [
[
1254,
1379
]
]
}
] | [
{
"id": "IEPA.d109.s256.e0",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
12,
18
]
],
"normalized": []
},
{
"id": "IEPA.d109.s256.e1",
"type": "",
"text": [
"uncoupling protein"
],
"offsets": [
[
47,
65
]
],
"normalized": []
},
{
"id": "IEPA.d109.s257.e0",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
223,
229
]
],
"normalized": []
},
{
"id": "IEPA.d109.s257.e1",
"type": "",
"text": [
"uncoupling protein"
],
"offsets": [
[
285,
303
]
],
"normalized": []
},
{
"id": "IEPA.d109.s258.e0",
"type": "",
"text": [
"Leptin"
],
"offsets": [
[
374,
380
]
],
"normalized": []
},
{
"id": "IEPA.d109.s258.e1",
"type": "",
"text": [
"UCP-1"
],
"offsets": [
[
423,
428
]
],
"normalized": []
},
{
"id": "IEPA.d109.s258.e2",
"type": "",
"text": [
"UCP-3"
],
"offsets": [
[
432,
437
]
],
"normalized": []
},
{
"id": "IEPA.d109.s259.e0",
"type": "",
"text": [
"UCP-1"
],
"offsets": [
[
549,
554
]
],
"normalized": []
},
{
"id": "IEPA.d109.s259.e1",
"type": "",
"text": [
"UCP-3"
],
"offsets": [
[
559,
564
]
],
"normalized": []
},
{
"id": "IEPA.d109.s259.e2",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
689,
695
]
],
"normalized": []
},
{
"id": "IEPA.d109.s260.e0",
"type": "",
"text": [
"UCP-1"
],
"offsets": [
[
752,
757
]
],
"normalized": []
},
{
"id": "IEPA.d109.s260.e1",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
839,
845
]
],
"normalized": []
},
{
"id": "IEPA.d109.s261.e0",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
881,
887
]
],
"normalized": []
},
{
"id": "IEPA.d109.s261.e1",
"type": "",
"text": [
"UCP-2"
],
"offsets": [
[
923,
928
]
],
"normalized": []
},
{
"id": "IEPA.d109.s261.e2",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
944,
950
]
],
"normalized": []
},
{
"id": "IEPA.d109.s261.e3",
"type": "",
"text": [
"UCP-2"
],
"offsets": [
[
1017,
1022
]
],
"normalized": []
},
{
"id": "IEPA.d109.s262.e0",
"type": "",
"text": [
"UCP-3"
],
"offsets": [
[
1100,
1105
]
],
"normalized": []
},
{
"id": "IEPA.d109.s262.e1",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
1179,
1185
]
],
"normalized": []
},
{
"id": "IEPA.d109.s263.e0",
"type": "",
"text": [
"UCP"
],
"offsets": [
[
1266,
1269
]
],
"normalized": []
},
{
"id": "IEPA.d109.s263.e1",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
1352,
1358
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d109.s256.i0",
"type": "PPI",
"arg1_id": "IEPA.d109.s256.e0",
"arg2_id": "IEPA.d109.s256.e1",
"normalized": []
},
{
"id": "IEPA.d109.s259.i0",
"type": "PPI",
"arg1_id": "IEPA.d109.s259.e0",
"arg2_id": "IEPA.d109.s259.e2",
"normalized": []
},
{
"id": "IEPA.d109.s259.i1",
"type": "PPI",
"arg1_id": "IEPA.d109.s259.e1",
"arg2_id": "IEPA.d109.s259.e2",
"normalized": []
},
{
"id": "IEPA.d109.s261.i0",
"type": "PPI",
"arg1_id": "IEPA.d109.s261.e2",
"arg2_id": "IEPA.d109.s261.e3",
"normalized": []
},
{
"id": "IEPA.d109.s263.i0",
"type": "PPI",
"arg1_id": "IEPA.d109.s263.e0",
"arg2_id": "IEPA.d109.s263.e1",
"normalized": []
}
] |
IEPA.d111 | 10102788 | [
{
"id": "IEPA.d111.s269",
"type": "",
"text": [
"Plasma oxytocin, and some functionally related peptides (CCK, gastrin, somatostatin and insulin), were measured by standard radioimmunoassay techniques"
],
"offsets": [
[
0,
151
]
]
}
] | [
{
"id": "IEPA.d111.s269.e0",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
7,
15
]
],
"normalized": []
},
{
"id": "IEPA.d111.s269.e1",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
88,
95
]
],
"normalized": []
}
] | [] | [] | [] |
IEPA.d112 | 10198105 | [
{
"id": "IEPA.d112.s270",
"type": "",
"text": [
"Analyses of hormone regulation of expression of mRNA for the aleurone RNase revealed that, like the pattern for alpha-amylase, mRNA levels increased in the presence of gibberellic acid, and its antagonist abscisic acid prevented this effect"
],
"offsets": [
[
0,
240
]
]
},
{
"id": "IEPA.d112.s271",
"type": "",
"text": [
"Quantitative studies at early times demonstrated that cycloheximide treatment of aleurone layers increased mRNA levels 4-fold, whereas a combination of gibberellin plus cycloheximide treatment was required to increase alpha-amylase mRNA levels to the same extent"
],
"offsets": [
[
241,
503
]
]
}
] | [
{
"id": "IEPA.d112.s270.e0",
"type": "",
"text": [
"alpha-amylase"
],
"offsets": [
[
112,
125
]
],
"normalized": []
},
{
"id": "IEPA.d112.s270.e1",
"type": "",
"text": [
"gibberellic acid"
],
"offsets": [
[
168,
184
]
],
"normalized": []
},
{
"id": "IEPA.d112.s271.e0",
"type": "",
"text": [
"gibberellin"
],
"offsets": [
[
393,
404
]
],
"normalized": []
},
{
"id": "IEPA.d112.s271.e1",
"type": "",
"text": [
"alpha-amylase"
],
"offsets": [
[
459,
472
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d112.s270.i0",
"type": "PPI",
"arg1_id": "IEPA.d112.s270.e0",
"arg2_id": "IEPA.d112.s270.e1",
"normalized": []
},
{
"id": "IEPA.d112.s271.i0",
"type": "PPI",
"arg1_id": "IEPA.d112.s271.e0",
"arg2_id": "IEPA.d112.s271.e1",
"normalized": []
}
] |
IEPA.d113 | 10235637 | [
{
"id": "IEPA.d113.s272",
"type": "",
"text": [
"The experiments were concluded by taking blood samples for later analysis of plasma glucose and plasma levels of the following hormones: insulin, gastrin, CCK, glucagon, somatostatin, oxytocin and corticosterone"
],
"offsets": [
[
0,
211
]
]
},
{
"id": "IEPA.d113.s273",
"type": "",
"text": [
"The low-performing Stock B animals were characterized by [1] being more reactive to sensory stimulation: higher startle amplitude and shorter startle latency; [2] having higher plasma insulin and corticosterone levels, whereas plasma gastrin and oxytocin were significantly lowered and a strong tendency for a decrease also in plasma CCK"
],
"offsets": [
[
212,
549
]
]
}
] | [
{
"id": "IEPA.d113.s272.e0",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
137,
144
]
],
"normalized": []
},
{
"id": "IEPA.d113.s272.e1",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
184,
192
]
],
"normalized": []
},
{
"id": "IEPA.d113.s273.e0",
"type": "",
"text": [
"insulin"
],
"offsets": [
[
396,
403
]
],
"normalized": []
},
{
"id": "IEPA.d113.s273.e1",
"type": "",
"text": [
"oxytocin"
],
"offsets": [
[
458,
466
]
],
"normalized": []
}
] | [] | [] | [] |
IEPA.d114 | 10331406 | [
{
"id": "IEPA.d114.s274",
"type": "",
"text": [
"In normal pancreatic islets, UCP-2 is upregulated by leptin and is low in leptin-resistant islets of ZDF rats"
],
"offsets": [
[
0,
109
]
]
},
{
"id": "IEPA.d114.s275",
"type": "",
"text": [
"To determine whether UCP-2 does, in fact, have uncoupling activity and, if so, whether such activity would favorably influence the abnormalities in leptin-unresponsive UCP-2-underexpressing islets of diabetic ZDF rats, we transferred the UCP-2 gene to the islets of diabetic ZDF rats and lean (+/+) ZDF control rats"
],
"offsets": [
[
110,
425
]
]
},
{
"id": "IEPA.d114.s276",
"type": "",
"text": [
"We conclude that UCP-2 has uncoupling function when overexpressed in leptin-insensitive islets and that its overexpression corrects the underexpression of the insulin gene and ameliorates glucose-stimulated insulin secretion, possibly by increasing the ATP:ADP ratio"
],
"offsets": [
[
426,
692
]
]
}
] | [
{
"id": "IEPA.d114.s274.e0",
"type": "",
"text": [
"UCP-2"
],
"offsets": [
[
29,
34
]
],
"normalized": []
},
{
"id": "IEPA.d114.s274.e1",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
53,
59
]
],
"normalized": []
},
{
"id": "IEPA.d114.s274.e2",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
74,
80
]
],
"normalized": []
},
{
"id": "IEPA.d114.s275.e0",
"type": "",
"text": [
"UCP-2"
],
"offsets": [
[
131,
136
]
],
"normalized": []
},
{
"id": "IEPA.d114.s275.e1",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
258,
264
]
],
"normalized": []
},
{
"id": "IEPA.d114.s275.e2",
"type": "",
"text": [
"UCP-2"
],
"offsets": [
[
278,
283
]
],
"normalized": []
},
{
"id": "IEPA.d114.s275.e3",
"type": "",
"text": [
"UCP-2"
],
"offsets": [
[
348,
353
]
],
"normalized": []
},
{
"id": "IEPA.d114.s276.e0",
"type": "",
"text": [
"UCP-2"
],
"offsets": [
[
443,
448
]
],
"normalized": []
},
{
"id": "IEPA.d114.s276.e1",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
495,
501
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d114.s274.i0",
"type": "PPI",
"arg1_id": "IEPA.d114.s274.e0",
"arg2_id": "IEPA.d114.s274.e1",
"normalized": []
}
] |
IEPA.d117 | 10364415 | [
{
"id": "IEPA.d117.s285",
"type": "",
"text": [
"The second class of mutant, gse (GA sensitivity), differed principally in GA sensitivity, requiring approximately 100-fold higher [GA3] for both leaf elongation and alpha-amylase production by aleurone"
],
"offsets": [
[
0,
201
]
]
}
] | [
{
"id": "IEPA.d117.s285.e0",
"type": "",
"text": [
"GA"
],
"offsets": [
[
33,
35
]
],
"normalized": []
},
{
"id": "IEPA.d117.s285.e1",
"type": "",
"text": [
"GA"
],
"offsets": [
[
74,
76
]
],
"normalized": []
},
{
"id": "IEPA.d117.s285.e2",
"type": "",
"text": [
"GA3"
],
"offsets": [
[
131,
134
]
],
"normalized": []
},
{
"id": "IEPA.d117.s285.e3",
"type": "",
"text": [
"alpha-amylase"
],
"offsets": [
[
165,
178
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d117.s285.i0",
"type": "PPI",
"arg1_id": "IEPA.d117.s285.e2",
"arg2_id": "IEPA.d117.s285.e3",
"normalized": []
}
] |
IEPA.d118 | 10375750 | [
{
"id": "IEPA.d118.s286",
"type": "",
"text": [
"Phorbol myristate acetate (TPA), an activator of PKC, elicited an increase of MAPK activity, but did not further influence the level of AVP4-8-enhanced MAPK activity; Nevertheless, the extent of CaMKII activation was attenuated by TPA"
],
"offsets": [
[
0,
234
]
]
}
] | [
{
"id": "IEPA.d118.s286.e0",
"type": "",
"text": [
"PKC"
],
"offsets": [
[
49,
52
]
],
"normalized": []
},
{
"id": "IEPA.d118.s286.e1",
"type": "",
"text": [
"AVP"
],
"offsets": [
[
136,
139
]
],
"normalized": []
}
] | [] | [] | [] |
IEPA.d119 | 10394640 | [
{
"id": "IEPA.d119.s287",
"type": "",
"text": [
"The gibberellin-responsive elements conserved in cereal alpha-amylase genes are not included in the 5'-upstream region of Rep1 or RepA"
],
"offsets": [
[
0,
134
]
]
}
] | [
{
"id": "IEPA.d119.s287.e0",
"type": "",
"text": [
"gibberellin"
],
"offsets": [
[
4,
15
]
],
"normalized": []
},
{
"id": "IEPA.d119.s287.e1",
"type": "",
"text": [
"alpha-amylase"
],
"offsets": [
[
56,
69
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d119.s287.i0",
"type": "PPI",
"arg1_id": "IEPA.d119.s287.e0",
"arg2_id": "IEPA.d119.s287.e1",
"normalized": []
}
] |
IEPA.d120 | 10405973 | [
{
"id": "IEPA.d120.s288",
"type": "",
"text": [
"Furthermore, our 14C-acetate-labeling studies showed a 50% reduction in cholesteryl ester synthesis in the presence of either flavonoid, which could account for the reduction in net apoB secretion caused by incubation with these compounds"
],
"offsets": [
[
0,
238
]
]
}
] | [
{
"id": "IEPA.d120.s288.e0",
"type": "",
"text": [
"cholesteryl ester"
],
"offsets": [
[
72,
89
]
],
"normalized": []
},
{
"id": "IEPA.d120.s288.e1",
"type": "",
"text": [
"flavonoid"
],
"offsets": [
[
126,
135
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d120.s288.i0",
"type": "PPI",
"arg1_id": "IEPA.d120.s288.e0",
"arg2_id": "IEPA.d120.s288.e1",
"normalized": []
}
] |
IEPA.d121 | 10432317 | [
{
"id": "IEPA.d121.s289",
"type": "",
"text": [
"An inhibitor of PKC, Ro31-8220 (10 microM), abolished the ability of PDBu to decrease [Ca(2+)](i), without affecting the response to maximal or submaximal concentrations of AVP"
],
"offsets": [
[
0,
176
]
]
}
] | [
{
"id": "IEPA.d121.s289.e0",
"type": "",
"text": [
"PKC"
],
"offsets": [
[
16,
19
]
],
"normalized": []
},
{
"id": "IEPA.d121.s289.e1",
"type": "",
"text": [
"AVP"
],
"offsets": [
[
173,
176
]
],
"normalized": []
}
] | [] | [] | [] |
IEPA.d122 | 10433228 | [
{
"id": "IEPA.d122.s290",
"type": "",
"text": [
"Effects of intravenously infused leptin on insulin sensitivity and on the expression of uncoupling proteins in brown adipose tissue"
],
"offsets": [
[
0,
131
]
]
},
{
"id": "IEPA.d122.s291",
"type": "",
"text": [
"Centrally administered leptin has been shown to increase insulin-stimulated glucose utilization and to favor the expression of uncoupling proteins (UCPs)"
],
"offsets": [
[
132,
285
]
]
},
{
"id": "IEPA.d122.s292",
"type": "",
"text": [
"To study if leptin also has direct peripherally mediated effects on these processes, this hormone (1 mg/day) or its vehicle was infused i.v. for 4 days to lean rats and insulin-stimulated glucose utilization in skeletal muscle and adipose tissue as well as the expression of UCP messenger RNAs (mRNAs) in brown adipose tissue were measured"
],
"offsets": [
[
286,
625
]
]
},
{
"id": "IEPA.d122.s293",
"type": "",
"text": [
"I.v. leptin infusion also favored the expression of UCPs in brown adipose tissue, either by increasing their expression or preventing the fall occurring during the pair-feeding regimen."
],
"offsets": [
[
626,
811
]
]
},
{
"id": "IEPA.d122.s294",
"type": "",
"text": [
"Relative UCP expression levels were 100, 104, and 33 for UCP1, 100, 191, and 125 for UCP2 and 100, 107, and 29 for UCP3 in ad libitum fed control rats, in leptin-treated rats and in pair-fed control rats, respectively"
],
"offsets": [
[
812,
1029
]
]
},
{
"id": "IEPA.d122.s295",
"type": "",
"text": [
"These results suggest that the overall effect of leptin on glucose utilization and on the expression of UCPs may be mediated through central mechanism"
],
"offsets": [
[
1030,
1180
]
]
}
] | [
{
"id": "IEPA.d122.s290.e0",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
33,
39
]
],
"normalized": []
},
{
"id": "IEPA.d122.s290.e1",
"type": "",
"text": [
"uncoupling proteins"
],
"offsets": [
[
88,
107
]
],
"normalized": []
},
{
"id": "IEPA.d122.s291.e0",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
155,
161
]
],
"normalized": []
},
{
"id": "IEPA.d122.s291.e1",
"type": "",
"text": [
"uncoupling proteins"
],
"offsets": [
[
259,
278
]
],
"normalized": []
},
{
"id": "IEPA.d122.s292.e0",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
298,
304
]
],
"normalized": []
},
{
"id": "IEPA.d122.s292.e1",
"type": "",
"text": [
"UCP"
],
"offsets": [
[
561,
564
]
],
"normalized": []
},
{
"id": "IEPA.d122.s293.e0",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
631,
637
]
],
"normalized": []
},
{
"id": "IEPA.d122.s293.e1",
"type": "",
"text": [
"UCPs"
],
"offsets": [
[
678,
682
]
],
"normalized": []
},
{
"id": "IEPA.d122.s294.e0",
"type": "",
"text": [
"UCP"
],
"offsets": [
[
821,
824
]
],
"normalized": []
},
{
"id": "IEPA.d122.s294.e1",
"type": "",
"text": [
"UCP1"
],
"offsets": [
[
869,
873
]
],
"normalized": []
},
{
"id": "IEPA.d122.s294.e2",
"type": "",
"text": [
"UCP2"
],
"offsets": [
[
897,
901
]
],
"normalized": []
},
{
"id": "IEPA.d122.s294.e3",
"type": "",
"text": [
"UCP3"
],
"offsets": [
[
927,
931
]
],
"normalized": []
},
{
"id": "IEPA.d122.s294.e4",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
967,
973
]
],
"normalized": []
},
{
"id": "IEPA.d122.s295.e0",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
1079,
1085
]
],
"normalized": []
},
{
"id": "IEPA.d122.s295.e1",
"type": "",
"text": [
"UCPs"
],
"offsets": [
[
1134,
1138
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d122.s290.i0",
"type": "PPI",
"arg1_id": "IEPA.d122.s290.e0",
"arg2_id": "IEPA.d122.s290.e1",
"normalized": []
},
{
"id": "IEPA.d122.s291.i0",
"type": "PPI",
"arg1_id": "IEPA.d122.s291.e0",
"arg2_id": "IEPA.d122.s291.e1",
"normalized": []
},
{
"id": "IEPA.d122.s293.i0",
"type": "PPI",
"arg1_id": "IEPA.d122.s293.e0",
"arg2_id": "IEPA.d122.s293.e1",
"normalized": []
},
{
"id": "IEPA.d122.s295.i0",
"type": "PPI",
"arg1_id": "IEPA.d122.s295.e0",
"arg2_id": "IEPA.d122.s295.e1",
"normalized": []
}
] |
IEPA.d126 | 10477827 | [
{
"id": "IEPA.d126.s299",
"type": "",
"text": [
"The expression of uterine UCP2 and UCP3 were up-regulated by 3.2- and 1.5-fold, respectively, during the late stage of pregnancy with an increase of WAT leptin mRNA expression and exogenous administration of leptin resulted in induction of the uterine UCP2 and UCP3 levels"
],
"offsets": [
[
0,
272
]
]
},
{
"id": "IEPA.d126.s300",
"type": "",
"text": [
"These results indicate that UCP gene expressions during pregnancy are regulated tissue-dependently, and up-regulation of uterine UCP2 and UCP3 mRNA may be due to increased leptin levels"
],
"offsets": [
[
273,
458
]
]
}
] | [
{
"id": "IEPA.d126.s299.e0",
"type": "",
"text": [
"UCP2"
],
"offsets": [
[
26,
30
]
],
"normalized": []
},
{
"id": "IEPA.d126.s299.e1",
"type": "",
"text": [
"UCP3"
],
"offsets": [
[
35,
39
]
],
"normalized": []
},
{
"id": "IEPA.d126.s299.e2",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
153,
159
]
],
"normalized": []
},
{
"id": "IEPA.d126.s299.e3",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
208,
214
]
],
"normalized": []
},
{
"id": "IEPA.d126.s299.e4",
"type": "",
"text": [
"UCP2"
],
"offsets": [
[
252,
256
]
],
"normalized": []
},
{
"id": "IEPA.d126.s299.e5",
"type": "",
"text": [
"UCP3"
],
"offsets": [
[
261,
265
]
],
"normalized": []
},
{
"id": "IEPA.d126.s300.e0",
"type": "",
"text": [
"UCP"
],
"offsets": [
[
301,
304
]
],
"normalized": []
},
{
"id": "IEPA.d126.s300.e1",
"type": "",
"text": [
"UCP2"
],
"offsets": [
[
402,
406
]
],
"normalized": []
},
{
"id": "IEPA.d126.s300.e2",
"type": "",
"text": [
"UCP3"
],
"offsets": [
[
411,
415
]
],
"normalized": []
},
{
"id": "IEPA.d126.s300.e3",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
445,
451
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d126.s299.i0",
"type": "PPI",
"arg1_id": "IEPA.d126.s299.e3",
"arg2_id": "IEPA.d126.s299.e4",
"normalized": []
},
{
"id": "IEPA.d126.s299.i1",
"type": "PPI",
"arg1_id": "IEPA.d126.s299.e3",
"arg2_id": "IEPA.d126.s299.e5",
"normalized": []
},
{
"id": "IEPA.d126.s300.i0",
"type": "PPI",
"arg1_id": "IEPA.d126.s300.e1",
"arg2_id": "IEPA.d126.s300.e3",
"normalized": []
},
{
"id": "IEPA.d126.s300.i1",
"type": "PPI",
"arg1_id": "IEPA.d126.s300.e2",
"arg2_id": "IEPA.d126.s300.e3",
"normalized": []
}
] |
IEPA.d127 | 10480887 | [
{
"id": "IEPA.d127.s301",
"type": "",
"text": [
"PI-PLC treatment of fetal guinea pig brain cultures substantially reduced the amount of Abeta40 and Abeta42 in the medium but had no effect on sAPPalpha"
],
"offsets": [
[
0,
152
]
]
},
{
"id": "IEPA.d127.s302",
"type": "",
"text": [
"When this parental line was treated with PI-PLC, Abeta40, Abeta42, and sAPPbeta decreased to levels similar to those observed in the mutant line, and the mutant line was resistant to these effects of PI-PLC"
],
"offsets": [
[
153,
359
]
]
}
] | [
{
"id": "IEPA.d127.s301.e0",
"type": "",
"text": [
"PI-PLC"
],
"offsets": [
[
0,
6
]
],
"normalized": []
},
{
"id": "IEPA.d127.s301.e1",
"type": "",
"text": [
"Abeta40"
],
"offsets": [
[
88,
95
]
],
"normalized": []
},
{
"id": "IEPA.d127.s301.e2",
"type": "",
"text": [
"Abeta42"
],
"offsets": [
[
100,
107
]
],
"normalized": []
},
{
"id": "IEPA.d127.s302.e0",
"type": "",
"text": [
"PI-PLC"
],
"offsets": [
[
194,
200
]
],
"normalized": []
},
{
"id": "IEPA.d127.s302.e1",
"type": "",
"text": [
"Abeta40"
],
"offsets": [
[
202,
209
]
],
"normalized": []
},
{
"id": "IEPA.d127.s302.e2",
"type": "",
"text": [
"Abeta42"
],
"offsets": [
[
211,
218
]
],
"normalized": []
},
{
"id": "IEPA.d127.s302.e3",
"type": "",
"text": [
"PI-PLC"
],
"offsets": [
[
353,
359
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d127.s301.i0",
"type": "PPI",
"arg1_id": "IEPA.d127.s301.e0",
"arg2_id": "IEPA.d127.s301.e1",
"normalized": []
},
{
"id": "IEPA.d127.s301.i1",
"type": "PPI",
"arg1_id": "IEPA.d127.s301.e0",
"arg2_id": "IEPA.d127.s301.e2",
"normalized": []
},
{
"id": "IEPA.d127.s302.i0",
"type": "PPI",
"arg1_id": "IEPA.d127.s302.e0",
"arg2_id": "IEPA.d127.s302.e1",
"normalized": []
},
{
"id": "IEPA.d127.s302.i1",
"type": "PPI",
"arg1_id": "IEPA.d127.s302.e0",
"arg2_id": "IEPA.d127.s302.e2",
"normalized": []
}
] |
IEPA.d128 | 10492523 | [
{
"id": "IEPA.d128.s303",
"type": "",
"text": [
"A neurotoxic fragment of amyloid, Abeta 25-35, incubated in the presence of endogenous Ca2+, increased significantly the PI-PLC activity of normoxic brain"
],
"offsets": [
[
0,
154
]
]
},
{
"id": "IEPA.d128.s304",
"type": "",
"text": [
"In its non-aggregated form, Abeta 25-35 activates PI-PLC but in the aggregated form the enzymatic activity decreased"
],
"offsets": [
[
155,
271
]
]
},
{
"id": "IEPA.d128.s305",
"type": "",
"text": [
"Thus, Abeta 25-35 exerts a similar effect on the membrane-bound PI-PLC from normoxic brain or subjected to ischemia reperfusion injury"
],
"offsets": [
[
272,
406
]
]
},
{
"id": "IEPA.d128.s306",
"type": "",
"text": [
"Ischemia-reperfusion injury had no effect on Abeta-evoked alterations of synaptic plasma membrane-bound PI-PLC"
],
"offsets": [
[
407,
517
]
]
}
] | [
{
"id": "IEPA.d128.s303.e0",
"type": "",
"text": [
"amyloid"
],
"offsets": [
[
25,
32
]
],
"normalized": []
},
{
"id": "IEPA.d128.s303.e1",
"type": "",
"text": [
"PI-PLC"
],
"offsets": [
[
121,
127
]
],
"normalized": []
},
{
"id": "IEPA.d128.s304.e0",
"type": "",
"text": [
"Abeta 25-35"
],
"offsets": [
[
183,
194
]
],
"normalized": []
},
{
"id": "IEPA.d128.s304.e1",
"type": "",
"text": [
"PI-PLC"
],
"offsets": [
[
205,
211
]
],
"normalized": []
},
{
"id": "IEPA.d128.s305.e0",
"type": "",
"text": [
"Abeta 25-35"
],
"offsets": [
[
278,
289
]
],
"normalized": []
},
{
"id": "IEPA.d128.s305.e1",
"type": "",
"text": [
"PI-PLC"
],
"offsets": [
[
336,
342
]
],
"normalized": []
},
{
"id": "IEPA.d128.s306.e0",
"type": "",
"text": [
"Abeta"
],
"offsets": [
[
452,
457
]
],
"normalized": []
},
{
"id": "IEPA.d128.s306.e1",
"type": "",
"text": [
"PI-PLC"
],
"offsets": [
[
511,
517
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d128.s303.i0",
"type": "PPI",
"arg1_id": "IEPA.d128.s303.e0",
"arg2_id": "IEPA.d128.s303.e1",
"normalized": []
},
{
"id": "IEPA.d128.s304.i0",
"type": "PPI",
"arg1_id": "IEPA.d128.s304.e0",
"arg2_id": "IEPA.d128.s304.e1",
"normalized": []
},
{
"id": "IEPA.d128.s305.i0",
"type": "PPI",
"arg1_id": "IEPA.d128.s305.e0",
"arg2_id": "IEPA.d128.s305.e1",
"normalized": []
},
{
"id": "IEPA.d128.s306.i0",
"type": "PPI",
"arg1_id": "IEPA.d128.s306.e0",
"arg2_id": "IEPA.d128.s306.e1",
"normalized": []
}
] |
IEPA.d129 | 10516126 | [
{
"id": "IEPA.d129.s307",
"type": "",
"text": [
"Sympathetic inhibition, leptin, and uncoupling protein subtype expression in normal fasting rats"
],
"offsets": [
[
0,
96
]
]
},
{
"id": "IEPA.d129.s308",
"type": "",
"text": [
"To further investigate neural effects on leptin and uncoupling proteins (UCPs), we studied in vivo perturbations intended to block adrenergic input to peripheral tissues"
],
"offsets": [
[
97,
266
]
]
},
{
"id": "IEPA.d129.s309",
"type": "",
"text": [
"We examined plasma leptin, leptin mRNA, and adipose and muscle UCP subtype mRNA in rats treated with alpha-methyl-p-tyrosine methyl ester (AMPT-ME), which inhibits catecholamine synthesis and 6-hydroxydopamine (6HDA), which is toxic to catecholinergic nerve terminals but, unlike AMPT-ME, does not enter the central nervous system"
],
"offsets": [
[
267,
597
]
]
},
{
"id": "IEPA.d129.s310",
"type": "",
"text": [
"Intraperitoneal 6HDA, 100 mg/kg, as a single dose at 1800, increased plasma leptin approximately twofold after 18-20 h, increased IBAT (but not epididymal fat) leptin mRNA by two- to threefold, and decreased IBAT UCP-3 mRNA to 30-40% of control"
],
"offsets": [
[
598,
842
]
]
},
{
"id": "IEPA.d129.s311",
"type": "",
"text": [
"However, the in vivo modulation of leptin and UCPs appears complex and, beyond a causal effect of SNA per se, may depend on concurrent changes in plasma insulin, glucose, and circulatory hemodynamics"
],
"offsets": [
[
843,
1042
]
]
}
] | [
{
"id": "IEPA.d129.s307.e0",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
24,
30
]
],
"normalized": []
},
{
"id": "IEPA.d129.s307.e1",
"type": "",
"text": [
"uncoupling protein"
],
"offsets": [
[
36,
54
]
],
"normalized": []
},
{
"id": "IEPA.d129.s308.e0",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
138,
144
]
],
"normalized": []
},
{
"id": "IEPA.d129.s308.e1",
"type": "",
"text": [
"uncoupling proteins"
],
"offsets": [
[
149,
168
]
],
"normalized": []
},
{
"id": "IEPA.d129.s309.e0",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
294,
300
]
],
"normalized": []
},
{
"id": "IEPA.d129.s309.e1",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
286,
292
]
],
"normalized": []
},
{
"id": "IEPA.d129.s309.e2",
"type": "",
"text": [
"UCP"
],
"offsets": [
[
330,
333
]
],
"normalized": []
},
{
"id": "IEPA.d129.s310.e0",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
674,
680
]
],
"normalized": []
},
{
"id": "IEPA.d129.s310.e1",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
758,
764
]
],
"normalized": []
},
{
"id": "IEPA.d129.s310.e2",
"type": "",
"text": [
"UCP-3"
],
"offsets": [
[
811,
816
]
],
"normalized": []
},
{
"id": "IEPA.d129.s311.e0",
"type": "",
"text": [
"leptin"
],
"offsets": [
[
878,
884
]
],
"normalized": []
},
{
"id": "IEPA.d129.s311.e1",
"type": "",
"text": [
"UCPs"
],
"offsets": [
[
889,
893
]
],
"normalized": []
}
] | [] | [] | [] |
IEPA.d130 | 10527454 | [
{
"id": "IEPA.d130.s312",
"type": "",
"text": [
"Amyloid beta peptide 25-35 modulates hydrolysis of phosphoinositides by membrane phospholipase(s) C of adult brain cortex"
],
"offsets": [
[
0,
121
]
]
},
{
"id": "IEPA.d130.s313",
"type": "",
"text": [
"Fresh-water-soluble A beta 25-35 activated PI-PLC in SPM markedly by two- to threefold, but this effect was absent in the presence of 2 mM CaCl2"
],
"offsets": [
[
122,
266
]
]
},
{
"id": "IEPA.d130.s314",
"type": "",
"text": [
"Moreover, A beta 25-35 had no effect on basal PIP2-PLC activity and cytosolic PI-PLC and PIP2-PLC"
],
"offsets": [
[
267,
364
]
]
},
{
"id": "IEPA.d130.s315",
"type": "",
"text": [
"The aggregated form of A beta 25-35 significantly inhibited PIP2-PLC only in the presence of endogenous CaCl2"
],
"offsets": [
[
365,
474
]
]
}
] | [
{
"id": "IEPA.d130.s312.e0",
"type": "",
"text": [
"Amyloid"
],
"offsets": [
[
0,
7
]
],
"normalized": []
},
{
"id": "IEPA.d130.s312.e1",
"type": "",
"text": [
"phospholipase(s) C"
],
"offsets": [
[
81,
99
]
],
"normalized": []
},
{
"id": "IEPA.d130.s313.e0",
"type": "",
"text": [
"A beta"
],
"offsets": [
[
142,
148
]
],
"normalized": []
},
{
"id": "IEPA.d130.s313.e1",
"type": "",
"text": [
"PI-PLC"
],
"offsets": [
[
165,
171
]
],
"normalized": []
},
{
"id": "IEPA.d130.s314.e0",
"type": "",
"text": [
"A beta"
],
"offsets": [
[
277,
283
]
],
"normalized": []
},
{
"id": "IEPA.d130.s314.e1",
"type": "",
"text": [
"PIP2-PLC"
],
"offsets": [
[
313,
321
]
],
"normalized": []
},
{
"id": "IEPA.d130.s314.e2",
"type": "",
"text": [
"PI-PLC"
],
"offsets": [
[
345,
351
]
],
"normalized": []
},
{
"id": "IEPA.d130.s314.e3",
"type": "",
"text": [
"PIP2-PLC"
],
"offsets": [
[
356,
364
]
],
"normalized": []
},
{
"id": "IEPA.d130.s315.e0",
"type": "",
"text": [
"A beta"
],
"offsets": [
[
388,
394
]
],
"normalized": []
},
{
"id": "IEPA.d130.s315.e1",
"type": "",
"text": [
"PIP2-PLC"
],
"offsets": [
[
425,
433
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d130.s312.i0",
"type": "PPI",
"arg1_id": "IEPA.d130.s312.e0",
"arg2_id": "IEPA.d130.s312.e1",
"normalized": []
},
{
"id": "IEPA.d130.s313.i0",
"type": "PPI",
"arg1_id": "IEPA.d130.s313.e0",
"arg2_id": "IEPA.d130.s313.e1",
"normalized": []
},
{
"id": "IEPA.d130.s315.i0",
"type": "PPI",
"arg1_id": "IEPA.d130.s315.e0",
"arg2_id": "IEPA.d130.s315.e1",
"normalized": []
}
] |
IEPA.d131 | 10562440 | [
{
"id": "IEPA.d131.s316",
"type": "",
"text": [
"Vasopressin stimulates tyrosine phosphorylation by activation of PKC in the rat smooth muscle cell line, A-10"
],
"offsets": [
[
0,
109
]
]
},
{
"id": "IEPA.d131.s317",
"type": "",
"text": [
"The protein kinase C (PKC) inhibitors: staurosporine, H7 and GF109203X are able to block the AVP-stimulated phosphorylation"
],
"offsets": [
[
110,
233
]
]
},
{
"id": "IEPA.d131.s318",
"type": "",
"text": [
"These results indicate that PKC is upstream of the phosphorylation, a motion which is supported by the fact that the AVP-stimulated phosphorylation was downregulated by phorbol esters"
],
"offsets": [
[
234,
417
]
]
}
] | [
{
"id": "IEPA.d131.s316.e0",
"type": "",
"text": [
"Vasopressin"
],
"offsets": [
[
0,
11
]
],
"normalized": []
},
{
"id": "IEPA.d131.s316.e1",
"type": "",
"text": [
"PKC"
],
"offsets": [
[
65,
68
]
],
"normalized": []
},
{
"id": "IEPA.d131.s317.e0",
"type": "",
"text": [
"protein kinase C"
],
"offsets": [
[
114,
130
]
],
"normalized": []
},
{
"id": "IEPA.d131.s317.e1",
"type": "",
"text": [
"AVP"
],
"offsets": [
[
203,
206
]
],
"normalized": []
},
{
"id": "IEPA.d131.s318.e0",
"type": "",
"text": [
"PKC"
],
"offsets": [
[
262,
265
]
],
"normalized": []
},
{
"id": "IEPA.d131.s318.e1",
"type": "",
"text": [
"AVP"
],
"offsets": [
[
351,
354
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "IEPA.d131.s316.i0",
"type": "PPI",
"arg1_id": "IEPA.d131.s316.e0",
"arg2_id": "IEPA.d131.s316.e1",
"normalized": []
},
{
"id": "IEPA.d131.s317.i0",
"type": "PPI",
"arg1_id": "IEPA.d131.s317.e0",
"arg2_id": "IEPA.d131.s317.e1",
"normalized": []
},
{
"id": "IEPA.d131.s318.i0",
"type": "PPI",
"arg1_id": "IEPA.d131.s318.e0",
"arg2_id": "IEPA.d131.s318.e1",
"normalized": []
}
] |
End of preview. Expand
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Dataset Card for IEPA
The IEPA benchmark PPI corpus is designed for relation extraction. It was created from 303 PubMed abstracts, each of which contains a specific pair of co-occurring chemicals.
Citation Information
@ARTICLE{ding2001mining,
title = "Mining {MEDLINE}: abstracts, sentences, or phrases?",
author = "Ding, J and Berleant, D and Nettleton, D and Wurtele, E",
journal = "Pac Symp Biocomput",
pages = "326--337",
year = 2002,
address = "United States",
language = "en"
}
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