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567 | BioInfer.d461.s0 | [
{
"id": "BioInfer.d461.s0__text",
"type": "Sentence",
"text": [
"One, MORT1 (also called FADD), binds to Fas/APO1 but not to p55-R; another, TRADD, binds to the p55 TNF receptor but not to Fas/APO1; and the third, RIP, binds weakly to both receptors."
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568 | BioInfer.d463.s0 | [
{
"id": "BioInfer.d463.s0__text",
"type": "Sentence",
"text": [
"One such protein is the yeast actin-binding protein Sac6p, which is homologous to vertebrate fimbrin (Adams, A. E. M., D. Botstein, and D. G. Drubin. 1991. Nature (Lond.). 354:404-408.)."
],
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0,
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]
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] | [
{
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569 | BioInfer.d464.s0 | [
{
"id": "BioInfer.d464.s0__text",
"type": "Sentence",
"text": [
"Only the unphosphorylated form of cofilin is an active form that binds actin, whereas the regulatory mechanisms of cofilin have not been elucidated."
],
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"id": "BioInfer.d464.s0.e0",
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570 | BioInfer.d465.s0 | [
{
"id": "BioInfer.d465.s0__text",
"type": "Sentence",
"text": [
"On the basis of these results, we present a model for prereplicative site formation in infected cells in which the helicase-primase components (UL5, UL8, and UL52), the origin-binding protein (UL9), and the viral single-stranded DNA-binding protein (ICP8) assemble together to initiate the process."
],
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] | [
{
"id": "BioInfer.d465.s0.e0",
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{
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571 | BioInfer.d465.s1 | [
{
"id": "BioInfer.d465.s1__text",
"type": "Sentence",
"text": [
"We observed that four replication proteins, UL5, UL8 UL52, and UL9, are necessary for the localization of ICP8 (UL29) to prereplicative sites natural infection conditions."
],
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[
0,
171
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] | [
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572 | BioInfer.d466.s0 | [
{
"id": "BioInfer.d466.s0__text",
"type": "Sentence",
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"On the internal (cytoplasmic) side of focal contacts, several proteins, including talin and vinculin, mediate interactions with the actin filament bundles of the cytoskeleton."
],
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[
0,
175
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]
}
] | [
{
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] | [] | [] | [] |
573 | BioInfer.d467.s0 | [
{
"id": "BioInfer.d467.s0__text",
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"On the other hand, we have recently proposed the importance of cofilin, an actin-binding phosphoprotein, in phagocyte functions through dephosphorylation and translocation to the plasma membrane regions."
],
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574 | BioInfer.d468.s0 | [
{
"id": "BioInfer.d468.s0__text",
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"Opposite effects of cofilin and profilin from porcine brain on rate of exchange of actin-bound adenosine 5'-triphosphate."
],
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[
0,
121
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{
"id": "BioInfer.d468.s0.e0",
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"profilin"
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32,
40
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83,
88
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"type": "Individual_protein",
"text": [
"cofilin"
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20,
27
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],
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}
] | [] | [] | [] |
575 | BioInfer.d469.s0 | [
{
"id": "BioInfer.d469.s0__text",
"type": "Sentence",
"text": [
"Other mammalian actin-binding proteins such as profilin and CapG but also fragmin from Physarum polycephalum are similar targets for PIP2-stimulated pp60(c-src) phosphorylation."
],
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[
0,
177
]
]
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] | [
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"text": [
"CapG"
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60,
64
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74,
81
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{
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"pp60"
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149,
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154,
159
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"id": "BioInfer.d469.s0.e4",
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16,
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47,
55
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"arg2_id": "BioInfer.d469.s0.e2",
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"arg2_id": "BioInfer.d469.s0.e3",
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{
"id": "BioInfer.d469.s0.i8",
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"arg1_id": "BioInfer.d469.s0.e4",
"arg2_id": "BioInfer.d469.s0.e5",
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}
] |
576 | BioInfer.d470.s0 | [
{
"id": "BioInfer.d470.s0__text",
"type": "Sentence",
"text": [
"p53-mediated cell injury exhibited proteolysis of the caspase protein substrate lamin B without appreciable breakdown of TnI."
],
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[
0,
125
]
]
}
] | [
{
"id": "BioInfer.d470.s0.e0",
"type": "Individual_protein",
"text": [
"p53"
],
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0,
3
]
],
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{
"id": "BioInfer.d470.s0.e1",
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"caspase"
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54,
61
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],
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{
"id": "BioInfer.d470.s0.e2",
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121,
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{
"id": "BioInfer.d470.s0.e3",
"type": "Individual_protein",
"text": [
"lamin B"
],
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[
80,
87
]
],
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}
] | [] | [] | [] |
577 | BioInfer.d471.s0 | [
{
"id": "BioInfer.d471.s0__text",
"type": "Sentence",
"text": [
"Other than monomeric actin, no major profilin ligands are detected in crude extracts."
],
"offsets": [
[
0,
85
]
]
}
] | [
{
"id": "BioInfer.d471.s0.e0",
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21,
26
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{
"id": "BioInfer.d471.s0.e1",
"type": "Individual_protein",
"text": [
"profilin"
],
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[
37,
45
]
],
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}
] | [] | [] | [
{
"id": "BioInfer.d471.s0.i0",
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"arg2_id": "BioInfer.d471.s0.e1",
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}
] |
578 | BioInfer.d471.s1 | [
{
"id": "BioInfer.d471.s1__text",
"type": "Sentence",
"text": [
"Our results show that the major pool of polymerizable actin monomers is complexed with profilin and spread throughout the cytoplasm."
],
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[
0,
132
]
]
}
] | [
{
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87,
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"id": "BioInfer.d471.s1.e1",
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"actin"
],
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54,
59
]
],
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}
] | [] | [] | [
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"arg2_id": "BioInfer.d471.s1.e1",
"normalized": []
}
] |
579 | BioInfer.d471.s2 | [
{
"id": "BioInfer.d471.s2__text",
"type": "Sentence",
"text": [
"Selective monoclonal antibodies confirm that most of the profilin is bound to actin: 65% in extract immunoadsorption assays and 74-89% by fluorescent antibody staining."
],
"offsets": [
[
0,
168
]
]
}
] | [
{
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57,
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{
"id": "BioInfer.d471.s2.e1",
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"text": [
"actin"
],
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78,
83
]
],
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}
] | [] | [] | [
{
"id": "BioInfer.d471.s2.i0",
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"arg2_id": "BioInfer.d471.s2.e1",
"normalized": []
}
] |
580 | BioInfer.d471.s3 | [
{
"id": "BioInfer.d471.s3__text",
"type": "Sentence",
"text": [
"We used biochemical fractionation, immunoassays and microscopy of live and fixed Acanthamoeba to determine how much profilin is bound to its known ligands: actin, membrane PIP(2), Arp2/3 complex and polyproline sequences."
],
"offsets": [
[
0,
221
]
]
}
] | [
{
"id": "BioInfer.d471.s3.e0",
"type": "Individual_protein",
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],
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180,
184
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116,
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{
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156,
161
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{
"id": "BioInfer.d471.s3.e3",
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"3"
],
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[
180,
183
],
[
185,
186
]
],
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}
] | [] | [] | [
{
"id": "BioInfer.d471.s3.i0",
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"arg2_id": "BioInfer.d471.s3.e3",
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}
] |
581 | BioInfer.d473.s0 | [
{
"id": "BioInfer.d473.s0__text",
"type": "Sentence",
"text": [
"Our data, which suggest that pollen profilin can regulate actin-based cytoskeletal protein assembly and protein kinase or phosphatase activity, indicate a possible role for the involvement of profilin in signaling pathways that may regulate pollen tube growth."
],
"offsets": [
[
0,
260
]
]
}
] | [
{
"id": "BioInfer.d473.s0.e0",
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],
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58,
63
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},
{
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36,
44
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},
{
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192,
200
]
],
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},
{
"id": "BioInfer.d473.s0.e3",
"type": "Protein_family_or_group",
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],
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104,
118
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],
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},
{
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"phosphatase"
],
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104,
111
],
[
122,
133
]
],
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}
] | [] | [] | [
{
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{
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"arg1_id": "BioInfer.d473.s0.e1",
"arg2_id": "BioInfer.d473.s0.e4",
"normalized": []
}
] |
582 | BioInfer.d474.s0 | [
{
"id": "BioInfer.d474.s0__text",
"type": "Sentence",
"text": [
"Our in vitro recombinant protein-protein interaction studies demonstrated that Stat1 could directly interact with TNFR1 and TRADD but not with FADD."
],
"offsets": [
[
0,
148
]
]
}
] | [
{
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"text": [
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],
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79,
84
]
],
"normalized": []
},
{
"id": "BioInfer.d474.s0.e1",
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],
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124,
129
]
],
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},
{
"id": "BioInfer.d474.s0.e2",
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],
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114,
119
]
],
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},
{
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"type": "Individual_protein",
"text": [
"FADD"
],
"offsets": [
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143,
147
]
],
"normalized": []
}
] | [] | [] | [
{
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"arg2_id": "BioInfer.d474.s0.e3",
"normalized": []
}
] |
583 | BioInfer.d479.s0 | [
{
"id": "BioInfer.d479.s0__text",
"type": "Sentence",
"text": [
"p21 (p21WAF1/Cip1), a cyclin-dependent kinase inhibitor, induces G1 arrest and can inhibit the activity of the proliferating cell nuclear antigen (PCNA)."
],
"offsets": [
[
0,
153
]
]
}
] | [
{
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],
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0,
3
]
],
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},
{
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"text": [
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],
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147,
151
]
],
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},
{
"id": "BioInfer.d479.s0.e2",
"type": "Individual_protein",
"text": [
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],
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13,
17
]
],
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},
{
"id": "BioInfer.d479.s0.e3",
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"text": [
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],
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5,
12
]
],
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},
{
"id": "BioInfer.d479.s0.e4",
"type": "Individual_protein",
"text": [
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],
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[
111,
145
]
],
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},
{
"id": "BioInfer.d479.s0.e5",
"type": "Protein_family_or_group",
"text": [
"cyclin-dependent kinase inhibitor"
],
"offsets": [
[
22,
55
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d479.s0.i0",
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{
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{
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"arg1_id": "BioInfer.d479.s0.e3",
"arg2_id": "BioInfer.d479.s0.e5",
"normalized": []
}
] |
584 | BioInfer.d480.s0 | [
{
"id": "BioInfer.d480.s0__text",
"type": "Sentence",
"text": [
"Panels of six to 31 MAbs against the haemagglutinin (H), fusion (F), nucleocapsid protein (NP), phosphoprotein (P) and matrix (M) proteins of MV and the H, F, NP and P proteins of CDV were employed."
],
"offsets": [
[
0,
198
]
]
}
] | [
{
"id": "BioInfer.d480.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"NP",
"proteins"
],
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159,
161
],
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168,
176
]
],
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},
{
"id": "BioInfer.d480.s0.e1",
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65,
66
]
],
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},
{
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57,
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130,
138
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{
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119,
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130,
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{
"id": "BioInfer.d480.s0.e4",
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37,
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130,
138
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{
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69,
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130,
138
]
],
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},
{
"id": "BioInfer.d480.s0.e6",
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"proteins"
],
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153,
154
],
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168,
176
]
],
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{
"id": "BioInfer.d480.s0.e7",
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166,
176
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{
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96,
110
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130,
138
]
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},
{
"id": "BioInfer.d480.s0.e9",
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156,
157
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168,
176
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{
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53,
54
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],
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{
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112,
113
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{
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"type": "Individual_protein",
"text": [
"NP"
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91,
93
]
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{
"id": "BioInfer.d480.s0.e13",
"type": "Individual_protein",
"text": [
"M"
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[
127,
128
]
],
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}
] | [] | [] | [] |
585 | BioInfer.d481.s0 | [
{
"id": "BioInfer.d481.s0__text",
"type": "Sentence",
"text": [
"Particle aggregates associated with this array of actin microfilaments also labeled with antibodies to vinculin, talin and beta 1-integrin."
],
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[
0,
139
]
]
}
] | [
{
"id": "BioInfer.d481.s0.e0",
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"actin"
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50,
55
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113,
118
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103,
111
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{
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"text": [
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123,
138
]
],
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}
] | [] | [] | [] |
586 | BioInfer.d482.s0 | [
{
"id": "BioInfer.d482.s0__text",
"type": "Sentence",
"text": [
"P-cadherin expression is a better indicator of clinical outcome than alterations in the expression of E-cadherin, N-cadherin, alpha-catenin, or beta-catenin."
],
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[
0,
157
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]
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"id": "BioInfer.d482.s0.e0",
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"alpha-catenin"
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126,
139
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102,
112
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144,
156
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{
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"text": [
"P-cadherin"
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0,
10
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{
"id": "BioInfer.d482.s0.e4",
"type": "Gene/protein/RNA",
"text": [
"N-cadherin"
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114,
124
]
],
"normalized": []
}
] | [] | [] | [] |
587 | BioInfer.d484.s0 | [
{
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"type": "Sentence",
"text": [
"Pervanadate caused a dramatic augmentation of the phosphorylation of E-cadherin, beta-catenin, and gamma-catenin (plakoglobin), but alpha-catenin was not detectably phosphorylated."
],
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[
0,
180
]
]
}
] | [
{
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"type": "Individual_protein",
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99,
112
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69,
79
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{
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114,
125
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{
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81,
93
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{
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"text": [
"alpha-catenin"
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[
132,
145
]
],
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}
] | [] | [] | [] |
588 | BioInfer.d486.s0 | [
{
"id": "BioInfer.d486.s0__text",
"type": "Sentence",
"text": [
"Phosphoinositides bind to profilin and regulate actin-based cytoskeletal protein assembly."
],
"offsets": [
[
0,
90
]
]
}
] | [
{
"id": "BioInfer.d486.s0.e0",
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"actin"
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48,
53
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{
"id": "BioInfer.d486.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"profilin"
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26,
34
]
],
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}
] | [] | [] | [] |
589 | BioInfer.d486.s1 | [
{
"id": "BioInfer.d486.s1__text",
"type": "Sentence",
"text": [
"Phosphorylation of profilin by PKC was not affected by the presence of various concentrations of actin."
],
"offsets": [
[
0,
103
]
]
}
] | [
{
"id": "BioInfer.d486.s1.e0",
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],
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97,
102
]
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},
{
"id": "BioInfer.d486.s1.e1",
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19,
27
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},
{
"id": "BioInfer.d486.s1.e2",
"type": "Individual_protein",
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],
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31,
34
]
],
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}
] | [] | [] | [
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"arg2_id": "BioInfer.d486.s1.e2",
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}
] |
590 | BioInfer.d487.s0 | [
{
"id": "BioInfer.d487.s0__text",
"type": "Sentence",
"text": [
"Phosphorylation of the headpiece domain could regulate the actin binding and bundling properties of fimbrin, or it could regulate the interaction of fimbrin with other proteins."
],
"offsets": [
[
0,
177
]
]
}
] | [
{
"id": "BioInfer.d487.s0.e0",
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59,
64
]
],
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},
{
"id": "BioInfer.d487.s0.e1",
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100,
107
]
],
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},
{
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"type": "Individual_protein",
"text": [
"fimbrin"
],
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149,
156
]
],
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}
] | [] | [] | [
{
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"arg1_id": "BioInfer.d487.s0.e1",
"arg2_id": "BioInfer.d487.s0.e2",
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}
] |
591 | BioInfer.d488.s0 | [
{
"id": "BioInfer.d488.s0__text",
"type": "Sentence",
"text": [
"Photochemical cleavage of myosin heavy chain and the effect on the interaction with actin."
],
"offsets": [
[
0,
90
]
]
}
] | [
{
"id": "BioInfer.d488.s0.e0",
"type": "Individual_protein",
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],
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84,
89
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],
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},
{
"id": "BioInfer.d488.s0.e1",
"type": "Individual_protein",
"text": [
"myosin heavy chain"
],
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[
26,
44
]
],
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}
] | [] | [] | [
{
"id": "BioInfer.d488.s0.i0",
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"arg2_id": "BioInfer.d488.s0.e1",
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}
] |
592 | BioInfer.d490.s0 | [
{
"id": "BioInfer.d490.s0__text",
"type": "Sentence",
"text": [
"Polyacrylamide gels of platelets heated at 45 degrees C for 90 minutes showed an increase in talin incorporation into heated platelet cytoskeletons but no increase in filamentous actin."
],
"offsets": [
[
0,
185
]
]
}
] | [
{
"id": "BioInfer.d490.s0.e0",
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],
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179,
184
]
],
"normalized": []
},
{
"id": "BioInfer.d490.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"talin"
],
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[
93,
98
]
],
"normalized": []
}
] | [] | [] | [] |
593 | BioInfer.d492.s0 | [
{
"id": "BioInfer.d492.s0__text",
"type": "Sentence",
"text": [
"Previously, we have shown that in the absence of RAD52, repair is nearly absent and diploid cells lose the broken chromosome; however, in cells lacking RAD51, gene conversion is absent but cells can repair the DSB by BIR."
],
"offsets": [
[
0,
221
]
]
}
] | [
{
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49,
54
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{
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"type": "Gene/protein/RNA",
"text": [
"RAD51"
],
"offsets": [
[
152,
157
]
],
"normalized": []
}
] | [] | [] | [] |
594 | BioInfer.d493.s0 | [
{
"id": "BioInfer.d493.s0__text",
"type": "Sentence",
"text": [
"Previous studies have yielded conflicting results concerning the physiological role of profilin, a 12-15-kD actin- and phosphoinositide-binding protein, as a regulator of actin polymerization."
],
"offsets": [
[
0,
192
]
]
}
] | [
{
"id": "BioInfer.d493.s0.e0",
"type": "Individual_protein",
"text": [
"profilin"
],
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87,
95
]
],
"normalized": []
},
{
"id": "BioInfer.d493.s0.e1",
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"text": [
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108,
113
]
],
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},
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"text": [
"actin"
],
"offsets": [
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171,
176
]
],
"normalized": []
}
] | [] | [] | [
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"arg2_id": "BioInfer.d493.s0.e2",
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}
] |
595 | BioInfer.d494.s0 | [
{
"id": "BioInfer.d494.s0__text",
"type": "Sentence",
"text": [
"Production of PIP and PIP2 may be important downstream signals since these polyphosphoinositides are able to regulate the interaction of gelsolin and profilin with actin."
],
"offsets": [
[
0,
170
]
]
}
] | [
{
"id": "BioInfer.d494.s0.e0",
"type": "Individual_protein",
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],
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164,
169
]
],
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},
{
"id": "BioInfer.d494.s0.e1",
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],
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137,
145
]
],
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{
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"type": "Individual_protein",
"text": [
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],
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150,
158
]
],
"normalized": []
}
] | [] | [] | [
{
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"arg2_id": "BioInfer.d494.s0.e2",
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}
] |
596 | BioInfer.d495.s0 | [
{
"id": "BioInfer.d495.s0__text",
"type": "Sentence",
"text": [
"Profilin I and profilin II have similar affinities for PtdIns(4,5)P2 and poly(L-proline), and both accelerate nucleotide exchange on monomeric actin to the same extent."
],
"offsets": [
[
0,
168
]
]
}
] | [
{
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],
"offsets": [
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143,
148
]
],
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},
{
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15,
26
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},
{
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"type": "Individual_protein",
"text": [
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],
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0,
10
]
],
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}
] | [] | [] | [
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"arg1_id": "BioInfer.d495.s0.e1",
"arg2_id": "BioInfer.d495.s0.e2",
"normalized": []
}
] |
597 | BioInfer.d496.s0 | [
{
"id": "BioInfer.d496.s0__text",
"type": "Sentence",
"text": [
"Profilin II binds actin with a similar affinity to that of profilin I, although it inhibits actin polymerization more strongly than profilin I under non-equilibrium conditions."
],
"offsets": [
[
0,
176
]
]
}
] | [
{
"id": "BioInfer.d496.s0.e0",
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59,
69
]
],
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},
{
"id": "BioInfer.d496.s0.e1",
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0,
11
]
],
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},
{
"id": "BioInfer.d496.s0.e2",
"type": "Individual_protein",
"text": [
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132,
142
]
],
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{
"id": "BioInfer.d496.s0.e3",
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18,
23
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},
{
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"text": [
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],
"offsets": [
[
92,
97
]
],
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}
] | [] | [] | [
{
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"arg2_id": "BioInfer.d496.s0.e4",
"normalized": []
}
] |
598 | BioInfer.d496.s1 | [
{
"id": "BioInfer.d496.s1__text",
"type": "Sentence",
"text": [
"Since functional characteristics for profilin II are lacking, we assayed the actin, the phosphatidylinositol 4,5-bisphosphate and the poly(L-proline) binding properties of this isoform."
],
"offsets": [
[
0,
185
]
]
}
] | [
{
"id": "BioInfer.d496.s1.e0",
"type": "Individual_protein",
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37,
48
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],
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},
{
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"type": "Individual_protein",
"text": [
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],
"offsets": [
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77,
82
]
],
"normalized": []
}
] | [] | [] | [
{
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"arg2_id": "BioInfer.d496.s1.e1",
"normalized": []
}
] |
599 | BioInfer.d497.s0 | [
{
"id": "BioInfer.d497.s0__text",
"type": "Sentence",
"text": [
"Profilin is generally thought to regulate actin polymerization, but the observation that acidic phospholipids dissociate the complex of profilin and actin raised the possibility that profilin might also regulate lipid metabolism."
],
"offsets": [
[
0,
229
]
]
}
] | [
{
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149,
154
]
],
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},
{
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0,
8
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{
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136,
144
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],
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{
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42,
47
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"type": "Gene/protein/RNA",
"text": [
"profilin"
],
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[
183,
191
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d497.s0.i0",
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"arg1_id": "BioInfer.d497.s0.e1",
"arg2_id": "BioInfer.d497.s0.e3",
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}
] |
600 | BioInfer.d497.s1 | [
{
"id": "BioInfer.d497.s1__text",
"type": "Sentence",
"text": [
"The actin-binding protein profilin binds to PIP2 and inhibits its hydrolysis by phospholipase C."
],
"offsets": [
[
0,
96
]
]
}
] | [
{
"id": "BioInfer.d497.s1.e0",
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],
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4,
25
]
],
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},
{
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26,
34
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},
{
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"type": "Individual_protein",
"text": [
"phospholipase C"
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80,
95
]
],
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}
] | [] | [] | [
{
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"arg1_id": "BioInfer.d497.s1.e0",
"arg2_id": "BioInfer.d497.s1.e1",
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] |
601 | BioInfer.d497.s2 | [
{
"id": "BioInfer.d497.s2__text",
"type": "Sentence",
"text": [
"The cellular concentrations and binding characteristics of these molecules are consistent with profilin being a negative regulator of the phosphoinositide signaling pathway in addition to its established function as an inhibitor of actin polymerization."
],
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[
0,
253
]
]
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] | [
{
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232,
237
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},
{
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"type": "Individual_protein",
"text": [
"profilin"
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[
95,
103
]
],
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}
] | [] | [] | [
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"arg2_id": "BioInfer.d497.s2.e1",
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}
] |
602 | BioInfer.d498.s0 | [
{
"id": "BioInfer.d498.s0__text",
"type": "Sentence",
"text": [
"Profilins also bind polyphosphoinositides, which can disrupt the profilin-actin complex, and proline-rich ligands which localize profilin to sites requiring extensive actin filament accumulation."
],
"offsets": [
[
0,
195
]
]
}
] | [
{
"id": "BioInfer.d498.s0.e0",
"type": "Individual_protein",
"text": [
"actin"
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74,
79
]
],
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},
{
"id": "BioInfer.d498.s0.e1",
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65,
73
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},
{
"id": "BioInfer.d498.s0.e2",
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167,
172
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],
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},
{
"id": "BioInfer.d498.s0.e3",
"type": "Individual_protein",
"text": [
"Profilins"
],
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0,
9
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],
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},
{
"id": "BioInfer.d498.s0.e4",
"type": "Individual_protein",
"text": [
"profilin"
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129,
137
]
],
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}
] | [] | [] | [
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"id": "BioInfer.d498.s0.i0",
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"arg2_id": "BioInfer.d498.s0.e1",
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{
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{
"id": "BioInfer.d498.s0.i2",
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"arg1_id": "BioInfer.d498.s0.e1",
"arg2_id": "BioInfer.d498.s0.e3",
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}
] |
603 | BioInfer.d500.s0 | [
{
"id": "BioInfer.d500.s0__text",
"type": "Sentence",
"text": [
"Proteolytic activity was not detected with casein, actin, or myosin heavy-chain substrates."
],
"offsets": [
[
0,
91
]
]
}
] | [
{
"id": "BioInfer.d500.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"actin"
],
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[
51,
56
]
],
"normalized": []
},
{
"id": "BioInfer.d500.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"myosin heavy-chain"
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[
61,
79
]
],
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},
{
"id": "BioInfer.d500.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"casein"
],
"offsets": [
[
43,
49
]
],
"normalized": []
}
] | [] | [] | [] |
604 | BioInfer.d501.s0 | [
{
"id": "BioInfer.d501.s0__text",
"type": "Sentence",
"text": [
"PS1 fragments form complexes with E-cadherin, beta-catenin, and alpha-catenin, all components of adherens junctions."
],
"offsets": [
[
0,
116
]
]
}
] | [
{
"id": "BioInfer.d501.s0.e0",
"type": "Individual_protein",
"text": [
"PS1"
],
"offsets": [
[
0,
3
]
],
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},
{
"id": "BioInfer.d501.s0.e1",
"type": "Individual_protein",
"text": [
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],
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46,
58
]
],
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},
{
"id": "BioInfer.d501.s0.e2",
"type": "Individual_protein",
"text": [
"E-cadherin"
],
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[
34,
44
]
],
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},
{
"id": "BioInfer.d501.s0.e3",
"type": "Individual_protein",
"text": [
"alpha-catenin"
],
"offsets": [
[
64,
77
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d501.s0.i0",
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"arg1_id": "BioInfer.d501.s0.e0",
"arg2_id": "BioInfer.d501.s0.e1",
"normalized": []
},
{
"id": "BioInfer.d501.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d501.s0.e0",
"arg2_id": "BioInfer.d501.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d501.s0.i2",
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"arg1_id": "BioInfer.d501.s0.e0",
"arg2_id": "BioInfer.d501.s0.e3",
"normalized": []
},
{
"id": "BioInfer.d501.s0.i3",
"type": "PPI",
"arg1_id": "BioInfer.d501.s0.e1",
"arg2_id": "BioInfer.d501.s0.e2",
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},
{
"id": "BioInfer.d501.s0.i4",
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"arg1_id": "BioInfer.d501.s0.e1",
"arg2_id": "BioInfer.d501.s0.e3",
"normalized": []
},
{
"id": "BioInfer.d501.s0.i5",
"type": "PPI",
"arg1_id": "BioInfer.d501.s0.e2",
"arg2_id": "BioInfer.d501.s0.e3",
"normalized": []
}
] |
605 | BioInfer.d502.s0 | [
{
"id": "BioInfer.d502.s0__text",
"type": "Sentence",
"text": [
"PtK2 cells of exceptionally large size were microinjected with fluorescently labeled probes for actin, myosin, filamin, and talin in order to follow the assembly of the contractile proteins into the cleavage furrows."
],
"offsets": [
[
0,
216
]
]
}
] | [
{
"id": "BioInfer.d502.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"filamin"
],
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[
111,
118
]
],
"normalized": []
},
{
"id": "BioInfer.d502.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"actin"
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[
96,
101
]
],
"normalized": []
},
{
"id": "BioInfer.d502.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"talin"
],
"offsets": [
[
124,
129
]
],
"normalized": []
},
{
"id": "BioInfer.d502.s0.e3",
"type": "Gene/protein/RNA",
"text": [
"myosin"
],
"offsets": [
[
103,
109
]
],
"normalized": []
}
] | [] | [] | [] |
606 | BioInfer.d502.s1 | [
{
"id": "BioInfer.d502.s1__text",
"type": "Sentence",
"text": [
"The presence of filamin in the cleavage furrows also suggests the possibility of an overlapping mechanism in addition to that of a talin mediated mechanism for the attachment of actin filaments to the cell surfaces in the cleavage furrow."
],
"offsets": [
[
0,
238
]
]
}
] | [
{
"id": "BioInfer.d502.s1.e0",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
178,
183
]
],
"normalized": []
},
{
"id": "BioInfer.d502.s1.e1",
"type": "Individual_protein",
"text": [
"talin"
],
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131,
136
]
],
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},
{
"id": "BioInfer.d502.s1.e2",
"type": "Gene/protein/RNA",
"text": [
"filamin"
],
"offsets": [
[
16,
23
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d502.s1.i0",
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"arg1_id": "BioInfer.d502.s1.e0",
"arg2_id": "BioInfer.d502.s1.e1",
"normalized": []
}
] |
607 | BioInfer.d505.s0 | [
{
"id": "BioInfer.d505.s0__text",
"type": "Sentence",
"text": [
"Pyrenyliodoacetamide labeling of cysteine 374 of muscle actin reduces the affinity for profilin 10-fold."
],
"offsets": [
[
0,
104
]
]
}
] | [
{
"id": "BioInfer.d505.s0.e0",
"type": "Individual_protein",
"text": [
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],
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49,
61
]
],
"normalized": []
},
{
"id": "BioInfer.d505.s0.e1",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
87,
95
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d505.s0.i0",
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"arg1_id": "BioInfer.d505.s0.e0",
"arg2_id": "BioInfer.d505.s0.e1",
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}
] |
608 | BioInfer.d505.s1 | [
{
"id": "BioInfer.d505.s1__text",
"type": "Sentence",
"text": [
"Replacement of serine 38 with cysteine created a unique site where labeling with rhodamine did not alter the affinity of profilin for actin."
],
"offsets": [
[
0,
140
]
]
}
] | [
{
"id": "BioInfer.d505.s1.e0",
"type": "Individual_protein",
"text": [
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],
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134,
139
]
],
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},
{
"id": "BioInfer.d505.s1.e1",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
121,
129
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d505.s1.i0",
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"arg1_id": "BioInfer.d505.s1.e0",
"arg2_id": "BioInfer.d505.s1.e1",
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}
] |
609 | BioInfer.d505.s2 | [
{
"id": "BioInfer.d505.s2__text",
"type": "Sentence",
"text": [
"Three methods, fluorescence anisotropy of rhodamine-labeled profilin, intrinsic fluorescence and nucleotide exchange, give the same affinity, Kd = 0.1 microM, for Acanthamoeba profilins binding amoeba actin monomers with bound Mg-ATP."
],
"offsets": [
[
0,
234
]
]
}
] | [
{
"id": "BioInfer.d505.s2.e0",
"type": "Individual_protein",
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],
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201,
206
]
],
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},
{
"id": "BioInfer.d505.s2.e1",
"type": "Gene/protein/RNA",
"text": [
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],
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60,
68
]
],
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},
{
"id": "BioInfer.d505.s2.e2",
"type": "Individual_protein",
"text": [
"profilins"
],
"offsets": [
[
176,
185
]
],
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}
] | [] | [] | [
{
"id": "BioInfer.d505.s2.i0",
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"arg1_id": "BioInfer.d505.s2.e0",
"arg2_id": "BioInfer.d505.s2.e2",
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}
] |
610 | BioInfer.d506.s0 | [
{
"id": "BioInfer.d506.s0__text",
"type": "Sentence",
"text": [
"Quantitation of the appearance of X22 banding in primary cultures of myotubes indicates that it precedes that of other myofibrillar proteins and that assembly takes place in the following order: X22, titin, myosin heavy chain, actin, and desmin."
],
"offsets": [
[
0,
245
]
]
}
] | [
{
"id": "BioInfer.d506.s0.e0",
"type": "Individual_protein",
"text": [
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227,
232
]
],
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},
{
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195,
198
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},
{
"id": "BioInfer.d506.s0.e2",
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200,
205
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],
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},
{
"id": "BioInfer.d506.s0.e3",
"type": "Gene/protein/RNA",
"text": [
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34,
37
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},
{
"id": "BioInfer.d506.s0.e4",
"type": "Individual_protein",
"text": [
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238,
244
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},
{
"id": "BioInfer.d506.s0.e5",
"type": "Individual_protein",
"text": [
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],
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[
207,
225
]
],
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}
] | [] | [] | [
{
"id": "BioInfer.d506.s0.i0",
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{
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{
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{
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{
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{
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"arg2_id": "BioInfer.d506.s0.e4",
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},
{
"id": "BioInfer.d506.s0.i8",
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{
"id": "BioInfer.d506.s0.i9",
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"arg1_id": "BioInfer.d506.s0.e4",
"arg2_id": "BioInfer.d506.s0.e5",
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}
] |
611 | BioInfer.d507.s0 | [
{
"id": "BioInfer.d507.s0__text",
"type": "Sentence",
"text": [
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],
"offsets": [
[
0,
273
]
]
}
] | [
{
"id": "BioInfer.d507.s0.e0",
"type": "Protein_family_or_group",
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151,
166
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177,
182
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{
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113,
122
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{
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"type": "Individual_protein",
"text": [
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],
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124,
130
]
],
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}
] | [] | [] | [
{
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}
] |
612 | BioInfer.d509.s0 | [
{
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"type": "Sentence",
"text": [
"Recombinant human beta-catenin can simultaneously bind to the alpha-catenin/actin complex but does not bind actin directly."
],
"offsets": [
[
0,
123
]
]
}
] | [
{
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18,
30
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108,
113
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{
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{
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"text": [
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],
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62,
75
]
],
"normalized": []
}
] | [] | [] | [
{
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}
] |
613 | BioInfer.d510.s0 | [
{
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"type": "Sentence",
"text": [
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],
"offsets": [
[
0,
86
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]
}
] | [
{
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46,
51
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},
{
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17,
42
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],
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] | [] | [] | [
{
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"arg1_id": "BioInfer.d510.s0.e0",
"arg2_id": "BioInfer.d510.s0.e1",
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}
] |
614 | BioInfer.d512.s0 | [
{
"id": "BioInfer.d512.s0__text",
"type": "Sentence",
"text": [
"Reduced E-cadherin, alpha-catenin, beta-catenin and plakoglobin expression correlated closely with the differentiation grade of the esophageal squamous cell carcinoma (p < 0.05)."
],
"offsets": [
[
0,
178
]
]
}
] | [
{
"id": "BioInfer.d512.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"plakoglobin"
],
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52,
63
]
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{
"id": "BioInfer.d512.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"alpha-catenin"
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20,
33
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{
"id": "BioInfer.d512.s0.e2",
"type": "Gene/protein/RNA",
"text": [
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35,
47
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{
"id": "BioInfer.d512.s0.e3",
"type": "Gene/protein/RNA",
"text": [
"E-cadherin"
],
"offsets": [
[
8,
18
]
],
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}
] | [] | [] | [] |
615 | BioInfer.d514.s0 | [
{
"id": "BioInfer.d514.s0__text",
"type": "Sentence",
"text": [
"Reduced expression of E-cadherin and alpha-catenin, as well as mutations in the E-cadherin gene, have been found in various carcinomas, whereas mutations in the alpha- and beta-catenin genes have been described only in carcinoma cell lines."
],
"offsets": [
[
0,
240
]
]
}
] | [
{
"id": "BioInfer.d514.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"alpha-",
"catenin"
],
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161,
167
],
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177,
184
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"id": "BioInfer.d514.s0.e1",
"type": "Gene/protein/RNA",
"text": [
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37,
50
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"id": "BioInfer.d514.s0.e2",
"type": "Gene/protein/RNA",
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172,
184
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{
"id": "BioInfer.d514.s0.e3",
"type": "Gene/protein/RNA",
"text": [
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22,
32
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{
"id": "BioInfer.d514.s0.e4",
"type": "Gene/protein/RNA",
"text": [
"E-cadherin"
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[
80,
90
]
],
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}
] | [] | [] | [] |
616 | BioInfer.d515.s0 | [
{
"id": "BioInfer.d515.s0__text",
"type": "Sentence",
"text": [
"Regulation of myosin heavy chain and actin isogenes during cardiac growth and hypertrophy."
],
"offsets": [
[
0,
90
]
]
}
] | [
{
"id": "BioInfer.d515.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"myosin heavy chain"
],
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14,
32
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],
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},
{
"id": "BioInfer.d515.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"actin"
],
"offsets": [
[
37,
42
]
],
"normalized": []
}
] | [] | [] | [] |
617 | BioInfer.d517.s0 | [
{
"id": "BioInfer.d517.s0__text",
"type": "Sentence",
"text": [
"Removal of one nonhomologous DNA end during gene conversion by a RAD1- and MSH2-independent pathway."
],
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[
0,
100
]
]
}
] | [
{
"id": "BioInfer.d517.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"RAD1"
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65,
69
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],
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{
"id": "BioInfer.d517.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"MSH2"
],
"offsets": [
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75,
79
]
],
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}
] | [] | [] | [] |
618 | BioInfer.d519.s0 | [
{
"id": "BioInfer.d519.s0__text",
"type": "Sentence",
"text": [
"Requirement of the yeast MSH3 and MSH6 genes for MSH2-dependent genomic stability."
],
"offsets": [
[
0,
82
]
]
}
] | [
{
"id": "BioInfer.d519.s0.e0",
"type": "Gene",
"text": [
"MSH2"
],
"offsets": [
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49,
53
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],
"normalized": []
},
{
"id": "BioInfer.d519.s0.e1",
"type": "Gene",
"text": [
"MSH6"
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34,
38
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],
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},
{
"id": "BioInfer.d519.s0.e2",
"type": "Gene",
"text": [
"MSH3"
],
"offsets": [
[
25,
29
]
],
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}
] | [] | [] | [
{
"id": "BioInfer.d519.s0.i0",
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"arg2_id": "BioInfer.d519.s0.e1",
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{
"id": "BioInfer.d519.s0.i1",
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"arg1_id": "BioInfer.d519.s0.e0",
"arg2_id": "BioInfer.d519.s0.e2",
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}
] |
619 | BioInfer.d519.s1 | [
{
"id": "BioInfer.d519.s1__text",
"type": "Sentence",
"text": [
"Results from epistasis analyses indicate that MSH2 functions in mismatch repair in conjunction with MSH3 or MSH6 and that MSH3 and MSH6 constitute alternate pathways of MSH2-dependent mismatch repair."
],
"offsets": [
[
0,
200
]
]
}
] | [
{
"id": "BioInfer.d519.s1.e0",
"type": "Gene",
"text": [
"MSH6"
],
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108,
112
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],
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},
{
"id": "BioInfer.d519.s1.e1",
"type": "Gene",
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46,
50
]
],
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},
{
"id": "BioInfer.d519.s1.e2",
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131,
135
]
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},
{
"id": "BioInfer.d519.s1.e3",
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"text": [
"MSH3"
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100,
104
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],
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},
{
"id": "BioInfer.d519.s1.e4",
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169,
173
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},
{
"id": "BioInfer.d519.s1.e5",
"type": "Gene",
"text": [
"MSH3"
],
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122,
126
]
],
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}
] | [] | [] | [
{
"id": "BioInfer.d519.s1.i0",
"type": "PPI",
"arg1_id": "BioInfer.d519.s1.e0",
"arg2_id": "BioInfer.d519.s1.e1",
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{
"id": "BioInfer.d519.s1.i1",
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"arg2_id": "BioInfer.d519.s1.e3",
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{
"id": "BioInfer.d519.s1.i2",
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{
"id": "BioInfer.d519.s1.i3",
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"arg1_id": "BioInfer.d519.s1.e4",
"arg2_id": "BioInfer.d519.s1.e5",
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}
] |
620 | BioInfer.d520.s0 | [
{
"id": "BioInfer.d520.s0__text",
"type": "Sentence",
"text": [
"Requirement of yeast fimbrin for actin organization and morphogenesis in vivo."
],
"offsets": [
[
0,
78
]
]
}
] | [
{
"id": "BioInfer.d520.s0.e0",
"type": "Individual_protein",
"text": [
"actin"
],
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33,
38
]
],
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},
{
"id": "BioInfer.d520.s0.e1",
"type": "Individual_protein",
"text": [
"fimbrin"
],
"offsets": [
[
21,
28
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d520.s0.i0",
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"arg1_id": "BioInfer.d520.s0.e0",
"arg2_id": "BioInfer.d520.s0.e1",
"normalized": []
}
] |
621 | BioInfer.d521.s0 | [
{
"id": "BioInfer.d521.s0__text",
"type": "Sentence",
"text": [
"Resonance energy transfer determination of the following distances, using a hybrid myosin: those between Cys-55 on the Mercenaria regulatory light chain, SH-1 on the Aequipecten myosin heavy chain, and Cys-374 of actin."
],
"offsets": [
[
0,
219
]
]
}
] | [
{
"id": "BioInfer.d521.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"myosin heavy chain"
],
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178,
196
]
],
"normalized": []
},
{
"id": "BioInfer.d521.s0.e1",
"type": "Gene/protein/RNA",
"text": [
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83,
89
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],
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},
{
"id": "BioInfer.d521.s0.e2",
"type": "Gene/protein/RNA",
"text": [
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213,
218
]
],
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},
{
"id": "BioInfer.d521.s0.e3",
"type": "Gene/protein/RNA",
"text": [
"regulatory light chain"
],
"offsets": [
[
130,
152
]
],
"normalized": []
}
] | [] | [] | [] |
622 | BioInfer.d522.s0 | [
{
"id": "BioInfer.d522.s0__text",
"type": "Sentence",
"text": [
"Reversible binding of actin to gelsolin and profilin in human platelet extracts."
],
"offsets": [
[
0,
80
]
]
}
] | [
{
"id": "BioInfer.d522.s0.e0",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
44,
52
]
],
"normalized": []
},
{
"id": "BioInfer.d522.s0.e1",
"type": "Individual_protein",
"text": [
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"offsets": [
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22,
27
]
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},
{
"id": "BioInfer.d522.s0.e2",
"type": "Individual_protein",
"text": [
"gelsolin"
],
"offsets": [
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31,
39
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d522.s0.i0",
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"arg1_id": "BioInfer.d522.s0.e0",
"arg2_id": "BioInfer.d522.s0.e1",
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{
"id": "BioInfer.d522.s0.i1",
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"arg1_id": "BioInfer.d522.s0.e1",
"arg2_id": "BioInfer.d522.s0.e2",
"normalized": []
}
] |
623 | BioInfer.d522.s1 | [
{
"id": "BioInfer.d522.s1__text",
"type": "Sentence",
"text": [
"Sepharose beads coupled to either monoclonal anti-gelsolin antibodies or to polyproline were used to extract gelsolin and profilin, respectively, from EGTA-containing platelet extracts and determine the proportion of these molecules bound to actin with sufficient affinity to withstand dilution (high-affinity complexes)."
],
"offsets": [
[
0,
321
]
]
}
] | [
{
"id": "BioInfer.d522.s1.e0",
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242,
247
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},
{
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122,
130
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},
{
"id": "BioInfer.d522.s1.e2",
"type": "Individual_protein",
"text": [
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109,
117
]
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},
{
"id": "BioInfer.d522.s1.e3",
"type": "Gene/protein/RNA",
"text": [
"gelsolin"
],
"offsets": [
[
50,
58
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d522.s1.i0",
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{
"id": "BioInfer.d522.s1.i1",
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"arg1_id": "BioInfer.d522.s1.e0",
"arg2_id": "BioInfer.d522.s1.e2",
"normalized": []
}
] |
624 | BioInfer.d522.s2 | [
{
"id": "BioInfer.d522.s2__text",
"type": "Sentence",
"text": [
"Thrombin, within seconds, caused quantitative conversion of platelet profilin and gelsolin to high-affinity complexes with actin, but these complexes were not present 5 min after stimulation."
],
"offsets": [
[
0,
191
]
]
}
] | [
{
"id": "BioInfer.d522.s2.e0",
"type": "Individual_protein",
"text": [
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0,
8
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{
"id": "BioInfer.d522.s2.e1",
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123,
128
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],
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},
{
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"text": [
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60,
77
]
],
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},
{
"id": "BioInfer.d522.s2.e3",
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"text": [
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"gelsolin"
],
"offsets": [
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60,
68
],
[
82,
90
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],
"normalized": []
}
] | [] | [] | [
{
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{
"id": "BioInfer.d522.s2.i1",
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{
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{
"id": "BioInfer.d522.s2.i3",
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{
"id": "BioInfer.d522.s2.i4",
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"arg1_id": "BioInfer.d522.s2.e1",
"arg2_id": "BioInfer.d522.s2.e3",
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}
] |
625 | BioInfer.d523.s0 | [
{
"id": "BioInfer.d523.s0__text",
"type": "Sentence",
"text": [
"RIPc, one of the cleavage products, enhanced interaction between TRADD and FADD/MORT1 and increased cells' sensitivity to TNF."
],
"offsets": [
[
0,
126
]
]
}
] | [
{
"id": "BioInfer.d523.s0.e0",
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"text": [
"TNF"
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122,
125
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],
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},
{
"id": "BioInfer.d523.s0.e1",
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75,
79
]
],
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},
{
"id": "BioInfer.d523.s0.e2",
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"text": [
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0,
4
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},
{
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80,
85
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],
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},
{
"id": "BioInfer.d523.s0.e4",
"type": "Individual_protein",
"text": [
"TRADD"
],
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[
65,
70
]
],
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}
] | [] | [] | [
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{
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},
{
"id": "BioInfer.d523.s0.i2",
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{
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{
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{
"id": "BioInfer.d523.s0.i5",
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"arg1_id": "BioInfer.d523.s0.e3",
"arg2_id": "BioInfer.d523.s0.e4",
"normalized": []
}
] |
626 | BioInfer.d526.s0 | [
{
"id": "BioInfer.d526.s0__text",
"type": "Sentence",
"text": [
"Saccharomyces cerevisiae PAC2 functions with CIN1, 2 and 4 in a pathway leading to normal microtubule stability."
],
"offsets": [
[
0,
112
]
]
}
] | [
{
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"text": [
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],
"offsets": [
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25,
29
]
],
"normalized": []
},
{
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"type": "Individual_protein",
"text": [
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],
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45,
49
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],
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},
{
"id": "BioInfer.d526.s0.e2",
"type": "Individual_protein",
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"4"
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45,
48
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57,
58
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{
"id": "BioInfer.d526.s0.e3",
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"2"
],
"offsets": [
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45,
48
],
[
51,
52
]
],
"normalized": []
}
] | [] | [] | [
{
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"arg2_id": "BioInfer.d526.s0.e3",
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}
] |
627 | BioInfer.d528.s0 | [
{
"id": "BioInfer.d528.s0__text",
"type": "Sentence",
"text": [
"SDS-PAGE analysis of growth cone cytoskeletons revealed the presence of several major bands, identified by their mobility as actin (43 kDa Mr), myosin heavy chain (195 kDa Mr), spectrin (235 and 240 kDa Mr), and tubulin (51-54 kDa Mr)."
],
"offsets": [
[
0,
235
]
]
}
] | [
{
"id": "BioInfer.d528.s0.e0",
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177,
185
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],
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{
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"type": "Gene/protein/RNA",
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125,
130
]
],
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},
{
"id": "BioInfer.d528.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"tubulin"
],
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[
212,
219
]
],
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},
{
"id": "BioInfer.d528.s0.e3",
"type": "Gene/protein/RNA",
"text": [
"myosin heavy chain"
],
"offsets": [
[
144,
162
]
],
"normalized": []
}
] | [] | [] | [] |
628 | BioInfer.d529.s0 | [
{
"id": "BioInfer.d529.s0__text",
"type": "Sentence",
"text": [
"Semiserial sections were subjected to immunohistochemical staining with antibodies to alpha-smooth muscle actin (alpha-SMA), desmin and smooth muscle myosin heavy chain isoforms: SM1, SM2 and SMemb."
],
"offsets": [
[
0,
198
]
]
}
] | [
{
"id": "BioInfer.d529.s0.e0",
"type": "Individual_protein",
"text": [
"SM2"
],
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184,
187
]
],
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},
{
"id": "BioInfer.d529.s0.e1",
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113,
122
]
],
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},
{
"id": "BioInfer.d529.s0.e2",
"type": "Individual_protein",
"text": [
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],
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136,
168
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],
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},
{
"id": "BioInfer.d529.s0.e3",
"type": "Individual_protein",
"text": [
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86,
111
]
],
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},
{
"id": "BioInfer.d529.s0.e4",
"type": "Individual_protein",
"text": [
"SM1"
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179,
182
]
],
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},
{
"id": "BioInfer.d529.s0.e5",
"type": "Gene/protein/RNA",
"text": [
"desmin"
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125,
131
]
],
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},
{
"id": "BioInfer.d529.s0.e6",
"type": "Individual_protein",
"text": [
"SMemb"
],
"offsets": [
[
192,
197
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d529.s0.i0",
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"arg2_id": "BioInfer.d529.s0.e2",
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{
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{
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"arg1_id": "BioInfer.d529.s0.e2",
"arg2_id": "BioInfer.d529.s0.e6",
"normalized": []
}
] |
629 | BioInfer.d530.s0 | [
{
"id": "BioInfer.d530.s0__text",
"type": "Sentence",
"text": [
"Sequence analysis of the genes encoding the nucleocapsid protein and phosphoprotein (P) of phocid distemper virus, and editing of the P gene transcript."
],
"offsets": [
[
0,
152
]
]
}
] | [
{
"id": "BioInfer.d530.s0.e0",
"type": "Gene/protein/RNA",
"text": [
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],
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[
44,
64
]
],
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},
{
"id": "BioInfer.d530.s0.e1",
"type": "Gene/protein/RNA",
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"P"
],
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[
134,
135
]
],
"normalized": []
},
{
"id": "BioInfer.d530.s0.e2",
"type": "Individual_protein",
"text": [
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],
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69,
83
]
],
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},
{
"id": "BioInfer.d530.s0.e3",
"type": "Individual_protein",
"text": [
"P"
],
"offsets": [
[
85,
86
]
],
"normalized": []
}
] | [] | [] | [] |
630 | BioInfer.d532.s0 | [
{
"id": "BioInfer.d532.s0__text",
"type": "Sentence",
"text": [
"Ser-133 phosphorylation enhances CREB activity by promoting interaction with a 265-kDa CREB binding protein referred to as CBP (Arias, J., Alberts, A., Brindle, P., Claret, F., Smeal, T., Karin, M., Feramisco, J., and Montminy, M. (1994) Nature 370, 226-228; Chrivia, J. C., Kwok, R. P., Lamb, N., Hagiwara, M., Montminy, M. R., and Goodman, R. H. (1993) Nature 365, 855-859)."
],
"offsets": [
[
0,
376
]
]
}
] | [
{
"id": "BioInfer.d532.s0.e0",
"type": "Individual_protein",
"text": [
"CBP"
],
"offsets": [
[
123,
126
]
],
"normalized": []
},
{
"id": "BioInfer.d532.s0.e1",
"type": "Individual_protein",
"text": [
"CREB"
],
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[
33,
37
]
],
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},
{
"id": "BioInfer.d532.s0.e2",
"type": "Individual_protein",
"text": [
"CREB binding protein"
],
"offsets": [
[
87,
107
]
],
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}
] | [] | [] | [
{
"id": "BioInfer.d532.s0.i0",
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"arg2_id": "BioInfer.d532.s0.e1",
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},
{
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"arg1_id": "BioInfer.d532.s0.e1",
"arg2_id": "BioInfer.d532.s0.e2",
"normalized": []
}
] |
631 | BioInfer.d533.s0 | [
{
"id": "BioInfer.d533.s0__text",
"type": "Sentence",
"text": [
"Seventeen embryonic genes were identified as embryonic alpha-tubulin, embryonic beta-tubulin, hnRNP, protein L-isoaspartyl methyltransferase (PIMT), ferritin heavy chain, type IV collagen, actin-binding protein cofilin, profilin and nine novel sequences designated as A1-9."
],
"offsets": [
[
0,
273
]
]
}
] | [
{
"id": "BioInfer.d533.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"ferritin heavy chain"
],
"offsets": [
[
149,
169
]
],
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},
{
"id": "BioInfer.d533.s0.e1",
"type": "Protein_family_or_group",
"text": [
"actin-binding protein"
],
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[
189,
210
]
],
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},
{
"id": "BioInfer.d533.s0.e2",
"type": "Gene/protein/RNA",
"text": [
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],
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171,
187
]
],
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},
{
"id": "BioInfer.d533.s0.e3",
"type": "Gene/protein/RNA",
"text": [
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],
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220,
228
]
],
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},
{
"id": "BioInfer.d533.s0.e4",
"type": "Gene/protein/RNA",
"text": [
"embryonic alpha-tubulin"
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45,
68
]
],
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},
{
"id": "BioInfer.d533.s0.e5",
"type": "Gene/protein/RNA",
"text": [
"hnRNP"
],
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[
94,
99
]
],
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},
{
"id": "BioInfer.d533.s0.e6",
"type": "Gene/protein/RNA",
"text": [
"embryonic beta-tubulin"
],
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[
70,
92
]
],
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},
{
"id": "BioInfer.d533.s0.e7",
"type": "Individual_protein",
"text": [
"cofilin"
],
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[
211,
218
]
],
"normalized": []
},
{
"id": "BioInfer.d533.s0.e8",
"type": "Gene",
"text": [
"PIMT"
],
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[
142,
146
]
],
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},
{
"id": "BioInfer.d533.s0.e9",
"type": "Gene",
"text": [
"protein L-isoaspartyl methyltransferase"
],
"offsets": [
[
101,
140
]
],
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}
] | [] | [] | [
{
"id": "BioInfer.d533.s0.i0",
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"arg1_id": "BioInfer.d533.s0.e1",
"arg2_id": "BioInfer.d533.s0.e7",
"normalized": []
}
] |
632 | BioInfer.d534.s0 | [
{
"id": "BioInfer.d534.s0__text",
"type": "Sentence",
"text": [
"Several intracellular proteins termed catenins, including alpha-catenin, beta-catenin, and plakoglobin, are tightly associated with these cadherins and serve to link them to the cytoskeleton."
],
"offsets": [
[
0,
191
]
]
}
] | [
{
"id": "BioInfer.d534.s0.e0",
"type": "Individual_protein",
"text": [
"cadherins"
],
"offsets": [
[
138,
147
]
],
"normalized": []
},
{
"id": "BioInfer.d534.s0.e1",
"type": "Individual_protein",
"text": [
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91,
102
]
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},
{
"id": "BioInfer.d534.s0.e2",
"type": "Individual_protein",
"text": [
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38,
46
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},
{
"id": "BioInfer.d534.s0.e3",
"type": "Individual_protein",
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58,
71
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{
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"type": "Individual_protein",
"text": [
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],
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73,
85
]
],
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}
] | [] | [] | [
{
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{
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"arg2_id": "BioInfer.d534.s0.e2",
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{
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{
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"arg1_id": "BioInfer.d534.s0.e2",
"arg2_id": "BioInfer.d534.s0.e4",
"normalized": []
}
] |
633 | BioInfer.d535.s0 | [
{
"id": "BioInfer.d535.s0__text",
"type": "Sentence",
"text": [
"Several lines of evidence show that the profilins fully renature after removal of the urea by dialysis: 1) dialyzed Acanthamoeba and human profilins rebind quantitatively to poly-L-proline and bind to actin in the same way as native, conventionally purified profilin without urea treatment; 2) dialyzed profilins form 3-D crystals under the same conditions as native profilins; 3) dialyzed Acanthamoeba profilin-I has an NMR spectrum identical with that of native profilin-I; and 4) dialyzed human and Acanthamoeba profilins inhibit actin polymerization."
],
"offsets": [
[
0,
554
]
]
}
] | [
{
"id": "BioInfer.d535.s0.e0",
"type": "Individual_protein",
"text": [
"profilins"
],
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367,
376
]
],
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},
{
"id": "BioInfer.d535.s0.e1",
"type": "Individual_protein",
"text": [
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258,
266
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},
{
"id": "BioInfer.d535.s0.e2",
"type": "Gene/protein/RNA",
"text": [
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40,
49
]
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{
"id": "BioInfer.d535.s0.e3",
"type": "Individual_protein",
"text": [
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201,
206
]
],
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},
{
"id": "BioInfer.d535.s0.e4",
"type": "Individual_protein",
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303,
312
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},
{
"id": "BioInfer.d535.s0.e5",
"type": "Individual_protein",
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464,
474
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{
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515,
524
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},
{
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403,
413
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{
"id": "BioInfer.d535.s0.e8",
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139,
148
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{
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"type": "Individual_protein",
"text": [
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],
"offsets": [
[
533,
538
]
],
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}
] | [] | [] | [
{
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{
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{
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"arg1_id": "BioInfer.d535.s0.e6",
"arg2_id": "BioInfer.d535.s0.e9",
"normalized": []
}
] |
634 | BioInfer.d536.s0 | [
{
"id": "BioInfer.d536.s0__text",
"type": "Sentence",
"text": [
"Several proteins, such as calmodulin, calbindin, actin, tubulin, and fimbrin, have previously been described."
],
"offsets": [
[
0,
109
]
]
}
] | [
{
"id": "BioInfer.d536.s0.e0",
"type": "Gene/protein/RNA",
"text": [
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],
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38,
47
]
],
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},
{
"id": "BioInfer.d536.s0.e1",
"type": "Gene/protein/RNA",
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69,
76
]
],
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},
{
"id": "BioInfer.d536.s0.e2",
"type": "Gene/protein/RNA",
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],
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26,
36
]
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"type": "Gene/protein/RNA",
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49,
54
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"id": "BioInfer.d536.s0.e4",
"type": "Gene/protein/RNA",
"text": [
"tubulin"
],
"offsets": [
[
56,
63
]
],
"normalized": []
}
] | [] | [] | [] |
635 | BioInfer.d537.s0 | [
{
"id": "BioInfer.d537.s0__text",
"type": "Sentence",
"text": [
"Signaling pathways involved in dephosphorylation and localization of the actin-binding protein cofilin in stimulated human neutrophils."
],
"offsets": [
[
0,
135
]
]
}
] | [
{
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"type": "Protein_family_or_group",
"text": [
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73,
94
]
],
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{
"id": "BioInfer.d537.s0.e1",
"type": "Individual_protein",
"text": [
"cofilin"
],
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[
95,
102
]
],
"normalized": []
}
] | [] | [] | [
{
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"arg1_id": "BioInfer.d537.s0.e0",
"arg2_id": "BioInfer.d537.s0.e1",
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}
] |
636 | BioInfer.d537.s1 | [
{
"id": "BioInfer.d537.s1__text",
"type": "Sentence",
"text": [
"These findings suggest a role of cofilin in stimulus-dependent actin remodeling in motile neutrophils."
],
"offsets": [
[
0,
102
]
]
}
] | [
{
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33,
40
]
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{
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"text": [
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[
63,
68
]
],
"normalized": []
}
] | [] | [] | [
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"arg2_id": "BioInfer.d537.s1.e1",
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}
] |
637 | BioInfer.d538.s0 | [
{
"id": "BioInfer.d538.s0__text",
"type": "Sentence",
"text": [
"Significantly, those actin mutants exhibiting the most severe phenotypes in all three processes have altered residues that cluster to a small region of the actin crystal structure previously defined as the fimbrin (Sac6p)-binding site."
],
"offsets": [
[
0,
235
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]
}
] | [
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156,
161
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206,
213
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{
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215,
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"text": [
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21,
26
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],
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] | [] | [] | [
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}
] |
638 | BioInfer.d539.s0 | [
{
"id": "BioInfer.d539.s0__text",
"type": "Sentence",
"text": [
"Silencing mediated by GBD-SIR1 requires the trans-acting factors that normally participate in repression, namely, SIR2, SIR3, SIR4, and histone H4."
],
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[
0,
147
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]
}
] | [
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126,
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22,
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{
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{
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120,
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},
{
"id": "BioInfer.d539.s0.e5",
"type": "Individual_protein",
"text": [
"SIR2"
],
"offsets": [
[
114,
118
]
],
"normalized": []
},
{
"id": "BioInfer.d539.s0.e6",
"type": "Protein_family_or_group",
"text": [
"histone"
],
"offsets": [
[
136,
143
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d539.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d539.s0.e1",
"arg2_id": "BioInfer.d539.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d539.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d539.s0.e4",
"arg2_id": "BioInfer.d539.s0.e6",
"normalized": []
}
] |
639 | BioInfer.d540.s0 | [
{
"id": "BioInfer.d540.s0__text",
"type": "Sentence",
"text": [
"Since alpha-catenin is required for cadherin-mediated adhesion, the armadillo repeat region alone probably cannot promote cell adhesion, making it unlikely that beta-catenin induces axis duplication by increasing cell adhesion."
],
"offsets": [
[
0,
227
]
]
}
] | [
{
"id": "BioInfer.d540.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"armadillo"
],
"offsets": [
[
68,
77
]
],
"normalized": []
},
{
"id": "BioInfer.d540.s0.e1",
"type": "Individual_protein",
"text": [
"cadherin"
],
"offsets": [
[
36,
44
]
],
"normalized": []
},
{
"id": "BioInfer.d540.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"beta-catenin"
],
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[
161,
173
]
],
"normalized": []
},
{
"id": "BioInfer.d540.s0.e3",
"type": "Individual_protein",
"text": [
"alpha-catenin"
],
"offsets": [
[
6,
19
]
],
"normalized": []
}
] | [] | [] | [] |
640 | BioInfer.d542.s0 | [
{
"id": "BioInfer.d542.s0__text",
"type": "Sentence",
"text": [
"Since RAD54 is a recombinational protein associated with RAD51, this is the first genetic evidence that cancer arises from a defect in repair processes involving homologous recombination."
],
"offsets": [
[
0,
187
]
]
}
] | [
{
"id": "BioInfer.d542.s0.e0",
"type": "Individual_protein",
"text": [
"RAD51"
],
"offsets": [
[
57,
62
]
],
"normalized": []
},
{
"id": "BioInfer.d542.s0.e1",
"type": "Individual_protein",
"text": [
"RAD54"
],
"offsets": [
[
6,
11
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d542.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d542.s0.e0",
"arg2_id": "BioInfer.d542.s0.e1",
"normalized": []
}
] |
641 | BioInfer.d543.s0 | [
{
"id": "BioInfer.d543.s0__text",
"type": "Sentence",
"text": [
"Single-headed myosin, which consists of a full length myosin heavy chain and a tagged tail, was isolated on the basis of the affinities for Nickel agarose and actin."
],
"offsets": [
[
0,
165
]
]
}
] | [
{
"id": "BioInfer.d543.s0.e0",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
159,
164
]
],
"normalized": []
},
{
"id": "BioInfer.d543.s0.e1",
"type": "Protein_complex",
"text": [
"Single-headed myosin"
],
"offsets": [
[
0,
20
]
],
"normalized": []
},
{
"id": "BioInfer.d543.s0.e2",
"type": "Individual_protein",
"text": [
"myosin heavy chain"
],
"offsets": [
[
54,
72
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d543.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d543.s0.e0",
"arg2_id": "BioInfer.d543.s0.e1",
"normalized": []
},
{
"id": "BioInfer.d543.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d543.s0.e1",
"arg2_id": "BioInfer.d543.s0.e2",
"normalized": []
}
] |
642 | BioInfer.d544.s0 | [
{
"id": "BioInfer.d544.s0__text",
"type": "Sentence",
"text": [
"Smooth muscle alpha actin and myosin heavy chain expression in the vascular smooth muscle cells surrounding human endometrial arterioles."
],
"offsets": [
[
0,
137
]
]
}
] | [
{
"id": "BioInfer.d544.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"Smooth muscle alpha actin"
],
"offsets": [
[
0,
25
]
],
"normalized": []
},
{
"id": "BioInfer.d544.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"Smooth muscle",
"myosin heavy chain"
],
"offsets": [
[
0,
13
],
[
30,
48
]
],
"normalized": []
}
] | [] | [] | [] |
643 | BioInfer.d545.s0 | [
{
"id": "BioInfer.d545.s0__text",
"type": "Sentence",
"text": [
"Smooth muscle talin prepared from chicken gizzard binds to skeletal muscle actin in vitro."
],
"offsets": [
[
0,
90
]
]
}
] | [
{
"id": "BioInfer.d545.s0.e0",
"type": "Individual_protein",
"text": [
"Smooth muscle talin"
],
"offsets": [
[
0,
19
]
],
"normalized": []
},
{
"id": "BioInfer.d545.s0.e1",
"type": "Individual_protein",
"text": [
"skeletal muscle actin"
],
"offsets": [
[
59,
80
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d545.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d545.s0.e0",
"arg2_id": "BioInfer.d545.s0.e1",
"normalized": []
}
] |
644 | BioInfer.d546.s0 | [
{
"id": "BioInfer.d546.s0__text",
"type": "Sentence",
"text": [
"Specific antibodies to myosin heavy chain isoforms (SM1, SM2, SMemb), caldesmon, and alpha-smooth muscle actin and cDNAs for SMemb were used."
],
"offsets": [
[
0,
141
]
]
}
] | [
{
"id": "BioInfer.d546.s0.e0",
"type": "Individual_protein",
"text": [
"SM1"
],
"offsets": [
[
52,
55
]
],
"normalized": []
},
{
"id": "BioInfer.d546.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"alpha-smooth muscle actin"
],
"offsets": [
[
85,
110
]
],
"normalized": []
},
{
"id": "BioInfer.d546.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"caldesmon"
],
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[
70,
79
]
],
"normalized": []
},
{
"id": "BioInfer.d546.s0.e3",
"type": "Individual_protein",
"text": [
"SM2"
],
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[
57,
60
]
],
"normalized": []
},
{
"id": "BioInfer.d546.s0.e4",
"type": "Gene/protein/RNA",
"text": [
"SMemb"
],
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[
125,
130
]
],
"normalized": []
},
{
"id": "BioInfer.d546.s0.e5",
"type": "Individual_protein",
"text": [
"SMemb"
],
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[
62,
67
]
],
"normalized": []
},
{
"id": "BioInfer.d546.s0.e6",
"type": "Individual_protein",
"text": [
"myosin heavy chain"
],
"offsets": [
[
23,
41
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d546.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d546.s0.e0",
"arg2_id": "BioInfer.d546.s0.e6",
"normalized": []
},
{
"id": "BioInfer.d546.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d546.s0.e3",
"arg2_id": "BioInfer.d546.s0.e6",
"normalized": []
},
{
"id": "BioInfer.d546.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d546.s0.e5",
"arg2_id": "BioInfer.d546.s0.e6",
"normalized": []
}
] |
645 | BioInfer.d547.s0 | [
{
"id": "BioInfer.d547.s0__text",
"type": "Sentence",
"text": [
"Specific interaction between the nucleocapsid protein (N) and the phosphoprotein (P) of vesicular stomatitis virus (VSV), an important step in the life-cycle of the virus, was studied by using a two-hybrid system."
],
"offsets": [
[
0,
213
]
]
}
] | [
{
"id": "BioInfer.d547.s0.e0",
"type": "Individual_protein",
"text": [
"P"
],
"offsets": [
[
82,
83
]
],
"normalized": []
},
{
"id": "BioInfer.d547.s0.e1",
"type": "Individual_protein",
"text": [
"phosphoprotein"
],
"offsets": [
[
66,
80
]
],
"normalized": []
},
{
"id": "BioInfer.d547.s0.e2",
"type": "Individual_protein",
"text": [
"nucleocapsid protein"
],
"offsets": [
[
33,
53
]
],
"normalized": []
},
{
"id": "BioInfer.d547.s0.e3",
"type": "Individual_protein",
"text": [
"N"
],
"offsets": [
[
55,
56
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d547.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d547.s0.e0",
"arg2_id": "BioInfer.d547.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d547.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d547.s0.e0",
"arg2_id": "BioInfer.d547.s0.e3",
"normalized": []
},
{
"id": "BioInfer.d547.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d547.s0.e1",
"arg2_id": "BioInfer.d547.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d547.s0.i3",
"type": "PPI",
"arg1_id": "BioInfer.d547.s0.e1",
"arg2_id": "BioInfer.d547.s0.e3",
"normalized": []
}
] |
646 | BioInfer.d549.s0 | [
{
"id": "BioInfer.d549.s0__text",
"type": "Sentence",
"text": [
"Spontaneous and mitomycin C-induced SCE levels were significantly reduced for chicken DT40 B cells lacking the key HR genes RAD51 and RAD54 but not for nonhomologous DNA end-joining (NHEJ)-defective KU70(-/-) cells."
],
"offsets": [
[
0,
215
]
]
}
] | [
{
"id": "BioInfer.d549.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"RAD51"
],
"offsets": [
[
124,
129
]
],
"normalized": []
},
{
"id": "BioInfer.d549.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"RAD54"
],
"offsets": [
[
134,
139
]
],
"normalized": []
}
] | [] | [] | [] |
647 | BioInfer.d550.s0 | [
{
"id": "BioInfer.d550.s0__text",
"type": "Sentence",
"text": [
"Stable transfection of mutant plakoglobin molecules showed that deletion of the N-cadherin binding domain, but not the alpha-catenin binding domain, abolished beta-catenin downregulation."
],
"offsets": [
[
0,
187
]
]
}
] | [
{
"id": "BioInfer.d550.s0.e0",
"type": "Individual_protein",
"text": [
"N-cadherin"
],
"offsets": [
[
80,
90
]
],
"normalized": []
},
{
"id": "BioInfer.d550.s0.e1",
"type": "Individual_protein",
"text": [
"alpha-catenin"
],
"offsets": [
[
119,
132
]
],
"normalized": []
},
{
"id": "BioInfer.d550.s0.e2",
"type": "Individual_protein",
"text": [
"beta-catenin"
],
"offsets": [
[
159,
171
]
],
"normalized": []
},
{
"id": "BioInfer.d550.s0.e3",
"type": "Individual_protein",
"text": [
"plakoglobin"
],
"offsets": [
[
30,
41
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d550.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d550.s0.e0",
"arg2_id": "BioInfer.d550.s0.e3",
"normalized": []
},
{
"id": "BioInfer.d550.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d550.s0.e1",
"arg2_id": "BioInfer.d550.s0.e3",
"normalized": []
},
{
"id": "BioInfer.d550.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d550.s0.e2",
"arg2_id": "BioInfer.d550.s0.e3",
"normalized": []
}
] |
648 | BioInfer.d551.s0 | [
{
"id": "BioInfer.d551.s0__text",
"type": "Sentence",
"text": [
"Structural studies on the ribbon-to-helix transition in profilin: actin crystals."
],
"offsets": [
[
0,
81
]
]
}
] | [
{
"id": "BioInfer.d551.s0.e0",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
56,
64
]
],
"normalized": []
},
{
"id": "BioInfer.d551.s0.e1",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
66,
71
]
],
"normalized": []
}
] | [] | [] | [] |
649 | BioInfer.d552.s0 | [
{
"id": "BioInfer.d552.s0__text",
"type": "Sentence",
"text": [
"Studies on cultured cells have suggested that both alpha-catenin and plakoglobin are important for the adhesive function of cadherins."
],
"offsets": [
[
0,
134
]
]
}
] | [
{
"id": "BioInfer.d552.s0.e0",
"type": "Protein_family_or_group",
"text": [
"cadherins"
],
"offsets": [
[
124,
133
]
],
"normalized": []
},
{
"id": "BioInfer.d552.s0.e1",
"type": "Individual_protein",
"text": [
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],
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51,
64
]
],
"normalized": []
},
{
"id": "BioInfer.d552.s0.e2",
"type": "Individual_protein",
"text": [
"plakoglobin"
],
"offsets": [
[
69,
80
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d552.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d552.s0.e0",
"arg2_id": "BioInfer.d552.s0.e1",
"normalized": []
},
{
"id": "BioInfer.d552.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d552.s0.e0",
"arg2_id": "BioInfer.d552.s0.e2",
"normalized": []
}
] |
650 | BioInfer.d553.s0 | [
{
"id": "BioInfer.d553.s0__text",
"type": "Sentence",
"text": [
"Studies on the interaction between actin and cofilin purified by a new method."
],
"offsets": [
[
0,
78
]
]
}
] | [
{
"id": "BioInfer.d553.s0.e0",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
35,
40
]
],
"normalized": []
},
{
"id": "BioInfer.d553.s0.e1",
"type": "Individual_protein",
"text": [
"cofilin"
],
"offsets": [
[
45,
52
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d553.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d553.s0.e0",
"arg2_id": "BioInfer.d553.s0.e1",
"normalized": []
}
] |
651 | BioInfer.d554.s0 | [
{
"id": "BioInfer.d554.s0__text",
"type": "Sentence",
"text": [
"Study of mutated yeast profilins and profilins from Acanthamoeba suggests that the ability of profilin to suppress cap- cells is dependent upon a property other than, or in addition to, its ability to bind actin."
],
"offsets": [
[
0,
212
]
]
}
] | [
{
"id": "BioInfer.d554.s0.e0",
"type": "Gene",
"text": [
"cap-"
],
"offsets": [
[
115,
119
]
],
"normalized": []
},
{
"id": "BioInfer.d554.s0.e1",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
94,
102
]
],
"normalized": []
},
{
"id": "BioInfer.d554.s0.e2",
"type": "Individual_protein",
"text": [
"actin"
],
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[
206,
211
]
],
"normalized": []
},
{
"id": "BioInfer.d554.s0.e3",
"type": "Gene/protein/RNA",
"text": [
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],
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23,
32
]
],
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},
{
"id": "BioInfer.d554.s0.e4",
"type": "Gene/protein/RNA",
"text": [
"profilins"
],
"offsets": [
[
37,
46
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d554.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d554.s0.e1",
"arg2_id": "BioInfer.d554.s0.e2",
"normalized": []
}
] |
652 | BioInfer.d556.s0 | [
{
"id": "BioInfer.d556.s0__text",
"type": "Sentence",
"text": [
"Suppression of cell transformation by the cyclin-dependent kinase inhibitor p57KIP2 requires binding to proliferating cell nuclear antigen."
],
"offsets": [
[
0,
139
]
]
}
] | [
{
"id": "BioInfer.d556.s0.e0",
"type": "Individual_protein",
"text": [
"proliferating cell nuclear antigen"
],
"offsets": [
[
104,
138
]
],
"normalized": []
},
{
"id": "BioInfer.d556.s0.e1",
"type": "Individual_protein",
"text": [
"p57KIP2"
],
"offsets": [
[
76,
83
]
],
"normalized": []
},
{
"id": "BioInfer.d556.s0.e2",
"type": "Protein_family_or_group",
"text": [
"cyclin-dependent kinase inhibitor"
],
"offsets": [
[
42,
75
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d556.s0.i0",
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"arg1_id": "BioInfer.d556.s0.e0",
"arg2_id": "BioInfer.d556.s0.e1",
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},
{
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"arg1_id": "BioInfer.d556.s0.e1",
"arg2_id": "BioInfer.d556.s0.e2",
"normalized": []
}
] |
653 | BioInfer.d557.s0 | [
{
"id": "BioInfer.d557.s0__text",
"type": "Sentence",
"text": [
"Surprisingly, although maintained in mitogen-rich medium, this ectopic expression was associated with a transactivation of the endogenous myogenin and myosin light chain 2 gene but not the endogenous MyoD1, MRF4, Myf5, the skeletal muscle actin, or the myosin heavy chain genes."
],
"offsets": [
[
0,
278
]
]
}
] | [
{
"id": "BioInfer.d557.s0.e0",
"type": "Gene/protein/RNA",
"text": [
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],
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[
253,
271
]
],
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},
{
"id": "BioInfer.d557.s0.e1",
"type": "Gene/protein/RNA",
"text": [
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],
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223,
244
]
],
"normalized": []
},
{
"id": "BioInfer.d557.s0.e2",
"type": "Gene/protein/RNA",
"text": [
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],
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213,
217
]
],
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},
{
"id": "BioInfer.d557.s0.e3",
"type": "Gene/protein/RNA",
"text": [
"MRF4"
],
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207,
211
]
],
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},
{
"id": "BioInfer.d557.s0.e4",
"type": "Gene/protein/RNA",
"text": [
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],
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200,
205
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],
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},
{
"id": "BioInfer.d557.s0.e5",
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151,
171
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{
"id": "BioInfer.d557.s0.e6",
"type": "Gene/protein/RNA",
"text": [
"myogenin"
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138,
146
]
],
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}
] | [] | [] | [] |
654 | BioInfer.d558.s0 | [
{
"id": "BioInfer.d558.s0__text",
"type": "Sentence",
"text": [
"Targeting by antisense 3'UTI significantly increased motility compared with the corresponding sense ODN."
],
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[
0,
104
]
]
}
] | [] | [] | [] | [] |
655 | BioInfer.d558.s1 | [
{
"id": "BioInfer.d558.s1__text",
"type": "Sentence",
"text": [
"alpha-Sm actin inhibition also led to the formation of less prominent focal adhesions as revealed by immunofluorescence staining against vinculin, talin, and beta1-integrin."
],
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[
0,
173
]
]
}
] | [
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147,
152
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0,
14
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158,
172
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"vinculin"
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137,
145
]
],
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}
] | [] | [] | [] |
656 | BioInfer.d559.s0 | [
{
"id": "BioInfer.d559.s0__text",
"type": "Sentence",
"text": [
"Testicular protein kinase 1 (TESK1) is a serine/threonine kinase highly expressed in testicular germ cells and has the potential to phosphorylate cofilin and induce actin cytoskeletal reorganization."
],
"offsets": [
[
0,
199
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]
}
] | [
{
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"type": "Individual_protein",
"text": [
"actin"
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165,
170
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{
"id": "BioInfer.d559.s0.e1",
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29,
34
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{
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27
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41,
64
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146,
153
]
],
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"arg2_id": "BioInfer.d559.s0.e4",
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}
] |
657 | BioInfer.d560.s0 | [
{
"id": "BioInfer.d560.s0__text",
"type": "Sentence",
"text": [
"The 16236 nt genome encodes eight proteins, nucleocapsid protein (NP), phosphoprotein (P), V protein, matrix protein (M), fusion protein (F), small hydrophobic (SH) protein, haemagglutinin-neuraminidase (HN) protein and large (L) protein, which are flanked by a 55 nt leader sequence and a 54 nt trailer sequence."
],
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[
0,
313
]
]
}
] | [
{
"id": "BioInfer.d560.s0.e0",
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91,
100
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71,
85
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{
"id": "BioInfer.d560.s0.e2",
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122,
136
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],
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},
{
"id": "BioInfer.d560.s0.e3",
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"protein"
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142,
159
],
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165,
172
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{
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44,
64
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{
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220,
225
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230,
237
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{
"id": "BioInfer.d560.s0.e6",
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118,
119
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{
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204,
206
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{
"id": "BioInfer.d560.s0.e8",
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66,
68
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{
"id": "BioInfer.d560.s0.e9",
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102,
116
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},
{
"id": "BioInfer.d560.s0.e10",
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174,
202
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208,
215
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{
"id": "BioInfer.d560.s0.e11",
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87,
88
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{
"id": "BioInfer.d560.s0.e12",
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161,
163
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{
"id": "BioInfer.d560.s0.e13",
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138,
139
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{
"id": "BioInfer.d560.s0.e14",
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"L"
],
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[
227,
228
]
],
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}
] | [] | [] | [] |
658 | BioInfer.d561.s0 | [
{
"id": "BioInfer.d561.s0__text",
"type": "Sentence",
"text": [
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],
"offsets": [
[
0,
169
]
]
}
] | [
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"id": "BioInfer.d561.s0.e0",
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4,
25
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26,
34
]
],
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}
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}
] |
659 | BioInfer.d562.s0 | [
{
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0,
139
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]
}
] | [
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4,
9
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],
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{
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],
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[
56,
63
]
],
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}
] | [] | [] | [
{
"id": "BioInfer.d562.s0.i0",
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}
] |
660 | BioInfer.d563.s0 | [
{
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],
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[
0,
88
]
]
}
] | [
{
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4,
9
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42,
47
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{
"id": "BioInfer.d563.s0.e2",
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57,
66
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],
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},
{
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68,
76
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"id": "BioInfer.d563.s0.e4",
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82,
87
]
],
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}
] | [] | [] | [
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"arg1_id": "BioInfer.d563.s0.e1",
"arg2_id": "BioInfer.d563.s0.e4",
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}
] |
661 | BioInfer.d564.s0 | [
{
"id": "BioInfer.d564.s0__text",
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],
"offsets": [
[
0,
120
]
]
}
] | [
{
"id": "BioInfer.d564.s0.e0",
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61,
71
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],
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{
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45,
57
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{
"id": "BioInfer.d564.s0.e2",
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33,
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72,
83
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4,
17
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101,
106
]
],
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}
] | [] | [] | [
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{
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{
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] |
662 | BioInfer.d566.s0 | [
{
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],
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[
0,
124
]
]
}
] | [
{
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100,
108
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30,
39
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],
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] | [] | [] | [
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}
] |
663 | BioInfer.d566.s1 | [
{
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],
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[
0,
148
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]
}
] | [
{
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11,
20
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22,
25
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] | [] | [] | [
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}
] |
664 | BioInfer.d567.s0 | [
{
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],
"offsets": [
[
0,
74
]
]
}
] | [
{
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27,
30
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{
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4,
8
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59,
64
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] | [] | [] | [
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665 | BioInfer.d568.s0 | [
{
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208
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666 | BioInfer.d569.s0 | [
{
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155
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] | [] | [] | [] |