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500 | BioInfer.d397.s2 | [
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501 | BioInfer.d398.s0 | [
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502 | BioInfer.d398.s1 | [
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503 | BioInfer.d399.s0 | [
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"type": "Sentence",
"text": [
"Kinetic studies on the effect of yeast cofilin on yeast actin polymerization."
],
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0,
77
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504 | BioInfer.d399.s1 | [
{
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"type": "Sentence",
"text": [
"The results suggest some cooperativity with respect to cofilin binding to filamentous actin which may be pH dependent."
],
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0,
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505 | BioInfer.d400.s0 | [
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"text": [
"Lack of detection in these preparations of a constituent that binds RBC alpha-spectrin antibody plus the presence of significant quantities of actin, further suggests that the principal membrane skeletal element is actin with perhaps smaller quantities of a 240-kd component, identified by others as the protein talin."
],
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0,
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312,
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"text": [
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72,
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506 | BioInfer.d401.s0 | [
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"type": "Sentence",
"text": [
"Lethality of the srs2Delta rad54Delta and srs2Delta rdh54Delta double mutants can also be rescued by mutations in the DNA damage checkpoint functions RAD9, RAD17, RAD24, and MEC3, indicating that the srs2 rad54 and srs2 rdh54 mutant combinations lead to an intermediate that is sensed by these checkpoint functions."
],
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0,
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200,
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507 | BioInfer.d404.s0 | [
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508 | BioInfer.d405.s0 | [
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"LIM-kinase 1 (LIMK1) phosphorylates cofilin, an actin-depolymerizing factor, and regulates actin cytoskeletal reorganization."
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125
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509 | BioInfer.d406.s0 | [
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510 | BioInfer.d407.s0 | [
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0,
100
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511 | BioInfer.d407.s1 | [
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512 | BioInfer.d408.s0 | [
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513 | BioInfer.d409.s0 | [
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0,
177
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514 | BioInfer.d410.s0 | [
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"text": [
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0,
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34,
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515 | BioInfer.d410.s1 | [
{
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"type": "Sentence",
"text": [
"There was a trend towards an association between advanced tumour stage and loss of membranous expression of alpha-catenin or beta-catenin, although these associations were not statistically significant."
],
"offsets": [
[
0,
202
]
]
}
] | [
{
"id": "BioInfer.d410.s1.e0",
"type": "Gene/protein/RNA",
"text": [
"alpha-catenin"
],
"offsets": [
[
108,
121
]
],
"normalized": []
},
{
"id": "BioInfer.d410.s1.e1",
"type": "Gene/protein/RNA",
"text": [
"beta-catenin"
],
"offsets": [
[
125,
137
]
],
"normalized": []
}
] | [] | [] | [] |
516 | BioInfer.d411.s0 | [
{
"id": "BioInfer.d411.s0__text",
"type": "Sentence",
"text": [
"Mammalian homologues of two important yeast genes involved in DNA double-strand break repair and recombination, RAD51 and RAD54, have been isolated."
],
"offsets": [
[
0,
148
]
]
}
] | [
{
"id": "BioInfer.d411.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"RAD54"
],
"offsets": [
[
122,
127
]
],
"normalized": []
},
{
"id": "BioInfer.d411.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"RAD51"
],
"offsets": [
[
112,
117
]
],
"normalized": []
}
] | [] | [] | [] |
517 | BioInfer.d412.s0 | [
{
"id": "BioInfer.d412.s0__text",
"type": "Sentence",
"text": [
"Mammalian LIM-kinases (LIMKs) phosphorylate cofilin and induce actin cytoskeletal reorganization."
],
"offsets": [
[
0,
97
]
]
}
] | [
{
"id": "BioInfer.d412.s0.e0",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
63,
68
]
],
"normalized": []
},
{
"id": "BioInfer.d412.s0.e1",
"type": "Individual_protein",
"text": [
"LIMKs"
],
"offsets": [
[
23,
28
]
],
"normalized": []
},
{
"id": "BioInfer.d412.s0.e2",
"type": "Individual_protein",
"text": [
"LIM-kinases"
],
"offsets": [
[
10,
21
]
],
"normalized": []
},
{
"id": "BioInfer.d412.s0.e3",
"type": "Individual_protein",
"text": [
"cofilin"
],
"offsets": [
[
44,
51
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d412.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d412.s0.e0",
"arg2_id": "BioInfer.d412.s0.e1",
"normalized": []
},
{
"id": "BioInfer.d412.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d412.s0.e0",
"arg2_id": "BioInfer.d412.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d412.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d412.s0.e1",
"arg2_id": "BioInfer.d412.s0.e3",
"normalized": []
},
{
"id": "BioInfer.d412.s0.i3",
"type": "PPI",
"arg1_id": "BioInfer.d412.s0.e2",
"arg2_id": "BioInfer.d412.s0.e3",
"normalized": []
}
] |
518 | BioInfer.d413.s0 | [
{
"id": "BioInfer.d413.s0__text",
"type": "Sentence",
"text": [
"MATERIALS AND METHODS: A mutation in the myosin heavy chain (Myh) predicted to interfere strongly with myosin's binding to actin was designed and used to create an animal model for HCM."
],
"offsets": [
[
0,
185
]
]
}
] | [
{
"id": "BioInfer.d413.s0.e0",
"type": "Individual_protein",
"text": [
"myosin"
],
"offsets": [
[
103,
109
]
],
"normalized": []
},
{
"id": "BioInfer.d413.s0.e1",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
123,
128
]
],
"normalized": []
},
{
"id": "BioInfer.d413.s0.e2",
"type": "Individual_protein",
"text": [
"myosin heavy chain"
],
"offsets": [
[
41,
59
]
],
"normalized": []
},
{
"id": "BioInfer.d413.s0.e3",
"type": "Individual_protein",
"text": [
"Myh"
],
"offsets": [
[
61,
64
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d413.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d413.s0.e0",
"arg2_id": "BioInfer.d413.s0.e1",
"normalized": []
},
{
"id": "BioInfer.d413.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d413.s0.e0",
"arg2_id": "BioInfer.d413.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d413.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d413.s0.e0",
"arg2_id": "BioInfer.d413.s0.e3",
"normalized": []
},
{
"id": "BioInfer.d413.s0.i3",
"type": "PPI",
"arg1_id": "BioInfer.d413.s0.e1",
"arg2_id": "BioInfer.d413.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d413.s0.i4",
"type": "PPI",
"arg1_id": "BioInfer.d413.s0.e1",
"arg2_id": "BioInfer.d413.s0.e3",
"normalized": []
}
] |
519 | BioInfer.d416.s0 | [
{
"id": "BioInfer.d416.s0__text",
"type": "Sentence",
"text": [
"Mechanism of inhibition of proliferating cell nuclear antigen-dependent DNA synthesis by the cyclin-dependent kinase inhibitor p21."
],
"offsets": [
[
0,
131
]
]
}
] | [
{
"id": "BioInfer.d416.s0.e0",
"type": "Individual_protein",
"text": [
"proliferating cell nuclear antigen"
],
"offsets": [
[
27,
61
]
],
"normalized": []
},
{
"id": "BioInfer.d416.s0.e1",
"type": "Individual_protein",
"text": [
"p21"
],
"offsets": [
[
127,
130
]
],
"normalized": []
},
{
"id": "BioInfer.d416.s0.e2",
"type": "Protein_family_or_group",
"text": [
"cyclin-dependent kinase inhibitor"
],
"offsets": [
[
93,
126
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d416.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d416.s0.e1",
"arg2_id": "BioInfer.d416.s0.e2",
"normalized": []
}
] |
520 | BioInfer.d417.s0 | [
{
"id": "BioInfer.d417.s0__text",
"type": "Sentence",
"text": [
"Mechanism of regulation of actin polymerization by Physarum profilin."
],
"offsets": [
[
0,
69
]
]
}
] | [
{
"id": "BioInfer.d417.s0.e0",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
60,
68
]
],
"normalized": []
},
{
"id": "BioInfer.d417.s0.e1",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
27,
32
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d417.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d417.s0.e0",
"arg2_id": "BioInfer.d417.s0.e1",
"normalized": []
}
] |
521 | BioInfer.d417.s1 | [
{
"id": "BioInfer.d417.s1__text",
"type": "Sentence",
"text": [
"The apparent critical concentration for polymerization of actin is increased by the addition of profilin."
],
"offsets": [
[
0,
105
]
]
}
] | [
{
"id": "BioInfer.d417.s1.e0",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
58,
63
]
],
"normalized": []
},
{
"id": "BioInfer.d417.s1.e1",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
96,
104
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d417.s1.i0",
"type": "PPI",
"arg1_id": "BioInfer.d417.s1.e0",
"arg2_id": "BioInfer.d417.s1.e1",
"normalized": []
}
] |
522 | BioInfer.d418.s0 | [
{
"id": "BioInfer.d418.s0__text",
"type": "Sentence",
"text": [
"Membranous staining and concomitant cytoplasmic localization of E-cadherin, alpha-catenin and gamma-catenin were seen in one case with abnormal beta-catenin immunoreactivity."
],
"offsets": [
[
0,
174
]
]
}
] | [
{
"id": "BioInfer.d418.s0.e0",
"type": "Individual_protein",
"text": [
"gamma-catenin"
],
"offsets": [
[
94,
107
]
],
"normalized": []
},
{
"id": "BioInfer.d418.s0.e1",
"type": "Individual_protein",
"text": [
"alpha-catenin"
],
"offsets": [
[
76,
89
]
],
"normalized": []
},
{
"id": "BioInfer.d418.s0.e2",
"type": "Individual_protein",
"text": [
"E-cadherin"
],
"offsets": [
[
64,
74
]
],
"normalized": []
},
{
"id": "BioInfer.d418.s0.e3",
"type": "Gene/protein/RNA",
"text": [
"beta-catenin"
],
"offsets": [
[
144,
156
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d418.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d418.s0.e0",
"arg2_id": "BioInfer.d418.s0.e1",
"normalized": []
},
{
"id": "BioInfer.d418.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d418.s0.e0",
"arg2_id": "BioInfer.d418.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d418.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d418.s0.e1",
"arg2_id": "BioInfer.d418.s0.e2",
"normalized": []
}
] |
523 | BioInfer.d420.s0 | [
{
"id": "BioInfer.d420.s0__text",
"type": "Sentence",
"text": [
"METHODS: Ileal and colonic biopsy specimens from 19 SpA patients with subclinical inflammatory gut lesions and from seven controls were stained with monoclonal antibodies against E-cadherin, beta-catenin and plakoglobin and a polyclonal antibody against alpha-catenin."
],
"offsets": [
[
0,
268
]
]
}
] | [
{
"id": "BioInfer.d420.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"beta-catenin"
],
"offsets": [
[
191,
203
]
],
"normalized": []
},
{
"id": "BioInfer.d420.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"alpha-catenin"
],
"offsets": [
[
254,
267
]
],
"normalized": []
},
{
"id": "BioInfer.d420.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"E-cadherin"
],
"offsets": [
[
179,
189
]
],
"normalized": []
},
{
"id": "BioInfer.d420.s0.e3",
"type": "Gene/protein/RNA",
"text": [
"plakoglobin"
],
"offsets": [
[
208,
219
]
],
"normalized": []
}
] | [] | [] | [] |
524 | BioInfer.d421.s0 | [
{
"id": "BioInfer.d421.s0__text",
"type": "Sentence",
"text": [
"METHODS: Paraffin-embedded sections of five AVMs, CCMs, and control brain tissues were stained immunohistochemically with antibodies to alpha-smooth muscle actin (alpha-SMA), myosin heavy chain, and smoothelin, a novel marker for contractile VSMC phenotype."
],
"offsets": [
[
0,
257
]
]
}
] | [
{
"id": "BioInfer.d421.s0.e0",
"type": "Individual_protein",
"text": [
"alpha-SMA"
],
"offsets": [
[
163,
172
]
],
"normalized": []
},
{
"id": "BioInfer.d421.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"myosin heavy chain"
],
"offsets": [
[
175,
193
]
],
"normalized": []
},
{
"id": "BioInfer.d421.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"smoothelin"
],
"offsets": [
[
199,
209
]
],
"normalized": []
},
{
"id": "BioInfer.d421.s0.e3",
"type": "Individual_protein",
"text": [
"alpha-smooth muscle actin"
],
"offsets": [
[
136,
161
]
],
"normalized": []
}
] | [] | [] | [] |
525 | BioInfer.d423.s0 | [
{
"id": "BioInfer.d423.s0__text",
"type": "Sentence",
"text": [
"METHODS: We have performed a detailed study of the pattern of expression of myosin heavy chain (MHC), myosin light chain (MLC), troponin I (TnI) isoforms, connexin 43 (Cx43), desmin and alpha-smooth muscle actin (alpha-SMA), in the ventricular conduction system of normal and congenitally malformed mouse hearts (iv background) from embryonic day 14.5 to 19.5."
],
"offsets": [
[
0,
360
]
]
}
] | [
{
"id": "BioInfer.d423.s0.e0",
"type": "Individual_protein",
"text": [
"MLC"
],
"offsets": [
[
122,
125
]
],
"normalized": []
},
{
"id": "BioInfer.d423.s0.e1",
"type": "Individual_protein",
"text": [
"alpha-SMA"
],
"offsets": [
[
213,
222
]
],
"normalized": []
},
{
"id": "BioInfer.d423.s0.e2",
"type": "Individual_protein",
"text": [
"Cx43"
],
"offsets": [
[
168,
172
]
],
"normalized": []
},
{
"id": "BioInfer.d423.s0.e3",
"type": "Individual_protein",
"text": [
"connexin 43"
],
"offsets": [
[
155,
166
]
],
"normalized": []
},
{
"id": "BioInfer.d423.s0.e4",
"type": "Individual_protein",
"text": [
"MHC"
],
"offsets": [
[
96,
99
]
],
"normalized": []
},
{
"id": "BioInfer.d423.s0.e5",
"type": "Individual_protein",
"text": [
"alpha-smooth muscle actin"
],
"offsets": [
[
186,
211
]
],
"normalized": []
},
{
"id": "BioInfer.d423.s0.e6",
"type": "Individual_protein",
"text": [
"TnI"
],
"offsets": [
[
140,
143
]
],
"normalized": []
},
{
"id": "BioInfer.d423.s0.e7",
"type": "Individual_protein",
"text": [
"myosin heavy chain"
],
"offsets": [
[
76,
94
]
],
"normalized": []
},
{
"id": "BioInfer.d423.s0.e8",
"type": "Individual_protein",
"text": [
"troponin I"
],
"offsets": [
[
128,
138
]
],
"normalized": []
},
{
"id": "BioInfer.d423.s0.e9",
"type": "Individual_protein",
"text": [
"myosin light chain"
],
"offsets": [
[
102,
120
]
],
"normalized": []
},
{
"id": "BioInfer.d423.s0.e10",
"type": "Gene/protein/RNA",
"text": [
"desmin"
],
"offsets": [
[
175,
181
]
],
"normalized": []
}
] | [] | [] | [] |
526 | BioInfer.d425.s0 | [
{
"id": "BioInfer.d425.s0__text",
"type": "Sentence",
"text": [
"Microinjection or stable expression of V12Ras into keratinocytes promotes the loss of E-cadherin and alpha-catenin and relocalization of beta-catenin to the cytoplasm and nucleus."
],
"offsets": [
[
0,
179
]
]
}
] | [
{
"id": "BioInfer.d425.s0.e0",
"type": "Individual_protein",
"text": [
"beta-catenin"
],
"offsets": [
[
137,
149
]
],
"normalized": []
},
{
"id": "BioInfer.d425.s0.e1",
"type": "Individual_protein",
"text": [
"E-cadherin"
],
"offsets": [
[
86,
96
]
],
"normalized": []
},
{
"id": "BioInfer.d425.s0.e2",
"type": "Individual_protein",
"text": [
"alpha-catenin"
],
"offsets": [
[
101,
114
]
],
"normalized": []
},
{
"id": "BioInfer.d425.s0.e3",
"type": "Individual_protein",
"text": [
"V12Ras"
],
"offsets": [
[
39,
45
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d425.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d425.s0.e0",
"arg2_id": "BioInfer.d425.s0.e3",
"normalized": []
},
{
"id": "BioInfer.d425.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d425.s0.e1",
"arg2_id": "BioInfer.d425.s0.e3",
"normalized": []
},
{
"id": "BioInfer.d425.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d425.s0.e2",
"arg2_id": "BioInfer.d425.s0.e3",
"normalized": []
}
] |
527 | BioInfer.d427.s0 | [
{
"id": "BioInfer.d427.s0__text",
"type": "Sentence",
"text": [
"MLL is fused in-frame to a different exon of CBP in two patients producing chimeric proteins containing the AT-hooks, methyltransferase homology domain, and transcriptional repression domain of MLL fused to the CREB binding domain or to the bromodomain of CBP."
],
"offsets": [
[
0,
260
]
]
}
] | [
{
"id": "BioInfer.d427.s0.e0",
"type": "Gene",
"text": [
"MLL"
],
"offsets": [
[
0,
3
]
],
"normalized": []
},
{
"id": "BioInfer.d427.s0.e1",
"type": "Gene",
"text": [
"CBP"
],
"offsets": [
[
45,
48
]
],
"normalized": []
},
{
"id": "BioInfer.d427.s0.e2",
"type": "Individual_protein",
"text": [
"CBP"
],
"offsets": [
[
256,
259
]
],
"normalized": []
},
{
"id": "BioInfer.d427.s0.e3",
"type": "Individual_protein",
"text": [
"CREB"
],
"offsets": [
[
211,
215
]
],
"normalized": []
},
{
"id": "BioInfer.d427.s0.e4",
"type": "Individual_protein",
"text": [
"MLL"
],
"offsets": [
[
194,
197
]
],
"normalized": []
},
{
"id": "BioInfer.d427.s0.e5",
"type": "Individual_protein",
"text": [
"methyltransferase"
],
"offsets": [
[
118,
135
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d427.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d427.s0.e2",
"arg2_id": "BioInfer.d427.s0.e3",
"normalized": []
},
{
"id": "BioInfer.d427.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d427.s0.e4",
"arg2_id": "BioInfer.d427.s0.e5",
"normalized": []
}
] |
528 | BioInfer.d428.s0 | [
{
"id": "BioInfer.d428.s0__text",
"type": "Sentence",
"text": [
"Modifying preselected sites on proteins: the stretch of residues 633-642 of the myosin heavy chain is part of the actin-binding site."
],
"offsets": [
[
0,
133
]
]
}
] | [
{
"id": "BioInfer.d428.s0.e0",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
114,
119
]
],
"normalized": []
},
{
"id": "BioInfer.d428.s0.e1",
"type": "Individual_protein",
"text": [
"myosin heavy chain"
],
"offsets": [
[
80,
98
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d428.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d428.s0.e0",
"arg2_id": "BioInfer.d428.s0.e1",
"normalized": []
}
] |
529 | BioInfer.d429.s0 | [
{
"id": "BioInfer.d429.s0__text",
"type": "Sentence",
"text": [
"Molecular analysis of the cadherin-catenin complex elucidated the central role of beta-catenin in this adhesion complex, as it binds to the cytoplasmic domain of E-cadherin and to alpha-catenin."
],
"offsets": [
[
0,
194
]
]
}
] | [
{
"id": "BioInfer.d429.s0.e0",
"type": "Individual_protein",
"text": [
"beta-catenin"
],
"offsets": [
[
82,
94
]
],
"normalized": []
},
{
"id": "BioInfer.d429.s0.e1",
"type": "Individual_protein",
"text": [
"cadherin"
],
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[
26,
34
]
],
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},
{
"id": "BioInfer.d429.s0.e2",
"type": "Individual_protein",
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"catenin"
],
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35,
42
]
],
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},
{
"id": "BioInfer.d429.s0.e3",
"type": "Individual_protein",
"text": [
"alpha-catenin"
],
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180,
193
]
],
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},
{
"id": "BioInfer.d429.s0.e4",
"type": "Individual_protein",
"text": [
"E-cadherin"
],
"offsets": [
[
162,
172
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d429.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d429.s0.e0",
"arg2_id": "BioInfer.d429.s0.e1",
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},
{
"id": "BioInfer.d429.s0.i1",
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{
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{
"id": "BioInfer.d429.s0.i3",
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{
"id": "BioInfer.d429.s0.i4",
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"arg1_id": "BioInfer.d429.s0.e1",
"arg2_id": "BioInfer.d429.s0.e2",
"normalized": []
}
] |
530 | BioInfer.d429.s1 | [
{
"id": "BioInfer.d429.s1__text",
"type": "Sentence",
"text": [
"beta-Catenin may also function in signalling pathways, given its homology to the gene product of the Drosophila segment polarity gene armadillo, which is known to be involved in the wingless signalling cascade."
],
"offsets": [
[
0,
210
]
]
}
] | [
{
"id": "BioInfer.d429.s1.e0",
"type": "Gene",
"text": [
"armadillo"
],
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134,
143
]
],
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},
{
"id": "BioInfer.d429.s1.e1",
"type": "Individual_protein",
"text": [
"beta-Catenin"
],
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[
0,
12
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d429.s1.i0",
"type": "PPI",
"arg1_id": "BioInfer.d429.s1.e0",
"arg2_id": "BioInfer.d429.s1.e1",
"normalized": []
}
] |
531 | BioInfer.d430.s0 | [
{
"id": "BioInfer.d430.s0__text",
"type": "Sentence",
"text": [
"Molecular cloning and primary structure analysis demonstrated that alpha-catenin is homologous to vinculin and the beta-catenin is homologous to human plakoglobin and the Drosophila gene product armadillo."
],
"offsets": [
[
0,
205
]
]
}
] | [
{
"id": "BioInfer.d430.s0.e0",
"type": "Individual_protein",
"text": [
"plakoglobin"
],
"offsets": [
[
151,
162
]
],
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},
{
"id": "BioInfer.d430.s0.e1",
"type": "Individual_protein",
"text": [
"armadillo"
],
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195,
204
]
],
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},
{
"id": "BioInfer.d430.s0.e2",
"type": "Individual_protein",
"text": [
"vinculin"
],
"offsets": [
[
98,
106
]
],
"normalized": []
},
{
"id": "BioInfer.d430.s0.e3",
"type": "Individual_protein",
"text": [
"beta-catenin"
],
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[
115,
127
]
],
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},
{
"id": "BioInfer.d430.s0.e4",
"type": "Individual_protein",
"text": [
"alpha-catenin"
],
"offsets": [
[
67,
80
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d430.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d430.s0.e0",
"arg2_id": "BioInfer.d430.s0.e3",
"normalized": []
},
{
"id": "BioInfer.d430.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d430.s0.e1",
"arg2_id": "BioInfer.d430.s0.e3",
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},
{
"id": "BioInfer.d430.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d430.s0.e2",
"arg2_id": "BioInfer.d430.s0.e4",
"normalized": []
}
] |
532 | BioInfer.d430.s1 | [
{
"id": "BioInfer.d430.s1__text",
"type": "Sentence",
"text": [
"One complex is composed of E-cadherin, alpha- and beta-catenin, the other of E-cadherin, alpha-catenin and plakoglobin."
],
"offsets": [
[
0,
119
]
]
}
] | [
{
"id": "BioInfer.d430.s1.e0",
"type": "Individual_protein",
"text": [
"E-cadherin"
],
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[
77,
87
]
],
"normalized": []
},
{
"id": "BioInfer.d430.s1.e1",
"type": "Individual_protein",
"text": [
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],
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107,
118
]
],
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},
{
"id": "BioInfer.d430.s1.e2",
"type": "Individual_protein",
"text": [
"alpha-",
"catenin"
],
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39,
45
],
[
55,
62
]
],
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},
{
"id": "BioInfer.d430.s1.e3",
"type": "Individual_protein",
"text": [
"alpha-catenin"
],
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[
89,
102
]
],
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},
{
"id": "BioInfer.d430.s1.e4",
"type": "Individual_protein",
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"E-cadherin"
],
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27,
37
]
],
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},
{
"id": "BioInfer.d430.s1.e5",
"type": "Individual_protein",
"text": [
"beta-catenin"
],
"offsets": [
[
50,
62
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d430.s1.i0",
"type": "PPI",
"arg1_id": "BioInfer.d430.s1.e0",
"arg2_id": "BioInfer.d430.s1.e1",
"normalized": []
},
{
"id": "BioInfer.d430.s1.i1",
"type": "PPI",
"arg1_id": "BioInfer.d430.s1.e0",
"arg2_id": "BioInfer.d430.s1.e3",
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},
{
"id": "BioInfer.d430.s1.i2",
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},
{
"id": "BioInfer.d430.s1.i3",
"type": "PPI",
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"arg2_id": "BioInfer.d430.s1.e4",
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},
{
"id": "BioInfer.d430.s1.i4",
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"arg2_id": "BioInfer.d430.s1.e5",
"normalized": []
},
{
"id": "BioInfer.d430.s1.i5",
"type": "PPI",
"arg1_id": "BioInfer.d430.s1.e4",
"arg2_id": "BioInfer.d430.s1.e5",
"normalized": []
}
] |
533 | BioInfer.d431.s0 | [
{
"id": "BioInfer.d431.s0__text",
"type": "Sentence",
"text": [
"[Molecular functions of cofilin which regulates reorganization of actin cytoskeleton]."
],
"offsets": [
[
0,
86
]
]
}
] | [
{
"id": "BioInfer.d431.s0.e0",
"type": "Individual_protein",
"text": [
"actin"
],
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[
66,
71
]
],
"normalized": []
},
{
"id": "BioInfer.d431.s0.e1",
"type": "Individual_protein",
"text": [
"cofilin"
],
"offsets": [
[
24,
31
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d431.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d431.s0.e0",
"arg2_id": "BioInfer.d431.s0.e1",
"normalized": []
}
] |
534 | BioInfer.d432.s0 | [
{
"id": "BioInfer.d432.s0__text",
"type": "Sentence",
"text": [
"Molecules known to link actin filaments to membrane were also examined, including alpha-catenin, beta-catenin, plakoglobin, and zyxin, but none was identified at the host-parasite junction."
],
"offsets": [
[
0,
189
]
]
}
] | [
{
"id": "BioInfer.d432.s0.e0",
"type": "Individual_protein",
"text": [
"beta-catenin"
],
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97,
109
]
],
"normalized": []
},
{
"id": "BioInfer.d432.s0.e1",
"type": "Individual_protein",
"text": [
"plakoglobin"
],
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[
111,
122
]
],
"normalized": []
},
{
"id": "BioInfer.d432.s0.e2",
"type": "Individual_protein",
"text": [
"zyxin"
],
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[
128,
133
]
],
"normalized": []
},
{
"id": "BioInfer.d432.s0.e3",
"type": "Individual_protein",
"text": [
"actin"
],
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[
24,
29
]
],
"normalized": []
},
{
"id": "BioInfer.d432.s0.e4",
"type": "Individual_protein",
"text": [
"alpha-catenin"
],
"offsets": [
[
82,
95
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d432.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d432.s0.e0",
"arg2_id": "BioInfer.d432.s0.e3",
"normalized": []
},
{
"id": "BioInfer.d432.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d432.s0.e1",
"arg2_id": "BioInfer.d432.s0.e3",
"normalized": []
},
{
"id": "BioInfer.d432.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d432.s0.e2",
"arg2_id": "BioInfer.d432.s0.e3",
"normalized": []
},
{
"id": "BioInfer.d432.s0.i3",
"type": "PPI",
"arg1_id": "BioInfer.d432.s0.e3",
"arg2_id": "BioInfer.d432.s0.e4",
"normalized": []
}
] |
535 | BioInfer.d432.s1 | [
{
"id": "BioInfer.d432.s1__text",
"type": "Sentence",
"text": [
"Other actin-associated proteins, including vinculin, talin, and ezrin, are not present."
],
"offsets": [
[
0,
87
]
]
}
] | [
{
"id": "BioInfer.d432.s1.e0",
"type": "Individual_protein",
"text": [
"vinculin"
],
"offsets": [
[
43,
51
]
],
"normalized": []
},
{
"id": "BioInfer.d432.s1.e1",
"type": "Individual_protein",
"text": [
"actin"
],
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[
6,
11
]
],
"normalized": []
},
{
"id": "BioInfer.d432.s1.e2",
"type": "Individual_protein",
"text": [
"ezrin"
],
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[
64,
69
]
],
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},
{
"id": "BioInfer.d432.s1.e3",
"type": "Individual_protein",
"text": [
"talin"
],
"offsets": [
[
53,
58
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d432.s1.i0",
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"arg1_id": "BioInfer.d432.s1.e0",
"arg2_id": "BioInfer.d432.s1.e1",
"normalized": []
},
{
"id": "BioInfer.d432.s1.i1",
"type": "PPI",
"arg1_id": "BioInfer.d432.s1.e1",
"arg2_id": "BioInfer.d432.s1.e2",
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},
{
"id": "BioInfer.d432.s1.i2",
"type": "PPI",
"arg1_id": "BioInfer.d432.s1.e1",
"arg2_id": "BioInfer.d432.s1.e3",
"normalized": []
}
] |
536 | BioInfer.d433.s0 | [
{
"id": "BioInfer.d433.s0__text",
"type": "Sentence",
"text": [
"Monoclonal antibodies recognizing the N- and C-terminal regions of talin disrupt actin stress fibers when microinjected into human fibroblasts."
],
"offsets": [
[
0,
143
]
]
}
] | [
{
"id": "BioInfer.d433.s0.e0",
"type": "Individual_protein",
"text": [
"talin"
],
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67,
72
]
],
"normalized": []
},
{
"id": "BioInfer.d433.s0.e1",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
81,
86
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d433.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d433.s0.e0",
"arg2_id": "BioInfer.d433.s0.e1",
"normalized": []
}
] |
537 | BioInfer.d433.s1 | [
{
"id": "BioInfer.d433.s1__text",
"type": "Sentence",
"text": [
"These results show that the C-terminal actin-binding site is distinct from the region recognized by the anti-functional antibody TD77, raising the possibility that it binds to a novel functionally important ligand-binding site in the talin molecule."
],
"offsets": [
[
0,
249
]
]
}
] | [
{
"id": "BioInfer.d433.s1.e0",
"type": "Individual_protein",
"text": [
"talin"
],
"offsets": [
[
234,
239
]
],
"normalized": []
},
{
"id": "BioInfer.d433.s1.e1",
"type": "Individual_protein",
"text": [
"TD77"
],
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[
129,
133
]
],
"normalized": []
},
{
"id": "BioInfer.d433.s1.e2",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
39,
44
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d433.s1.i0",
"type": "PPI",
"arg1_id": "BioInfer.d433.s1.e0",
"arg2_id": "BioInfer.d433.s1.e1",
"normalized": []
},
{
"id": "BioInfer.d433.s1.i1",
"type": "PPI",
"arg1_id": "BioInfer.d433.s1.e0",
"arg2_id": "BioInfer.d433.s1.e2",
"normalized": []
}
] |
538 | BioInfer.d433.s2 | [
{
"id": "BioInfer.d433.s2__text",
"type": "Sentence",
"text": [
"To investigate the possibility that TD77 disrupts actin stress fibers by binding directly to the C-terminal actin binding site, additional talin fusion proteins were generated and analyzed for TD77 and actin binding."
],
"offsets": [
[
0,
216
]
]
}
] | [
{
"id": "BioInfer.d433.s2.e0",
"type": "Individual_protein",
"text": [
"talin"
],
"offsets": [
[
139,
144
]
],
"normalized": []
},
{
"id": "BioInfer.d433.s2.e1",
"type": "Individual_protein",
"text": [
"TD77"
],
"offsets": [
[
36,
40
]
],
"normalized": []
},
{
"id": "BioInfer.d433.s2.e2",
"type": "Individual_protein",
"text": [
"actin"
],
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108,
113
]
],
"normalized": []
},
{
"id": "BioInfer.d433.s2.e3",
"type": "Individual_protein",
"text": [
"actin"
],
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[
202,
207
]
],
"normalized": []
},
{
"id": "BioInfer.d433.s2.e4",
"type": "Individual_protein",
"text": [
"TD77"
],
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[
193,
197
]
],
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},
{
"id": "BioInfer.d433.s2.e5",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
50,
55
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d433.s2.i0",
"type": "PPI",
"arg1_id": "BioInfer.d433.s2.e0",
"arg2_id": "BioInfer.d433.s2.e1",
"normalized": []
},
{
"id": "BioInfer.d433.s2.i1",
"type": "PPI",
"arg1_id": "BioInfer.d433.s2.e0",
"arg2_id": "BioInfer.d433.s2.e2",
"normalized": []
},
{
"id": "BioInfer.d433.s2.i2",
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"arg2_id": "BioInfer.d433.s2.e3",
"normalized": []
},
{
"id": "BioInfer.d433.s2.i3",
"type": "PPI",
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},
{
"id": "BioInfer.d433.s2.i4",
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},
{
"id": "BioInfer.d433.s2.i5",
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"arg1_id": "BioInfer.d433.s2.e1",
"arg2_id": "BioInfer.d433.s2.e5",
"normalized": []
}
] |
539 | BioInfer.d434.s0 | [
{
"id": "BioInfer.d434.s0__text",
"type": "Sentence",
"text": [
"Monocytes and in vitro differentiated U937 cells induce focal loss in the staining of VE-cadherin, alpha-catenin, beta-catenin, and plakoglobin during transendothelial migration under physiological flow conditions."
],
"offsets": [
[
0,
214
]
]
}
] | [
{
"id": "BioInfer.d434.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"plakoglobin"
],
"offsets": [
[
132,
143
]
],
"normalized": []
},
{
"id": "BioInfer.d434.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"alpha-catenin"
],
"offsets": [
[
99,
112
]
],
"normalized": []
},
{
"id": "BioInfer.d434.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"beta-catenin"
],
"offsets": [
[
114,
126
]
],
"normalized": []
},
{
"id": "BioInfer.d434.s0.e3",
"type": "Gene/protein/RNA",
"text": [
"VE-cadherin"
],
"offsets": [
[
86,
97
]
],
"normalized": []
}
] | [] | [] | [] |
540 | BioInfer.d435.s0 | [
{
"id": "BioInfer.d435.s0__text",
"type": "Sentence",
"text": [
"Moreover, talin, but not vinculin or tubulin, appears to co-localize with actin microfilaments in the membrane ruffles of NK cells that undergo cytoskeleton rearrangement following CD31 cross-linking."
],
"offsets": [
[
0,
200
]
]
}
] | [
{
"id": "BioInfer.d435.s0.e0",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
74,
79
]
],
"normalized": []
},
{
"id": "BioInfer.d435.s0.e1",
"type": "Individual_protein",
"text": [
"vinculin"
],
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[
25,
33
]
],
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},
{
"id": "BioInfer.d435.s0.e2",
"type": "Individual_protein",
"text": [
"tubulin"
],
"offsets": [
[
37,
44
]
],
"normalized": []
},
{
"id": "BioInfer.d435.s0.e3",
"type": "Individual_protein",
"text": [
"talin"
],
"offsets": [
[
10,
15
]
],
"normalized": []
},
{
"id": "BioInfer.d435.s0.e4",
"type": "Gene/protein/RNA",
"text": [
"CD31"
],
"offsets": [
[
181,
185
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541 | BioInfer.d437.s0 | [
{
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],
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157
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101
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],
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29,
36
]
],
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] | [] | [] | [] |
542 | BioInfer.d437.s1 | [
{
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"type": "Sentence",
"text": [
"pH control of actin polymerization by cofilin."
],
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0,
46
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] | [
{
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38,
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14,
19
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] |
543 | BioInfer.d438.s0 | [
{
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"type": "Sentence",
"text": [
"Moreover, the virus-encoded profilin homolog was not required for actin-associated events, including intracellular virus movement to the periphery of the cell, formation of specialized microvilli, or release of mature virions, as shown by electron microscopy and yields of infectious intra- and extracellular virus."
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0,
315
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]
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] | [
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28,
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66,
71
]
],
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}
] | [] | [] | [] |
544 | BioInfer.d440.s0 | [
{
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"type": "Sentence",
"text": [
"Most previous studies have focused on profilin itself rather than its complex with actin."
],
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0,
89
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]
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] | [
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83,
88
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"arg2_id": "BioInfer.d440.s0.e1",
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] |
545 | BioInfer.d441.s0 | [
{
"id": "BioInfer.d441.s0__text",
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"text": [
"Motile areas of leech neurites are rich in microfilaments and two actin-binding proteins: gelsolin and profilin."
],
"offsets": [
[
0,
112
]
]
}
] | [
{
"id": "BioInfer.d441.s0.e0",
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],
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90,
98
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],
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{
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66,
88
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],
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] | [] | [] | [
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] |
546 | BioInfer.d441.s1 | [
{
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"type": "Sentence",
"text": [
"The colocalization of gelsolin and profilin in motile, microfilament-rich areas supports the hypothesis that they synergistically regulate the actin dynamics that underlie neurite growth."
],
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[
0,
187
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]
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] | [
{
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35,
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143,
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22,
30
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],
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"arg2_id": "BioInfer.d441.s1.e2",
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}
] |
547 | BioInfer.d442.s0 | [
{
"id": "BioInfer.d442.s0__text",
"type": "Sentence",
"text": [
"Mutants of cdc3 and cdc8, which encode profilin and tropomyosin respectively, display disorganized actin patches in all cells."
],
"offsets": [
[
0,
126
]
]
}
] | [
{
"id": "BioInfer.d442.s0.e0",
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],
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52,
63
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],
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20,
24
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99,
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"arg2_id": "BioInfer.d442.s0.e2",
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}
] |
548 | BioInfer.d443.s0 | [
{
"id": "BioInfer.d443.s0__text",
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"text": [
"Mutations in BUD3, BUD4, and AXL1 cause a and alpha cells to exhibit the bipolar pattern, indicating that these genes are necessary to specify the axial budding pattern (Chant, J., and I. Herskowitz. 1991. Cell. 65:1203-1212; Fujita, A., C. Oka, Y. Arikawa, T. Katagi, A. Tonouchi, S. Kuhara, and Y. Misumi. 1994. Nature (Lond.). 372:567-570)."
],
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[
0,
343
]
]
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] | [
{
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19,
23
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],
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[
13,
17
]
],
"normalized": []
}
] | [] | [] | [] |
549 | BioInfer.d444.s0 | [
{
"id": "BioInfer.d444.s0__text",
"type": "Sentence",
"text": [
"Mutations in RVS161 and RVS167, the two yeast amphiphysin homologs, cause very similar growth phenotypes, a depolarized actin cytoskeleton, and a defect in the internalization step of endocytosis."
],
"offsets": [
[
0,
196
]
]
}
] | [
{
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24,
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13,
19
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] | [] | [] | [
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}
] |
550 | BioInfer.d446.s0 | [
{
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"Mutations in Saccharomyces cerevisiae RFC5, DPB11, MEC1, DDC2 MEC3, RAD53, CHK1, PDS1, and DUN1 increased the rate of genome rearrangements up to 200-fold whereas mutations in RAD9, RAD17, RAD24, BUB3, and MAD3 had little effect."
],
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0,
229
]
]
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] | [
{
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57,
61
]
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189,
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{
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91,
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176,
180
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{
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81,
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182,
187
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68,
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]
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{
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44,
49
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51,
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{
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62,
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{
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196,
200
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{
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[
206,
210
]
],
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}
] | [] | [] | [] |
551 | BioInfer.d447.s0 | [
{
"id": "BioInfer.d447.s0__text",
"type": "Sentence",
"text": [
"Mutations that alter putative RNA-binding residues of either HSH49 RRM are lethal in vivo, but do not prevent binding to CUS1 in vitro, suggesting that the predicted RNA-binding surfaces of HSH49 are not required for interaction with CUS1."
],
"offsets": [
[
0,
239
]
]
}
] | [
{
"id": "BioInfer.d447.s0.e0",
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234,
238
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61,
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}
] |
552 | BioInfer.d447.s1 | [
{
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"type": "Sentence",
"text": [
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],
"offsets": [
[
0,
88
]
]
}
] | [
{
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12,
17
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] | [] | [] | [
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] |
553 | BioInfer.d448.s0 | [
{
"id": "BioInfer.d448.s0__text",
"type": "Sentence",
"text": [
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],
"offsets": [
[
0,
165
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]
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] | [
{
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164
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0,
5
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{
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],
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85,
111
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],
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] | [] | [] | [
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] |
554 | BioInfer.d449.s0 | [
{
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"type": "Sentence",
"text": [
"Myogenin mRNAs were transiently expressed in forming myotubes."
],
"offsets": [
[
0,
62
]
]
}
] | [
{
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0,
8
]
],
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] | [] | [] | [] |
555 | BioInfer.d449.s1 | [
{
"id": "BioInfer.d449.s1__text",
"type": "Sentence",
"text": [
"alpha-Skeletal actin and fast myosin heavy chain mRNAs were detected precociously, before the young myotube stage."
],
"offsets": [
[
0,
114
]
]
}
] | [
{
"id": "BioInfer.d449.s1.e0",
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25,
48
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] | [] | [] | [] |
556 | BioInfer.d450.s0 | [
{
"id": "BioInfer.d450.s0__text",
"type": "Sentence",
"text": [
"Neither can profilin I, in the presence of the peptide, promote actin polymerization during its early phase consistent with a lower affinity."
],
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[
0,
141
]
]
}
] | [
{
"id": "BioInfer.d450.s0.e0",
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"profilin I"
],
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[
12,
22
]
],
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},
{
"id": "BioInfer.d450.s0.e1",
"type": "Individual_protein",
"text": [
"actin"
],
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[
64,
69
]
],
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}
] | [] | [] | [
{
"id": "BioInfer.d450.s0.i0",
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] |
557 | BioInfer.d450.s1 | [
{
"id": "BioInfer.d450.s1__text",
"type": "Sentence",
"text": [
"The resulting profilin II-peptide complex overcomes the combined capacity of thymosin beta4 and profilin II to inhibit actin nucleation and restores the extent of filament formation."
],
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[
0,
182
]
]
}
] | [
{
"id": "BioInfer.d450.s1.e0",
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"actin"
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119,
124
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{
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96,
107
]
],
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},
{
"id": "BioInfer.d450.s1.e2",
"type": "Individual_protein",
"text": [
"thymosin beta4"
],
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77,
91
]
],
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},
{
"id": "BioInfer.d450.s1.e3",
"type": "Individual_protein",
"text": [
"profilin II"
],
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[
14,
25
]
],
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}
] | [] | [] | [
{
"id": "BioInfer.d450.s1.i0",
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{
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"arg1_id": "BioInfer.d450.s1.e0",
"arg2_id": "BioInfer.d450.s1.e3",
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}
] |
558 | BioInfer.d451.s0 | [
{
"id": "BioInfer.d451.s0__text",
"type": "Sentence",
"text": [
"Newly disclosed interactions between gephyrin, exchange factors for G proteins of the Rho and Rac families, the translational regulator RAFT1, and actin-binding proteins like profilin might integrate activity-dependent and trophic-factor-mediated signals at developing postsynaptic sites."
],
"offsets": [
[
0,
288
]
]
}
] | [
{
"id": "BioInfer.d451.s0.e0",
"type": "Individual_protein",
"text": [
"Rho"
],
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86,
89
]
],
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},
{
"id": "BioInfer.d451.s0.e1",
"type": "Individual_protein",
"text": [
"G proteins"
],
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68,
78
]
],
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},
{
"id": "BioInfer.d451.s0.e2",
"type": "Individual_protein",
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68,
78
]
],
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},
{
"id": "BioInfer.d451.s0.e3",
"type": "Individual_protein",
"text": [
"RAFT1"
],
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136,
141
]
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},
{
"id": "BioInfer.d451.s0.e4",
"type": "Individual_protein",
"text": [
"profilin"
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[
175,
183
]
],
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},
{
"id": "BioInfer.d451.s0.e5",
"type": "Protein_family_or_group",
"text": [
"actin-binding proteins"
],
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[
147,
169
]
],
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},
{
"id": "BioInfer.d451.s0.e6",
"type": "Individual_protein",
"text": [
"gephyrin"
],
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[
37,
45
]
],
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},
{
"id": "BioInfer.d451.s0.e7",
"type": "Individual_protein",
"text": [
"Rac"
],
"offsets": [
[
94,
97
]
],
"normalized": []
}
] | [] | [] | [
{
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{
"id": "BioInfer.d451.s0.i6",
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{
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{
"id": "BioInfer.d451.s0.i8",
"type": "PPI",
"arg1_id": "BioInfer.d451.s0.e5",
"arg2_id": "BioInfer.d451.s0.e6",
"normalized": []
}
] |
559 | BioInfer.d452.s0 | [
{
"id": "BioInfer.d452.s0__text",
"type": "Sentence",
"text": [
"N-formyl peptide chemoattractants in neutrophils stimulate the formation of phosphatidylinositol-4,5-bisphosphate (PIP2), a reservoir for second messenger molecules and regulator of actin assembly through its association with the actin-binding proteins, profilin, and gelsolin."
],
"offsets": [
[
0,
277
]
]
}
] | [
{
"id": "BioInfer.d452.s0.e0",
"type": "Protein_family_or_group",
"text": [
"actin-binding proteins"
],
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[
230,
252
]
],
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},
{
"id": "BioInfer.d452.s0.e1",
"type": "Individual_protein",
"text": [
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],
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254,
262
]
],
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},
{
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"text": [
"actin"
],
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182,
187
]
],
"normalized": []
},
{
"id": "BioInfer.d452.s0.e3",
"type": "Individual_protein",
"text": [
"gelsolin"
],
"offsets": [
[
268,
276
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d452.s0.i0",
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{
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{
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"arg1_id": "BioInfer.d452.s0.e2",
"arg2_id": "BioInfer.d452.s0.e3",
"normalized": []
}
] |
560 | BioInfer.d453.s0 | [
{
"id": "BioInfer.d453.s0__text",
"type": "Sentence",
"text": [
"No evidence for the surface expression of the phosphoprotein (P), matrix (M) or nucleocapsid (N) proteins was found."
],
"offsets": [
[
0,
116
]
]
}
] | [
{
"id": "BioInfer.d453.s0.e0",
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"text": [
"P"
],
"offsets": [
[
62,
63
]
],
"normalized": []
},
{
"id": "BioInfer.d453.s0.e1",
"type": "Individual_protein",
"text": [
"N"
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94,
95
]
],
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},
{
"id": "BioInfer.d453.s0.e2",
"type": "Individual_protein",
"text": [
"nucleocapsid",
"proteins"
],
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[
80,
92
],
[
97,
105
]
],
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},
{
"id": "BioInfer.d453.s0.e3",
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"text": [
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"proteins"
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46,
60
],
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97,
105
]
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{
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74,
75
]
],
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{
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"proteins"
],
"offsets": [
[
66,
72
],
[
97,
105
]
],
"normalized": []
}
] | [] | [] | [] |
561 | BioInfer.d454.s0 | [
{
"id": "BioInfer.d454.s0__text",
"type": "Sentence",
"text": [
"No significant changes in glomerular vinculin, talin, beta 1-integrin, or total actin expression occurred at any time point during disease development."
],
"offsets": [
[
0,
151
]
]
}
] | [
{
"id": "BioInfer.d454.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"beta 1-integrin"
],
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[
54,
69
]
],
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},
{
"id": "BioInfer.d454.s0.e1",
"type": "Gene/protein/RNA",
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37,
45
]
],
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},
{
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80,
85
]
],
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},
{
"id": "BioInfer.d454.s0.e3",
"type": "Gene/protein/RNA",
"text": [
"talin"
],
"offsets": [
[
47,
52
]
],
"normalized": []
}
] | [] | [] | [] |
562 | BioInfer.d455.s0 | [
{
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"type": "Sentence",
"text": [
"Notably, the two pro-apoptotic adapter proteins TRADD and FADD are also involved in the activation of A-SMase."
],
"offsets": [
[
0,
110
]
]
}
] | [
{
"id": "BioInfer.d455.s0.e0",
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"text": [
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],
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[
58,
62
]
],
"normalized": []
},
{
"id": "BioInfer.d455.s0.e1",
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"text": [
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],
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48,
53
]
],
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},
{
"id": "BioInfer.d455.s0.e2",
"type": "Individual_protein",
"text": [
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],
"offsets": [
[
102,
109
]
],
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}
] | [] | [] | [
{
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}
] |
563 | BioInfer.d456.s0 | [
{
"id": "BioInfer.d456.s0__text",
"type": "Sentence",
"text": [
"OBJECTIVE: To determine whether other glycoprotein 130 (gp130) binding cytokines can mimic the effects of oncostatin M (OSM) in acting synergistically with interleukin-1alpha (IL-1alpha) to induce cartilage collagen breakdown and collagenase expression, and to determine which receptors mediate these effects."
],
"offsets": [
[
0,
309
]
]
}
] | [
{
"id": "BioInfer.d456.s0.e0",
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"text": [
"oncostatin M"
],
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[
106,
118
]
],
"normalized": []
},
{
"id": "BioInfer.d456.s0.e1",
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"text": [
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],
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[
230,
241
]
],
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},
{
"id": "BioInfer.d456.s0.e2",
"type": "Protein_family_or_group",
"text": [
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],
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71,
80
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},
{
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"text": [
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[
156,
174
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],
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{
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"text": [
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176,
185
]
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{
"id": "BioInfer.d456.s0.e5",
"type": "Individual_protein",
"text": [
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207,
215
]
],
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},
{
"id": "BioInfer.d456.s0.e6",
"type": "Individual_protein",
"text": [
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],
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38,
54
]
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{
"id": "BioInfer.d456.s0.e7",
"type": "Individual_protein",
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],
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120,
123
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{
"id": "BioInfer.d456.s0.e8",
"type": "Individual_protein",
"text": [
"gp130"
],
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56,
61
]
],
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}
] | [] | [] | [
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{
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{
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"normalized": []
}
] |
564 | BioInfer.d457.s0 | [
{
"id": "BioInfer.d457.s0__text",
"type": "Sentence",
"text": [
"Of the five major structural proteins of MV, only nucleocapsid (N) protein and phosphoprotein (P protein) were consistently detected in diseased brain areas."
],
"offsets": [
[
0,
157
]
]
}
] | [
{
"id": "BioInfer.d457.s0.e0",
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"protein"
],
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50,
62
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67,
74
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},
{
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64,
65
]
],
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},
{
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79,
93
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],
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},
{
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"text": [
"P protein"
],
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[
95,
104
]
],
"normalized": []
}
] | [] | [] | [] |
565 | BioInfer.d459.s0 | [
{
"id": "BioInfer.d459.s0__text",
"type": "Sentence",
"text": [
"Once the actin monomer is bound to the filament, the profilin is released, and is available to bind to additional actin monomers."
],
"offsets": [
[
0,
129
]
]
}
] | [
{
"id": "BioInfer.d459.s0.e0",
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"actin"
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114,
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53,
61
]
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"type": "Gene/protein/RNA",
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"actin"
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9,
14
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] | [] | [] | [
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] |
566 | BioInfer.d460.s0 | [
{
"id": "BioInfer.d460.s0__text",
"type": "Sentence",
"text": [
"One involves talin, which has recently been shown to bind actin directly."
],
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[
0,
73
]
]
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] | [
{
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13,
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] | [] | [] | [
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] |
567 | BioInfer.d461.s0 | [
{
"id": "BioInfer.d461.s0__text",
"type": "Sentence",
"text": [
"One, MORT1 (also called FADD), binds to Fas/APO1 but not to p55-R; another, TRADD, binds to the p55 TNF receptor but not to Fas/APO1; and the third, RIP, binds weakly to both receptors."
],
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185
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] | [
{
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132
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{
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96,
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] | [] | [] | [
{
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},
{
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{
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{
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"arg2_id": "BioInfer.d461.s0.e10",
"normalized": []
}
] |
568 | BioInfer.d463.s0 | [
{
"id": "BioInfer.d463.s0__text",
"type": "Sentence",
"text": [
"One such protein is the yeast actin-binding protein Sac6p, which is homologous to vertebrate fimbrin (Adams, A. E. M., D. Botstein, and D. G. Drubin. 1991. Nature (Lond.). 354:404-408.)."
],
"offsets": [
[
0,
186
]
]
}
] | [
{
"id": "BioInfer.d463.s0.e0",
"type": "Protein_family_or_group",
"text": [
"actin-binding protein"
],
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[
30,
51
]
],
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},
{
"id": "BioInfer.d463.s0.e1",
"type": "Individual_protein",
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52,
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]
],
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},
{
"id": "BioInfer.d463.s0.e2",
"type": "Individual_protein",
"text": [
"fimbrin"
],
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[
93,
100
]
],
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}
] | [] | [] | [
{
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}
] |
569 | BioInfer.d464.s0 | [
{
"id": "BioInfer.d464.s0__text",
"type": "Sentence",
"text": [
"Only the unphosphorylated form of cofilin is an active form that binds actin, whereas the regulatory mechanisms of cofilin have not been elucidated."
],
"offsets": [
[
0,
148
]
]
}
] | [
{
"id": "BioInfer.d464.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"cofilin"
],
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[
115,
122
]
],
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},
{
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71,
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]
],
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{
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"text": [
"cofilin"
],
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34,
41
]
],
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}
] | [] | [] | [
{
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}
] |
570 | BioInfer.d465.s0 | [
{
"id": "BioInfer.d465.s0__text",
"type": "Sentence",
"text": [
"On the basis of these results, we present a model for prereplicative site formation in infected cells in which the helicase-primase components (UL5, UL8, and UL52), the origin-binding protein (UL9), and the viral single-stranded DNA-binding protein (ICP8) assemble together to initiate the process."
],
"offsets": [
[
0,
298
]
]
}
] | [
{
"id": "BioInfer.d465.s0.e0",
"type": "Individual_protein",
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"UL52"
],
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[
158,
162
]
],
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},
{
"id": "BioInfer.d465.s0.e1",
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193,
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]
],
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},
{
"id": "BioInfer.d465.s0.e2",
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250,
254
]
],
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},
{
"id": "BioInfer.d465.s0.e3",
"type": "Protein_complex",
"text": [
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],
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115,
131
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],
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},
{
"id": "BioInfer.d465.s0.e4",
"type": "Individual_protein",
"text": [
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213,
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{
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144,
147
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{
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"type": "Individual_protein",
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149,
152
]
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{
"id": "BioInfer.d465.s0.e7",
"type": "Individual_protein",
"text": [
"origin-binding protein"
],
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169,
191
]
],
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}
] | [] | [] | [
{
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"arg2_id": "BioInfer.d465.s0.e7",
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}
] |
571 | BioInfer.d465.s1 | [
{
"id": "BioInfer.d465.s1__text",
"type": "Sentence",
"text": [
"We observed that four replication proteins, UL5, UL8 UL52, and UL9, are necessary for the localization of ICP8 (UL29) to prereplicative sites natural infection conditions."
],
"offsets": [
[
0,
171
]
]
}
] | [
{
"id": "BioInfer.d465.s1.e0",
"type": "Individual_protein",
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"ICP8"
],
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[
106,
110
]
],
"normalized": []
},
{
"id": "BioInfer.d465.s1.e1",
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"UL29"
],
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[
112,
116
]
],
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},
{
"id": "BioInfer.d465.s1.e2",
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],
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[
63,
66
]
],
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},
{
"id": "BioInfer.d465.s1.e3",
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"UL52"
],
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53,
57
]
],
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{
"id": "BioInfer.d465.s1.e4",
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49,
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],
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{
"id": "BioInfer.d465.s1.e5",
"type": "Individual_protein",
"text": [
"UL5"
],
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[
44,
47
]
],
"normalized": []
}
] | [] | [] | [
{
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}
] |
572 | BioInfer.d466.s0 | [
{
"id": "BioInfer.d466.s0__text",
"type": "Sentence",
"text": [
"On the internal (cytoplasmic) side of focal contacts, several proteins, including talin and vinculin, mediate interactions with the actin filament bundles of the cytoskeleton."
],
"offsets": [
[
0,
175
]
]
}
] | [
{
"id": "BioInfer.d466.s0.e0",
"type": "Individual_protein",
"text": [
"vinculin"
],
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[
92,
100
]
],
"normalized": []
},
{
"id": "BioInfer.d466.s0.e1",
"type": "Individual_protein",
"text": [
"talin"
],
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[
82,
87
]
],
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573 | BioInfer.d467.s0 | [
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574 | BioInfer.d468.s0 | [
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575 | BioInfer.d469.s0 | [
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576 | BioInfer.d470.s0 | [
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"p53-mediated cell injury exhibited proteolysis of the caspase protein substrate lamin B without appreciable breakdown of TnI."
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0,
125
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577 | BioInfer.d471.s0 | [
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"Other than monomeric actin, no major profilin ligands are detected in crude extracts."
],
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0,
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37,
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578 | BioInfer.d471.s1 | [
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0,
132
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] |
579 | BioInfer.d471.s2 | [
{
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"Selective monoclonal antibodies confirm that most of the profilin is bound to actin: 65% in extract immunoadsorption assays and 74-89% by fluorescent antibody staining."
],
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[
0,
168
]
]
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78,
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}
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580 | BioInfer.d471.s3 | [
{
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0,
221
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185,
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] |
581 | BioInfer.d473.s0 | [
{
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"text": [
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],
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0,
260
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]
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104,
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122,
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],
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}
] |
582 | BioInfer.d474.s0 | [
{
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[
0,
148
]
]
}
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143,
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}
] |
583 | BioInfer.d479.s0 | [
{
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"text": [
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0,
153
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]
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147,
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13,
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111,
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{
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"text": [
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],
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[
22,
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]
],
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}
] | [] | [] | [
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}
] |
584 | BioInfer.d480.s0 | [
{
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"type": "Sentence",
"text": [
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],
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0,
198
]
]
}
] | [
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168,
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130,
138
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"id": "BioInfer.d480.s0.e6",
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153,
154
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168,
176
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166,
176
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{
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"phosphoprotein",
"proteins"
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96,
110
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130,
138
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"F",
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156,
157
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168,
176
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{
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53,
54
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{
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112,
113
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{
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"NP"
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91,
93
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"M"
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127,
128
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}
] | [] | [] | [] |
585 | BioInfer.d481.s0 | [
{
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"text": [
"Particle aggregates associated with this array of actin microfilaments also labeled with antibodies to vinculin, talin and beta 1-integrin."
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0,
139
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50,
55
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118
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103,
111
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123,
138
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] | [] | [] | [] |
586 | BioInfer.d482.s0 | [
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0,
157
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126,
139
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102,
112
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144,
156
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0,
10
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114,
124
]
],
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}
] | [] | [] | [] |
587 | BioInfer.d484.s0 | [
{
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"Pervanadate caused a dramatic augmentation of the phosphorylation of E-cadherin, beta-catenin, and gamma-catenin (plakoglobin), but alpha-catenin was not detectably phosphorylated."
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0,
180
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99,
112
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69,
79
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114,
125
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81,
93
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132,
145
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],
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}
] | [] | [] | [] |
588 | BioInfer.d486.s0 | [
{
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"text": [
"Phosphoinositides bind to profilin and regulate actin-based cytoskeletal protein assembly."
],
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0,
90
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]
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48,
53
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26,
34
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],
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}
] | [] | [] | [] |
589 | BioInfer.d486.s1 | [
{
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"text": [
"Phosphorylation of profilin by PKC was not affected by the presence of various concentrations of actin."
],
"offsets": [
[
0,
103
]
]
}
] | [
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97,
102
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19,
27
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31,
34
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],
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"arg2_id": "BioInfer.d486.s1.e2",
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}
] |
590 | BioInfer.d487.s0 | [
{
"id": "BioInfer.d487.s0__text",
"type": "Sentence",
"text": [
"Phosphorylation of the headpiece domain could regulate the actin binding and bundling properties of fimbrin, or it could regulate the interaction of fimbrin with other proteins."
],
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[
0,
177
]
]
}
] | [
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59,
64
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100,
107
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149,
156
]
],
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}
] |
591 | BioInfer.d488.s0 | [
{
"id": "BioInfer.d488.s0__text",
"type": "Sentence",
"text": [
"Photochemical cleavage of myosin heavy chain and the effect on the interaction with actin."
],
"offsets": [
[
0,
90
]
]
}
] | [
{
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84,
89
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{
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26,
44
]
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"arg2_id": "BioInfer.d488.s0.e1",
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}
] |
592 | BioInfer.d490.s0 | [
{
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"type": "Sentence",
"text": [
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],
"offsets": [
[
0,
185
]
]
}
] | [
{
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179,
184
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{
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"text": [
"talin"
],
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[
93,
98
]
],
"normalized": []
}
] | [] | [] | [] |
593 | BioInfer.d492.s0 | [
{
"id": "BioInfer.d492.s0__text",
"type": "Sentence",
"text": [
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[
0,
221
]
]
}
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{
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49,
54
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152,
157
]
],
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}
] | [] | [] | [] |
594 | BioInfer.d493.s0 | [
{
"id": "BioInfer.d493.s0__text",
"type": "Sentence",
"text": [
"Previous studies have yielded conflicting results concerning the physiological role of profilin, a 12-15-kD actin- and phosphoinositide-binding protein, as a regulator of actin polymerization."
],
"offsets": [
[
0,
192
]
]
}
] | [
{
"id": "BioInfer.d493.s0.e0",
"type": "Individual_protein",
"text": [
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],
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87,
95
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{
"id": "BioInfer.d493.s0.e1",
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108,
113
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"text": [
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171,
176
]
],
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}
] |
595 | BioInfer.d494.s0 | [
{
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"type": "Sentence",
"text": [
"Production of PIP and PIP2 may be important downstream signals since these polyphosphoinositides are able to regulate the interaction of gelsolin and profilin with actin."
],
"offsets": [
[
0,
170
]
]
}
] | [
{
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164,
169
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{
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137,
145
]
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],
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150,
158
]
],
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}
] | [] | [] | [
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] |
596 | BioInfer.d495.s0 | [
{
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"text": [
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],
"offsets": [
[
0,
168
]
]
}
] | [
{
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143,
148
]
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15,
26
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{
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],
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0,
10
]
],
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}
] | [] | [] | [
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"arg2_id": "BioInfer.d495.s0.e2",
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}
] |
597 | BioInfer.d496.s0 | [
{
"id": "BioInfer.d496.s0__text",
"type": "Sentence",
"text": [
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],
"offsets": [
[
0,
176
]
]
}
] | [
{
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59,
69
]
],
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},
{
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0,
11
]
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{
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132,
142
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18,
23
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92,
97
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}
] | [] | [] | [
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598 | BioInfer.d496.s1 | [
{
"id": "BioInfer.d496.s1__text",
"type": "Sentence",
"text": [
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],
"offsets": [
[
0,
185
]
]
}
] | [
{
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37,
48
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77,
82
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],
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}
] | [] | [] | [
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] |
599 | BioInfer.d497.s0 | [
{
"id": "BioInfer.d497.s0__text",
"type": "Sentence",
"text": [
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],
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[
0,
229
]
]
}
] | [
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149,
154
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0,
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136,
144
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42,
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{
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"type": "Gene/protein/RNA",
"text": [
"profilin"
],
"offsets": [
[
183,
191
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d497.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d497.s0.e0",
"arg2_id": "BioInfer.d497.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d497.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d497.s0.e1",
"arg2_id": "BioInfer.d497.s0.e3",
"normalized": []
}
] |