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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."
],
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[
0,
96
]
]
}
] | [
{
"id": "BioInfer.d497.s1.e0",
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"actin-binding protein"
],
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4,
25
]
],
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{
"id": "BioInfer.d497.s1.e1",
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"profilin"
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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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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."
],
"offsets": [
[
0,
253
]
]
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] | [
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232,
237
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{
"id": "BioInfer.d497.s2.e1",
"type": "Individual_protein",
"text": [
"profilin"
],
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95,
103
]
],
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] | [] | [] | [
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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
]
]
}
] | [
{
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"actin"
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74,
79
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{
"id": "BioInfer.d498.s0.e1",
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65,
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167,
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{
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{
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"type": "Individual_protein",
"text": [
"profilin"
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129,
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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
]
],
"normalized": []
},
{
"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"
],
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[
0,
3
]
],
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},
{
"id": "BioInfer.d501.s0.e1",
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"text": [
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},
{
"id": "BioInfer.d501.s0.e2",
"type": "Individual_protein",
"text": [
"E-cadherin"
],
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34,
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},
{
"id": "BioInfer.d501.s0.e3",
"type": "Individual_protein",
"text": [
"alpha-catenin"
],
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[
64,
77
]
],
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}
] | [] | [] | [
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{
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{
"id": "BioInfer.d501.s0.i2",
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"arg1_id": "BioInfer.d501.s0.e0",
"arg2_id": "BioInfer.d501.s0.e3",
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{
"id": "BioInfer.d501.s0.i3",
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"arg1_id": "BioInfer.d501.s0.e1",
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{
"id": "BioInfer.d501.s0.i4",
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"arg2_id": "BioInfer.d501.s0.e3",
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{
"id": "BioInfer.d501.s0.i5",
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"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"
],
"offsets": [
[
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"
],
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[
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
]
]
}
] | [
{
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178,
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]
],
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},
{
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131,
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],
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},
{
"id": "BioInfer.d502.s1.e2",
"type": "Gene/protein/RNA",
"text": [
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],
"offsets": [
[
16,
23
]
],
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}
] | [] | [] | [
{
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] |
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",
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],
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49,
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]
],
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},
{
"id": "BioInfer.d505.s0.e1",
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"profilin"
],
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87,
95
]
],
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}
] | [] | [] | [
{
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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",
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134,
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],
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121,
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]
],
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}
] | [] | [] | [
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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."
],
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[
0,
234
]
]
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60,
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176,
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],
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] | [] | [] | [
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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."
],
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0,
245
]
]
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] | [
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227,
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195,
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34,
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207,
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611 | BioInfer.d507.s0 | [
{
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"type": "Sentence",
"text": [
"Recently it has been established, through a detailed biochemical analysis, that recombinant Arabidopsis thaliana fimbrin 1 (AtFim1) is a member of the fimbrin/plastin family of actin filament bundling or cross-linking proteins [D.R. Kovar et al. (2000) Plant J 24:625-636]."
],
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]
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] |
612 | BioInfer.d509.s0 | [
{
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],
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[
0,
123
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]
}
] | [
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18,
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62,
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] | [] | [] | [
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"arg2_id": "BioInfer.d509.s0.e3",
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] |
613 | BioInfer.d510.s0 | [
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"type": "Sentence",
"text": [
"Recruitment of a myosin heavy chain kinase to actin-rich protrusions in Dictyostelium."
],
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0,
86
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46,
51
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17,
42
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614 | BioInfer.d512.s0 | [
{
"id": "BioInfer.d512.s0__text",
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0,
178
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] | [
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52,
63
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20,
33
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35,
47
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"text": [
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8,
18
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615 | BioInfer.d514.s0 | [
{
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"type": "Sentence",
"text": [
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[
0,
240
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"id": "BioInfer.d514.s0.e0",
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"alpha-",
"catenin"
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161,
167
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177,
184
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37,
50
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172,
184
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22,
32
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80,
90
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616 | BioInfer.d515.s0 | [
{
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"type": "Sentence",
"text": [
"Regulation of myosin heavy chain and actin isogenes during cardiac growth and hypertrophy."
],
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0,
90
]
]
}
] | [
{
"id": "BioInfer.d515.s0.e0",
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14,
32
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"type": "Gene/protein/RNA",
"text": [
"actin"
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37,
42
]
],
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}
] | [] | [] | [] |
617 | BioInfer.d517.s0 | [
{
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0,
100
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65,
69
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75,
79
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] | [] | [] | [] |
618 | BioInfer.d519.s0 | [
{
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"Requirement of the yeast MSH3 and MSH6 genes for MSH2-dependent genomic stability."
],
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0,
82
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]
}
] | [
{
"id": "BioInfer.d519.s0.e0",
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49,
53
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34,
38
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"text": [
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25,
29
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] |
619 | BioInfer.d519.s1 | [
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0,
200
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]
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] | [
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108,
112
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46,
50
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131,
135
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100,
104
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173
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122,
126
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],
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] |
620 | BioInfer.d520.s0 | [
{
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"text": [
"Requirement of yeast fimbrin for actin organization and morphogenesis in vivo."
],
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0,
78
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]
}
] | [
{
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33,
38
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21,
28
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621 | BioInfer.d521.s0 | [
{
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"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."
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0,
219
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]
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178,
196
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83,
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213,
218
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130,
152
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] | [] | [] | [] |
622 | BioInfer.d522.s0 | [
{
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"text": [
"Reversible binding of actin to gelsolin and profilin in human platelet extracts."
],
"offsets": [
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0,
80
]
]
}
] | [
{
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44,
52
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22,
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{
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"text": [
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31,
39
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] |
623 | BioInfer.d522.s1 | [
{
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],
"offsets": [
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0,
321
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]
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] | [
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242,
247
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122,
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109,
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"text": [
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],
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50,
58
]
],
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}
] | [] | [] | [
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"arg2_id": "BioInfer.d522.s1.e2",
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}
] |
624 | BioInfer.d522.s2 | [
{
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"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."
],
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0,
191
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0,
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123,
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60,
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60,
68
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82,
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625 | BioInfer.d523.s0 | [
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0,
126
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122,
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65,
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] |
626 | BioInfer.d526.s0 | [
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0,
112
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25,
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45,
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51,
52
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"arg1_id": "BioInfer.d526.s0.e0",
"arg2_id": "BioInfer.d526.s0.e3",
"normalized": []
}
] |
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",
"type": "Gene/protein/RNA",
"text": [
"spectrin"
],
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177,
185
]
],
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},
{
"id": "BioInfer.d528.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"actin"
],
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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",
"type": "Individual_protein",
"text": [
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],
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113,
122
]
],
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},
{
"id": "BioInfer.d529.s0.e2",
"type": "Individual_protein",
"text": [
"smooth muscle myosin heavy chain"
],
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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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],
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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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{
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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": [
"nucleocapsid protein"
],
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[
44,
64
]
],
"normalized": []
},
{
"id": "BioInfer.d530.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"P"
],
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[
134,
135
]
],
"normalized": []
},
{
"id": "BioInfer.d530.s0.e2",
"type": "Individual_protein",
"text": [
"phosphoprotein"
],
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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
]
],
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},
{
"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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"arg1_id": "BioInfer.d532.s0.e0",
"arg2_id": "BioInfer.d532.s0.e1",
"normalized": []
},
{
"id": "BioInfer.d532.s0.i1",
"type": "PPI",
"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
]
],
"normalized": []
},
{
"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": [
"type IV collagen"
],
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[
171,
187
]
],
"normalized": []
},
{
"id": "BioInfer.d533.s0.e3",
"type": "Gene/protein/RNA",
"text": [
"profilin"
],
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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
]
],
"normalized": []
},
{
"id": "BioInfer.d533.s0.e6",
"type": "Gene/protein/RNA",
"text": [
"embryonic beta-tubulin"
],
"offsets": [
[
70,
92
]
],
"normalized": []
},
{
"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
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d533.s0.i0",
"type": "PPI",
"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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],
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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",
"text": [
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],
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58,
71
]
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},
{
"id": "BioInfer.d534.s0.e4",
"type": "Individual_protein",
"text": [
"beta-catenin"
],
"offsets": [
[
73,
85
]
],
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}
] | [] | [] | [
{
"id": "BioInfer.d534.s0.i0",
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"arg2_id": "BioInfer.d534.s0.e2",
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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"
],
"offsets": [
[
367,
376
]
],
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},
{
"id": "BioInfer.d535.s0.e1",
"type": "Individual_protein",
"text": [
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258,
266
]
],
"normalized": []
},
{
"id": "BioInfer.d535.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"profilins"
],
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[
40,
49
]
],
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{
"id": "BioInfer.d535.s0.e3",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
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201,
206
]
],
"normalized": []
},
{
"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",
"text": [
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],
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[
464,
474
]
],
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},
{
"id": "BioInfer.d535.s0.e6",
"type": "Individual_protein",
"text": [
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515,
524
]
],
"normalized": []
},
{
"id": "BioInfer.d535.s0.e7",
"type": "Individual_protein",
"text": [
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403,
413
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},
{
"id": "BioInfer.d535.s0.e8",
"type": "Individual_protein",
"text": [
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],
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139,
148
]
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},
{
"id": "BioInfer.d535.s0.e9",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
533,
538
]
],
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}
] | [] | [] | [
{
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{
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"arg2_id": "BioInfer.d535.s0.e8",
"normalized": []
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{
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{
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"type": "PPI",
"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": [
"calbindin"
],
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[
38,
47
]
],
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},
{
"id": "BioInfer.d536.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"fimbrin"
],
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[
69,
76
]
],
"normalized": []
},
{
"id": "BioInfer.d536.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"calmodulin"
],
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26,
36
]
],
"normalized": []
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{
"id": "BioInfer.d536.s0.e3",
"type": "Gene/protein/RNA",
"text": [
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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
]
]
}
] | [
{
"id": "BioInfer.d537.s0.e0",
"type": "Protein_family_or_group",
"text": [
"actin-binding protein"
],
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[
73,
94
]
],
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},
{
"id": "BioInfer.d537.s0.e1",
"type": "Individual_protein",
"text": [
"cofilin"
],
"offsets": [
[
95,
102
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d537.s0.i0",
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"arg1_id": "BioInfer.d537.s0.e0",
"arg2_id": "BioInfer.d537.s0.e1",
"normalized": []
}
] |
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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"text": [
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],
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[
33,
40
]
],
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},
{
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"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
63,
68
]
],
"normalized": []
}
] | [] | [] | [
{
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"arg1_id": "BioInfer.d537.s1.e0",
"arg2_id": "BioInfer.d537.s1.e1",
"normalized": []
}
] |
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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156,
161
]
],
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},
{
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206,
213
]
],
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},
{
"id": "BioInfer.d538.s0.e2",
"type": "Individual_protein",
"text": [
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215,
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"type": "Gene/protein/RNA",
"text": [
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],
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[
21,
26
]
],
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}
] | [] | [] | [
{
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"arg2_id": "BioInfer.d538.s0.e2",
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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."
],
"offsets": [
[
0,
147
]
]
}
] | [
{
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"type": "Individual_protein",
"text": [
"SIR4"
],
"offsets": [
[
126,
130
]
],
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},
{
"id": "BioInfer.d539.s0.e1",
"type": "Individual_protein",
"text": [
"GBD"
],
"offsets": [
[
22,
25
]
],
"normalized": []
},
{
"id": "BioInfer.d539.s0.e2",
"type": "Individual_protein",
"text": [
"SIR1"
],
"offsets": [
[
26,
30
]
],
"normalized": []
},
{
"id": "BioInfer.d539.s0.e3",
"type": "Individual_protein",
"text": [
"SIR3"
],
"offsets": [
[
120,
124
]
],
"normalized": []
},
{
"id": "BioInfer.d539.s0.e4",
"type": "Individual_protein",
"text": [
"H4"
],
"offsets": [
[
144,
146
]
],
"normalized": []
},
{
"id": "BioInfer.d539.s0.e5",
"type": "Individual_protein",
"text": [
"SIR2"
],
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[
114,
118
]
],
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},
{
"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"
],
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[
52,
55
]
],
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},
{
"id": "BioInfer.d546.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"alpha-smooth muscle actin"
],
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[
85,
110
]
],
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},
{
"id": "BioInfer.d546.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"caldesmon"
],
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[
70,
79
]
],
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},
{
"id": "BioInfer.d546.s0.e3",
"type": "Individual_protein",
"text": [
"SM2"
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[
57,
60
]
],
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},
{
"id": "BioInfer.d546.s0.e4",
"type": "Gene/protein/RNA",
"text": [
"SMemb"
],
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125,
130
]
],
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},
{
"id": "BioInfer.d546.s0.e5",
"type": "Individual_protein",
"text": [
"SMemb"
],
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62,
67
]
],
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},
{
"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",
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},
{
"id": "BioInfer.d546.s0.i1",
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"arg2_id": "BioInfer.d546.s0.e6",
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},
{
"id": "BioInfer.d546.s0.i2",
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"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"
],
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[
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",
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"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",
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},
{
"id": "BioInfer.d547.s0.i3",
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"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"
],
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[
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",
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"arg2_id": "BioInfer.d550.s0.e3",
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},
{
"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": [
"alpha-catenin"
],
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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",
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},
{
"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": [
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],
"offsets": [
[
94,
102
]
],
"normalized": []
},
{
"id": "BioInfer.d554.s0.e2",
"type": "Individual_protein",
"text": [
"actin"
],
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206,
211
]
],
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},
{
"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"
],
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[
37,
46
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d554.s0.i0",
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"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"
],
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[
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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},
{
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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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253,
271
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223,
244
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"id": "BioInfer.d557.s0.e2",
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213,
217
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"id": "BioInfer.d557.s0.e3",
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207,
211
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200,
205
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151,
171
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{
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138,
146
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],
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}
] | [] | [] | [] |
654 | BioInfer.d558.s0 | [
{
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[
0,
104
]
]
}
] | [] | [] | [] | [] |
655 | BioInfer.d558.s1 | [
{
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"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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137,
145
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}
] | [] | [] | [] |
656 | BioInfer.d559.s0 | [
{
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0,
199
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] | [
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165,
170
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29,
34
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27
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41,
64
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146,
153
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}
] |
657 | BioInfer.d560.s0 | [
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"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
]
]
}
] | [
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"id": "BioInfer.d560.s0.e0",
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91,
100
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71,
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122,
136
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{
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142,
159
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165,
172
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44,
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220,
225
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230,
237
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118,
119
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204,
206
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66,
68
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{
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102,
116
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{
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174,
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208,
215
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87,
88
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161,
163
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138,
139
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{
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],
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227,
228
]
],
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}
] | [] | [] | [] |
658 | BioInfer.d561.s0 | [
{
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],
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[
0,
169
]
]
}
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4,
25
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26,
34
]
],
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659 | BioInfer.d562.s0 | [
{
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0,
139
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4,
9
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],
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56,
63
]
],
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}
] | [] | [] | [
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] |
660 | BioInfer.d563.s0 | [
{
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0,
88
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]
}
] | [
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4,
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42,
47
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57,
66
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68,
76
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82,
87
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] | [] | [] | [
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}
] |
661 | BioInfer.d564.s0 | [
{
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[
0,
120
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]
}
] | [
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61,
71
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72,
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4,
17
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101,
106
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] |
662 | BioInfer.d566.s0 | [
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0,
124
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100,
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30,
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] |
663 | BioInfer.d566.s1 | [
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0,
148
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11,
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] | [] | [] | [
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] |
664 | BioInfer.d567.s0 | [
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0,
74
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{
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27,
30
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59,
64
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] |
665 | BioInfer.d568.s0 | [
{
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0,
208
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22,
33
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88,
97
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138,
171
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130,
137
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] |
666 | BioInfer.d569.s0 | [
{
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"The adventitial tissue underlying PTCA-induced lesions temporarily expressed alpha-SM actin, desmin, and SM myosin heavy chain isoforms, but not smoothelin."
],
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[
0,
156
]
]
}
] | [
{
"id": "BioInfer.d569.s0.e0",
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145,
155
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93,
99
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105,
126
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"text": [
"alpha-SM actin"
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[
77,
91
]
],
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}
] | [] | [] | [] |
667 | BioInfer.d571.s0 | [
{
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"type": "Sentence",
"text": [
"The aim of our study on human seminiferous tubules of adolescent testes was to study the localization of two actin-associated proteins of the adherens junctions, such as vinculin and talin, and to verify if there were modifications in their pattern in varicocele, a frequent disease of the testis in adolescent age."
],
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[
0,
315
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]
}
] | [
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"id": "BioInfer.d571.s0.e0",
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170,
178
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183,
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109,
114
]
],
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] | [] | [] | [
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}
] |
668 | BioInfer.d573.s0 | [
{
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"The amount of unassembled actin (12 microM) is accounted for by the sequestering functions of T beta 4Xen (20 microM) and profilin (5 microM), the barbed ends being capped."
],
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[
0,
172
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]
}
] | [
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122,
130
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94,
105
]
],
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] | [] | [] | [
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}
] |
669 | BioInfer.d574.s0 | [
{
"id": "BioInfer.d574.s0__text",
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"text": [
"The analysis of the viral proteins by electrophoresis indicates molecular weight differences between CDV and PDV in the fusion (F), phosphoprotein (P), H, nucleocapsid (N) and matrix (M) proteins."
],
"offsets": [
[
0,
196
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]
}
] | [
{
"id": "BioInfer.d574.s0.e0",
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184,
185
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128,
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155,
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187,
195
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148,
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169,
170
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152,
153
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187,
195
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120,
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187,
195
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176,
182
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187,
195
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[
132,
146
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[
187,
195
]
],
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}
] | [] | [] | [] |
670 | BioInfer.d575.s0 | [
{
"id": "BioInfer.d575.s0__text",
"type": "Sentence",
"text": [
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],
"offsets": [
[
0,
234
]
]
}
] | [
{
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4,
7
]
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{
"id": "BioInfer.d575.s0.e1",
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220,
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162,
165
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24,
36
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115,
127
]
],
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] | [] | [] | [
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"arg2_id": "BioInfer.d575.s0.e4",
"normalized": []
}
] |
671 | BioInfer.d575.s1 | [
{
"id": "BioInfer.d575.s1__text",
"type": "Sentence",
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"The APC protein and E-cadherin form similar but independent complexes with alpha-catenin, beta-catenin, and plakoglobin."
],
"offsets": [
[
0,
120
]
]
}
] | [
{
"id": "BioInfer.d575.s1.e0",
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"text": [
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],
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20,
30
]
],
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},
{
"id": "BioInfer.d575.s1.e1",
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4,
7
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},
{
"id": "BioInfer.d575.s1.e2",
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108,
119
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{
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75,
88
]
],
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},
{
"id": "BioInfer.d575.s1.e4",
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"beta-catenin"
],
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90,
102
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d575.s1.i0",
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{
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}
] |
672 | BioInfer.d575.s2 | [
{
"id": "BioInfer.d575.s2__text",
"type": "Sentence",
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],
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[
0,
177
]
]
}
] | [
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],
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89,
101
]
],
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{
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74,
87
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{
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107,
118
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150,
158
]
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{
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6,
9
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{
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159,
166
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],
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}
] | [] | [] | [
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] |
673 | BioInfer.d576.s0 | [
{
"id": "BioInfer.d576.s0__text",
"type": "Sentence",
"text": [
"The Arp2/3 complex, first isolated from Acanthamoeba castellani by affinity chromatography on profilin, consists of seven polypeptides; two actin-related proteins, Arp2 and Arp3; and five apparently novel proteins, p40, p35, p19, p18, and p14 (Machesky et al., 1994)."
],
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[
0,
267
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]
}
] | [
{
"id": "BioInfer.d576.s0.e0",
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"p18"
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230,
233
]
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"id": "BioInfer.d576.s0.e1",
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239,
242
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{
"id": "BioInfer.d576.s0.e2",
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4,
8
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{
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"Arp",
"3"
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4,
7
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9,
10
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220,
223
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173,
177
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215,
218
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140,
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94,
102
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225,
228
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164,
168
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] | [] | [] | [
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}
] |
674 | BioInfer.d577.s0 | [
{
"id": "BioInfer.d577.s0__text",
"type": "Sentence",
"text": [
"The Arp2/3 complex with full-length Scar, Scar containing P, W, and A domains, or Scar containing W and A domains overcomes inhibition of nucleation by the actin monomer-binding protein profilin, giving active nucleation over a low background of spontaneous nucleation."
],
"offsets": [
[
0,
269
]
]
}
] | [
{
"id": "BioInfer.d577.s0.e0",
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],
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156,
161
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186,
194
]
],
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36,
40
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{
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4,
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9,
10
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42,
46
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82,
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{
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],
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4,
8
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],
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] | [] | [] | [
{
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] |
675 | BioInfer.d579.s0 | [
{
"id": "BioInfer.d579.s0__text",
"type": "Sentence",
"text": [
"The assembly of complete HSV replication compartments and incorporation of BrdU were both abolished by treatment with phosphonoacetic acid (PAA) and by omission of any one of the seven viral replication proteins, UL5, UL8, UL9, UL42, UL52, SSB, and Pol, that are essential for viral DNA replication."
],
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[
0,
299
]
]
}
] | [
{
"id": "BioInfer.d579.s0.e0",
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240,
243
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249,
252
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228,
232
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{
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234,
238
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{
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218,
221
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223,
226
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{
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"UL5"
],
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[
213,
216
]
],
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}
] | [] | [] | [] |
676 | BioInfer.d580.s0 | [
{
"id": "BioInfer.d580.s0__text",
"type": "Sentence",
"text": [
"The UL8 component of the herpes simplex virus helicase-primase complex stimulates primer synthesis by a subassembly of the UL5 and UL52 components."
],
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[
0,
147
]
]
}
] | [
{
"id": "BioInfer.d580.s0.e0",
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],
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131,
135
]
],
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},
{
"id": "BioInfer.d580.s0.e1",
"type": "Protein_complex",
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[
46,
62
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],
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{
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4,
7
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{
"id": "BioInfer.d580.s0.e3",
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"UL5"
],
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[
123,
126
]
],
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}
] | [] | [] | [
{
"id": "BioInfer.d580.s0.i0",
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"id": "BioInfer.d580.s0.i3",
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}
] |
677 | BioInfer.d580.s1 | [
{
"id": "BioInfer.d580.s1__text",
"type": "Sentence",
"text": [
"The herpes simplex virus type 1 (HSV) UL5, UL8, and UL52 proteins form a helicase-primase complex in infected cells."
],
"offsets": [
[
0,
116
]
]
}
] | [
{
"id": "BioInfer.d580.s1.e0",
"type": "Individual_protein",
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"UL52"
],
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[
52,
56
]
],
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},
{
"id": "BioInfer.d580.s1.e1",
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43,
46
]
],
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},
{
"id": "BioInfer.d580.s1.e2",
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"text": [
"UL5"
],
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[
38,
41
]
],
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}
] | [] | [] | [
{
"id": "BioInfer.d580.s1.i0",
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}
] |
678 | BioInfer.d581.s0 | [
{
"id": "BioInfer.d581.s0__text",
"type": "Sentence",
"text": [
"The adenosine deaminase-binding region is distinct from major anti-CD26 mAb epitopes on the human dipeptidyl peptidase IV(CD26) molecule."
],
"offsets": [
[
0,
137
]
]
}
] | [
{
"id": "BioInfer.d581.s0.e0",
"type": "Gene/protein/RNA",
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],
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[
4,
23
]
],
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{
"id": "BioInfer.d581.s0.e1",
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],
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122,
126
]
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{
"id": "BioInfer.d581.s0.e2",
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],
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67,
71
]
],
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},
{
"id": "BioInfer.d581.s0.e3",
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],
"offsets": [
[
98,
121
]
],
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}
] | [] | [] | [
{
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}
] |
679 | BioInfer.d583.s0 | [
{
"id": "BioInfer.d583.s0__text",
"type": "Sentence",
"text": [
"The binding surfaces for segment 1 and profilin are different, although they peripherally overlap on actin."
],
"offsets": [
[
0,
107
]
]
}
] | [
{
"id": "BioInfer.d583.s0.e0",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
101,
106
]
],
"normalized": []
},
{
"id": "BioInfer.d583.s0.e1",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
39,
47
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d583.s0.i0",
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"arg1_id": "BioInfer.d583.s0.e0",
"arg2_id": "BioInfer.d583.s0.e1",
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}
] |
680 | BioInfer.d583.s1 | [
{
"id": "BioInfer.d583.s1__text",
"type": "Sentence",
"text": [
"This review describes three structures of actin complexed with different monomer-binding proteins, namely with DNase I, gelsolin segment 1, and profilin."
],
"offsets": [
[
0,
153
]
]
}
] | [
{
"id": "BioInfer.d583.s1.e0",
"type": "Individual_protein",
"text": [
"actin"
],
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42,
47
]
],
"normalized": []
},
{
"id": "BioInfer.d583.s1.e1",
"type": "Individual_protein",
"text": [
"DNase I"
],
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[
111,
118
]
],
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},
{
"id": "BioInfer.d583.s1.e2",
"type": "Individual_protein",
"text": [
"profilin"
],
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144,
152
]
],
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},
{
"id": "BioInfer.d583.s1.e3",
"type": "Individual_protein",
"text": [
"gelsolin"
],
"offsets": [
[
120,
128
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d583.s1.i0",
"type": "PPI",
"arg1_id": "BioInfer.d583.s1.e0",
"arg2_id": "BioInfer.d583.s1.e1",
"normalized": []
},
{
"id": "BioInfer.d583.s1.i1",
"type": "PPI",
"arg1_id": "BioInfer.d583.s1.e0",
"arg2_id": "BioInfer.d583.s1.e2",
"normalized": []
},
{
"id": "BioInfer.d583.s1.i2",
"type": "PPI",
"arg1_id": "BioInfer.d583.s1.e0",
"arg2_id": "BioInfer.d583.s1.e3",
"normalized": []
}
] |
681 | BioInfer.d584.s0 | [
{
"id": "BioInfer.d584.s0__text",
"type": "Sentence",
"text": [
"The myosin heavy chain (MHC) contains the actin- and ATP-binding sites and represents the molecular motor of muscle contraction."
],
"offsets": [
[
0,
128
]
]
}
] | [
{
"id": "BioInfer.d584.s0.e0",
"type": "Individual_protein",
"text": [
"myosin heavy chain"
],
"offsets": [
[
4,
22
]
],
"normalized": []
},
{
"id": "BioInfer.d584.s0.e1",
"type": "Individual_protein",
"text": [
"MHC"
],
"offsets": [
[
24,
27
]
],
"normalized": []
},
{
"id": "BioInfer.d584.s0.e2",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
42,
47
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d584.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d584.s0.e0",
"arg2_id": "BioInfer.d584.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d584.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d584.s0.e1",
"arg2_id": "BioInfer.d584.s0.e2",
"normalized": []
}
] |
682 | BioInfer.d586.s0 | [
{
"id": "BioInfer.d586.s0__text",
"type": "Sentence",
"text": [
"The RAD54 and RAD51 genes are involved in genetic recombination and double-strand break repair in the yeast Saccharomyces cerevisiae."
],
"offsets": [
[
0,
133
]
]
}
] | [
{
"id": "BioInfer.d586.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"RAD54"
],
"offsets": [
[
4,
9
]
],
"normalized": []
},
{
"id": "BioInfer.d586.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"RAD51"
],
"offsets": [
[
14,
19
]
],
"normalized": []
}
] | [] | [] | [] |
683 | BioInfer.d587.s0 | [
{
"id": "BioInfer.d587.s0__text",
"type": "Sentence",
"text": [
"The verprolin-like central (vc) region of Wiskott-Aldrich syndrome protein induces Arp2/3 complex-dependent actin nucleation."
],
"offsets": [
[
0,
125
]
]
}
] | [
{
"id": "BioInfer.d587.s0.e0",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
108,
113
]
],
"normalized": []
},
{
"id": "BioInfer.d587.s0.e1",
"type": "Individual_protein",
"text": [
"verprolin"
],
"offsets": [
[
4,
13
]
],
"normalized": []
},
{
"id": "BioInfer.d587.s0.e2",
"type": "Individual_protein",
"text": [
"Arp",
"3"
],
"offsets": [
[
83,
86
],
[
88,
89
]
],
"normalized": []
},
{
"id": "BioInfer.d587.s0.e3",
"type": "Individual_protein",
"text": [
"Arp2"
],
"offsets": [
[
83,
87
]
],
"normalized": []
},
{
"id": "BioInfer.d587.s0.e4",
"type": "Individual_protein",
"text": [
"Wiskott-Aldrich syndrome protein"
],
"offsets": [
[
42,
74
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d587.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d587.s0.e0",
"arg2_id": "BioInfer.d587.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d587.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d587.s0.e0",
"arg2_id": "BioInfer.d587.s0.e3",
"normalized": []
},
{
"id": "BioInfer.d587.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d587.s0.e0",
"arg2_id": "BioInfer.d587.s0.e4",
"normalized": []
},
{
"id": "BioInfer.d587.s0.i3",
"type": "PPI",
"arg1_id": "BioInfer.d587.s0.e1",
"arg2_id": "BioInfer.d587.s0.e4",
"normalized": []
},
{
"id": "BioInfer.d587.s0.i4",
"type": "PPI",
"arg1_id": "BioInfer.d587.s0.e2",
"arg2_id": "BioInfer.d587.s0.e3",
"normalized": []
}
] |
684 | BioInfer.d588.s0 | [
{
"id": "BioInfer.d588.s0__text",
"type": "Sentence",
"text": [
"The C374S mutation had the most pronounced effect; it reduced the polymerizability of the actin, abolished its binding to profilin, and filaments containing this mutation moved at reduced rates in the in vitro 'motility assay'."
],
"offsets": [
[
0,
227
]
]
}
] | [
{
"id": "BioInfer.d588.s0.e0",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
90,
95
]
],
"normalized": []
},
{
"id": "BioInfer.d588.s0.e1",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
122,
130
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d588.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d588.s0.e0",
"arg2_id": "BioInfer.d588.s0.e1",
"normalized": []
}
] |
685 | BioInfer.d590.s0 | [
{
"id": "BioInfer.d590.s0__text",
"type": "Sentence",
"text": [
"The cardiac myosin heavy chain Arg-403-->Gln mutation that causes hypertrophic cardiomyopathy does not affect the actin- or ATP-binding capacities of two size-limited recombinant myosin heavy chain fragments."
],
"offsets": [
[
0,
208
]
]
}
] | [
{
"id": "BioInfer.d590.s0.e0",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
114,
119
]
],
"normalized": []
},
{
"id": "BioInfer.d590.s0.e1",
"type": "Individual_protein",
"text": [
"myosin heavy chain"
],
"offsets": [
[
179,
197
]
],
"normalized": []
},
{
"id": "BioInfer.d590.s0.e2",
"type": "Individual_protein",
"text": [
"cardiac myosin heavy chain"
],
"offsets": [
[
4,
30
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d590.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d590.s0.e0",
"arg2_id": "BioInfer.d590.s0.e1",
"normalized": []
},
{
"id": "BioInfer.d590.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d590.s0.e0",
"arg2_id": "BioInfer.d590.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d590.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d590.s0.e1",
"arg2_id": "BioInfer.d590.s0.e2",
"normalized": []
}
] |
686 | BioInfer.d591.s0 | [
{
"id": "BioInfer.d591.s0__text",
"type": "Sentence",
"text": [
"The cellular morphological changes were analyzed and correlated with the distribution of cell-substratum contacts viewed by confocal images obtained after immunostaining with antibodies raised against the fibronectin receptor, talin, vinculin and actin."
],
"offsets": [
[
0,
253
]
]
}
] | [
{
"id": "BioInfer.d591.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"vinculin"
],
"offsets": [
[
234,
242
]
],
"normalized": []
},
{
"id": "BioInfer.d591.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"fibronectin receptor"
],
"offsets": [
[
205,
225
]
],
"normalized": []
},
{
"id": "BioInfer.d591.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"actin"
],
"offsets": [
[
247,
252
]
],
"normalized": []
},
{
"id": "BioInfer.d591.s0.e3",
"type": "Gene/protein/RNA",
"text": [
"talin"
],
"offsets": [
[
227,
232
]
],
"normalized": []
}
] | [] | [] | [] |
687 | BioInfer.d592.s0 | [
{
"id": "BioInfer.d592.s0__text",
"type": "Sentence",
"text": [
"The cellular transcription co-activators p300 and the CREB-binding protein CBP are cellular targets for transformation by the E1A proteins of non-oncogenic adenovirus 5 (Ad5)."
],
"offsets": [
[
0,
175
]
]
}
] | [
{
"id": "BioInfer.d592.s0.e0",
"type": "Protein_family_or_group",
"text": [
"CREB-binding protein"
],
"offsets": [
[
54,
74
]
],
"normalized": []
},
{
"id": "BioInfer.d592.s0.e1",
"type": "Individual_protein",
"text": [
"CBP"
],
"offsets": [
[
75,
78
]
],
"normalized": []
},
{
"id": "BioInfer.d592.s0.e2",
"type": "Individual_protein",
"text": [
"p300"
],
"offsets": [
[
41,
45
]
],
"normalized": []
},
{
"id": "BioInfer.d592.s0.e3",
"type": "Gene",
"text": [
"E1A"
],
"offsets": [
[
126,
129
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d592.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d592.s0.e0",
"arg2_id": "BioInfer.d592.s0.e1",
"normalized": []
},
{
"id": "BioInfer.d592.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d592.s0.e1",
"arg2_id": "BioInfer.d592.s0.e3",
"normalized": []
},
{
"id": "BioInfer.d592.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d592.s0.e2",
"arg2_id": "BioInfer.d592.s0.e3",
"normalized": []
}
] |
688 | BioInfer.d595.s0 | [
{
"id": "BioInfer.d595.s0__text",
"type": "Sentence",
"text": [
"The common denominator is impaired beta-catenin association with either E-cadherin (PaTuII) or alpha-catenin (BxPc3 and T3M4)."
],
"offsets": [
[
0,
126
]
]
}
] | [
{
"id": "BioInfer.d595.s0.e0",
"type": "Individual_protein",
"text": [
"beta-catenin"
],
"offsets": [
[
35,
47
]
],
"normalized": []
},
{
"id": "BioInfer.d595.s0.e1",
"type": "Individual_protein",
"text": [
"E-cadherin"
],
"offsets": [
[
72,
82
]
],
"normalized": []
},
{
"id": "BioInfer.d595.s0.e2",
"type": "Individual_protein",
"text": [
"alpha-catenin"
],
"offsets": [
[
95,
108
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d595.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d595.s0.e0",
"arg2_id": "BioInfer.d595.s0.e1",
"normalized": []
},
{
"id": "BioInfer.d595.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d595.s0.e0",
"arg2_id": "BioInfer.d595.s0.e2",
"normalized": []
}
] |
689 | BioInfer.d596.s0 | [
{
"id": "BioInfer.d596.s0__text",
"type": "Sentence",
"text": [
"The comparison of E-CD proteins synthesized by E62 and E24 cell lines revealed no structural or functional differences because both localized at cell-cell contacts and associated with alpha-catenin, beta-catenin, and plakoglobin."
],
"offsets": [
[
0,
229
]
]
}
] | [
{
"id": "BioInfer.d596.s0.e0",
"type": "Individual_protein",
"text": [
"E-CD"
],
"offsets": [
[
18,
22
]
],
"normalized": []
},
{
"id": "BioInfer.d596.s0.e1",
"type": "Individual_protein",
"text": [
"plakoglobin"
],
"offsets": [
[
217,
228
]
],
"normalized": []
},
{
"id": "BioInfer.d596.s0.e2",
"type": "Individual_protein",
"text": [
"beta-catenin"
],
"offsets": [
[
199,
211
]
],
"normalized": []
},
{
"id": "BioInfer.d596.s0.e3",
"type": "Individual_protein",
"text": [
"alpha-catenin"
],
"offsets": [
[
184,
197
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d596.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d596.s0.e0",
"arg2_id": "BioInfer.d596.s0.e1",
"normalized": []
},
{
"id": "BioInfer.d596.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d596.s0.e0",
"arg2_id": "BioInfer.d596.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d596.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d596.s0.e0",
"arg2_id": "BioInfer.d596.s0.e3",
"normalized": []
}
] |
690 | BioInfer.d597.s0 | [
{
"id": "BioInfer.d597.s0__text",
"type": "Sentence",
"text": [
"The concentration of beta-catenin was constant during the follicular phase, whereas the content of alpha-catenin decreased in granulosa cells after treatment with diethylstilboestrol or hCG."
],
"offsets": [
[
0,
190
]
]
}
] | [
{
"id": "BioInfer.d597.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"alpha-catenin"
],
"offsets": [
[
99,
112
]
],
"normalized": []
},
{
"id": "BioInfer.d597.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"beta-catenin"
],
"offsets": [
[
21,
33
]
],
"normalized": []
}
] | [] | [] | [] |
691 | BioInfer.d597.s1 | [
{
"id": "BioInfer.d597.s1__text",
"type": "Sentence",
"text": [
"alpha- and beta-catenin were present in most ovarian cells at all stages of folliculogenesis."
],
"offsets": [
[
0,
93
]
]
}
] | [
{
"id": "BioInfer.d597.s1.e0",
"type": "Gene/protein/RNA",
"text": [
"beta-catenin"
],
"offsets": [
[
11,
23
]
],
"normalized": []
},
{
"id": "BioInfer.d597.s1.e1",
"type": "Gene/protein/RNA",
"text": [
"alpha-",
"catenin"
],
"offsets": [
[
0,
6
],
[
16,
23
]
],
"normalized": []
}
] | [] | [] | [] |
692 | BioInfer.d599.s0 | [
{
"id": "BioInfer.d599.s0__text",
"type": "Sentence",
"text": [
"The core histones from Physarum, histones H2A, H2B, H3, and H4, are rapidly acetylated; histone H4 shows five subfractions, analogous to the five subfractions of mammalian histone H4 (containing zero to four acetyllysine residues per molecule); histone H3 has a more complex pattern that we interpret as zero to four acetyllysine residues on each of two sequence variants of histone H3; histones H2A and H2B show less heterogeneity."
],
"offsets": [
[
0,
432
]
]
}
] | [
{
"id": "BioInfer.d599.s0.e0",
"type": "Individual_protein",
"text": [
"histones"
],
"offsets": [
[
387,
395
]
],
"normalized": []
},
{
"id": "BioInfer.d599.s0.e1",
"type": "Protein_family_or_group",
"text": [
"histone"
],
"offsets": [
[
172,
179
]
],
"normalized": []
},
{
"id": "BioInfer.d599.s0.e2",
"type": "Individual_protein",
"text": [
"histones"
],
"offsets": [
[
9,
17
]
],
"normalized": []
},
{
"id": "BioInfer.d599.s0.e3",
"type": "Protein_family_or_group",
"text": [
"histone"
],
"offsets": [
[
375,
382
]
],
"normalized": []
},
{
"id": "BioInfer.d599.s0.e4",
"type": "Protein_family_or_group",
"text": [
"histone"
],
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[
88,
95
]
],
"normalized": []
},
{
"id": "BioInfer.d599.s0.e5",
"type": "Individual_protein",
"text": [
"H2B"
],
"offsets": [
[
404,
407
]
],
"normalized": []
},
{
"id": "BioInfer.d599.s0.e6",
"type": "Protein_family_or_group",
"text": [
"histone"
],
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[
245,
252
]
],
"normalized": []
},
{
"id": "BioInfer.d599.s0.e7",
"type": "Individual_protein",
"text": [
"histones"
],
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[
33,
41
]
],
"normalized": []
},
{
"id": "BioInfer.d599.s0.e8",
"type": "Individual_protein",
"text": [
"H4"
],
"offsets": [
[
96,
98
]
],
"normalized": []
},
{
"id": "BioInfer.d599.s0.e9",
"type": "Individual_protein",
"text": [
"H4"
],
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[
60,
62
]
],
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},
{
"id": "BioInfer.d599.s0.e10",
"type": "Individual_protein",
"text": [
"H3"
],
"offsets": [
[
253,
255
]
],
"normalized": []
},
{
"id": "BioInfer.d599.s0.e11",
"type": "Individual_protein",
"text": [
"H4"
],
"offsets": [
[
180,
182
]
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52,
54
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47,
50
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396,
399
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"H3"
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383,
385
]
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] | [] | [] | [
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}
] |
693 | BioInfer.d602.s0 | [
{
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],
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[
0,
99
]
]
}
] | [
{
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63,
67
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],
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{
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72,
76
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25,
29
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],
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] | [] | [] | [
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}
] |
694 | BioInfer.d603.s0 | [
{
"id": "BioInfer.d603.s0__text",
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"text": [
"The cytoplasmic domain of E-cadherin cannot directly associate with alpha-catenin but interacts with high affinity with beta-catenin, whereas the binding of gamma-catenin (plakoglobin) to E-cadherin is less efficient."
],
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0,
217
]
]
}
] | [
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68,
81
]
],
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},
{
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],
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172,
183
]
],
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},
{
"id": "BioInfer.d603.s0.e2",
"type": "Individual_protein",
"text": [
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26,
36
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},
{
"id": "BioInfer.d603.s0.e3",
"type": "Individual_protein",
"text": [
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188,
198
]
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},
{
"id": "BioInfer.d603.s0.e4",
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],
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157,
170
]
],
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},
{
"id": "BioInfer.d603.s0.e5",
"type": "Individual_protein",
"text": [
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],
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120,
132
]
],
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}
] | [] | [] | [
{
"id": "BioInfer.d603.s0.i0",
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{
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{
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"arg1_id": "BioInfer.d603.s0.e3",
"arg2_id": "BioInfer.d603.s0.e4",
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}
] |
695 | BioInfer.d603.s1 | [
{
"id": "BioInfer.d603.s1__text",
"type": "Sentence",
"text": [
"alpha- and beta-catenin assemble into a 1:1 heterodimeric complex."
],
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[
0,
66
]
]
}
] | [
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11,
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},
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0,
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],
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16,
23
]
],
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}
] | [] | [] | [
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"arg2_id": "BioInfer.d603.s1.e1",
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}
] |
696 | BioInfer.d604.s0 | [
{
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"type": "Sentence",
"text": [
"The deduced peptide sequence contained a nuclear localization signal and a putative actin-binding sequence as reported in NM-type cofilin."
],
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[
0,
138
]
]
}
] | [
{
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],
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122,
137
]
],
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{
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],
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84,
89
]
],
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}
] | [] | [] | [
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}
] |
697 | BioInfer.d605.s0 | [
{
"id": "BioInfer.d605.s0__text",
"type": "Sentence",
"text": [
"The domain consists of a mixed alpha-helical/beta-sheet fold that resembles a circular permutation of the actin/poly-proline binding protein, profilin, and the GAF/PAS family of regulatory modules."
],
"offsets": [
[
0,
197
]
]
}
] | [
{
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],
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106,
111
]
],
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},
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160,
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{
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"text": [
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],
"offsets": [
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142,
150
]
],
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}
] | [] | [] | [
{
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"arg2_id": "BioInfer.d605.s0.e2",
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}
] |
698 | BioInfer.d606.s0 | [
{
"id": "BioInfer.d606.s0__text",
"type": "Sentence",
"text": [
"The domains in CBP that are involved in CREB binding and transcriptional activation are highly related to the adenoviral E1A-associated cellular protein p300 (refs 2, 3), and to two hypothetical proteins from Caenorhabditis elegans, R10E11.1 and K03H1.10 (refs 4 and 5, respectively), whose functions are unknown."
],
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[
0,
313
]
]
}
] | [
{
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121,
124
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246,
254
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{
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153,
157
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{
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233,
241
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{
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40,
44
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"text": [
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],
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15,
18
]
],
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}
] | [] | [] | [
{
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{
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}
] |
699 | BioInfer.d607.s0 | [
{
"id": "BioInfer.d607.s0__text",
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"text": [
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],
"offsets": [
[
0,
127
]
]
}
] | [
{
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48,
53
]
],
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},
{
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"text": [
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],
"offsets": [
[
37,
44
]
],
"normalized": []
}
] | [] | [] | [
{
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"arg1_id": "BioInfer.d607.s0.e0",
"arg2_id": "BioInfer.d607.s0.e1",
"normalized": []
}
] |