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167 | BioInfer.d117.s0 | [
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"type": "Sentence",
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"By 1 h the cells were well spread with straight actin bundles many of which ended at more central sites terminating on patches containing vinculin and talin; thus the cells assemble typical stress fibers but do not appear to polarize."
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168 | BioInfer.d118.s0 | [
{
"id": "BioInfer.d118.s0__text",
"type": "Sentence",
"text": [
"By indirect immunofluorescence, both R. rickettsii and Listeria monocytogenes actin tails were shown to contain the cytoskeletal proteins vasodilator-stimulated phosphoprotein profilin, vinculin, and filamin."
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169 | BioInfer.d119.s0 | [
{
"id": "BioInfer.d119.s0__text",
"type": "Sentence",
"text": [
"By site-directed mutagenesis of profilin II from Dictyostelium discoideum the point mutations K114E and W3N were generated by PCR thus changing actin and poly-(L)-proline-binding activity respectively."
],
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0,
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170 | BioInfer.d119.s1 | [
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"id": "BioInfer.d119.s1__text",
"type": "Sentence",
"text": [
"The K114E profilin exhibited a profound decrease in its ability to interact with actin, whereas binding to poly-(L)-proline was essentially unchanged."
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0,
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171 | BioInfer.d121.s0 | [
{
"id": "BioInfer.d121.s0__text",
"type": "Sentence",
"text": [
"By this method, it was shown that four of these large RNA species are polycistronic transcripts containing sequences from two genes: one species contains nucleocapsid protein (NP) and phosphoprotein (P) gene sequences; another, P and membrane protein (M) gene sequences; another, M and fusion protein (F0) gene sequences; and another, F0 and hemagglutinin-neuraminidase protein (HN) gene sequences."
],
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0,
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280,
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172 | BioInfer.d122.s0 | [
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"By two-hybrid screening we have identified two partners that directly associate with TIF34: PRT1, a previously characterized eIF3 subunit, and a novel protein of 33 kDa (eIF3-p33) which is part of the eIF3 complex and has an RNA binding domain."
],
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0,
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173 | BioInfer.d122.s1 | [
{
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0,
139
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174 | BioInfer.d123.s0 | [
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"By using a chromatin immunoprecipitation (ChIP) assay, we observed that histone H4, and not histone H3, was acetylated from the endogenous p21/waf1 promoter in vivo, implying that CBP/p300, and not the SAGA complex, was critical in complexing with E2A in up-regulation of p21/waf1 in HTLV-1-infected cells."
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175 | BioInfer.d124.s0 | [
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0,
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176 | BioInfer.d124.s1 | [
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177 | BioInfer.d126.s0 | [
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"type": "Sentence",
"text": [
"Calorimetric data show ternary complex formation between talin, vinculin, and actin."
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[
0,
84
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] | [
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78,
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64,
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57,
62
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178 | BioInfer.d127.s0 | [
{
"id": "BioInfer.d127.s0__text",
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0,
133
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68,
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0,
7
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] |
179 | BioInfer.d129.s0 | [
{
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"CD26, a T cell activation Ag, also known as dipeptidyl peptidase IV, is directly associated with adenosine deaminase (ADA) on the surface of T cells and T cell lines."
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[
0,
166
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] | [
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0,
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44,
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"text": [
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97,
116
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] |
180 | BioInfer.d130.s0 | [
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],
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[
0,
112
]
]
}
] | [
{
"id": "BioInfer.d130.s0.e0",
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0,
4
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79,
102
]
],
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}
] | [] | [] | [
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] |
181 | BioInfer.d131.s0 | [
{
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"CD26 is a T cell activation antigen that contains dipeptidyl peptidase IV activity and is known to bind adenosine deaminase."
],
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[
0,
124
]
]
}
] | [
{
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"dipeptidyl peptidase IV"
],
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50,
73
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104,
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"CD26"
],
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[
0,
4
]
],
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}
] | [] | [] | [
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] |
182 | BioInfer.d133.s0 | [
{
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],
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[
0,
127
]
]
}
] | [
{
"id": "BioInfer.d133.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"actomyosin"
],
"offsets": [
[
75,
85
]
],
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}
] | [] | [] | [] |
183 | BioInfer.d134.s0 | [
{
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"type": "Sentence",
"text": [
"Changes in beta-catenin binding to cadherin or APC protein, and the ensuing effects on cell morphology and adhesion, are independent of beta-catenin binding to alpha-catenin."
],
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[
0,
174
]
]
}
] | [
{
"id": "BioInfer.d134.s0.e0",
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],
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35,
43
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160,
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136,
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47,
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] |
184 | BioInfer.d134.s1 | [
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"text": [
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],
"offsets": [
[
0,
324
]
]
}
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177,
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221,
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26,
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111,
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122,
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26,
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91,
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12,
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137,
150
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] |
185 | BioInfer.d135.s0 | [
{
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0,
130
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]
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20,
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75,
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] |
186 | BioInfer.d135.s1 | [
{
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0,
164
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13,
21
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] |
187 | BioInfer.d135.s2 | [
{
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0,
132
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114,
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188 | BioInfer.d136.s0 | [
{
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0,
104
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189 | BioInfer.d137.s0 | [
{
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0,
120
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190 | BioInfer.d139.s0 | [
{
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0,
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191 | BioInfer.d139.s1 | [
{
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],
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0,
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47,
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192 | BioInfer.d140.s0 | [
{
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0,
102
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59,
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77,
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] |
193 | BioInfer.d140.s1 | [
{
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],
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[
0,
171
]
]
}
] | [
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136,
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157,
170
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] |
194 | BioInfer.d140.s2 | [
{
"id": "BioInfer.d140.s2__text",
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],
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0,
192
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]
}
] | [
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16,
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0,
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141,
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150,
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106,
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173,
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93,
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] |
195 | BioInfer.d141.s0 | [
{
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0,
227
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]
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194,
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206,
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53,
58
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],
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}
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"arg2_id": "BioInfer.d141.s0.e2",
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}
] |
196 | BioInfer.d142.s0 | [
{
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"type": "Sentence",
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"Chick embryo fibroblasts contain about 75-100 microM unpolymerized actin and at least four proteins which can bind actin monomers, actin depolymerizing factor (ADF), gelsolin, profilin, and thymosin beta4 (Tbeta4)."
],
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[
0,
214
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]
}
] | [
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115,
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{
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190,
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{
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166,
174
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{
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160,
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131,
158
]
],
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}
] | [] | [] | [
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}
] |
197 | BioInfer.d143.s0 | [
{
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],
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[
0,
122
]
]
}
] | [
{
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104,
121
]
],
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{
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89,
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],
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{
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"text": [
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],
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0,
18
]
],
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}
] | [] | [] | [
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}
] |
198 | BioInfer.d143.s1 | [
{
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],
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[
0,
126
]
]
}
] | [
{
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],
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] | [] | [] | [
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}
] |
199 | BioInfer.d143.s2 | [
{
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[
0,
149
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]
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200 | BioInfer.d144.s0 | [
{
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],
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0,
94
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]
}
] | [
{
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20,
23
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],
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] | [] | [] | [
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] |
201 | BioInfer.d144.s1 | [
{
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"type": "Sentence",
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0,
249
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]
}
] | [
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30
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],
"normalized": []
},
{
"id": "BioInfer.d144.s1.e1",
"type": "Gene/protein/RNA",
"text": [
"VITF-3"
],
"offsets": [
[
180,
186
]
],
"normalized": []
},
{
"id": "BioInfer.d144.s1.e2",
"type": "Gene/protein/RNA",
"text": [
"A8R"
],
"offsets": [
[
18,
21
]
],
"normalized": []
}
] | [] | [] | [] |
202 | BioInfer.d144.s2 | [
{
"id": "BioInfer.d144.s2__text",
"type": "Sentence",
"text": [
"We found that the 34- and 45-kDa polypeptides encoded by vaccinia virus ORFs A8R and A23R, respectively, were necessary to reconstitute transcription of a template with an intermediate stage promoter."
],
"offsets": [
[
0,
200
]
]
}
] | [
{
"id": "BioInfer.d144.s2.e0",
"type": "Gene/protein/RNA",
"text": [
"A8R"
],
"offsets": [
[
77,
80
]
],
"normalized": []
},
{
"id": "BioInfer.d144.s2.e1",
"type": "Gene/protein/RNA",
"text": [
"A23R"
],
"offsets": [
[
85,
89
]
],
"normalized": []
}
] | [] | [] | [] |
203 | BioInfer.d147.s0 | [
{
"id": "BioInfer.d147.s0__text",
"type": "Sentence",
"text": [
"Cofilin was identified by peptide sequencing, and cofilin recruitment and Listeria tail length were found to be pH-dependent, in agreement with its recently reported role in enhancing actin filament turnover."
],
"offsets": [
[
0,
208
]
]
}
] | [
{
"id": "BioInfer.d147.s0.e0",
"type": "Individual_protein",
"text": [
"Cofilin"
],
"offsets": [
[
0,
7
]
],
"normalized": []
},
{
"id": "BioInfer.d147.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"cofilin"
],
"offsets": [
[
50,
57
]
],
"normalized": []
},
{
"id": "BioInfer.d147.s0.e2",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
184,
189
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d147.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d147.s0.e0",
"arg2_id": "BioInfer.d147.s0.e2",
"normalized": []
}
] |
204 | BioInfer.d148.s0 | [
{
"id": "BioInfer.d148.s0__text",
"type": "Sentence",
"text": [
"Compared with control and contralateral kidneys, the ligated kidneys displayed a dynamic expression of mRNAs for many apoptosis-related molecules, which included an up to threefold increase for Fas, Fas ligand, TNF-R1, TRAIL, TRADD, RIP, and caspase-8, and an up to twofold increase for FADD and FAP, but there was little change for FAF."
],
"offsets": [
[
0,
337
]
]
}
] | [
{
"id": "BioInfer.d148.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"caspase-8"
],
"offsets": [
[
242,
251
]
],
"normalized": []
},
{
"id": "BioInfer.d148.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"TRAIL"
],
"offsets": [
[
219,
224
]
],
"normalized": []
},
{
"id": "BioInfer.d148.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"FAP"
],
"offsets": [
[
296,
299
]
],
"normalized": []
},
{
"id": "BioInfer.d148.s0.e3",
"type": "Gene/protein/RNA",
"text": [
"RIP"
],
"offsets": [
[
233,
236
]
],
"normalized": []
},
{
"id": "BioInfer.d148.s0.e4",
"type": "Gene/protein/RNA",
"text": [
"TNF-R1"
],
"offsets": [
[
211,
217
]
],
"normalized": []
},
{
"id": "BioInfer.d148.s0.e5",
"type": "Gene/protein/RNA",
"text": [
"Fas"
],
"offsets": [
[
194,
197
]
],
"normalized": []
},
{
"id": "BioInfer.d148.s0.e6",
"type": "Gene/protein/RNA",
"text": [
"TRADD"
],
"offsets": [
[
226,
231
]
],
"normalized": []
},
{
"id": "BioInfer.d148.s0.e7",
"type": "Gene/protein/RNA",
"text": [
"Fas ligand"
],
"offsets": [
[
199,
209
]
],
"normalized": []
},
{
"id": "BioInfer.d148.s0.e8",
"type": "Gene/protein/RNA",
"text": [
"FAF"
],
"offsets": [
[
333,
336
]
],
"normalized": []
},
{
"id": "BioInfer.d148.s0.e9",
"type": "Gene/protein/RNA",
"text": [
"FADD"
],
"offsets": [
[
287,
291
]
],
"normalized": []
}
] | [] | [] | [] |
205 | BioInfer.d148.s1 | [
{
"id": "BioInfer.d148.s1__text",
"type": "Sentence",
"text": [
"To detect the expression of apoptosis-related molecules, ribonuclease protection assay was used with specific antisense RNA probes for Fas, Fas ligand, TNFR-1, TRAIL, FADD, TRADD, RIP, FAF, FAP, and caspase-8."
],
"offsets": [
[
0,
209
]
]
}
] | [
{
"id": "BioInfer.d148.s1.e0",
"type": "Gene/protein/RNA",
"text": [
"TRAIL"
],
"offsets": [
[
160,
165
]
],
"normalized": []
},
{
"id": "BioInfer.d148.s1.e1",
"type": "Gene/protein/RNA",
"text": [
"ribonuclease"
],
"offsets": [
[
57,
69
]
],
"normalized": []
},
{
"id": "BioInfer.d148.s1.e2",
"type": "Gene/protein/RNA",
"text": [
"FAF"
],
"offsets": [
[
185,
188
]
],
"normalized": []
},
{
"id": "BioInfer.d148.s1.e3",
"type": "Gene/protein/RNA",
"text": [
"FAP"
],
"offsets": [
[
190,
193
]
],
"normalized": []
},
{
"id": "BioInfer.d148.s1.e4",
"type": "Gene/protein/RNA",
"text": [
"TRADD"
],
"offsets": [
[
173,
178
]
],
"normalized": []
},
{
"id": "BioInfer.d148.s1.e5",
"type": "Gene/protein/RNA",
"text": [
"RIP"
],
"offsets": [
[
180,
183
]
],
"normalized": []
},
{
"id": "BioInfer.d148.s1.e6",
"type": "Gene/protein/RNA",
"text": [
"caspase-8"
],
"offsets": [
[
199,
208
]
],
"normalized": []
},
{
"id": "BioInfer.d148.s1.e7",
"type": "Gene/protein/RNA",
"text": [
"FADD"
],
"offsets": [
[
167,
171
]
],
"normalized": []
},
{
"id": "BioInfer.d148.s1.e8",
"type": "Gene/protein/RNA",
"text": [
"Fas ligand"
],
"offsets": [
[
140,
150
]
],
"normalized": []
},
{
"id": "BioInfer.d148.s1.e9",
"type": "Gene/protein/RNA",
"text": [
"TNFR-1"
],
"offsets": [
[
152,
158
]
],
"normalized": []
},
{
"id": "BioInfer.d148.s1.e10",
"type": "Gene/protein/RNA",
"text": [
"Fas"
],
"offsets": [
[
135,
138
]
],
"normalized": []
}
] | [] | [] | [] |
206 | BioInfer.d149.s0 | [
{
"id": "BioInfer.d149.s0__text",
"type": "Sentence",
"text": [
"Complete gene sequences for the nucleocapsid protein (N) and phosphoprotein (P/V) have been determined and recombinant N and V proteins produced in baculovirus."
],
"offsets": [
[
0,
160
]
]
}
] | [
{
"id": "BioInfer.d149.s0.e0",
"type": "Individual_protein",
"text": [
"N"
],
"offsets": [
[
54,
55
]
],
"normalized": []
},
{
"id": "BioInfer.d149.s0.e1",
"type": "Individual_protein",
"text": [
"V"
],
"offsets": [
[
79,
80
]
],
"normalized": []
},
{
"id": "BioInfer.d149.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"V"
],
"offsets": [
[
125,
126
]
],
"normalized": []
},
{
"id": "BioInfer.d149.s0.e3",
"type": "Individual_protein",
"text": [
"P"
],
"offsets": [
[
77,
78
]
],
"normalized": []
},
{
"id": "BioInfer.d149.s0.e4",
"type": "Gene/protein/RNA",
"text": [
"N"
],
"offsets": [
[
119,
120
]
],
"normalized": []
},
{
"id": "BioInfer.d149.s0.e5",
"type": "Individual_protein",
"text": [
"phosphoprotein"
],
"offsets": [
[
61,
75
]
],
"normalized": []
},
{
"id": "BioInfer.d149.s0.e6",
"type": "Individual_protein",
"text": [
"nucleocapsid protein"
],
"offsets": [
[
32,
52
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d149.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d149.s0.e1",
"arg2_id": "BioInfer.d149.s0.e5",
"normalized": []
},
{
"id": "BioInfer.d149.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d149.s0.e3",
"arg2_id": "BioInfer.d149.s0.e5",
"normalized": []
}
] |
207 | BioInfer.d150.s0 | [
{
"id": "BioInfer.d150.s0__text",
"type": "Sentence",
"text": [
"CONCLUSIONS: The expression of alpha-catenin, beta-catenin, and gamma-catenin is related to histological type and differentiation in NSCLC, although catenins have no independent prognostic value."
],
"offsets": [
[
0,
195
]
]
}
] | [
{
"id": "BioInfer.d150.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"catenins"
],
"offsets": [
[
149,
157
]
],
"normalized": []
},
{
"id": "BioInfer.d150.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"beta-catenin"
],
"offsets": [
[
46,
58
]
],
"normalized": []
},
{
"id": "BioInfer.d150.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"gamma-catenin"
],
"offsets": [
[
64,
77
]
],
"normalized": []
},
{
"id": "BioInfer.d150.s0.e3",
"type": "Gene/protein/RNA",
"text": [
"alpha-catenin"
],
"offsets": [
[
31,
44
]
],
"normalized": []
}
] | [] | [] | [] |
208 | BioInfer.d150.s1 | [
{
"id": "BioInfer.d150.s1__text",
"type": "Sentence",
"text": [
"Reduced expression of alpha-catenin, beta-catenin, and gamma-catenin is associated with high cell proliferative activity and poor differentiation in non-small cell lung cancer."
],
"offsets": [
[
0,
176
]
]
}
] | [
{
"id": "BioInfer.d150.s1.e0",
"type": "Gene/protein/RNA",
"text": [
"gamma-catenin"
],
"offsets": [
[
55,
68
]
],
"normalized": []
},
{
"id": "BioInfer.d150.s1.e1",
"type": "Gene/protein/RNA",
"text": [
"alpha-catenin"
],
"offsets": [
[
22,
35
]
],
"normalized": []
},
{
"id": "BioInfer.d150.s1.e2",
"type": "Gene/protein/RNA",
"text": [
"beta-catenin"
],
"offsets": [
[
37,
49
]
],
"normalized": []
}
] | [] | [] | [] |
209 | BioInfer.d151.s0 | [
{
"id": "BioInfer.d151.s0__text",
"type": "Sentence",
"text": [
"CONCLUSIONS: These results suggest the cooperative modulation of the actin cytoskeleton by cofilin and Aip1."
],
"offsets": [
[
0,
108
]
]
}
] | [
{
"id": "BioInfer.d151.s0.e0",
"type": "Individual_protein",
"text": [
"Aip1"
],
"offsets": [
[
103,
107
]
],
"normalized": []
},
{
"id": "BioInfer.d151.s0.e1",
"type": "Individual_protein",
"text": [
"cofilin"
],
"offsets": [
[
91,
98
]
],
"normalized": []
},
{
"id": "BioInfer.d151.s0.e2",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
69,
74
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d151.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d151.s0.e0",
"arg2_id": "BioInfer.d151.s0.e1",
"normalized": []
},
{
"id": "BioInfer.d151.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d151.s0.e0",
"arg2_id": "BioInfer.d151.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d151.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d151.s0.e1",
"arg2_id": "BioInfer.d151.s0.e2",
"normalized": []
}
] |
210 | BioInfer.d151.s1 | [
{
"id": "BioInfer.d151.s1__text",
"type": "Sentence",
"text": [
"Immunofluorescence staining of a wild-type strain using anti-Aip1 antibodies revealed that Aip1 was distributed in cortical actin patches where cofilin was also co-localized."
],
"offsets": [
[
0,
174
]
]
}
] | [
{
"id": "BioInfer.d151.s1.e0",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
124,
129
]
],
"normalized": []
},
{
"id": "BioInfer.d151.s1.e1",
"type": "Individual_protein",
"text": [
"cofilin"
],
"offsets": [
[
144,
151
]
],
"normalized": []
},
{
"id": "BioInfer.d151.s1.e2",
"type": "Individual_protein",
"text": [
"Aip1"
],
"offsets": [
[
91,
95
]
],
"normalized": []
},
{
"id": "BioInfer.d151.s1.e3",
"type": "Gene/protein/RNA",
"text": [
"Aip1"
],
"offsets": [
[
61,
65
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d151.s1.i0",
"type": "PPI",
"arg1_id": "BioInfer.d151.s1.e0",
"arg2_id": "BioInfer.d151.s1.e1",
"normalized": []
},
{
"id": "BioInfer.d151.s1.i1",
"type": "PPI",
"arg1_id": "BioInfer.d151.s1.e0",
"arg2_id": "BioInfer.d151.s1.e2",
"normalized": []
}
] |
211 | BioInfer.d153.s0 | [
{
"id": "BioInfer.d153.s0__text",
"type": "Sentence",
"text": [
"Confluent calf pulmonary artery endothelial monolayers exposed to 95% oxygen for 1, 2, or 3 days exhibit a time-dependent increase in adherence to substratum, which closely parallels changes in actin cytoarchitecture and the distribution of focal contact proteins vinculin and talin."
],
"offsets": [
[
0,
283
]
]
}
] | [
{
"id": "BioInfer.d153.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"actin"
],
"offsets": [
[
194,
199
]
],
"normalized": []
},
{
"id": "BioInfer.d153.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"talin"
],
"offsets": [
[
277,
282
]
],
"normalized": []
},
{
"id": "BioInfer.d153.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"vinculin"
],
"offsets": [
[
264,
272
]
],
"normalized": []
}
] | [] | [] | [] |
212 | BioInfer.d154.s0 | [
{
"id": "BioInfer.d154.s0__text",
"type": "Sentence",
"text": [
"Conversely, inhibition of LIMK's activity by expressing a dominant negative construct, LIMK1-, or expression of the constitutively active S3A cofilin mutant induces loss of actin filaments at the phagocytic cup and also inhibits phagocytosis."
],
"offsets": [
[
0,
242
]
]
}
] | [
{
"id": "BioInfer.d154.s0.e0",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
173,
178
]
],
"normalized": []
},
{
"id": "BioInfer.d154.s0.e1",
"type": "Individual_protein",
"text": [
"LIMK"
],
"offsets": [
[
26,
30
]
],
"normalized": []
},
{
"id": "BioInfer.d154.s0.e2",
"type": "Individual_protein",
"text": [
"cofilin"
],
"offsets": [
[
142,
149
]
],
"normalized": []
},
{
"id": "BioInfer.d154.s0.e3",
"type": "Individual_protein",
"text": [
"LIMK1-"
],
"offsets": [
[
87,
93
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d154.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d154.s0.e0",
"arg2_id": "BioInfer.d154.s0.e1",
"normalized": []
},
{
"id": "BioInfer.d154.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d154.s0.e0",
"arg2_id": "BioInfer.d154.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d154.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d154.s0.e0",
"arg2_id": "BioInfer.d154.s0.e3",
"normalized": []
},
{
"id": "BioInfer.d154.s0.i3",
"type": "PPI",
"arg1_id": "BioInfer.d154.s0.e1",
"arg2_id": "BioInfer.d154.s0.e3",
"normalized": []
}
] |
213 | BioInfer.d155.s0 | [
{
"id": "BioInfer.d155.s0__text",
"type": "Sentence",
"text": [
"Co-precipitation experiments using whole cell lysates indicate that the mutant form of alpha-catenin binds beta-catenin and plakoglobin, and can form a structural complex with E-cadherin via these interactions."
],
"offsets": [
[
0,
210
]
]
}
] | [
{
"id": "BioInfer.d155.s0.e0",
"type": "Individual_protein",
"text": [
"alpha-catenin"
],
"offsets": [
[
87,
100
]
],
"normalized": []
},
{
"id": "BioInfer.d155.s0.e1",
"type": "Individual_protein",
"text": [
"E-cadherin"
],
"offsets": [
[
176,
186
]
],
"normalized": []
},
{
"id": "BioInfer.d155.s0.e2",
"type": "Individual_protein",
"text": [
"beta-catenin"
],
"offsets": [
[
107,
119
]
],
"normalized": []
},
{
"id": "BioInfer.d155.s0.e3",
"type": "Individual_protein",
"text": [
"plakoglobin"
],
"offsets": [
[
124,
135
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d155.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d155.s0.e0",
"arg2_id": "BioInfer.d155.s0.e1",
"normalized": []
},
{
"id": "BioInfer.d155.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d155.s0.e0",
"arg2_id": "BioInfer.d155.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d155.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d155.s0.e0",
"arg2_id": "BioInfer.d155.s0.e3",
"normalized": []
},
{
"id": "BioInfer.d155.s0.i3",
"type": "PPI",
"arg1_id": "BioInfer.d155.s0.e1",
"arg2_id": "BioInfer.d155.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d155.s0.i4",
"type": "PPI",
"arg1_id": "BioInfer.d155.s0.e1",
"arg2_id": "BioInfer.d155.s0.e3",
"normalized": []
}
] |
214 | BioInfer.d156.s0 | [
{
"id": "BioInfer.d156.s0__text",
"type": "Sentence",
"text": [
"Coprecipitations revealed that transfected cadherin molecules are complexed with alpha-catenin and beta-catenin at plasma membranes."
],
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[
0,
132
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}
] | [
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"id": "BioInfer.d156.s0.e0",
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"beta-catenin"
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99,
111
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"id": "BioInfer.d156.s0.e1",
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81,
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"id": "BioInfer.d156.s0.e2",
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"text": [
"cadherin"
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43,
51
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215 | BioInfer.d157.s0 | [
{
"id": "BioInfer.d157.s0__text",
"type": "Sentence",
"text": [
"Cotransfections with different combinations of these genes demonstrated that a subset of four of them, coding for the HSV helicase-primase complex (UL5, UL8, UL52) and the major DNA-binding protein (UL29), was already sufficient to mediate the helper effect."
],
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[
0,
258
]
]
}
] | [
{
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"helicase-primase"
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122,
138
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"UL29"
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199,
203
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{
"id": "BioInfer.d157.s0.e2",
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158,
162
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172,
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148,
151
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"UL8"
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153,
156
]
],
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"arg1_id": "BioInfer.d157.s0.e4",
"arg2_id": "BioInfer.d157.s0.e5",
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}
] |
216 | BioInfer.d158.s0 | [
{
"id": "BioInfer.d158.s0__text",
"type": "Sentence",
"text": [
"Crystallization and preliminary crystallographic analysis of the N-terminal actin binding domain of human fimbrin."
],
"offsets": [
[
0,
114
]
]
}
] | [
{
"id": "BioInfer.d158.s0.e0",
"type": "Individual_protein",
"text": [
"fimbrin"
],
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106,
113
]
],
"normalized": []
},
{
"id": "BioInfer.d158.s0.e1",
"type": "Individual_protein",
"text": [
"actin"
],
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[
76,
81
]
],
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}
] | [] | [] | [
{
"id": "BioInfer.d158.s0.i0",
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"arg2_id": "BioInfer.d158.s0.e1",
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}
] |
217 | BioInfer.d159.s0 | [
{
"id": "BioInfer.d159.s0__text",
"type": "Sentence",
"text": [
"CV-1 cells were transfected with cloned genes from wild-type HPIV-3 encoding the large protein (L), phosphoprotein (P), and nucleocapsid protein (NP), alone or together, for the expression of biologically active proteins."
],
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[
0,
221
]
]
}
] | [
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"id": "BioInfer.d159.s0.e0",
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96,
97
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{
"id": "BioInfer.d159.s0.e1",
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146,
148
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{
"id": "BioInfer.d159.s0.e2",
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124,
144
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{
"id": "BioInfer.d159.s0.e3",
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81,
94
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116,
117
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{
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"text": [
"phosphoprotein"
],
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[
100,
114
]
],
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}
] | [] | [] | [] |
218 | BioInfer.d160.s0 | [
{
"id": "BioInfer.d160.s0__text",
"type": "Sentence",
"text": [
"Cytoplasmic staining included stress fibers that colocalized with actin, probably as a consequence of the myosin heavy chain component of the fusion protein."
],
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[
0,
157
]
]
}
] | [
{
"id": "BioInfer.d160.s0.e0",
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66,
71
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{
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"myosin heavy chain"
],
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106,
124
]
],
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}
] | [] | [] | [
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}
] |
219 | BioInfer.d161.s0 | [
{
"id": "BioInfer.d161.s0__text",
"type": "Sentence",
"text": [
"Data from affinity chromatography, analytical ultracentrifugation, covalent cross-linking, and fluorescence anisotropy show that profilin, thymosin beta(4), and actin form a ternary complex."
],
"offsets": [
[
0,
190
]
]
}
] | [
{
"id": "BioInfer.d161.s0.e0",
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"text": [
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139,
155
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{
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161,
166
]
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{
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"type": "Individual_protein",
"text": [
"profilin"
],
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129,
137
]
],
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] | [] | [] | [
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"arg2_id": "BioInfer.d161.s0.e2",
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}
] |
220 | BioInfer.d161.s1 | [
{
"id": "BioInfer.d161.s1__text",
"type": "Sentence",
"text": [
"Experiments using a peptide that corresponds to the N-terminus of thymosin beta(4) (residues 6-22) confirm the presence of an extensive binding surface between actin and thymosin beta(4), and explain why thymosin beta(4) and profilin can bind simultaneously to actin."
],
"offsets": [
[
0,
267
]
]
}
] | [
{
"id": "BioInfer.d161.s1.e0",
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261,
266
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204,
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160,
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170,
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],
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225,
233
]
],
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}
] | [] | [] | [
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}
] |
221 | BioInfer.d162.s0 | [
{
"id": "BioInfer.d162.s0__text",
"type": "Sentence",
"text": [
"Data is presented to suggest that the G1 cyclin D1 and the cyclin-dependent kinase inhibitor p27KIP1 may be involved in subversion of the G1/S traverse by signaling pathways activated by HER-2 function."
],
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[
0,
202
]
]
}
] | [
{
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41,
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187,
192
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{
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],
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59,
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]
],
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] | [] | [] | [
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] |
222 | BioInfer.d163.s0 | [
{
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"type": "Sentence",
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"Data presented here suggest that two of the repressed genes encode the proteins actin and myosin heavy chain."
],
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0,
109
]
]
}
] | [
{
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"actin"
],
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80,
85
]
],
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}
] | [] | [] | [] |
223 | BioInfer.d163.s1 | [
{
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"type": "Sentence",
"text": [
"Selective repression of actin and myosin heavy chain expression during the programmed death of insect skeletal muscle."
],
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[
0,
118
]
]
}
] | [
{
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34,
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"actin"
],
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24,
29
]
],
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}
] | [] | [] | [] |
224 | BioInfer.d163.s2 | [
{
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"type": "Sentence",
"text": [
"The reduction in actin and myosin heavy chain synthesis presumably plays a role in the rapid dissolution of the muscles."
],
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[
0,
120
]
]
}
] | [
{
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27,
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],
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17,
22
]
],
"normalized": []
}
] | [] | [] | [] |
225 | BioInfer.d164.s0 | [
{
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"type": "Sentence",
"text": [
"Death receptors belong to the TNF receptor family and are characterised by an intracellular death domain that serves to recruit adapter proteins such as TRADD and FADD and cysteine proteases such as Caspase-8."
],
"offsets": [
[
0,
209
]
]
}
] | [
{
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],
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0,
15
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199,
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153,
158
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{
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163,
167
]
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{
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172,
190
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{
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"type": "Protein_family_or_group",
"text": [
"TNF receptor"
],
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[
30,
42
]
],
"normalized": []
}
] | [] | [] | [
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] |
226 | BioInfer.d165.s0 | [
{
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],
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[
0,
129
]
]
}
] | [
{
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"SIR2"
],
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53,
57
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],
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{
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73,
77
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{
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81,
85
]
],
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}
] | [] | [] | [] |
227 | BioInfer.d166.s0 | [
{
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"type": "Sentence",
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],
"offsets": [
[
0,
100
]
]
}
] | [
{
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27,
32
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{
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17,
22
]
],
"normalized": []
}
] | [] | [] | [] |
228 | BioInfer.d166.s1 | [
{
"id": "BioInfer.d166.s1__text",
"type": "Sentence",
"text": [
"rad59 mutations completely abolished the ability to generate type II survivors, while rad50 mutations decreased the growth viability of type II survivors but did not completely eliminate their appearance."
],
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[
0,
204
]
]
}
] | [
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"rad59"
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0,
5
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"type": "Gene/protein/RNA",
"text": [
"rad50"
],
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[
86,
91
]
],
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}
] | [] | [] | [] |
229 | BioInfer.d167.s0 | [
{
"id": "BioInfer.d167.s0__text",
"type": "Sentence",
"text": [
"Deletion of SIR4 enhanced mURA3 and MET15 silencing, but deletion of SIR1 or SIR3 did not affect silencing, indicating that the mechanism of silencing differs from that at telomeres and silent mating loci."
],
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[
0,
205
]
]
}
] | [
{
"id": "BioInfer.d167.s0.e0",
"type": "Gene",
"text": [
"mURA3"
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26,
31
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},
{
"id": "BioInfer.d167.s0.e1",
"type": "Gene",
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12,
16
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},
{
"id": "BioInfer.d167.s0.e2",
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"SIR3"
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77,
81
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{
"id": "BioInfer.d167.s0.e3",
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69,
73
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{
"id": "BioInfer.d167.s0.e4",
"type": "Gene",
"text": [
"MET15"
],
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36,
41
]
],
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}
] | [] | [] | [
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"id": "BioInfer.d167.s0.i0",
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"arg2_id": "BioInfer.d167.s0.e1",
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{
"id": "BioInfer.d167.s0.i1",
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"arg2_id": "BioInfer.d167.s0.e2",
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{
"id": "BioInfer.d167.s0.i2",
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{
"id": "BioInfer.d167.s0.i3",
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"arg2_id": "BioInfer.d167.s0.e4",
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{
"id": "BioInfer.d167.s0.i4",
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"arg1_id": "BioInfer.d167.s0.e2",
"arg2_id": "BioInfer.d167.s0.e4",
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{
"id": "BioInfer.d167.s0.i5",
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"arg1_id": "BioInfer.d167.s0.e3",
"arg2_id": "BioInfer.d167.s0.e4",
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}
] |
230 | BioInfer.d168.s0 | [
{
"id": "BioInfer.d168.s0__text",
"type": "Sentence",
"text": [
"Demembranated stereociliary cores consisted primarily of protein bands corresponding to actin and fimbrin and several proteins ranging from 43 to 63 kDa."
],
"offsets": [
[
0,
153
]
]
}
] | [
{
"id": "BioInfer.d168.s0.e0",
"type": "Individual_protein",
"text": [
"fimbrin"
],
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[
98,
105
]
],
"normalized": []
},
{
"id": "BioInfer.d168.s0.e1",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
88,
93
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d168.s0.i0",
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"arg1_id": "BioInfer.d168.s0.e0",
"arg2_id": "BioInfer.d168.s0.e1",
"normalized": []
}
] |
231 | BioInfer.d169.s0 | [
{
"id": "BioInfer.d169.s0__text",
"type": "Sentence",
"text": [
"Depending on the nature of the divalent cation, recombinant plant (birch) profilin exhibited two different modes of interaction with actin, like mammalian profilin."
],
"offsets": [
[
0,
164
]
]
}
] | [
{
"id": "BioInfer.d169.s0.e0",
"type": "Individual_protein",
"text": [
"actin"
],
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133,
138
]
],
"normalized": []
},
{
"id": "BioInfer.d169.s0.e1",
"type": "Individual_protein",
"text": [
"profilin"
],
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[
74,
82
]
],
"normalized": []
},
{
"id": "BioInfer.d169.s0.e2",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
155,
163
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d169.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d169.s0.e0",
"arg2_id": "BioInfer.d169.s0.e1",
"normalized": []
},
{
"id": "BioInfer.d169.s0.i1",
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"arg1_id": "BioInfer.d169.s0.e0",
"arg2_id": "BioInfer.d169.s0.e2",
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}
] |
232 | BioInfer.d169.s1 | [
{
"id": "BioInfer.d169.s1__text",
"type": "Sentence",
"text": [
"In the presence of magnesium ions birch profilin promoted the polymerization of actin from A:Tbeta4."
],
"offsets": [
[
0,
100
]
]
}
] | [
{
"id": "BioInfer.d169.s1.e0",
"type": "Individual_protein",
"text": [
"A"
],
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[
91,
92
]
],
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},
{
"id": "BioInfer.d169.s1.e1",
"type": "Individual_protein",
"text": [
"actin"
],
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80,
85
]
],
"normalized": []
},
{
"id": "BioInfer.d169.s1.e2",
"type": "Individual_protein",
"text": [
"profilin"
],
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40,
48
]
],
"normalized": []
},
{
"id": "BioInfer.d169.s1.e3",
"type": "Individual_protein",
"text": [
"Tbeta4"
],
"offsets": [
[
93,
99
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d169.s1.i0",
"type": "PPI",
"arg1_id": "BioInfer.d169.s1.e0",
"arg2_id": "BioInfer.d169.s1.e1",
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{
"id": "BioInfer.d169.s1.i1",
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"arg2_id": "BioInfer.d169.s1.e3",
"normalized": []
},
{
"id": "BioInfer.d169.s1.i2",
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"arg2_id": "BioInfer.d169.s1.e2",
"normalized": []
},
{
"id": "BioInfer.d169.s1.i3",
"type": "PPI",
"arg1_id": "BioInfer.d169.s1.e1",
"arg2_id": "BioInfer.d169.s1.e3",
"normalized": []
}
] |
233 | BioInfer.d169.s2 | [
{
"id": "BioInfer.d169.s2__text",
"type": "Sentence",
"text": [
"Recombinant plant (birch) profilin was analyzed for its ability to promote actin polymerization from the actin:thymosin beta4 and beta9 complex."
],
"offsets": [
[
0,
144
]
]
}
] | [
{
"id": "BioInfer.d169.s2.e0",
"type": "Individual_protein",
"text": [
"thymosin",
"beta9"
],
"offsets": [
[
111,
119
],
[
130,
135
]
],
"normalized": []
},
{
"id": "BioInfer.d169.s2.e1",
"type": "Individual_protein",
"text": [
"profilin"
],
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26,
34
]
],
"normalized": []
},
{
"id": "BioInfer.d169.s2.e2",
"type": "Individual_protein",
"text": [
"thymosin beta4"
],
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111,
125
]
],
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},
{
"id": "BioInfer.d169.s2.e3",
"type": "Individual_protein",
"text": [
"actin"
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75,
80
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},
{
"id": "BioInfer.d169.s2.e4",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
105,
110
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d169.s2.i0",
"type": "PPI",
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"arg2_id": "BioInfer.d169.s2.e2",
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},
{
"id": "BioInfer.d169.s2.i1",
"type": "PPI",
"arg1_id": "BioInfer.d169.s2.e0",
"arg2_id": "BioInfer.d169.s2.e3",
"normalized": []
},
{
"id": "BioInfer.d169.s2.i2",
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"arg1_id": "BioInfer.d169.s2.e0",
"arg2_id": "BioInfer.d169.s2.e4",
"normalized": []
},
{
"id": "BioInfer.d169.s2.i3",
"type": "PPI",
"arg1_id": "BioInfer.d169.s2.e1",
"arg2_id": "BioInfer.d169.s2.e3",
"normalized": []
},
{
"id": "BioInfer.d169.s2.i4",
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"arg1_id": "BioInfer.d169.s2.e2",
"arg2_id": "BioInfer.d169.s2.e3",
"normalized": []
},
{
"id": "BioInfer.d169.s2.i5",
"type": "PPI",
"arg1_id": "BioInfer.d169.s2.e2",
"arg2_id": "BioInfer.d169.s2.e4",
"normalized": []
},
{
"id": "BioInfer.d169.s2.i6",
"type": "PPI",
"arg1_id": "BioInfer.d169.s2.e3",
"arg2_id": "BioInfer.d169.s2.e4",
"normalized": []
}
] |
234 | BioInfer.d169.s3 | [
{
"id": "BioInfer.d169.s3__text",
"type": "Sentence",
"text": [
"These data indicated a negative co-operativity between the profilin and DNase I binding sites on actin."
],
"offsets": [
[
0,
103
]
]
}
] | [
{
"id": "BioInfer.d169.s3.e0",
"type": "Individual_protein",
"text": [
"DNase I"
],
"offsets": [
[
72,
79
]
],
"normalized": []
},
{
"id": "BioInfer.d169.s3.e1",
"type": "Individual_protein",
"text": [
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],
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59,
67
]
],
"normalized": []
},
{
"id": "BioInfer.d169.s3.e2",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
97,
102
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d169.s3.i0",
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"arg1_id": "BioInfer.d169.s3.e0",
"arg2_id": "BioInfer.d169.s3.e1",
"normalized": []
},
{
"id": "BioInfer.d169.s3.i1",
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"arg1_id": "BioInfer.d169.s3.e0",
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},
{
"id": "BioInfer.d169.s3.i2",
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"arg1_id": "BioInfer.d169.s3.e1",
"arg2_id": "BioInfer.d169.s3.e2",
"normalized": []
}
] |
235 | BioInfer.d170.s0 | [
{
"id": "BioInfer.d170.s0__text",
"type": "Sentence",
"text": [
"Detection of a sequence involved in actin-binding and phosphoinositide-binding in the N-terminal side of cofilin."
],
"offsets": [
[
0,
113
]
]
}
] | [
{
"id": "BioInfer.d170.s0.e0",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
36,
41
]
],
"normalized": []
},
{
"id": "BioInfer.d170.s0.e1",
"type": "Individual_protein",
"text": [
"cofilin"
],
"offsets": [
[
105,
112
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d170.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d170.s0.e0",
"arg2_id": "BioInfer.d170.s0.e1",
"normalized": []
}
] |
236 | BioInfer.d170.s1 | [
{
"id": "BioInfer.d170.s1__text",
"type": "Sentence",
"text": [
"The truncated cofilin molecules produced in E. coli were purified and examined for their actin-binding and PIP2-binding ability."
],
"offsets": [
[
0,
128
]
]
}
] | [
{
"id": "BioInfer.d170.s1.e0",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
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89,
94
]
],
"normalized": []
},
{
"id": "BioInfer.d170.s1.e1",
"type": "Individual_protein",
"text": [
"cofilin"
],
"offsets": [
[
14,
21
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d170.s1.i0",
"type": "PPI",
"arg1_id": "BioInfer.d170.s1.e0",
"arg2_id": "BioInfer.d170.s1.e1",
"normalized": []
}
] |
237 | BioInfer.d171.s0 | [
{
"id": "BioInfer.d171.s0__text",
"type": "Sentence",
"text": [
"Detection of loss of heterozygosity at RAD51, RAD52, RAD54 and BRCA1 and BRCA2 loci in breast cancer: pathological correlations."
],
"offsets": [
[
0,
128
]
]
}
] | [
{
"id": "BioInfer.d171.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"BRCA2"
],
"offsets": [
[
73,
78
]
],
"normalized": []
},
{
"id": "BioInfer.d171.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"RAD52"
],
"offsets": [
[
46,
51
]
],
"normalized": []
},
{
"id": "BioInfer.d171.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"RAD54"
],
"offsets": [
[
53,
58
]
],
"normalized": []
},
{
"id": "BioInfer.d171.s0.e3",
"type": "Gene/protein/RNA",
"text": [
"RAD51"
],
"offsets": [
[
39,
44
]
],
"normalized": []
},
{
"id": "BioInfer.d171.s0.e4",
"type": "Gene/protein/RNA",
"text": [
"BRCA1"
],
"offsets": [
[
63,
68
]
],
"normalized": []
}
] | [] | [] | [] |
238 | BioInfer.d171.s1 | [
{
"id": "BioInfer.d171.s1__text",
"type": "Sentence",
"text": [
"LOH was found in the RAD51 region in 32% of tumours, in the RAD52 region in 16%, in RAD54 in 20% and in the BRCA1 and BRCA2 regions in 49% and 44% respectively."
],
"offsets": [
[
0,
160
]
]
}
] | [
{
"id": "BioInfer.d171.s1.e0",
"type": "Gene/protein/RNA",
"text": [
"BRCA2"
],
"offsets": [
[
118,
123
]
],
"normalized": []
},
{
"id": "BioInfer.d171.s1.e1",
"type": "Gene/protein/RNA",
"text": [
"RAD52"
],
"offsets": [
[
60,
65
]
],
"normalized": []
},
{
"id": "BioInfer.d171.s1.e2",
"type": "Gene/protein/RNA",
"text": [
"RAD54"
],
"offsets": [
[
84,
89
]
],
"normalized": []
},
{
"id": "BioInfer.d171.s1.e3",
"type": "Gene/protein/RNA",
"text": [
"RAD51"
],
"offsets": [
[
21,
26
]
],
"normalized": []
},
{
"id": "BioInfer.d171.s1.e4",
"type": "Gene/protein/RNA",
"text": [
"BRCA1"
],
"offsets": [
[
108,
113
]
],
"normalized": []
}
] | [] | [] | [] |
239 | BioInfer.d171.s2 | [
{
"id": "BioInfer.d171.s2__text",
"type": "Sentence",
"text": [
"We investigate allelic losses in microsatellites of the RAD51, RAD52, RAD54, BRCA1 and BRCA2 regions, and their correlations with nine pathologic parameters in 127 breast carcinomas."
],
"offsets": [
[
0,
182
]
]
}
] | [
{
"id": "BioInfer.d171.s2.e0",
"type": "Gene/protein/RNA",
"text": [
"BRCA1"
],
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[
77,
82
]
],
"normalized": []
},
{
"id": "BioInfer.d171.s2.e1",
"type": "Gene/protein/RNA",
"text": [
"RAD54"
],
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[
70,
75
]
],
"normalized": []
},
{
"id": "BioInfer.d171.s2.e2",
"type": "Gene/protein/RNA",
"text": [
"RAD51"
],
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[
56,
61
]
],
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},
{
"id": "BioInfer.d171.s2.e3",
"type": "Gene/protein/RNA",
"text": [
"BRCA2"
],
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[
87,
92
]
],
"normalized": []
},
{
"id": "BioInfer.d171.s2.e4",
"type": "Gene/protein/RNA",
"text": [
"RAD52"
],
"offsets": [
[
63,
68
]
],
"normalized": []
}
] | [] | [] | [] |
240 | BioInfer.d172.s0 | [
{
"id": "BioInfer.d172.s0__text",
"type": "Sentence",
"text": [
"Developmental changes in actin and myosin heavy chain isoform expression in smooth muscle."
],
"offsets": [
[
0,
90
]
]
}
] | [
{
"id": "BioInfer.d172.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"myosin heavy chain"
],
"offsets": [
[
35,
53
]
],
"normalized": []
},
{
"id": "BioInfer.d172.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"actin"
],
"offsets": [
[
25,
30
]
],
"normalized": []
}
] | [] | [] | [] |
241 | BioInfer.d173.s0 | [
{
"id": "BioInfer.d173.s0__text",
"type": "Sentence",
"text": [
"Digestion of isolated myofibrils with alkaline proteinase resulted in the degradation of myosin heavy chain and actin."
],
"offsets": [
[
0,
118
]
]
}
] | [
{
"id": "BioInfer.d173.s0.e0",
"type": "Individual_protein",
"text": [
"myosin heavy chain"
],
"offsets": [
[
89,
107
]
],
"normalized": []
},
{
"id": "BioInfer.d173.s0.e1",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
112,
117
]
],
"normalized": []
},
{
"id": "BioInfer.d173.s0.e2",
"type": "Individual_protein",
"text": [
"alkaline proteinase"
],
"offsets": [
[
38,
57
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d173.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d173.s0.e0",
"arg2_id": "BioInfer.d173.s0.e2",
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{
"id": "BioInfer.d173.s0.i1",
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"arg1_id": "BioInfer.d173.s0.e1",
"arg2_id": "BioInfer.d173.s0.e2",
"normalized": []
}
] |
242 | BioInfer.d174.s0 | [
{
"id": "BioInfer.d174.s0__text",
"type": "Sentence",
"text": [
"Direct binding of the verprolin-homology domain in N-WASP to actin is essential for cytoskeletal reorganization."
],
"offsets": [
[
0,
112
]
]
}
] | [
{
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243 | BioInfer.d174.s1 | [
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244 | BioInfer.d175.s0 | [
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0,
113
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] |
245 | BioInfer.d175.s1 | [
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168
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28,
32
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}
] | [] | [] | [] |
246 | BioInfer.d177.s0 | [
{
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],
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[
0,
149
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247 | BioInfer.d178.s0 | [
{
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],
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0,
107
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]
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] |
248 | BioInfer.d178.s1 | [
{
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],
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0,
108
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]
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}
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249 | BioInfer.d179.s0 | [
{
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],
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0,
102
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] |
250 | BioInfer.d180.s0 | [
{
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],
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0,
126
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]
}
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103,
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] |
251 | BioInfer.d181.s0 | [
{
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],
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[
0,
162
]
]
}
] | [
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97,
100
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{
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105,
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{
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142,
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],
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] |
252 | BioInfer.d182.s0 | [
{
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],
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[
0,
132
]
]
}
] | [
{
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55,
73
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90,
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75,
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]
],
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{
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100,
110
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],
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] | [] | [] | [] |
253 | BioInfer.d183.s0 | [
{
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"type": "Sentence",
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"Dynamic actin structures stabilized by profilin."
],
"offsets": [
[
0,
48
]
]
}
] | [
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39,
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],
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}
] | [] | [] | [
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"arg2_id": "BioInfer.d183.s0.e1",
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}
] |
254 | BioInfer.d183.s1 | [
{
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],
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[
0,
74
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]
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] | [
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] | [] | [] | [
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"arg2_id": "BioInfer.d183.s1.e1",
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}
] |
255 | BioInfer.d183.s2 | [
{
"id": "BioInfer.d183.s2__text",
"type": "Sentence",
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"While parallel actin bundles crossing the cells are virtually absent in cells overexpressing profilin, the submembranous actin network of these cells is denser than in control cells."
],
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[
0,
182
]
]
}
] | [
{
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15,
20
]
],
"normalized": []
},
{
"id": "BioInfer.d183.s2.e2",
"type": "Gene/protein/RNA",
"text": [
"profilin"
],
"offsets": [
[
93,
101
]
],
"normalized": []
}
] | [] | [] | [] |
256 | BioInfer.d184.s0 | [
{
"id": "BioInfer.d184.s0__text",
"type": "Sentence",
"text": [
"Effects of profilin-annexin I association on some properties of both profilin and annexin I: modification of the inhibitory activity of profilin on actin polymerization and inhibition of the self-association of annexin I and its interactions with liposomes."
],
"offsets": [
[
0,
257
]
]
}
] | [
{
"id": "BioInfer.d184.s0.e0",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
69,
77
]
],
"normalized": []
},
{
"id": "BioInfer.d184.s0.e1",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
11,
19
]
],
"normalized": []
},
{
"id": "BioInfer.d184.s0.e2",
"type": "Individual_protein",
"text": [
"annexin I"
],
"offsets": [
[
20,
29
]
],
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},
{
"id": "BioInfer.d184.s0.e3",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
136,
144
]
],
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},
{
"id": "BioInfer.d184.s0.e4",
"type": "Individual_protein",
"text": [
"annexin I"
],
"offsets": [
[
211,
220
]
],
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},
{
"id": "BioInfer.d184.s0.e5",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
148,
153
]
],
"normalized": []
},
{
"id": "BioInfer.d184.s0.e6",
"type": "Individual_protein",
"text": [
"annexin I"
],
"offsets": [
[
82,
91
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d184.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d184.s0.e0",
"arg2_id": "BioInfer.d184.s0.e1",
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},
{
"id": "BioInfer.d184.s0.i1",
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"arg2_id": "BioInfer.d184.s0.e2",
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},
{
"id": "BioInfer.d184.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d184.s0.e1",
"arg2_id": "BioInfer.d184.s0.e2",
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},
{
"id": "BioInfer.d184.s0.i3",
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"arg2_id": "BioInfer.d184.s0.e3",
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},
{
"id": "BioInfer.d184.s0.i4",
"type": "PPI",
"arg1_id": "BioInfer.d184.s0.e1",
"arg2_id": "BioInfer.d184.s0.e4",
"normalized": []
},
{
"id": "BioInfer.d184.s0.i5",
"type": "PPI",
"arg1_id": "BioInfer.d184.s0.e1",
"arg2_id": "BioInfer.d184.s0.e5",
"normalized": []
},
{
"id": "BioInfer.d184.s0.i6",
"type": "PPI",
"arg1_id": "BioInfer.d184.s0.e1",
"arg2_id": "BioInfer.d184.s0.e6",
"normalized": []
},
{
"id": "BioInfer.d184.s0.i7",
"type": "PPI",
"arg1_id": "BioInfer.d184.s0.e2",
"arg2_id": "BioInfer.d184.s0.e4",
"normalized": []
},
{
"id": "BioInfer.d184.s0.i8",
"type": "PPI",
"arg1_id": "BioInfer.d184.s0.e2",
"arg2_id": "BioInfer.d184.s0.e5",
"normalized": []
},
{
"id": "BioInfer.d184.s0.i9",
"type": "PPI",
"arg1_id": "BioInfer.d184.s0.e2",
"arg2_id": "BioInfer.d184.s0.e6",
"normalized": []
},
{
"id": "BioInfer.d184.s0.i10",
"type": "PPI",
"arg1_id": "BioInfer.d184.s0.e3",
"arg2_id": "BioInfer.d184.s0.e5",
"normalized": []
}
] |
257 | BioInfer.d185.s0 | [
{
"id": "BioInfer.d185.s0__text",
"type": "Sentence",
"text": [
"Effects of macrophage profilin on actin in the presence and absence of acumentin and gelsolin."
],
"offsets": [
[
0,
94
]
]
}
] | [
{
"id": "BioInfer.d185.s0.e0",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
34,
39
]
],
"normalized": []
},
{
"id": "BioInfer.d185.s0.e1",
"type": "Individual_protein",
"text": [
"acumentin"
],
"offsets": [
[
71,
80
]
],
"normalized": []
},
{
"id": "BioInfer.d185.s0.e2",
"type": "Individual_protein",
"text": [
"gelsolin"
],
"offsets": [
[
85,
93
]
],
"normalized": []
},
{
"id": "BioInfer.d185.s0.e3",
"type": "Individual_protein",
"text": [
"macrophage profilin"
],
"offsets": [
[
11,
30
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d185.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d185.s0.e0",
"arg2_id": "BioInfer.d185.s0.e3",
"normalized": []
}
] |
258 | BioInfer.d186.s0 | [
{
"id": "BioInfer.d186.s0__text",
"type": "Sentence",
"text": [
"Effects of mutations of RAD50, RAD51, RAD52, and related genes on illegitimate recombination in Saccharomyces cerevisiae."
],
"offsets": [
[
0,
121
]
]
}
] | [
{
"id": "BioInfer.d186.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"RAD50"
],
"offsets": [
[
24,
29
]
],
"normalized": []
},
{
"id": "BioInfer.d186.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"RAD52"
],
"offsets": [
[
38,
43
]
],
"normalized": []
},
{
"id": "BioInfer.d186.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"RAD51"
],
"offsets": [
[
31,
36
]
],
"normalized": []
}
] | [] | [] | [] |
259 | BioInfer.d187.s0 | [
{
"id": "BioInfer.d187.s0__text",
"type": "Sentence",
"text": [
"Effects of single amino acid substitutions in the actin-binding site on the biological activity of bovine profilin I."
],
"offsets": [
[
0,
117
]
]
}
] | [
{
"id": "BioInfer.d187.s0.e0",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
50,
55
]
],
"normalized": []
},
{
"id": "BioInfer.d187.s0.e1",
"type": "Individual_protein",
"text": [
"profilin I"
],
"offsets": [
[
106,
116
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d187.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d187.s0.e0",
"arg2_id": "BioInfer.d187.s0.e1",
"normalized": []
}
] |
260 | BioInfer.d187.s1 | [
{
"id": "BioInfer.d187.s1__text",
"type": "Sentence",
"text": [
"However, these mutants displayed a lower affinity for actin than wild-type profilin, suggesting that additional putative bonds created this way cannot increase profilin's affinity for actin."
],
"offsets": [
[
0,
190
]
]
}
] | [
{
"id": "BioInfer.d187.s1.e0",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
54,
59
]
],
"normalized": []
},
{
"id": "BioInfer.d187.s1.e1",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
184,
189
]
],
"normalized": []
},
{
"id": "BioInfer.d187.s1.e2",
"type": "Individual_protein",
"text": [
"profilin"
],
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[
75,
83
]
],
"normalized": []
},
{
"id": "BioInfer.d187.s1.e3",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
160,
168
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d187.s1.i0",
"type": "PPI",
"arg1_id": "BioInfer.d187.s1.e0",
"arg2_id": "BioInfer.d187.s1.e2",
"normalized": []
},
{
"id": "BioInfer.d187.s1.i1",
"type": "PPI",
"arg1_id": "BioInfer.d187.s1.e1",
"arg2_id": "BioInfer.d187.s1.e3",
"normalized": []
}
] |
261 | BioInfer.d187.s2 | [
{
"id": "BioInfer.d187.s2__text",
"type": "Sentence",
"text": [
"These results emphasize the highly conserved biological function of profilins with low sequence homology, and correlate specifically their actin-binding capacity with cell motility and proliferation."
],
"offsets": [
[
0,
199
]
]
}
] | [
{
"id": "BioInfer.d187.s2.e0",
"type": "Individual_protein",
"text": [
"profilins"
],
"offsets": [
[
68,
77
]
],
"normalized": []
},
{
"id": "BioInfer.d187.s2.e1",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
139,
144
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d187.s2.i0",
"type": "PPI",
"arg1_id": "BioInfer.d187.s2.e0",
"arg2_id": "BioInfer.d187.s2.e1",
"normalized": []
}
] |
262 | BioInfer.d188.s0 | [
{
"id": "BioInfer.d188.s0__text",
"type": "Sentence",
"text": [
"Electrical stimulation of cardiocyte contraction did not enhance alpha-cardiac actin or myosin heavy chain (alpha+beta) mRNA transcript levels relative to 28S rRNA during the period of rapid growth that occurred over the first 48 hours."
],
"offsets": [
[
0,
236
]
]
}
] | [
{
"id": "BioInfer.d188.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"myosin heavy chain",
"beta"
],
"offsets": [
[
88,
106
],
[
114,
118
]
],
"normalized": []
},
{
"id": "BioInfer.d188.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"myosin heavy chain",
"alpha"
],
"offsets": [
[
88,
106
],
[
108,
113
]
],
"normalized": []
},
{
"id": "BioInfer.d188.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"alpha-cardiac actin"
],
"offsets": [
[
65,
84
]
],
"normalized": []
},
{
"id": "BioInfer.d188.s0.e3",
"type": "Gene/protein/RNA",
"text": [
"28S rRNA"
],
"offsets": [
[
155,
163
]
],
"normalized": []
}
] | [] | [] | [] |
263 | BioInfer.d189.s0 | [
{
"id": "BioInfer.d189.s0__text",
"type": "Sentence",
"text": [
"Elevation of cAMP induced morphologic alterations indicative of changes in the adhesive status of the macrophage, including cell rounding and disassembly of structures that represent points of contact with substrate containing actin and talin."
],
"offsets": [
[
0,
243
]
]
}
] | [
{
"id": "BioInfer.d189.s0.e0",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
227,
232
]
],
"normalized": []
},
{
"id": "BioInfer.d189.s0.e1",
"type": "Individual_protein",
"text": [
"talin"
],
"offsets": [
[
237,
242
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d189.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d189.s0.e0",
"arg2_id": "BioInfer.d189.s0.e1",
"normalized": []
}
] |
264 | BioInfer.d190.s0 | [
{
"id": "BioInfer.d190.s0__text",
"type": "Sentence",
"text": [
"END5 encodes a proline-rich protein (End5p or verprolin) required for a polarised cortical actin cytoskeleton and endocytosis [2,3]."
],
"offsets": [
[
0,
132
]
]
}
] | [
{
"id": "BioInfer.d190.s0.e0",
"type": "Individual_protein",
"text": [
"End5p"
],
"offsets": [
[
37,
42
]
],
"normalized": []
},
{
"id": "BioInfer.d190.s0.e1",
"type": "Individual_protein",
"text": [
"verprolin"
],
"offsets": [
[
46,
55
]
],
"normalized": []
},
{
"id": "BioInfer.d190.s0.e2",
"type": "Gene",
"text": [
"END5"
],
"offsets": [
[
0,
4
]
],
"normalized": []
},
{
"id": "BioInfer.d190.s0.e3",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
91,
96
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d190.s0.i0",
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"normalized": []
},
{
"id": "BioInfer.d190.s0.i1",
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{
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"normalized": []
},
{
"id": "BioInfer.d190.s0.i3",
"type": "PPI",
"arg1_id": "BioInfer.d190.s0.e1",
"arg2_id": "BioInfer.d190.s0.e3",
"normalized": []
}
] |
265 | BioInfer.d191.s0 | [
{
"id": "BioInfer.d191.s0__text",
"type": "Sentence",
"text": [
"Equine satellite cell clone SE-11 and ovine satellite cell clone I(1)were evaluated for expression of myosin heavy chain, myogenin, desmin, and muscle-specific actin over a 240 h period in culture."
],
"offsets": [
[
0,
197
]
]
}
] | [
{
"id": "BioInfer.d191.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"muscle-specific actin"
],
"offsets": [
[
144,
165
]
],
"normalized": []
},
{
"id": "BioInfer.d191.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"myogenin"
],
"offsets": [
[
122,
130
]
],
"normalized": []
},
{
"id": "BioInfer.d191.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"desmin"
],
"offsets": [
[
132,
138
]
],
"normalized": []
},
{
"id": "BioInfer.d191.s0.e3",
"type": "Gene/protein/RNA",
"text": [
"myosin heavy chain"
],
"offsets": [
[
102,
120
]
],
"normalized": []
}
] | [] | [] | [] |
266 | BioInfer.d192.s0 | [
{
"id": "BioInfer.d192.s0__text",
"type": "Sentence",
"text": [
"Essential domains of the PRP21 splicing factor are implicated in the binding to PRP9 and PRP11 proteins and are conserved through evolution."
],
"offsets": [
[
0,
140
]
]
}
] | [
{
"id": "BioInfer.d192.s0.e0",
"type": "Individual_protein",
"text": [
"PRP21"
],
"offsets": [
[
25,
30
]
],
"normalized": []
},
{
"id": "BioInfer.d192.s0.e1",
"type": "Individual_protein",
"text": [
"PRP9"
],
"offsets": [
[
80,
84
]
],
"normalized": []
},
{
"id": "BioInfer.d192.s0.e2",
"type": "Individual_protein",
"text": [
"PRP11"
],
"offsets": [
[
89,
94
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d192.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d192.s0.e0",
"arg2_id": "BioInfer.d192.s0.e1",
"normalized": []
},
{
"id": "BioInfer.d192.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d192.s0.e0",
"arg2_id": "BioInfer.d192.s0.e2",
"normalized": []
}
] |
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