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split_0_train_100 | split_0_train_100 | [
{
"id": "split_0_train_100_passage",
"type": "progene_text",
"text": [
"BACKGROUND :"
],
"offsets": [
[
0,
12
]
]
}
] | [] | [] | [] | [] |
split_0_train_101 | split_0_train_101 | [
{
"id": "split_0_train_101_passage",
"type": "progene_text",
"text": [
"Several reports indicate that aprotinin treatment before and during cardiopulmonary bypass ( CPB ) might have a protective effect on the myocardium ."
],
"offsets": [
[
0,
149
]
]
}
] | [] | [] | [] | [] |
split_0_train_102 | split_0_train_102 | [
{
"id": "split_0_train_102_passage",
"type": "progene_text",
"text": [
"We evaluated the hemodynamic effects of perioperative aprotinin treatment ."
],
"offsets": [
[
0,
75
]
]
}
] | [] | [] | [] | [] |
split_0_train_103 | split_0_train_103 | [
{
"id": "split_0_train_103_passage",
"type": "progene_text",
"text": [
"METHODS :"
],
"offsets": [
[
0,
9
]
]
}
] | [] | [] | [] | [] |
split_0_train_104 | split_0_train_104 | [
{
"id": "split_0_train_104_passage",
"type": "progene_text",
"text": [
"We conducted a randomized , double - blind , placebo - controlled trial in 34 infants ( mean age , 2.5 years ) who had cardiac operations ."
],
"offsets": [
[
0,
139
]
]
}
] | [] | [] | [] | [] |
split_0_train_105 | split_0_train_105 | [
{
"id": "split_0_train_105_passage",
"type": "progene_text",
"text": [
"Half of the patients received high - dose aprotinin therapy ."
],
"offsets": [
[
0,
61
]
]
}
] | [] | [] | [] | [] |
split_0_train_106 | split_0_train_106 | [
{
"id": "split_0_train_106_passage",
"type": "progene_text",
"text": [
"There were no significant differences between the aprotinin and placebo groups with respect to age , weight , sex , aortic cross - clamp time , and CPB time ."
],
"offsets": [
[
0,
158
]
]
}
] | [] | [] | [] | [] |
split_0_train_107 | split_0_train_107 | [
{
"id": "split_0_train_107_passage",
"type": "progene_text",
"text": [
"The following data were recorded at arrival in the intensive care unit 6 , 12 , 24 , and 48 hours after termination of CPB : heart rate , blood pressure , left atrial pressure , central - peripheral temperature difference , arterial - central venous oxygen saturation difference , urine output , serum creatinine , lactate and neutrophil elastase levels , the Doppler echocardiographic factors shortening fraction and preejection period / left - ventricular ejection time , and cumulative doses of catecholamines ( epinephrine ) , enoximone , and furosemide ."
],
"offsets": [
[
0,
559
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]
}
] | [
{
"id": "split_0_train_142_entity",
"type": "progene_text",
"text": [
"elastase"
],
"offsets": [
[
338,
346
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_108 | split_0_train_108 | [
{
"id": "split_0_train_108_passage",
"type": "progene_text",
"text": [
"RESULTS :"
],
"offsets": [
[
0,
9
]
]
}
] | [] | [] | [] | [] |
split_0_train_109 | split_0_train_109 | [
{
"id": "split_0_train_109_passage",
"type": "progene_text",
"text": [
"No hemodynamic variable showed any significant difference between aprotinin and placebo groups ."
],
"offsets": [
[
0,
96
]
]
}
] | [] | [] | [] | [] |
split_0_train_110 | split_0_train_110 | [
{
"id": "split_0_train_110_passage",
"type": "progene_text",
"text": [
"Urine output , creatinine , lactate , and elastase levels , as well as the cumulative doses of furosemide and epinephrine were not significantly different ."
],
"offsets": [
[
0,
156
]
]
}
] | [] | [] | [] | [] |
split_0_train_111 | split_0_train_111 | [
{
"id": "split_0_train_111_passage",
"type": "progene_text",
"text": [
"Twelve hours after CPB 10 patients in the placebo group and 4 in the aprotinin group had received enoximone ( p < 0.05 ) ."
],
"offsets": [
[
0,
122
]
]
}
] | [] | [] | [] | [] |
split_0_train_112 | split_0_train_112 | [
{
"id": "split_0_train_112_passage",
"type": "progene_text",
"text": [
"The placebo group had received significantly larger doses of enoximone than the aprotinin group at arrival in the intensive care unit ( 0.13 +/- 0.05 versus 0 mg / kg ) , 12 hours after CPB ( 0.58 +/- 0.14 versus 0.18 +/- 0.09 mg / kg ) , 24 hours after CPB ( 1.11 +/- 0.24 versus 0.42 +/- 0.16 mg / kg ) , and 48 hours after CPB ( 1.61 +/- 0.40 versus 0.86 +/- 0.28 ) ."
],
"offsets": [
[
0,
370
]
]
}
] | [] | [] | [] | [] |
split_0_train_113 | split_0_train_113 | [
{
"id": "split_0_train_113_passage",
"type": "progene_text",
"text": [
"At 6 hours the difference did not reach statistical significance ."
],
"offsets": [
[
0,
66
]
]
}
] | [] | [] | [] | [] |
split_0_train_114 | split_0_train_114 | [
{
"id": "split_0_train_114_passage",
"type": "progene_text",
"text": [
"CONCLUSIONS :"
],
"offsets": [
[
0,
13
]
]
}
] | [] | [] | [] | [] |
split_0_train_115 | split_0_train_115 | [
{
"id": "split_0_train_115_passage",
"type": "progene_text",
"text": [
"Clinical and hemodynamic status of the aprotinin - treated patients was similar to that of the placebo - treated patients in the first 48 hours after CPB ."
],
"offsets": [
[
0,
155
]
]
}
] | [] | [] | [] | [] |
split_0_train_116 | split_0_train_116 | [
{
"id": "split_0_train_116_passage",
"type": "progene_text",
"text": [
"The placebo group , however , required significantly more inotropic support by enoximone than the aprotinin group to achieve this goal ."
],
"offsets": [
[
0,
136
]
]
}
] | [] | [] | [] | [] |
split_0_train_117 | split_0_train_117 | [
{
"id": "split_0_train_117_passage",
"type": "progene_text",
"text": [
"An alternatively spliced form of CD79b gene may account for altered B-cell receptor expression in B-chronic lymphocytic leukemia ."
],
"offsets": [
[
0,
130
]
]
}
] | [
{
"id": "split_0_train_143_entity",
"type": "progene_text",
"text": [
"CD79b"
],
"offsets": [
[
33,
38
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],
"normalized": []
},
{
"id": "split_0_train_144_entity",
"type": "progene_text",
"text": [
"B-cell receptor"
],
"offsets": [
[
68,
83
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_118 | split_0_train_118 | [
{
"id": "split_0_train_118_passage",
"type": "progene_text",
"text": [
"Several functional anomalies of B-chronic lymphocytic leukemia ( B-CLL ) cells may be explained by abnormalities of the B-cell receptor ( BCR ) , a multimeric complex formed by the sIg homodimer and the noncovalently bound heterodimer Igalpha / Igbeta ( CD79a / CD79b ) ."
],
"offsets": [
[
0,
271
]
]
}
] | [
{
"id": "split_0_train_145_entity",
"type": "progene_text",
"text": [
"B-cell receptor"
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"offsets": [
[
120,
135
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],
"normalized": []
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{
"id": "split_0_train_146_entity",
"type": "progene_text",
"text": [
"BCR"
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"offsets": [
[
138,
141
]
],
"normalized": []
},
{
"id": "split_0_train_147_entity",
"type": "progene_text",
"text": [
"sIg"
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"offsets": [
[
181,
184
]
],
"normalized": []
},
{
"id": "split_0_train_148_entity",
"type": "progene_text",
"text": [
"Igalpha"
],
"offsets": [
[
235,
242
]
],
"normalized": []
},
{
"id": "split_0_train_149_entity",
"type": "progene_text",
"text": [
"Igbeta"
],
"offsets": [
[
245,
251
]
],
"normalized": []
},
{
"id": "split_0_train_150_entity",
"type": "progene_text",
"text": [
"CD79a"
],
"offsets": [
[
254,
259
]
],
"normalized": []
},
{
"id": "split_0_train_151_entity",
"type": "progene_text",
"text": [
"CD79b"
],
"offsets": [
[
262,
267
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_119 | split_0_train_119 | [
{
"id": "split_0_train_119_passage",
"type": "progene_text",
"text": [
"Because the expression of the extracellular Ig - like domain of CD79b has been reported to be absent in the cells of most CLL cases , we have investigated the molecular mechanisms that may account for this defect ."
],
"offsets": [
[
0,
214
]
]
}
] | [
{
"id": "split_0_train_152_entity",
"type": "progene_text",
"text": [
"Ig"
],
"offsets": [
[
44,
46
]
],
"normalized": []
},
{
"id": "split_0_train_153_entity",
"type": "progene_text",
"text": [
"CD79b"
],
"offsets": [
[
64,
69
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_120 | split_0_train_120 | [
{
"id": "split_0_train_120_passage",
"type": "progene_text",
"text": [
"Peripheral blood lymphocytes ( PBL ) from 50 patients and two cell lines ( MEC1 , MEC2 ) obtained from the PBL of one of them were studied ."
],
"offsets": [
[
0,
140
]
]
}
] | [] | [] | [] | [] |
split_0_train_121 | split_0_train_121 | [
{
"id": "split_0_train_121_passage",
"type": "progene_text",
"text": [
"MEC1 , MEC2 , and 75 % of CLL cases did not express detectable levels of the extracellular Ig - like domain of CD79b , which was nevertheless present in greater than 80 % CD19 ( + ) cells from normal donors ."
],
"offsets": [
[
0,
208
]
]
}
] | [
{
"id": "split_0_train_154_entity",
"type": "progene_text",
"text": [
"Ig"
],
"offsets": [
[
91,
93
]
],
"normalized": []
},
{
"id": "split_0_train_155_entity",
"type": "progene_text",
"text": [
"CD79b"
],
"offsets": [
[
111,
116
]
],
"normalized": []
},
{
"id": "split_0_train_156_entity",
"type": "progene_text",
"text": [
"CD19"
],
"offsets": [
[
171,
175
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_122 | split_0_train_122 | [
{
"id": "split_0_train_122_passage",
"type": "progene_text",
"text": [
"In healthy subjects the expression of CD79b was equally distributed in CD5 ( + ) and CD5 ( - ) B-cell subsets ."
],
"offsets": [
[
0,
111
]
]
}
] | [
{
"id": "split_0_train_157_entity",
"type": "progene_text",
"text": [
"CD79b"
],
"offsets": [
[
38,
43
]
],
"normalized": []
},
{
"id": "split_0_train_158_entity",
"type": "progene_text",
"text": [
"CD5"
],
"offsets": [
[
71,
74
]
],
"normalized": []
},
{
"id": "split_0_train_159_entity",
"type": "progene_text",
"text": [
"CD5"
],
"offsets": [
[
85,
88
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_123 | split_0_train_123 | [
{
"id": "split_0_train_123_passage",
"type": "progene_text",
"text": [
"Reverse transcription - polymerase chain reaction ( RT - PCR ) analysis of CD79b RNA from all patients and from MEC1 and MEC2 cell lines consistently yielded two fragments of different size ( 709 bp and 397 bp ) ."
],
"offsets": [
[
0,
213
]
]
}
] | [
{
"id": "split_0_train_160_entity",
"type": "progene_text",
"text": [
"CD79b"
],
"offsets": [
[
75,
80
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_124 | split_0_train_124 | [
{
"id": "split_0_train_124_passage",
"type": "progene_text",
"text": [
"The 709 - bp band corresponds to CD79b entire transcript ; the 397 - bp band corresponds to an alternatively spliced form lacking exon 3 that encodes the extracellular Ig - like domain ."
],
"offsets": [
[
0,
186
]
]
}
] | [
{
"id": "split_0_train_161_entity",
"type": "progene_text",
"text": [
"CD79b"
],
"offsets": [
[
33,
38
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],
"normalized": []
},
{
"id": "split_0_train_162_entity",
"type": "progene_text",
"text": [
"Ig"
],
"offsets": [
[
168,
170
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_125 | split_0_train_125 | [
{
"id": "split_0_train_125_passage",
"type": "progene_text",
"text": [
"Both fragments were also visible in normal PBL ."
],
"offsets": [
[
0,
48
]
]
}
] | [] | [] | [] | [] |
split_0_train_126 | split_0_train_126 | [
{
"id": "split_0_train_126_passage",
"type": "progene_text",
"text": [
"The expression of the 397 - bp fragment was increased in normal activated B cells , while no difference was seen between CD5 ( + ) and CD5 ( - ) B cells ."
],
"offsets": [
[
0,
154
]
]
}
] | [
{
"id": "split_0_train_163_entity",
"type": "progene_text",
"text": [
"CD5"
],
"offsets": [
[
121,
124
]
],
"normalized": []
},
{
"id": "split_0_train_164_entity",
"type": "progene_text",
"text": [
"CD5"
],
"offsets": [
[
135,
138
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_127 | split_0_train_127 | [
{
"id": "split_0_train_127_passage",
"type": "progene_text",
"text": [
"To obtain a more accurate estimate of the relative proportions of the two spliced forms , a radioactive PCR was performed in 13 normal and 22 B-CLL samples and the results analyzed using a digital imager ."
],
"offsets": [
[
0,
205
]
]
}
] | [] | [] | [] | [] |
split_0_train_128 | split_0_train_128 | [
{
"id": "split_0_train_128_passage",
"type": "progene_text",
"text": [
"The mean value of the CD79b to the CD79b internally deleted ratio was 0.64 +/- 0.20 SD in normal donors and 0.44 +/- 0.27 SD in B-CLL ( P = .01 ) ."
],
"offsets": [
[
0,
147
]
]
}
] | [
{
"id": "split_0_train_165_entity",
"type": "progene_text",
"text": [
"CD79b"
],
"offsets": [
[
22,
27
]
],
"normalized": []
},
{
"id": "split_0_train_166_entity",
"type": "progene_text",
"text": [
"CD79b"
],
"offsets": [
[
35,
40
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_129 | split_0_train_129 | [
{
"id": "split_0_train_129_passage",
"type": "progene_text",
"text": [
"Direct sequencing of 397 - bp RT - PCR products and of genomic DNA corresponding to exon 3 from MEC1 , MEC2 , their parental cells , and five fresh B-CLL samples did not show any causal mutation ."
],
"offsets": [
[
0,
196
]
]
}
] | [] | [] | [] | [] |
split_0_train_130 | split_0_train_130 | [
{
"id": "split_0_train_130_passage",
"type": "progene_text",
"text": [
"Single - strand conformation polymorphism analysis of exon 3 performed in 18 additional B-CLL cases showed a single abnormal shift corresponding to a TGT --> TGC polymorphic change at amino acid 122 ."
],
"offsets": [
[
0,
200
]
]
}
] | [] | [] | [] | [] |
split_0_train_131 | split_0_train_131 | [
{
"id": "split_0_train_131_passage",
"type": "progene_text",
"text": [
"We propose a role for the alternative splicing of CD79b gene in causing the reduced expression of BCR on the surface of B-CLL cells ."
],
"offsets": [
[
0,
133
]
]
}
] | [
{
"id": "split_0_train_167_entity",
"type": "progene_text",
"text": [
"CD79b"
],
"offsets": [
[
50,
55
]
],
"normalized": []
},
{
"id": "split_0_train_168_entity",
"type": "progene_text",
"text": [
"BCR"
],
"offsets": [
[
98,
101
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_132 | split_0_train_132 | [
{
"id": "split_0_train_132_passage",
"type": "progene_text",
"text": [
"As normal B cells also present this variant , the mechanism of CD79b posttranscriptional regulation might reflect the activation stage of the normal B cell from which B-CLL derives ."
],
"offsets": [
[
0,
182
]
]
}
] | [
{
"id": "split_0_train_169_entity",
"type": "progene_text",
"text": [
"CD79b"
],
"offsets": [
[
63,
68
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_133 | split_0_train_133 | [
{
"id": "split_0_train_133_passage",
"type": "progene_text",
"text": [
"The major phase - variable outer membrane protein of Escherichia coli structurally resembles the immunoglobulin A1 protease class of exported protein and is regulated by a novel mechanism involving Dam and oxyR ."
],
"offsets": [
[
0,
212
]
]
}
] | [
{
"id": "split_0_train_170_entity",
"type": "progene_text",
"text": [
"immunoglobulin A1 protease"
],
"offsets": [
[
97,
123
]
],
"normalized": []
},
{
"id": "split_0_train_171_entity",
"type": "progene_text",
"text": [
"Dam"
],
"offsets": [
[
198,
201
]
],
"normalized": []
},
{
"id": "split_0_train_172_entity",
"type": "progene_text",
"text": [
"oxyR"
],
"offsets": [
[
206,
210
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_134 | split_0_train_134 | [
{
"id": "split_0_train_134_passage",
"type": "progene_text",
"text": [
"Here we report the characterization of an Escherichia coli gene ( agn43 ) which encodes the principal phase - variable outer membrane protein termed antigen 43 ( Ag43 ) ."
],
"offsets": [
[
0,
170
]
]
}
] | [
{
"id": "split_0_train_173_entity",
"type": "progene_text",
"text": [
"agn43"
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"offsets": [
[
66,
71
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],
"normalized": []
},
{
"id": "split_0_train_174_entity",
"type": "progene_text",
"text": [
"antigen 43"
],
"offsets": [
[
149,
159
]
],
"normalized": []
},
{
"id": "split_0_train_175_entity",
"type": "progene_text",
"text": [
"Ag43"
],
"offsets": [
[
162,
166
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_135 | split_0_train_135 | [
{
"id": "split_0_train_135_passage",
"type": "progene_text",
"text": [
"The agn43 gene encodes a precursor protein of 107 kDa containing a 52 - amino - acid signal sequence ."
],
"offsets": [
[
0,
102
]
]
}
] | [
{
"id": "split_0_train_176_entity",
"type": "progene_text",
"text": [
"agn43"
],
"offsets": [
[
4,
9
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_136 | split_0_train_136 | [
{
"id": "split_0_train_136_passage",
"type": "progene_text",
"text": [
"Posttranslational processing generates an alpha43 subunit ( predicted Mr of 49 , 789 ) and a C - terminal domain ( beta43 ) with features typical of a bacterial integral outer membrane protein ( predicted Mr of 51 , 642 ) ."
],
"offsets": [
[
0,
223
]
]
}
] | [] | [] | [] | [] |
split_0_train_137 | split_0_train_137 | [
{
"id": "split_0_train_137_passage",
"type": "progene_text",
"text": [
"Secondary structure analysis predicts that beta43 exists as an 18 - stranded beta barrel and that Ag43 shows structural organization closely resembling that of immunoglobulin A1 protease type of exoprotein produced by pathogenic Neisseria and Haemophilus spp. The correct processing of the polyprotein to alpha43 and beta43 in OmpT , OmpP , and DegP protease - deficient E. coli strains points to an autocatalytic cleavage mechanism , a hypothesis supported by the occurrence of an aspartyl protease active site within alpha43 ."
],
"offsets": [
[
0,
528
]
]
}
] | [
{
"id": "split_0_train_177_entity",
"type": "progene_text",
"text": [
"immunoglobulin A1 protease"
],
"offsets": [
[
160,
186
]
],
"normalized": []
},
{
"id": "split_0_train_178_entity",
"type": "progene_text",
"text": [
"OmpT"
],
"offsets": [
[
327,
331
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],
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334,
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{
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345,
349
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{
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"text": [
"protease"
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350,
358
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},
{
"id": "split_0_train_182_entity",
"type": "progene_text",
"text": [
"aspartyl protease"
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[
482,
499
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_138 | split_0_train_138 | [
{
"id": "split_0_train_138_passage",
"type": "progene_text",
"text": [
"Ag43 , a species - specific antigen , possesses two RGD motifs of the type implicated in binding to human integrins ."
],
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[
0,
117
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]
}
] | [
{
"id": "split_0_train_183_entity",
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"text": [
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0,
4
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{
"id": "split_0_train_184_entity",
"type": "progene_text",
"text": [
"integrins"
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[
106,
115
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_139 | split_0_train_139 | [
{
"id": "split_0_train_139_passage",
"type": "progene_text",
"text": [
"The mechanism of reversible phase variation was studied by immunochemical analysis of a panel of well - defined regulatory mutants and by analysis of DNA sequences upstream of agn43 ."
],
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[
0,
183
]
]
}
] | [
{
"id": "split_0_train_185_entity",
"type": "progene_text",
"text": [
"agn43"
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"offsets": [
[
176,
181
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],
"normalized": []
}
] | [] | [] | [] |
split_0_train_140 | split_0_train_140 | [
{
"id": "split_0_train_140_passage",
"type": "progene_text",
"text": [
"Evidence strongly suggests that phase variation is regulated by both deoxyadenosine methylase ( Dam ) and by OxyR ."
],
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[
0,
115
]
]
}
] | [
{
"id": "split_0_train_186_entity",
"type": "progene_text",
"text": [
"deoxyadenosine methylase"
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69,
93
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{
"id": "split_0_train_187_entity",
"type": "progene_text",
"text": [
"Dam"
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96,
99
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},
{
"id": "split_0_train_188_entity",
"type": "progene_text",
"text": [
"OxyR"
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"offsets": [
[
109,
113
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_141 | split_0_train_141 | [
{
"id": "split_0_train_141_passage",
"type": "progene_text",
"text": [
"Thus , oxyR mutants are locked on for Ag43 expression , whereas dam mutants are locked off for Ag43 expression ."
],
"offsets": [
[
0,
112
]
]
}
] | [
{
"id": "split_0_train_189_entity",
"type": "progene_text",
"text": [
"oxyR"
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[
7,
11
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},
{
"id": "split_0_train_190_entity",
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"text": [
"Ag43"
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38,
42
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},
{
"id": "split_0_train_191_entity",
"type": "progene_text",
"text": [
"dam"
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64,
67
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},
{
"id": "split_0_train_192_entity",
"type": "progene_text",
"text": [
"Ag43"
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"offsets": [
[
95,
99
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_142 | split_0_train_142 | [
{
"id": "split_0_train_142_passage",
"type": "progene_text",
"text": [
"We propose a novel mechanism for the regulation of phase switching in which OxyR competes with Dam for unmethylated GATC sites in the regulatory region of the agn43 gene ."
],
"offsets": [
[
0,
171
]
]
}
] | [
{
"id": "split_0_train_193_entity",
"type": "progene_text",
"text": [
"OxyR"
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[
76,
80
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],
"normalized": []
},
{
"id": "split_0_train_194_entity",
"type": "progene_text",
"text": [
"Dam"
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[
95,
98
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],
"normalized": []
},
{
"id": "split_0_train_195_entity",
"type": "progene_text",
"text": [
"agn43"
],
"offsets": [
[
159,
164
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_143 | split_0_train_143 | [
{
"id": "split_0_train_143_passage",
"type": "progene_text",
"text": [
"Ku autoimmune antigen is involved in placental regulation of rat P450c17 gene transcription ."
],
"offsets": [
[
0,
93
]
]
}
] | [
{
"id": "split_0_train_196_entity",
"type": "progene_text",
"text": [
"Ku"
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"offsets": [
[
0,
2
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},
{
"id": "split_0_train_197_entity",
"type": "progene_text",
"text": [
"P450c17"
],
"offsets": [
[
65,
72
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_144 | split_0_train_144 | [
{
"id": "split_0_train_144_passage",
"type": "progene_text",
"text": [
"The steroidogenic enzyme P450c17 ( 17alpha hydroxylase / C17 , 20 lyase ) regulates a key branchpoint in steroidogenesis , as its activity directs the steroid biosynthetic pathways toward glucocorticoid or sex hormone synthesis ."
],
"offsets": [
[
0,
229
]
]
}
] | [
{
"id": "split_0_train_198_entity",
"type": "progene_text",
"text": [
"P450c17"
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[
25,
32
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],
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},
{
"id": "split_0_train_199_entity",
"type": "progene_text",
"text": [
"17alpha hydroxylase"
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[
35,
54
]
],
"normalized": []
},
{
"id": "split_0_train_200_entity",
"type": "progene_text",
"text": [
"C17 , 20 lyase"
],
"offsets": [
[
57,
71
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_145 | split_0_train_145 | [
{
"id": "split_0_train_145_passage",
"type": "progene_text",
"text": [
"Expression of the P450c17 gene is transcriptionally regulated in steroidogenic tissues by cAMP ."
],
"offsets": [
[
0,
96
]
]
}
] | [
{
"id": "split_0_train_201_entity",
"type": "progene_text",
"text": [
"P450c17"
],
"offsets": [
[
18,
25
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_146 | split_0_train_146 | [
{
"id": "split_0_train_146_passage",
"type": "progene_text",
"text": [
"We showed that DNA between - 84 and - 55 in the rat P450c17 gene was bound uniquely by steroidogenic factor-1 ( SF-1 ) , which regulated both basal and cAMP - stimulated transcription in mouse adrenocortical and Leydig cells ."
],
"offsets": [
[
0,
226
]
]
}
] | [
{
"id": "split_0_train_202_entity",
"type": "progene_text",
"text": [
"P450c17"
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[
52,
59
]
],
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},
{
"id": "split_0_train_203_entity",
"type": "progene_text",
"text": [
"steroidogenic factor-1"
],
"offsets": [
[
87,
109
]
],
"normalized": []
},
{
"id": "split_0_train_204_entity",
"type": "progene_text",
"text": [
"SF-1"
],
"offsets": [
[
112,
116
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_147 | split_0_train_147 | [
{
"id": "split_0_train_147_passage",
"type": "progene_text",
"text": [
"SF-1 gene ablation experiments in mice indicate that SF-1 is not mandatory for placental steroidogenesis ."
],
"offsets": [
[
0,
106
]
]
}
] | [
{
"id": "split_0_train_205_entity",
"type": "progene_text",
"text": [
"SF-1"
],
"offsets": [
[
0,
4
]
],
"normalized": []
},
{
"id": "split_0_train_206_entity",
"type": "progene_text",
"text": [
"SF-1"
],
"offsets": [
[
53,
57
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_148 | split_0_train_148 | [
{
"id": "split_0_train_148_passage",
"type": "progene_text",
"text": [
"We studied P450c17 gene regulation in the placenta using human placental JEG-3 trophoblast cells ."
],
"offsets": [
[
0,
98
]
]
}
] | [
{
"id": "split_0_train_207_entity",
"type": "progene_text",
"text": [
"P450c17"
],
"offsets": [
[
11,
18
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_149 | split_0_train_149 | [
{
"id": "split_0_train_149_passage",
"type": "progene_text",
"text": [
"Transfection of reporter luciferase gene constructs containing serial deletions of the 5' flanking region of the rat P450c17 gene showed that DNA between - 98 and + 13 mediated basal and cAMP - regulated transcription in placental JEG-3 cells , as it did in adrenal and Leydig cells ."
],
"offsets": [
[
0,
284
]
]
}
] | [
{
"id": "split_0_train_208_entity",
"type": "progene_text",
"text": [
"luciferase"
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"offsets": [
[
25,
35
]
],
"normalized": []
},
{
"id": "split_0_train_209_entity",
"type": "progene_text",
"text": [
"P450c17"
],
"offsets": [
[
117,
124
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_150 | split_0_train_150 | [
{
"id": "split_0_train_150_passage",
"type": "progene_text",
"text": [
"DNase footprints further identified a region between - 88 and the TATA box that was bound by protein ."
],
"offsets": [
[
0,
102
]
]
}
] | [
{
"id": "split_0_train_210_entity",
"type": "progene_text",
"text": [
"DNase"
],
"offsets": [
[
0,
5
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_151 | split_0_train_151 | [
{
"id": "split_0_train_151_passage",
"type": "progene_text",
"text": [
"Transfection of luciferase reporter constructs containing - 84 to - 55 of the rat P450c17 DNA ligated to the minimal promoter of the thymidine kinase gene showed that this DNA increased both basal and cAMP - simulated luciferase activity ."
],
"offsets": [
[
0,
239
]
]
}
] | [
{
"id": "split_0_train_211_entity",
"type": "progene_text",
"text": [
"luciferase"
],
"offsets": [
[
16,
26
]
],
"normalized": []
},
{
"id": "split_0_train_212_entity",
"type": "progene_text",
"text": [
"P450c17"
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"offsets": [
[
82,
89
]
],
"normalized": []
},
{
"id": "split_0_train_213_entity",
"type": "progene_text",
"text": [
"thymidine kinase"
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[
133,
149
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],
"normalized": []
},
{
"id": "split_0_train_214_entity",
"type": "progene_text",
"text": [
"luciferase"
],
"offsets": [
[
218,
228
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_152 | split_0_train_152 | [
{
"id": "split_0_train_152_passage",
"type": "progene_text",
"text": [
"Gel mobility shift assays identified two DNA - protein complexes with JEG-3 cell nuclear extracts that were different from complexes formed with MA-10 cell extracts and did not involve SF-1 ."
],
"offsets": [
[
0,
191
]
]
}
] | [
{
"id": "split_0_train_215_entity",
"type": "progene_text",
"text": [
"SF-1"
],
"offsets": [
[
185,
189
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_153 | split_0_train_153 | [
{
"id": "split_0_train_153_passage",
"type": "progene_text",
"text": [
"Mutational analysis of the - 84 / - 55 DNA showed that JEG-3 nuclear proteins bound to a site containing , but not identical to , the SF-1 sequence ."
],
"offsets": [
[
0,
149
]
]
}
] | [
{
"id": "split_0_train_216_entity",
"type": "progene_text",
"text": [
"SF-1"
],
"offsets": [
[
134,
138
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_154 | split_0_train_154 | [
{
"id": "split_0_train_154_passage",
"type": "progene_text",
"text": [
"One complex involved Ku autoimmune antigen , which bound to DNA sequence specifically ."
],
"offsets": [
[
0,
87
]
]
}
] | [
{
"id": "split_0_train_217_entity",
"type": "progene_text",
"text": [
"Ku"
],
"offsets": [
[
21,
23
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_155 | split_0_train_155 | [
{
"id": "split_0_train_155_passage",
"type": "progene_text",
"text": [
"Overexpression of Ku antigen in MA-10 cells stimulated rat P450c17 gene transcription , thus demonstrating a biologic effect of Ku ."
],
"offsets": [
[
0,
132
]
]
}
] | [
{
"id": "split_0_train_218_entity",
"type": "progene_text",
"text": [
"Ku"
],
"offsets": [
[
18,
20
]
],
"normalized": []
},
{
"id": "split_0_train_219_entity",
"type": "progene_text",
"text": [
"P450c17"
],
"offsets": [
[
59,
66
]
],
"normalized": []
},
{
"id": "split_0_train_220_entity",
"type": "progene_text",
"text": [
"Ku"
],
"offsets": [
[
128,
130
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_156 | split_0_train_156 | [
{
"id": "split_0_train_156_passage",
"type": "progene_text",
"text": [
"Ku also bound to a similar region of the human P450c17 gene , and the DNA region to which Ku bound was transcriptionally active in JEG-3 cells ."
],
"offsets": [
[
0,
144
]
]
}
] | [
{
"id": "split_0_train_221_entity",
"type": "progene_text",
"text": [
"Ku"
],
"offsets": [
[
0,
2
]
],
"normalized": []
},
{
"id": "split_0_train_222_entity",
"type": "progene_text",
"text": [
"P450c17"
],
"offsets": [
[
47,
54
]
],
"normalized": []
},
{
"id": "split_0_train_223_entity",
"type": "progene_text",
"text": [
"Ku"
],
"offsets": [
[
90,
92
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_157 | split_0_train_157 | [
{
"id": "split_0_train_157_passage",
"type": "progene_text",
"text": [
"Ku was also found in extracts from rat placenta and bound to the - 84 / - 55 rat P450c17 DNA ."
],
"offsets": [
[
0,
94
]
]
}
] | [
{
"id": "split_0_train_224_entity",
"type": "progene_text",
"text": [
"Ku"
],
"offsets": [
[
0,
2
]
],
"normalized": []
},
{
"id": "split_0_train_225_entity",
"type": "progene_text",
"text": [
"P450c17"
],
"offsets": [
[
81,
88
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_158 | split_0_train_158 | [
{
"id": "split_0_train_158_passage",
"type": "progene_text",
"text": [
"These data demonstrate a role of Ku in regulating P450c17 gene expression ."
],
"offsets": [
[
0,
75
]
]
}
] | [
{
"id": "split_0_train_226_entity",
"type": "progene_text",
"text": [
"Ku"
],
"offsets": [
[
33,
35
]
],
"normalized": []
},
{
"id": "split_0_train_227_entity",
"type": "progene_text",
"text": [
"P450c17"
],
"offsets": [
[
50,
57
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_159 | split_0_train_159 | [
{
"id": "split_0_train_159_passage",
"type": "progene_text",
"text": [
"These data further indicate that although human P450c17 is not normally expressed in the placenta , factors that could activate this gene are indeed present ."
],
"offsets": [
[
0,
158
]
]
}
] | [
{
"id": "split_0_train_228_entity",
"type": "progene_text",
"text": [
"P450c17"
],
"offsets": [
[
48,
55
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_160 | split_0_train_160 | [
{
"id": "split_0_train_160_passage",
"type": "progene_text",
"text": [
"CRE DNA binding proteins bind to the AP-1 target sequence and suppress AP-1 transcriptional activity in mouse keratinocytes ."
],
"offsets": [
[
0,
125
]
]
}
] | [
{
"id": "split_0_train_229_entity",
"type": "progene_text",
"text": [
"AP-1"
],
"offsets": [
[
37,
41
]
],
"normalized": []
},
{
"id": "split_0_train_230_entity",
"type": "progene_text",
"text": [
"AP-1"
],
"offsets": [
[
71,
75
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_161 | split_0_train_161 | [
{
"id": "split_0_train_161_passage",
"type": "progene_text",
"text": [
"Previously , we have shown that nuclear extracts from cultured mouse keratinocytes induced to differentiate by increasing the levels of extra - cellular calcium contain Fra-1 , Fra-2 , Jun B , Jun D and c-Jun proteins that bind to the AP-1 DNA binding sequence ."
],
"offsets": [
[
0,
262
]
]
}
] | [
{
"id": "split_0_train_231_entity",
"type": "progene_text",
"text": [
"Fra-1"
],
"offsets": [
[
169,
174
]
],
"normalized": []
},
{
"id": "split_0_train_232_entity",
"type": "progene_text",
"text": [
"Fra-2"
],
"offsets": [
[
177,
182
]
],
"normalized": []
},
{
"id": "split_0_train_233_entity",
"type": "progene_text",
"text": [
"Jun B"
],
"offsets": [
[
185,
190
]
],
"normalized": []
},
{
"id": "split_0_train_234_entity",
"type": "progene_text",
"text": [
"Jun D"
],
"offsets": [
[
193,
198
]
],
"normalized": []
},
{
"id": "split_0_train_235_entity",
"type": "progene_text",
"text": [
"c-Jun"
],
"offsets": [
[
203,
208
]
],
"normalized": []
},
{
"id": "split_0_train_236_entity",
"type": "progene_text",
"text": [
"AP-1"
],
"offsets": [
[
235,
239
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_162 | split_0_train_162 | [
{
"id": "split_0_train_162_passage",
"type": "progene_text",
"text": [
"Despite this DNA binding activity , AP-1 reporter activity was suppressed in these cells ."
],
"offsets": [
[
0,
90
]
]
}
] | [
{
"id": "split_0_train_237_entity",
"type": "progene_text",
"text": [
"AP-1"
],
"offsets": [
[
36,
40
]
],
"normalized": []
}
] | [] | [] | [] |
split_0_train_163 | split_0_train_163 | [
{
"id": "split_0_train_163_passage",
"type": "progene_text",
"text": [
"Here , we have detected the CREB family proteins CREB and CREMalpha as additional participants in the AP-1 DNA binding complex in differentiating keratinocytes ."
],
"offsets": [
[
0,
161
]
]
}
] | [
{
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split_0_train_164 | split_0_train_164 | [
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split_0_train_165 | split_0_train_165 | [
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split_0_train_166 | split_0_train_166 | [
{
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split_0_train_167 | split_0_train_167 | [
{
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split_0_train_168 | split_0_train_168 | [
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split_0_train_169 | split_0_train_169 | [
{
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split_0_train_170 | split_0_train_170 | [
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split_0_train_171 | split_0_train_171 | [
{
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] | [] | [] | [] |
split_0_train_172 | split_0_train_172 | [
{
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] | [] | [] | [] |
split_0_train_173 | split_0_train_173 | [
{
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"text": [
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] | [] | [] | [] |
split_0_train_174 | split_0_train_174 | [
{
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"text": [
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] | [] | [] | [] |
split_0_train_175 | split_0_train_175 | [
{
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"text": [
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160,
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] | [] | [] | [] |
split_0_train_176 | split_0_train_176 | [
{
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] | [] | [] | [] |
split_0_train_177 | split_0_train_177 | [
{
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] | [] | [] | [] |
split_0_train_178 | split_0_train_178 | [
{
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] | [] | [] | [] |
split_0_train_179 | split_0_train_179 | [
{
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] | [] | [] | [] |
split_0_train_180 | split_0_train_180 | [
{
"id": "split_0_train_180_passage",
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"text": [
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100,
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split_0_train_181 | split_0_train_181 | [
{
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split_0_train_182 | split_0_train_182 | [
{
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split_0_train_183 | split_0_train_183 | [
{
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split_0_train_184 | split_0_train_184 | [
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split_0_train_185 | split_0_train_185 | [
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}
] | [] | [] | [] |
split_0_train_186 | split_0_train_186 | [
{
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] | [] | [] | [] |
split_0_train_187 | split_0_train_187 | [
{
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"type": "progene_text",
"text": [
"In vitro precipitation with a glutathione-S-transferase - fusion protein containing the C - terminal transactivation domain of STAT5a showed GH - regulated association of ERK1 / 2 with the fusion protein , while this was not seen when serine 780 in STAT5a was changed to alanine ."
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] | [] | [] | [] |
split_0_train_188 | split_0_train_188 | [
{
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"type": "progene_text",
"text": [
"In vitro phosphorylation of the glutathione-S-transferase - fusion proteins using active ERK only worked when the fusion protein contained wild - type STAT5a sequence ."
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151,
157
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}
] | [] | [] | [] |
split_0_train_189 | split_0_train_189 | [
{
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"type": "progene_text",
"text": [
"The same experiment , performed with full - length wild - type STAT5a and the corresponding S780A mutant , showed that serine 780 is the only substrate in full - length STAT5a for active ERK ."
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] | [] | [] | [] |
split_0_train_190 | split_0_train_190 | [
{
"id": "split_0_train_190_passage",
"type": "progene_text",
"text": [
"In coimmunoprecipitation experiments , larger amounts of STAT5a - ERK1 / 2 complexes were detected in cytosol from untreated CHOA cells than in cytosol from GH - treated cells , suggesting the presence of preformed STAT5a - ERK1 / 2 complexes in unstimulated cells ."
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224,
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] | [] | [] | [] |
split_0_train_191 | split_0_train_191 | [
{
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"type": "progene_text",
"text": [
"Transfection experiments with COS cells showed that kinase - inactive ERK1 decreased GH stimulation of STAT5 - regulated reporter gene expression ."
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] | [] | [] | [] |
split_0_train_192 | split_0_train_192 | [
{
"id": "split_0_train_192_passage",
"type": "progene_text",
"text": [
"These observations show , for the first time , direct physical interaction between ERK and STAT5a and also clearly identify serine 780 as a target for ERK ."
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151,
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}
] | [] | [] | [] |
split_0_train_193 | split_0_train_193 | [
{
"id": "split_0_train_193_passage",
"type": "progene_text",
"text": [
"Furthermore , it is also established that serine phosphorylation of STAT5a transactivation domain , via the MAPK pathway , is a means of modifying GH - induced transcriptional activation ."
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}
] | [
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"GH"
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147,
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}
] | [] | [] | [] |
split_0_train_194 | split_0_train_194 | [
{
"id": "split_0_train_194_passage",
"type": "progene_text",
"text": [
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{
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103,
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}
] | [] | [] | [] |
split_0_train_195 | split_0_train_195 | [
{
"id": "split_0_train_195_passage",
"type": "progene_text",
"text": [
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107
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]
}
] | [] | [] | [] | [] |
split_0_train_196 | split_0_train_196 | [
{
"id": "split_0_train_196_passage",
"type": "progene_text",
"text": [
"CCAAT displacement protein ( CDP ) is a cellular protein which has been shown in other cell types to negatively regulate gene expression in undifferentiated cells but not in differentiated cells ."
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}
] | [
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29,
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}
] | [] | [] | [] |
split_0_train_197 | split_0_train_197 | [
{
"id": "split_0_train_197_passage",
"type": "progene_text",
"text": [
"We have previously shown that a 66 - bp purine - thymidine - rich sequence ( the 66-mer ) binds CDP and negatively regulates the human papillomavirus type 6 ( HPV-6 ) E6 promoter ( S. Pattison , D. G. Skalnik , and A. Roman , J. Virol. 71 : 2013 - 2022 , 1997 ) ."
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167,
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}
] | [] | [] | [] |
split_0_train_198 | split_0_train_198 | [
{
"id": "split_0_train_198_passage",
"type": "progene_text",
"text": [
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225
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}
] | [
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163,
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}
] | [] | [] | [] |
split_0_train_199 | split_0_train_199 | [
{
"id": "split_0_train_199_passage",
"type": "progene_text",
"text": [
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}
] | [
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] | [] | [] | [] |