id
stringlengths 15
19
| document_id
stringlengths 15
19
| passages
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list | events
list | coreferences
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---|---|---|---|---|---|---|
split_0_train_5700
|
split_0_train_5700
|
[
{
"id": "split_0_train_5700_passage",
"type": "progene_text",
"text": [
"The results showed that molecular misreading of the ubiquitin B gene occurred in hepatocytes in virtually all of the MB - containing livers tested ."
],
"offsets": [
[
0,
148
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]
}
] |
[
{
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"type": "progene_text",
"text": [
"ubiquitin B"
],
"offsets": [
[
52,
63
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5701
|
split_0_train_5701
|
[
{
"id": "split_0_train_5701_passage",
"type": "progene_text",
"text": [
"Ubiquitin (+1) protein was only found within the MBs and therefore may act by interfering with the degradation of the MBs because ubiquitin (+1) may inhibit proteolytic function of the proteasome ."
],
"offsets": [
[
0,
197
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}
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{
"id": "split_0_train_8781_entity",
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"Ubiquitin"
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0,
9
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{
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"type": "progene_text",
"text": [
"ubiquitin"
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"offsets": [
[
130,
139
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],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5702
|
split_0_train_5702
|
[
{
"id": "split_0_train_5702_passage",
"type": "progene_text",
"text": [
"Connexin-43 interactions with ZO-1 and alpha - and beta - tubulin ."
],
"offsets": [
[
0,
67
]
]
}
] |
[
{
"id": "split_0_train_8783_entity",
"type": "progene_text",
"text": [
"Connexin-43"
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0,
11
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{
"id": "split_0_train_8784_entity",
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"text": [
"ZO-1"
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30,
34
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{
"id": "split_0_train_8785_entity",
"type": "progene_text",
"text": [
"alpha - and beta - tubulin"
],
"offsets": [
[
39,
65
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5703
|
split_0_train_5703
|
[
{
"id": "split_0_train_5703_passage",
"type": "progene_text",
"text": [
"Gap junctions are composed of connexins that form transmembrane channels between adjacent cells ."
],
"offsets": [
[
0,
97
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]
}
] |
[
{
"id": "split_0_train_8786_entity",
"type": "progene_text",
"text": [
"connexins"
],
"offsets": [
[
30,
39
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5704
|
split_0_train_5704
|
[
{
"id": "split_0_train_5704_passage",
"type": "progene_text",
"text": [
"The C - terminal tail of connexin-43 ( Cx43 ) , the most widely expressed connexin member , has been implicated in the regulation of Cx43 channel gating ."
],
"offsets": [
[
0,
154
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]
}
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{
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"connexin-43"
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25,
36
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{
"id": "split_0_train_8788_entity",
"type": "progene_text",
"text": [
"Cx43"
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39,
43
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{
"id": "split_0_train_8789_entity",
"type": "progene_text",
"text": [
"connexin"
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74,
82
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{
"id": "split_0_train_8790_entity",
"type": "progene_text",
"text": [
"Cx43"
],
"offsets": [
[
133,
137
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5705
|
split_0_train_5705
|
[
{
"id": "split_0_train_5705_passage",
"type": "progene_text",
"text": [
"Interestingly , channel - independent processes regulated by Cx43 have also been postulated ."
],
"offsets": [
[
0,
93
]
]
}
] |
[
{
"id": "split_0_train_8791_entity",
"type": "progene_text",
"text": [
"Cx43"
],
"offsets": [
[
61,
65
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5706
|
split_0_train_5706
|
[
{
"id": "split_0_train_5706_passage",
"type": "progene_text",
"text": [
"In our studies to elucidate the mechanism of Cx43 channel gating by growth factors and to explore additional functions of gap junctions , we have identified three interacting partners of the C - terminal tail of Cx43 ( Cx43CT ) ."
],
"offsets": [
[
0,
229
]
]
}
] |
[
{
"id": "split_0_train_8792_entity",
"type": "progene_text",
"text": [
"Cx43"
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[
45,
49
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},
{
"id": "split_0_train_8793_entity",
"type": "progene_text",
"text": [
"growth factors"
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[
68,
82
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{
"id": "split_0_train_8794_entity",
"type": "progene_text",
"text": [
"Cx43"
],
"offsets": [
[
212,
216
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],
"normalized": []
},
{
"id": "split_0_train_8795_entity",
"type": "progene_text",
"text": [
"Cx43CT"
],
"offsets": [
[
219,
225
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5707
|
split_0_train_5707
|
[
{
"id": "split_0_train_5707_passage",
"type": "progene_text",
"text": [
"(i) the c-Src tyrosine kinase , which phosphorylates Cx43CT and is involved in G protein - mediated inhibition of Cx43 gap junctional communication ."
],
"offsets": [
[
0,
149
]
]
}
] |
[
{
"id": "split_0_train_8796_entity",
"type": "progene_text",
"text": [
"c-Src"
],
"offsets": [
[
8,
13
]
],
"normalized": []
},
{
"id": "split_0_train_8797_entity",
"type": "progene_text",
"text": [
"tyrosine kinase"
],
"offsets": [
[
14,
29
]
],
"normalized": []
},
{
"id": "split_0_train_8798_entity",
"type": "progene_text",
"text": [
"Cx43CT"
],
"offsets": [
[
53,
59
]
],
"normalized": []
},
{
"id": "split_0_train_8799_entity",
"type": "progene_text",
"text": [
"G protein"
],
"offsets": [
[
79,
88
]
],
"normalized": []
},
{
"id": "split_0_train_8800_entity",
"type": "progene_text",
"text": [
"Cx43"
],
"offsets": [
[
114,
118
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5708
|
split_0_train_5708
|
[
{
"id": "split_0_train_5708_passage",
"type": "progene_text",
"text": [
"(ii) the ZO-1 'scaffold' protein , which might recruit signaling proteins into Cx43 - based gap junctions ."
],
"offsets": [
[
0,
107
]
]
}
] |
[
{
"id": "split_0_train_8801_entity",
"type": "progene_text",
"text": [
"ZO-1"
],
"offsets": [
[
9,
13
]
],
"normalized": []
},
{
"id": "split_0_train_8802_entity",
"type": "progene_text",
"text": [
"Cx43"
],
"offsets": [
[
79,
83
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5709
|
split_0_train_5709
|
[
{
"id": "split_0_train_5709_passage",
"type": "progene_text",
"text": [
"(iii) microtubules ( consisting of alpha/beta-tubulin dimers ) , which extend with their distal ends to Cx43 - based gap junctions , suggesting that Cx43 gap junctions may play a novel role in regulating microtubule stability in contacted cells ."
],
"offsets": [
[
0,
246
]
]
}
] |
[
{
"id": "split_0_train_8803_entity",
"type": "progene_text",
"text": [
"alpha/beta-tubulin"
],
"offsets": [
[
35,
53
]
],
"normalized": []
},
{
"id": "split_0_train_8804_entity",
"type": "progene_text",
"text": [
"Cx43"
],
"offsets": [
[
104,
108
]
],
"normalized": []
},
{
"id": "split_0_train_8805_entity",
"type": "progene_text",
"text": [
"Cx43"
],
"offsets": [
[
149,
153
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5710
|
split_0_train_5710
|
[
{
"id": "split_0_train_5710_passage",
"type": "progene_text",
"text": [
"Here we show that Cx43 binds alpha-tubulin equally well as beta-tubulin ."
],
"offsets": [
[
0,
73
]
]
}
] |
[
{
"id": "split_0_train_8806_entity",
"type": "progene_text",
"text": [
"Cx43"
],
"offsets": [
[
18,
22
]
],
"normalized": []
},
{
"id": "split_0_train_8807_entity",
"type": "progene_text",
"text": [
"alpha-tubulin"
],
"offsets": [
[
29,
42
]
],
"normalized": []
},
{
"id": "split_0_train_8808_entity",
"type": "progene_text",
"text": [
"beta-tubulin"
],
"offsets": [
[
59,
71
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5711
|
split_0_train_5711
|
[
{
"id": "split_0_train_5711_passage",
"type": "progene_text",
"text": [
"In addition , we show that the second , but not the first , PDZ domain of ZO-1 binds directly to Cx43 , and we confirm that the very C - terminal isoleucine residue of Cx43 is critical for ZO-1 binding ."
],
"offsets": [
[
0,
203
]
]
}
] |
[
{
"id": "split_0_train_8809_entity",
"type": "progene_text",
"text": [
"ZO-1"
],
"offsets": [
[
74,
78
]
],
"normalized": []
},
{
"id": "split_0_train_8810_entity",
"type": "progene_text",
"text": [
"Cx43"
],
"offsets": [
[
97,
101
]
],
"normalized": []
},
{
"id": "split_0_train_8811_entity",
"type": "progene_text",
"text": [
"Cx43"
],
"offsets": [
[
168,
172
]
],
"normalized": []
},
{
"id": "split_0_train_8812_entity",
"type": "progene_text",
"text": [
"ZO-1"
],
"offsets": [
[
189,
193
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5712
|
split_0_train_5712
|
[
{
"id": "split_0_train_5712_passage",
"type": "progene_text",
"text": [
"Crystallization and preliminary X - ray crystallographic studies on recombinant human carnitine acetyltransferase ."
],
"offsets": [
[
0,
115
]
]
}
] |
[
{
"id": "split_0_train_8813_entity",
"type": "progene_text",
"text": [
"carnitine acetyltransferase"
],
"offsets": [
[
86,
113
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5713
|
split_0_train_5713
|
[
{
"id": "split_0_train_5713_passage",
"type": "progene_text",
"text": [
"In this paper , the purification , crystallization and preliminary X-ray crystallographic studies of human carnitine acetyltransferase are reported ."
],
"offsets": [
[
0,
149
]
]
}
] |
[
{
"id": "split_0_train_8814_entity",
"type": "progene_text",
"text": [
"carnitine acetyltransferase"
],
"offsets": [
[
107,
134
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5714
|
split_0_train_5714
|
[
{
"id": "split_0_train_5714_passage",
"type": "progene_text",
"text": [
"Recombinant human carnitine acetyltransferase crystals were grown by the hanging - drop vapor - diffusion method and belong to the orthorhombic space group P2(1)2(1)2(1) , with unit - cell parameters a = 137.65 , b = 84.76 , c = 57.65 A and one molecule per asymmetric unit ."
],
"offsets": [
[
0,
275
]
]
}
] |
[
{
"id": "split_0_train_8815_entity",
"type": "progene_text",
"text": [
"carnitine acetyltransferase"
],
"offsets": [
[
18,
45
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5715
|
split_0_train_5715
|
[
{
"id": "split_0_train_5715_passage",
"type": "progene_text",
"text": [
"The intensity data were collected from a cryocooled crystal to 1.6 A resolution using a conventional X - ray source ."
],
"offsets": [
[
0,
117
]
]
}
] |
[] |
[] |
[] |
[] |
split_0_train_5716
|
split_0_train_5716
|
[
{
"id": "split_0_train_5716_passage",
"type": "progene_text",
"text": [
"Live - cell imaging reveals divergent intracellular dynamics of polyglutamine disease proteins and supports a sequestration model of pathogenesis ."
],
"offsets": [
[
0,
147
]
]
}
] |
[] |
[] |
[] |
[] |
split_0_train_5717
|
split_0_train_5717
|
[
{
"id": "split_0_train_5717_passage",
"type": "progene_text",
"text": [
"Protein misfolding and aggregation are central features of the polyglutamine neurodegenerative disorders , but the dynamic properties of expanded polyglutamine proteins are poorly understood ."
],
"offsets": [
[
0,
192
]
]
}
] |
[] |
[] |
[] |
[] |
split_0_train_5718
|
split_0_train_5718
|
[
{
"id": "split_0_train_5718_passage",
"type": "progene_text",
"text": [
"Here , we use fluorescence recovery after photobleaching ( FRAP ) and fluorescence loss in photobleaching ( FLIP ) with green fluorescent protein fusion proteins to study polyglutamine protein kinetics in living cells ."
],
"offsets": [
[
0,
219
]
]
}
] |
[
{
"id": "split_0_train_8816_entity",
"type": "progene_text",
"text": [
"green fluorescent protein"
],
"offsets": [
[
120,
145
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5719
|
split_0_train_5719
|
[
{
"id": "split_0_train_5719_passage",
"type": "progene_text",
"text": [
"Our results reveal markedly divergent mobility states for an expanded polyglutamine protein , ataxin-3 , and establish that nuclear inclusions formed by this protein are aggregates ."
],
"offsets": [
[
0,
182
]
]
}
] |
[
{
"id": "split_0_train_8817_entity",
"type": "progene_text",
"text": [
"ataxin-3"
],
"offsets": [
[
94,
102
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5720
|
split_0_train_5720
|
[
{
"id": "split_0_train_5720_passage",
"type": "progene_text",
"text": [
"Additional studies of green fluorescent protein - tagged cAMP response element binding protein coexpressed with either of two mutant polyglutamine proteins , ataxin - 3 and huntingtin , support a model of disease in which coaggregation of transcriptional components contributes to pathogenesis ."
],
"offsets": [
[
0,
295
]
]
}
] |
[
{
"id": "split_0_train_8818_entity",
"type": "progene_text",
"text": [
"green fluorescent protein"
],
"offsets": [
[
22,
47
]
],
"normalized": []
},
{
"id": "split_0_train_8819_entity",
"type": "progene_text",
"text": [
"cAMP response element binding protein"
],
"offsets": [
[
57,
94
]
],
"normalized": []
},
{
"id": "split_0_train_8820_entity",
"type": "progene_text",
"text": [
"ataxin - 3"
],
"offsets": [
[
158,
168
]
],
"normalized": []
},
{
"id": "split_0_train_8821_entity",
"type": "progene_text",
"text": [
"huntingtin"
],
"offsets": [
[
173,
183
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5721
|
split_0_train_5721
|
[
{
"id": "split_0_train_5721_passage",
"type": "progene_text",
"text": [
"Finally , studies of a third polyglutamine disease protein , ataxin-1 , reveal unexpected heterogeneity in the dynamics of inclusions formed by different disease proteins , a finding which may help explain disease - specific elements of pathogenesis in these neurodegenerative disorders ."
],
"offsets": [
[
0,
288
]
]
}
] |
[
{
"id": "split_0_train_8822_entity",
"type": "progene_text",
"text": [
"ataxin-1"
],
"offsets": [
[
61,
69
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5722
|
split_0_train_5722
|
[
{
"id": "split_0_train_5722_passage",
"type": "progene_text",
"text": [
"Molecular cloning and characterization of STAMP1 , a highly prostate - specific six transmembrane protein that is overexpressed in prostate cancer ."
],
"offsets": [
[
0,
148
]
]
}
] |
[
{
"id": "split_0_train_8823_entity",
"type": "progene_text",
"text": [
"STAMP1"
],
"offsets": [
[
42,
48
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5723
|
split_0_train_5723
|
[
{
"id": "split_0_train_5723_passage",
"type": "progene_text",
"text": [
"We have identified a novel gene , six transmembrane protein of prostate 1 ( STAMP1 ) , which is largely specific to prostate for expression and is predicted to code for a 490 - amino acid six transmembrane protein ."
],
"offsets": [
[
0,
215
]
]
}
] |
[
{
"id": "split_0_train_8824_entity",
"type": "progene_text",
"text": [
"six transmembrane protein of prostate 1"
],
"offsets": [
[
34,
73
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],
"normalized": []
},
{
"id": "split_0_train_8825_entity",
"type": "progene_text",
"text": [
"STAMP1"
],
"offsets": [
[
76,
82
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5724
|
split_0_train_5724
|
[
{
"id": "split_0_train_5724_passage",
"type": "progene_text",
"text": [
"Using a form of STAMP1 labeled with green fluorescent protein in quantitative time - lapse and immunofluorescence confocal microscopy , we show that STAMP1 is localized to the Golgi complex , predominantly to the trans - Golgi network , and to the plasma membrane ."
],
"offsets": [
[
0,
265
]
]
}
] |
[
{
"id": "split_0_train_8826_entity",
"type": "progene_text",
"text": [
"STAMP1"
],
"offsets": [
[
16,
22
]
],
"normalized": []
},
{
"id": "split_0_train_8827_entity",
"type": "progene_text",
"text": [
"green fluorescent protein"
],
"offsets": [
[
36,
61
]
],
"normalized": []
},
{
"id": "split_0_train_8828_entity",
"type": "progene_text",
"text": [
"STAMP1"
],
"offsets": [
[
149,
155
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5725
|
split_0_train_5725
|
[
{
"id": "split_0_train_5725_passage",
"type": "progene_text",
"text": [
"STAMP1 also localizes to vesicular tubular structures in the cytosol and colocalizes with the early endosome antigen 1 ( EEA1 ) , suggesting that it may be involved in the secretory / endocytic pathways ."
],
"offsets": [
[
0,
204
]
]
}
] |
[
{
"id": "split_0_train_8829_entity",
"type": "progene_text",
"text": [
"STAMP1"
],
"offsets": [
[
0,
6
]
],
"normalized": []
},
{
"id": "split_0_train_8830_entity",
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"type": "progene_text",
"text": [
"EEA1"
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[
121,
125
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5726
|
split_0_train_5726
|
[
{
"id": "split_0_train_5726_passage",
"type": "progene_text",
"text": [
"STAMP1 is highly expressed in the androgen - sensitive , androgen receptor - positive prostate cancer cell line LNCaP , but not in androgen receptor - negative prostate cancer cell lines PC-3 and DU145 ."
],
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[
0,
203
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]
}
] |
[
{
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"type": "progene_text",
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0,
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{
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"type": "progene_text",
"text": [
"androgen receptor"
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[
131,
148
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5727
|
split_0_train_5727
|
[
{
"id": "split_0_train_5727_passage",
"type": "progene_text",
"text": [
"Furthermore , STAMP1 expression is significantly lower in the androgen - dependent human prostate xenograft CWR22 compared with the relapsed derivative CWR22R , suggesting that its expression may be deregulated during prostate cancer progression ."
],
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[
0,
247
]
]
}
] |
[
{
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"type": "progene_text",
"text": [
"STAMP1"
],
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[
14,
20
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5728
|
split_0_train_5728
|
[
{
"id": "split_0_train_5728_passage",
"type": "progene_text",
"text": [
"Consistent with this notion , in situ analysis of human prostate cancer specimens indicated that STAMP1 is expressed exclusively in the epithelial cells of the prostate and its expression is significantly increased in prostate tumors compared with normal glands ."
],
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[
0,
263
]
]
}
] |
[
{
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"type": "progene_text",
"text": [
"STAMP1"
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[
97,
103
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5729
|
split_0_train_5729
|
[
{
"id": "split_0_train_5729_passage",
"type": "progene_text",
"text": [
"Taken together , these data suggest that STAMP1 may have an important role in the normal prostate cell as well as in prostate cancer progression ."
],
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[
0,
146
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]
}
] |
[
{
"id": "split_0_train_8837_entity",
"type": "progene_text",
"text": [
"STAMP1"
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[
41,
47
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5730
|
split_0_train_5730
|
[
{
"id": "split_0_train_5730_passage",
"type": "progene_text",
"text": [
"Nuclear localization of CDC25B1 and serine 146 integrity are required for induction of mitosis ."
],
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[
0,
96
]
]
}
] |
[
{
"id": "split_0_train_8838_entity",
"type": "progene_text",
"text": [
"CDC25B1"
],
"offsets": [
[
24,
31
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5731
|
split_0_train_5731
|
[
{
"id": "split_0_train_5731_passage",
"type": "progene_text",
"text": [
"CDC25B phosphatases are essential regulators that control cyclin - dependent kinases activities at the entry into mitosis ."
],
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[
0,
123
]
]
}
] |
[
{
"id": "split_0_train_8839_entity",
"type": "progene_text",
"text": [
"CDC25B phosphatases"
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0,
19
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{
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"type": "progene_text",
"text": [
"cyclin - dependent kinases"
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"offsets": [
[
58,
84
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5732
|
split_0_train_5732
|
[
{
"id": "split_0_train_5732_passage",
"type": "progene_text",
"text": [
"In this study , we demonstrate that serine 146 is required for two crucial features of CDC25B1 ."
],
"offsets": [
[
0,
96
]
]
}
] |
[
{
"id": "split_0_train_8841_entity",
"type": "progene_text",
"text": [
"CDC25B1"
],
"offsets": [
[
87,
94
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5733
|
split_0_train_5733
|
[
{
"id": "split_0_train_5733_passage",
"type": "progene_text",
"text": [
"It is essential for CDC25B1 to function as a mitotic inducer and to prevent CDC25B1 export from the nucleus ."
],
"offsets": [
[
0,
109
]
]
}
] |
[
{
"id": "split_0_train_8842_entity",
"type": "progene_text",
"text": [
"CDC25B1"
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20,
27
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{
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"type": "progene_text",
"text": [
"CDC25B1"
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[
76,
83
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"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5734
|
split_0_train_5734
|
[
{
"id": "split_0_train_5734_passage",
"type": "progene_text",
"text": [
"We also show that serine 146 is phosphorylated in vitro by CDK1 - cyclin B ."
],
"offsets": [
[
0,
76
]
]
}
] |
[
{
"id": "split_0_train_8844_entity",
"type": "progene_text",
"text": [
"CDK1"
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59,
63
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{
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"type": "progene_text",
"text": [
"cyclin B"
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"offsets": [
[
66,
74
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5735
|
split_0_train_5735
|
[
{
"id": "split_0_train_5735_passage",
"type": "progene_text",
"text": [
"However , phosphorylation of CDC25B does not stimulate its phosphatase activity , and mutation of serine 146 had no effect on its catalytic activity ."
],
"offsets": [
[
0,
150
]
]
}
] |
[
{
"id": "split_0_train_8846_entity",
"type": "progene_text",
"text": [
"CDC25B"
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29,
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{
"id": "split_0_train_8847_entity",
"type": "progene_text",
"text": [
"phosphatase"
],
"offsets": [
[
59,
70
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5736
|
split_0_train_5736
|
[
{
"id": "split_0_train_5736_passage",
"type": "progene_text",
"text": [
"Serine 146 phosphorylation is proposed to be a key event in the regulation of the CDC25B function in the initiation of mammalian mitosis ."
],
"offsets": [
[
0,
138
]
]
}
] |
[
{
"id": "split_0_train_8848_entity",
"type": "progene_text",
"text": [
"CDC25B"
],
"offsets": [
[
82,
88
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5737
|
split_0_train_5737
|
[
{
"id": "split_0_train_5737_passage",
"type": "progene_text",
"text": [
"SNAP-23 is a target for calpain cleavage in activated platelets ."
],
"offsets": [
[
0,
65
]
]
}
] |
[
{
"id": "split_0_train_8849_entity",
"type": "progene_text",
"text": [
"SNAP-23"
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[
0,
7
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{
"id": "split_0_train_8850_entity",
"type": "progene_text",
"text": [
"calpain"
],
"offsets": [
[
24,
31
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5738
|
split_0_train_5738
|
[
{
"id": "split_0_train_5738_passage",
"type": "progene_text",
"text": [
"The role of calpain in platelet function is generally associated with aggregation and clot retraction ."
],
"offsets": [
[
0,
103
]
]
}
] |
[
{
"id": "split_0_train_8851_entity",
"type": "progene_text",
"text": [
"calpain"
],
"offsets": [
[
12,
19
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5739
|
split_0_train_5739
|
[
{
"id": "split_0_train_5739_passage",
"type": "progene_text",
"text": [
"In this report , data are presented to show that one component of the platelet secretory machinery , SNAP-23 , is specifically cleaved by calpain in activated cells ."
],
"offsets": [
[
0,
166
]
]
}
] |
[
{
"id": "split_0_train_8852_entity",
"type": "progene_text",
"text": [
"SNAP-23"
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[
101,
108
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},
{
"id": "split_0_train_8853_entity",
"type": "progene_text",
"text": [
"calpain"
],
"offsets": [
[
138,
145
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5740
|
split_0_train_5740
|
[
{
"id": "split_0_train_5740_passage",
"type": "progene_text",
"text": [
"Other proteins of the membrane fusion machinery , e.g. syntaxins 2 and 4 and alpha-SNAP , are not affected ."
],
"offsets": [
[
0,
108
]
]
}
] |
[
{
"id": "split_0_train_8854_entity",
"type": "progene_text",
"text": [
"syntaxins 2 and 4"
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[
55,
72
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],
"normalized": []
},
{
"id": "split_0_train_8855_entity",
"type": "progene_text",
"text": [
"alpha-SNAP"
],
"offsets": [
[
77,
87
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5741
|
split_0_train_5741
|
[
{
"id": "split_0_train_5741_passage",
"type": "progene_text",
"text": [
"In vitro studies , using permeabilized platelets , demonstrate that cleavage is time - and calcium - dependent ."
],
"offsets": [
[
0,
112
]
]
}
] |
[] |
[] |
[] |
[] |
split_0_train_5742
|
split_0_train_5742
|
[
{
"id": "split_0_train_5742_passage",
"type": "progene_text",
"text": [
"Analysis of SNAP-23 cleavage products suggests that the calpain cleavage site(s) is in the C - terminal third of the molecule potentially between the cysteine - rich acyl attachment sites and the C - terminal coiled - coil domain ."
],
"offsets": [
[
0,
231
]
]
}
] |
[
{
"id": "split_0_train_8856_entity",
"type": "progene_text",
"text": [
"SNAP-23"
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"offsets": [
[
12,
19
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},
{
"id": "split_0_train_8857_entity",
"type": "progene_text",
"text": [
"calpain"
],
"offsets": [
[
56,
63
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5743
|
split_0_train_5743
|
[
{
"id": "split_0_train_5743_passage",
"type": "progene_text",
"text": [
"The time course of cleavage is most consistent with late calpain - mediated events such as pp60(c-src ) cleavage , but not early events such as protein - tyrosine phosphatase-1B activation ."
],
"offsets": [
[
0,
190
]
]
}
] |
[
{
"id": "split_0_train_8858_entity",
"type": "progene_text",
"text": [
"calpain"
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[
57,
64
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],
"normalized": []
},
{
"id": "split_0_train_8859_entity",
"type": "progene_text",
"text": [
"pp60(c-src )"
],
"offsets": [
[
91,
103
]
],
"normalized": []
},
{
"id": "split_0_train_8860_entity",
"type": "progene_text",
"text": [
"protein - tyrosine phosphatase-1B"
],
"offsets": [
[
144,
177
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5744
|
split_0_train_5744
|
[
{
"id": "split_0_train_5744_passage",
"type": "progene_text",
"text": [
"SNAP-23 cleavage is inhibited by calpeptin , calpastatin , calpain inhibitor IV , and E-64d , but not by caspase 3 inhibitor III or cathepsin inhibitor I ."
],
"offsets": [
[
0,
155
]
]
}
] |
[
{
"id": "split_0_train_8861_entity",
"type": "progene_text",
"text": [
"SNAP-23"
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"offsets": [
[
0,
7
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"normalized": []
},
{
"id": "split_0_train_8862_entity",
"type": "progene_text",
"text": [
"calpain"
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[
59,
66
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],
"normalized": []
},
{
"id": "split_0_train_8863_entity",
"type": "progene_text",
"text": [
"caspase 3"
],
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[
105,
114
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],
"normalized": []
},
{
"id": "split_0_train_8864_entity",
"type": "progene_text",
"text": [
"cathepsin"
],
"offsets": [
[
132,
141
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5745
|
split_0_train_5745
|
[
{
"id": "split_0_train_5745_passage",
"type": "progene_text",
"text": [
"When tested for their effect on secretion , none of the calpain - specific inhibitors significantly affected release of soluble components from any of the three platelet granule storage pools ."
],
"offsets": [
[
0,
193
]
]
}
] |
[
{
"id": "split_0_train_8865_entity",
"type": "progene_text",
"text": [
"calpain"
],
"offsets": [
[
56,
63
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5746
|
split_0_train_5746
|
[
{
"id": "split_0_train_5746_passage",
"type": "progene_text",
"text": [
"These results indicate that SNAP-23 cleavage occurs after granule release and therefore may play a role in affecting granule membrane exteriorization ."
],
"offsets": [
[
0,
151
]
]
}
] |
[
{
"id": "split_0_train_8866_entity",
"type": "progene_text",
"text": [
"SNAP-23"
],
"offsets": [
[
28,
35
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5747
|
split_0_train_5747
|
[
{
"id": "split_0_train_5747_passage",
"type": "progene_text",
"text": [
"This is consistent with the ultrastructural morphology of calpeptin - treated platelets after activation ."
],
"offsets": [
[
0,
106
]
]
}
] |
[] |
[] |
[] |
[] |
split_0_train_5748
|
split_0_train_5748
|
[
{
"id": "split_0_train_5748_passage",
"type": "progene_text",
"text": [
"Functional replacement of the tobacco rattle virus cysteine - rich protein by pathogenicity proteins from unrelated plant viruses ."
],
"offsets": [
[
0,
131
]
]
}
] |
[] |
[] |
[] |
[] |
split_0_train_5749
|
split_0_train_5749
|
[
{
"id": "split_0_train_5749_passage",
"type": "progene_text",
"text": [
"Mutation of the 16K gene encoded by RNA1 of Tobacco rattle virus ( TRV ) greatly reduced the levels of viral RNA that accumulated in both infected protoplasts and plants , showing that the 16K cysteine - rich protein ( CRP ) is required for efficient multiplication of TRV ."
],
"offsets": [
[
0,
274
]
]
}
] |
[
{
"id": "split_0_train_8867_entity",
"type": "progene_text",
"text": [
"16K"
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"offsets": [
[
16,
19
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"normalized": []
},
{
"id": "split_0_train_8868_entity",
"type": "progene_text",
"text": [
"16K"
],
"offsets": [
[
189,
192
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5750
|
split_0_train_5750
|
[
{
"id": "split_0_train_5750_passage",
"type": "progene_text",
"text": [
"Overexpression of the 16K protein , either from an additional copy of the gene carried on TRV RNA2 or from a PVX vector , led to an increase in the severity of disease symptoms , suggesting that the protein has a role in the pathogenicity of the virus ."
],
"offsets": [
[
0,
253
]
]
}
] |
[
{
"id": "split_0_train_8869_entity",
"type": "progene_text",
"text": [
"16K protein"
],
"offsets": [
[
22,
33
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5751
|
split_0_train_5751
|
[
{
"id": "split_0_train_5751_passage",
"type": "progene_text",
"text": [
"Mutation of the 16K gene could be overcome by expression from RNA2 of the Cucumber mosaic virus 2b gene , the Soil - borne wheat mosaic virus 19K gene , or the Barley stripe mosaic virus gammab gene , indicating that the proteins encoded by these diverse genes may have similar functions ."
],
"offsets": [
[
0,
289
]
]
}
] |
[
{
"id": "split_0_train_8870_entity",
"type": "progene_text",
"text": [
"16K"
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"offsets": [
[
16,
19
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],
"normalized": []
},
{
"id": "split_0_train_8871_entity",
"type": "progene_text",
"text": [
"2b"
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"offsets": [
[
96,
98
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],
"normalized": []
},
{
"id": "split_0_train_8872_entity",
"type": "progene_text",
"text": [
"19K"
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"offsets": [
[
142,
145
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],
"normalized": []
},
{
"id": "split_0_train_8873_entity",
"type": "progene_text",
"text": [
"gammab"
],
"offsets": [
[
187,
193
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5752
|
split_0_train_5752
|
[
{
"id": "split_0_train_5752_passage",
"type": "progene_text",
"text": [
"One known function of the CMV 2b gene is as a suppressor of posttranscriptional gene silencing , suggesting that the TRV 16K protein may also possess this activity ."
],
"offsets": [
[
0,
165
]
]
}
] |
[
{
"id": "split_0_train_8874_entity",
"type": "progene_text",
"text": [
"2b"
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[
30,
32
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],
"normalized": []
},
{
"id": "split_0_train_8875_entity",
"type": "progene_text",
"text": [
"16K"
],
"offsets": [
[
121,
124
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5753
|
split_0_train_5753
|
[
{
"id": "split_0_train_5753_passage",
"type": "progene_text",
"text": [
"PAX genes in development and disease : the role of PAX2 in urogenital tract development ."
],
"offsets": [
[
0,
89
]
]
}
] |
[
{
"id": "split_0_train_8876_entity",
"type": "progene_text",
"text": [
"PAX"
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"offsets": [
[
0,
3
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"normalized": []
},
{
"id": "split_0_train_8877_entity",
"type": "progene_text",
"text": [
"PAX2"
],
"offsets": [
[
51,
55
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5754
|
split_0_train_5754
|
[
{
"id": "split_0_train_5754_passage",
"type": "progene_text",
"text": [
"PAX genes play an important role in fetal development ."
],
"offsets": [
[
0,
55
]
]
}
] |
[
{
"id": "split_0_train_8878_entity",
"type": "progene_text",
"text": [
"PAX"
],
"offsets": [
[
0,
3
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5755
|
split_0_train_5755
|
[
{
"id": "split_0_train_5755_passage",
"type": "progene_text",
"text": [
"Moreover , heterozygous mutations in several PAX genes cause human disease ."
],
"offsets": [
[
0,
76
]
]
}
] |
[
{
"id": "split_0_train_8879_entity",
"type": "progene_text",
"text": [
"PAX"
],
"offsets": [
[
45,
48
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5756
|
split_0_train_5756
|
[
{
"id": "split_0_train_5756_passage",
"type": "progene_text",
"text": [
"Here we review the role of PAX2 in kidney development , focusing on the morphological effects of PAX2 mutations ."
],
"offsets": [
[
0,
113
]
]
}
] |
[
{
"id": "split_0_train_8880_entity",
"type": "progene_text",
"text": [
"PAX2"
],
"offsets": [
[
27,
31
]
],
"normalized": []
},
{
"id": "split_0_train_8881_entity",
"type": "progene_text",
"text": [
"PAX2"
],
"offsets": [
[
97,
101
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5757
|
split_0_train_5757
|
[
{
"id": "split_0_train_5757_passage",
"type": "progene_text",
"text": [
"We discuss the role of PAX2 in the context of an inhibitory field model of kidney branching morphogenesis and summarize recent progress in this area ."
],
"offsets": [
[
0,
150
]
]
}
] |
[
{
"id": "split_0_train_8882_entity",
"type": "progene_text",
"text": [
"PAX2"
],
"offsets": [
[
23,
27
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5758
|
split_0_train_5758
|
[
{
"id": "split_0_train_5758_passage",
"type": "progene_text",
"text": [
"Molecular cloning , functional expression , and tissue distribution of a novel human gap junction - forming protein , connexin - 31.9 ."
],
"offsets": [
[
0,
135
]
]
}
] |
[
{
"id": "split_0_train_8883_entity",
"type": "progene_text",
"text": [
"connexin - 31.9"
],
"offsets": [
[
118,
133
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5759
|
split_0_train_5759
|
[
{
"id": "split_0_train_5759_passage",
"type": "progene_text",
"text": [
"Interaction with zona occludens protein-1 ."
],
"offsets": [
[
0,
43
]
]
}
] |
[
{
"id": "split_0_train_8884_entity",
"type": "progene_text",
"text": [
"zona occludens protein-1"
],
"offsets": [
[
17,
41
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5760
|
split_0_train_5760
|
[
{
"id": "split_0_train_5760_passage",
"type": "progene_text",
"text": [
"A novel human connexin gene ( GJA11 ) was cloned from a genomic library ."
],
"offsets": [
[
0,
73
]
]
}
] |
[
{
"id": "split_0_train_8885_entity",
"type": "progene_text",
"text": [
"connexin"
],
"offsets": [
[
14,
22
]
],
"normalized": []
},
{
"id": "split_0_train_8886_entity",
"type": "progene_text",
"text": [
"GJA11"
],
"offsets": [
[
30,
35
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5761
|
split_0_train_5761
|
[
{
"id": "split_0_train_5761_passage",
"type": "progene_text",
"text": [
"The open reading frame encoded a hypothetical protein of 294 amino acid residues with a predicted molecular mass of 31 , 933 , hence referred to as connexin - 31.9 ( Cx31.9 ) or alpha 11 connexin ."
],
"offsets": [
[
0,
197
]
]
}
] |
[
{
"id": "split_0_train_8887_entity",
"type": "progene_text",
"text": [
"connexin - 31.9"
],
"offsets": [
[
148,
163
]
],
"normalized": []
},
{
"id": "split_0_train_8888_entity",
"type": "progene_text",
"text": [
"Cx31.9"
],
"offsets": [
[
166,
172
]
],
"normalized": []
},
{
"id": "split_0_train_8889_entity",
"type": "progene_text",
"text": [
"alpha 11 connexin"
],
"offsets": [
[
178,
195
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5762
|
split_0_train_5762
|
[
{
"id": "split_0_train_5762_passage",
"type": "progene_text",
"text": [
"A clone in GenBank containing the Cx31.9 gene localized to chromosome 17q21.2 ."
],
"offsets": [
[
0,
79
]
]
}
] |
[
{
"id": "split_0_train_8890_entity",
"type": "progene_text",
"text": [
"Cx31.9"
],
"offsets": [
[
34,
40
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5763
|
split_0_train_5763
|
[
{
"id": "split_0_train_5763_passage",
"type": "progene_text",
"text": [
"Northern analysis of Cx31.9 showed a major 4.4 - kilobase transcript , which was expressed at varying levels in all tissues analyzed ."
],
"offsets": [
[
0,
134
]
]
}
] |
[
{
"id": "split_0_train_8891_entity",
"type": "progene_text",
"text": [
"Cx31.9"
],
"offsets": [
[
21,
27
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5764
|
split_0_train_5764
|
[
{
"id": "split_0_train_5764_passage",
"type": "progene_text",
"text": [
"Two monoclonal antibodies generated against different domains of Cx31.9 recognized a 30 - 33 - kDa protein from cells overexpressing Cx31.9 ."
],
"offsets": [
[
0,
141
]
]
}
] |
[
{
"id": "split_0_train_8892_entity",
"type": "progene_text",
"text": [
"Cx31.9"
],
"offsets": [
[
65,
71
]
],
"normalized": []
},
{
"id": "split_0_train_8893_entity",
"type": "progene_text",
"text": [
"Cx31.9"
],
"offsets": [
[
133,
139
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5765
|
split_0_train_5765
|
[
{
"id": "split_0_train_5765_passage",
"type": "progene_text",
"text": [
"Immunofluorescence of overexpressing cells indicated the presence of Cx31.9 between adjacent cells , consistent with its localization to gap junctions ."
],
"offsets": [
[
0,
152
]
]
}
] |
[
{
"id": "split_0_train_8894_entity",
"type": "progene_text",
"text": [
"Cx31.9"
],
"offsets": [
[
69,
75
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5766
|
split_0_train_5766
|
[
{
"id": "split_0_train_5766_passage",
"type": "progene_text",
"text": [
"Double voltage clamp analyses of Cx31.9 - overexpressing cells , and of paired Xenopus oocytes injected with Cx31.9 cRNA , demonstrated junctional currents indicative of gap junction channel formation ."
],
"offsets": [
[
0,
202
]
]
}
] |
[
{
"id": "split_0_train_8895_entity",
"type": "progene_text",
"text": [
"Cx31.9"
],
"offsets": [
[
33,
39
]
],
"normalized": []
},
{
"id": "split_0_train_8896_entity",
"type": "progene_text",
"text": [
"Cx31.9"
],
"offsets": [
[
109,
115
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5767
|
split_0_train_5767
|
[
{
"id": "split_0_train_5767_passage",
"type": "progene_text",
"text": [
"In contrast to previously characterized connexins , Cx31.9 showed no voltage - dependent gating within a physiologically relevant range ."
],
"offsets": [
[
0,
137
]
]
}
] |
[
{
"id": "split_0_train_8897_entity",
"type": "progene_text",
"text": [
"connexins"
],
"offsets": [
[
40,
49
]
],
"normalized": []
},
{
"id": "split_0_train_8898_entity",
"type": "progene_text",
"text": [
"Cx31.9"
],
"offsets": [
[
52,
58
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5768
|
split_0_train_5768
|
[
{
"id": "split_0_train_5768_passage",
"type": "progene_text",
"text": [
"Cx31.9 was detected in human tissues by immunoblot analysis , and immunofluorescence localized Cx31.9 expression to vascular smooth muscle cells ."
],
"offsets": [
[
0,
146
]
]
}
] |
[
{
"id": "split_0_train_8899_entity",
"type": "progene_text",
"text": [
"Cx31.9"
],
"offsets": [
[
0,
6
]
],
"normalized": []
},
{
"id": "split_0_train_8900_entity",
"type": "progene_text",
"text": [
"Cx31.9"
],
"offsets": [
[
95,
101
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5769
|
split_0_train_5769
|
[
{
"id": "split_0_train_5769_passage",
"type": "progene_text",
"text": [
"Furthermore , it was demonstrated that Cx31.9 interacted with ZO-1 ."
],
"offsets": [
[
0,
68
]
]
}
] |
[
{
"id": "split_0_train_8901_entity",
"type": "progene_text",
"text": [
"Cx31.9"
],
"offsets": [
[
39,
45
]
],
"normalized": []
},
{
"id": "split_0_train_8902_entity",
"type": "progene_text",
"text": [
"ZO-1"
],
"offsets": [
[
62,
66
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5770
|
split_0_train_5770
|
[
{
"id": "split_0_train_5770_passage",
"type": "progene_text",
"text": [
"Thus , Cx31.9 represents a novel connexin gene that in vivo generates a protein with unique voltage gating properties ."
],
"offsets": [
[
0,
119
]
]
}
] |
[
{
"id": "split_0_train_8903_entity",
"type": "progene_text",
"text": [
"Cx31.9"
],
"offsets": [
[
7,
13
]
],
"normalized": []
},
{
"id": "split_0_train_8904_entity",
"type": "progene_text",
"text": [
"connexin"
],
"offsets": [
[
33,
41
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5771
|
split_0_train_5771
|
[
{
"id": "split_0_train_5771_passage",
"type": "progene_text",
"text": [
"The beta-barrel finder ( BBF ) program , allowing identification of outer membrane beta-barrel proteins encoded within prokaryotic genomes ."
],
"offsets": [
[
0,
140
]
]
}
] |
[] |
[] |
[] |
[] |
split_0_train_5772
|
split_0_train_5772
|
[
{
"id": "split_0_train_5772_passage",
"type": "progene_text",
"text": [
"Many outer membrane proteins ( OMPs ) in Gram - negative bacteria possess known beta-barrel three - dimensional ( 3D ) structures ."
],
"offsets": [
[
0,
131
]
]
}
] |
[] |
[] |
[] |
[] |
split_0_train_5773
|
split_0_train_5773
|
[
{
"id": "split_0_train_5773_passage",
"type": "progene_text",
"text": [
"These proteins , including channel - forming transmembrane porins , are diverse in sequence but exhibit common structural features ."
],
"offsets": [
[
0,
132
]
]
}
] |
[
{
"id": "split_0_train_8905_entity",
"type": "progene_text",
"text": [
"porins"
],
"offsets": [
[
59,
65
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5774
|
split_0_train_5774
|
[
{
"id": "split_0_train_5774_passage",
"type": "progene_text",
"text": [
"We here report computational analyses of six outer membrane proteins of known 3D structures with respect to (1) secondary structure , ( 2 ) hydropathy , and ( 3 ) amphipathicity ."
],
"offsets": [
[
0,
179
]
]
}
] |
[] |
[] |
[] |
[] |
split_0_train_5775
|
split_0_train_5775
|
[
{
"id": "split_0_train_5775_passage",
"type": "progene_text",
"text": [
"Using these characteristics , as well as the presence of an N - terminal targeting sequence , a program was developed allowing prediction of integral membrane beta-barrel proteins encoded within any completely sequenced prokaryotic genome ."
],
"offsets": [
[
0,
240
]
]
}
] |
[] |
[] |
[] |
[] |
split_0_train_5776
|
split_0_train_5776
|
[
{
"id": "split_0_train_5776_passage",
"type": "progene_text",
"text": [
"This program , termed the beta-barrel finder ( BBF ) program , was used to analyze the proteins encoded within the Escherichia coli genome ."
],
"offsets": [
[
0,
140
]
]
}
] |
[] |
[] |
[] |
[] |
split_0_train_5777
|
split_0_train_5777
|
[
{
"id": "split_0_train_5777_passage",
"type": "progene_text",
"text": [
"Out of 4290 sequences examined , 118 ( 2.8 % ) were retrieved ."
],
"offsets": [
[
0,
63
]
]
}
] |
[] |
[] |
[] |
[] |
split_0_train_5778
|
split_0_train_5778
|
[
{
"id": "split_0_train_5778_passage",
"type": "progene_text",
"text": [
"Of these , almost all known outer membrane proteins with established beta-barrel structures as well as many probable outer membrane proteins were identified ."
],
"offsets": [
[
0,
158
]
]
}
] |
[] |
[] |
[] |
[] |
split_0_train_5779
|
split_0_train_5779
|
[
{
"id": "split_0_train_5779_passage",
"type": "progene_text",
"text": [
"This program should be useful for predicting the occurrence of outer membrane proteins in bacteria with completely sequenced genomes ."
],
"offsets": [
[
0,
134
]
]
}
] |
[] |
[] |
[] |
[] |
split_0_train_5780
|
split_0_train_5780
|
[
{
"id": "split_0_train_5780_passage",
"type": "progene_text",
"text": [
"Largest subunits of the human SWI / SNF chromatin - remodeling complex promote transcriptional activation by steroid hormone receptors ."
],
"offsets": [
[
0,
136
]
]
}
] |
[
{
"id": "split_0_train_8906_entity",
"type": "progene_text",
"text": [
"SWI / SNF chromatin - remodeling complex"
],
"offsets": [
[
30,
70
]
],
"normalized": []
},
{
"id": "split_0_train_8907_entity",
"type": "progene_text",
"text": [
"steroid hormone receptors"
],
"offsets": [
[
109,
134
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5781
|
split_0_train_5781
|
[
{
"id": "split_0_train_5781_passage",
"type": "progene_text",
"text": [
"The mammalian SWI / SNF - related complexes facilitate gene transcription by remodeling chromatin using the energy of ATP hydrolysis ."
],
"offsets": [
[
0,
134
]
]
}
] |
[
{
"id": "split_0_train_8908_entity",
"type": "progene_text",
"text": [
"SWI / SNF - related complexes"
],
"offsets": [
[
14,
43
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5782
|
split_0_train_5782
|
[
{
"id": "split_0_train_5782_passage",
"type": "progene_text",
"text": [
"The recruitment of these complexes to promoters remains poorly understood and may involve histone modifications or direct interactions with site - specific transcription factors or other cofactors ."
],
"offsets": [
[
0,
198
]
]
}
] |
[
{
"id": "split_0_train_8909_entity",
"type": "progene_text",
"text": [
"histone"
],
"offsets": [
[
90,
97
]
],
"normalized": []
},
{
"id": "split_0_train_8910_entity",
"type": "progene_text",
"text": [
"transcription factors"
],
"offsets": [
[
156,
177
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5783
|
split_0_train_5783
|
[
{
"id": "split_0_train_5783_passage",
"type": "progene_text",
"text": [
"Here we report the isolation of two related but distinct cDNA clones , hOsa1 and hOsa2 , that encode the largest subunits of human SWI / SNF ."
],
"offsets": [
[
0,
142
]
]
}
] |
[
{
"id": "split_0_train_8911_entity",
"type": "progene_text",
"text": [
"hOsa1"
],
"offsets": [
[
71,
76
]
],
"normalized": []
},
{
"id": "split_0_train_8912_entity",
"type": "progene_text",
"text": [
"hOsa2"
],
"offsets": [
[
81,
86
]
],
"normalized": []
},
{
"id": "split_0_train_8913_entity",
"type": "progene_text",
"text": [
"SWI / SNF"
],
"offsets": [
[
131,
140
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5784
|
split_0_train_5784
|
[
{
"id": "split_0_train_5784_passage",
"type": "progene_text",
"text": [
"hOsa1 is identical to previously reported BAF250 , and hOsa2 shares a high degree of sequence similarity with hOsa1 ."
],
"offsets": [
[
0,
117
]
]
}
] |
[
{
"id": "split_0_train_8914_entity",
"type": "progene_text",
"text": [
"hOsa1"
],
"offsets": [
[
0,
5
]
],
"normalized": []
},
{
"id": "split_0_train_8915_entity",
"type": "progene_text",
"text": [
"BAF250"
],
"offsets": [
[
42,
48
]
],
"normalized": []
},
{
"id": "split_0_train_8916_entity",
"type": "progene_text",
"text": [
"hOsa2"
],
"offsets": [
[
55,
60
]
],
"normalized": []
},
{
"id": "split_0_train_8917_entity",
"type": "progene_text",
"text": [
"hOsa1"
],
"offsets": [
[
110,
115
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5785
|
split_0_train_5785
|
[
{
"id": "split_0_train_5785_passage",
"type": "progene_text",
"text": [
"Mass spectrometric analysis , and immunoblotting with antibodies specific to hOsa1 or hOsa2 demonstrate the presence of both proteins in SWI / SNF-A but not in the related polybromo - BRG1 - associated factors complex purified from HeLa cells ."
],
"offsets": [
[
0,
244
]
]
}
] |
[
{
"id": "split_0_train_8918_entity",
"type": "progene_text",
"text": [
"hOsa1"
],
"offsets": [
[
77,
82
]
],
"normalized": []
},
{
"id": "split_0_train_8919_entity",
"type": "progene_text",
"text": [
"hOsa2"
],
"offsets": [
[
86,
91
]
],
"normalized": []
},
{
"id": "split_0_train_8920_entity",
"type": "progene_text",
"text": [
"SWI / SNF-A"
],
"offsets": [
[
137,
148
]
],
"normalized": []
},
{
"id": "split_0_train_8921_entity",
"type": "progene_text",
"text": [
"BRG1"
],
"offsets": [
[
184,
188
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5786
|
split_0_train_5786
|
[
{
"id": "split_0_train_5786_passage",
"type": "progene_text",
"text": [
"Co - precipitation studies indicate that hOsa1 and hOsa2 associate with BRG1 and hBRM through the C - terminal domain of hOsa ."
],
"offsets": [
[
0,
127
]
]
}
] |
[
{
"id": "split_0_train_8922_entity",
"type": "progene_text",
"text": [
"hOsa1"
],
"offsets": [
[
41,
46
]
],
"normalized": []
},
{
"id": "split_0_train_8923_entity",
"type": "progene_text",
"text": [
"hOsa2"
],
"offsets": [
[
51,
56
]
],
"normalized": []
},
{
"id": "split_0_train_8924_entity",
"type": "progene_text",
"text": [
"BRG1"
],
"offsets": [
[
72,
76
]
],
"normalized": []
},
{
"id": "split_0_train_8925_entity",
"type": "progene_text",
"text": [
"hBRM"
],
"offsets": [
[
81,
85
]
],
"normalized": []
},
{
"id": "split_0_train_8926_entity",
"type": "progene_text",
"text": [
"hOsa"
],
"offsets": [
[
121,
125
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5787
|
split_0_train_5787
|
[
{
"id": "split_0_train_5787_passage",
"type": "progene_text",
"text": [
"We define multiple domains within hBRM and BRG1 that interact with the hOsa C terminus ."
],
"offsets": [
[
0,
88
]
]
}
] |
[
{
"id": "split_0_train_8927_entity",
"type": "progene_text",
"text": [
"hBRM"
],
"offsets": [
[
34,
38
]
],
"normalized": []
},
{
"id": "split_0_train_8928_entity",
"type": "progene_text",
"text": [
"BRG1"
],
"offsets": [
[
43,
47
]
],
"normalized": []
},
{
"id": "split_0_train_8929_entity",
"type": "progene_text",
"text": [
"hOsa"
],
"offsets": [
[
71,
75
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5788
|
split_0_train_5788
|
[
{
"id": "split_0_train_5788_passage",
"type": "progene_text",
"text": [
"In cultured mammalian cells , hOsa1 and hOsa2 stimulate transcription by the glucocorticoid , estrogen , and androgen receptors ."
],
"offsets": [
[
0,
129
]
]
}
] |
[
{
"id": "split_0_train_8930_entity",
"type": "progene_text",
"text": [
"hOsa1"
],
"offsets": [
[
30,
35
]
],
"normalized": []
},
{
"id": "split_0_train_8931_entity",
"type": "progene_text",
"text": [
"hOsa2"
],
"offsets": [
[
40,
45
]
],
"normalized": []
},
{
"id": "split_0_train_8932_entity",
"type": "progene_text",
"text": [
"glucocorticoid , estrogen , and androgen receptors"
],
"offsets": [
[
77,
127
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5789
|
split_0_train_5789
|
[
{
"id": "split_0_train_5789_passage",
"type": "progene_text",
"text": [
"The glucocorticoid receptor - mediated activation is not observed with the C - terminal domain or with the hOsa2 polypeptide lacking the ARID DNA binding domain ."
],
"offsets": [
[
0,
162
]
]
}
] |
[
{
"id": "split_0_train_8933_entity",
"type": "progene_text",
"text": [
"glucocorticoid receptor"
],
"offsets": [
[
4,
27
]
],
"normalized": []
},
{
"id": "split_0_train_8934_entity",
"type": "progene_text",
"text": [
"hOsa2"
],
"offsets": [
[
107,
112
]
],
"normalized": []
},
{
"id": "split_0_train_8935_entity",
"type": "progene_text",
"text": [
"ARID"
],
"offsets": [
[
137,
141
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5790
|
split_0_train_5790
|
[
{
"id": "split_0_train_5790_passage",
"type": "progene_text",
"text": [
"These results suggest that hOsa1 and hOsa2 participate in promoting transcriptional activation by the steroid hormone receptors ."
],
"offsets": [
[
0,
129
]
]
}
] |
[
{
"id": "split_0_train_8936_entity",
"type": "progene_text",
"text": [
"hOsa1"
],
"offsets": [
[
27,
32
]
],
"normalized": []
},
{
"id": "split_0_train_8937_entity",
"type": "progene_text",
"text": [
"hOsa2"
],
"offsets": [
[
37,
42
]
],
"normalized": []
},
{
"id": "split_0_train_8938_entity",
"type": "progene_text",
"text": [
"steroid hormone receptors"
],
"offsets": [
[
102,
127
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5791
|
split_0_train_5791
|
[
{
"id": "split_0_train_5791_passage",
"type": "progene_text",
"text": [
"C2PA is a nuclear protein implicated in the heat shock response ."
],
"offsets": [
[
0,
65
]
]
}
] |
[
{
"id": "split_0_train_8939_entity",
"type": "progene_text",
"text": [
"C2PA"
],
"offsets": [
[
0,
4
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5792
|
split_0_train_5792
|
[
{
"id": "split_0_train_5792_passage",
"type": "progene_text",
"text": [
"C2PA is a protein of unknown function that is expressed in spermatocytes ."
],
"offsets": [
[
0,
74
]
]
}
] |
[
{
"id": "split_0_train_8940_entity",
"type": "progene_text",
"text": [
"C2PA"
],
"offsets": [
[
0,
4
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5793
|
split_0_train_5793
|
[
{
"id": "split_0_train_5793_passage",
"type": "progene_text",
"text": [
"PDZ-RGS3 is a signaling molecule whose PDZ domain binds Ephrin - B2 and mediates reverse signaling of this protein ."
],
"offsets": [
[
0,
116
]
]
}
] |
[
{
"id": "split_0_train_8941_entity",
"type": "progene_text",
"text": [
"PDZ-RGS3"
],
"offsets": [
[
0,
8
]
],
"normalized": []
},
{
"id": "split_0_train_8942_entity",
"type": "progene_text",
"text": [
"Ephrin - B2"
],
"offsets": [
[
56,
67
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5794
|
split_0_train_5794
|
[
{
"id": "split_0_train_5794_passage",
"type": "progene_text",
"text": [
"C2PA and PDZ-RGS3 have identical PDZ domains ."
],
"offsets": [
[
0,
46
]
]
}
] |
[
{
"id": "split_0_train_8943_entity",
"type": "progene_text",
"text": [
"C2PA"
],
"offsets": [
[
0,
4
]
],
"normalized": []
},
{
"id": "split_0_train_8944_entity",
"type": "progene_text",
"text": [
"PDZ-RGS3"
],
"offsets": [
[
9,
17
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5795
|
split_0_train_5795
|
[
{
"id": "split_0_train_5795_passage",
"type": "progene_text",
"text": [
"To explore the function of C2PA , we compared it with PDZ-RGS3 with respect to tissue distribution , subcellular localization , and biochemistry ."
],
"offsets": [
[
0,
146
]
]
}
] |
[
{
"id": "split_0_train_8945_entity",
"type": "progene_text",
"text": [
"C2PA"
],
"offsets": [
[
27,
31
]
],
"normalized": []
},
{
"id": "split_0_train_8946_entity",
"type": "progene_text",
"text": [
"PDZ-RGS3"
],
"offsets": [
[
54,
62
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5796
|
split_0_train_5796
|
[
{
"id": "split_0_train_5796_passage",
"type": "progene_text",
"text": [
"C2PA is expressed only in testis , whereas PDZ-RGS3 is expressed in various tissues including brain , heart , lung , liver , spleen , kidney , small intestine , skeletal muscles , and testis ."
],
"offsets": [
[
0,
192
]
]
}
] |
[
{
"id": "split_0_train_8947_entity",
"type": "progene_text",
"text": [
"C2PA"
],
"offsets": [
[
0,
4
]
],
"normalized": []
},
{
"id": "split_0_train_8948_entity",
"type": "progene_text",
"text": [
"PDZ-RGS3"
],
"offsets": [
[
43,
51
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5797
|
split_0_train_5797
|
[
{
"id": "split_0_train_5797_passage",
"type": "progene_text",
"text": [
"These proteins also differ in their subcellular distribution , in that PDZ-RGS3 is cytosolic while C2PA is exclusively nuclear ."
],
"offsets": [
[
0,
128
]
]
}
] |
[
{
"id": "split_0_train_8949_entity",
"type": "progene_text",
"text": [
"PDZ-RGS3"
],
"offsets": [
[
71,
79
]
],
"normalized": []
},
{
"id": "split_0_train_8950_entity",
"type": "progene_text",
"text": [
"C2PA"
],
"offsets": [
[
99,
103
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5798
|
split_0_train_5798
|
[
{
"id": "split_0_train_5798_passage",
"type": "progene_text",
"text": [
"C2PA is distributed diffusely in the nucleus and forms a few foci at 37 degrees C ."
],
"offsets": [
[
0,
83
]
]
}
] |
[
{
"id": "split_0_train_8951_entity",
"type": "progene_text",
"text": [
"C2PA"
],
"offsets": [
[
0,
4
]
],
"normalized": []
}
] |
[] |
[] |
[] |
split_0_train_5799
|
split_0_train_5799
|
[
{
"id": "split_0_train_5799_passage",
"type": "progene_text",
"text": [
"However , when cells are exposed to 42 degrees C , the number of C2PA foci is increased ."
],
"offsets": [
[
0,
89
]
]
}
] |
[
{
"id": "split_0_train_8952_entity",
"type": "progene_text",
"text": [
"C2PA"
],
"offsets": [
[
65,
69
]
],
"normalized": []
}
] |
[] |
[] |
[] |
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