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367 | BioInfer.d279.s1 | [
{
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"type": "Sentence",
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"In cultured cells, cofilin, as well as ADF, translocates from the cytoplasm into the nucleus together with actin and forms rod-like structures in response to heat shock or dimethylsulfoxide (DMSO) treatment."
],
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[
0,
207
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]
}
] | [
{
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"ADF"
],
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39,
42
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107,
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"text": [
"cofilin"
],
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19,
26
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],
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] | [] | [] | [
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"arg2_id": "BioInfer.d279.s1.e2",
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}
] |
368 | BioInfer.d279.s2 | [
{
"id": "BioInfer.d279.s2__text",
"type": "Sentence",
"text": [
"Stimulus-dependent disorganization of actin filaments induced by overexpression of cofilin in C2 myoblasts."
],
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[
0,
107
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]
}
] | [
{
"id": "BioInfer.d279.s2.e0",
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38,
43
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"cofilin"
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83,
90
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369 | BioInfer.d280.s0 | [
{
"id": "BioInfer.d280.s0__text",
"type": "Sentence",
"text": [
"However, when all of the four proteins (E-cadherin, alpha-catenin, beta-catenin, and gamma-catenin) were analysed as one group, a significant association was seen between reduction in immunoreactivity of at least one of these four proteins and the presence of metastases."
],
"offsets": [
[
0,
271
]
]
}
] | [
{
"id": "BioInfer.d280.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"beta-catenin"
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67,
79
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},
{
"id": "BioInfer.d280.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"E-cadherin"
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40,
50
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{
"id": "BioInfer.d280.s0.e2",
"type": "Gene/protein/RNA",
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85,
98
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"id": "BioInfer.d280.s0.e3",
"type": "Gene/protein/RNA",
"text": [
"alpha-catenin"
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52,
65
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] | [] | [] | [] |
370 | BioInfer.d280.s1 | [
{
"id": "BioInfer.d280.s1__text",
"type": "Sentence",
"text": [
"Reduced or absent immunoreactivity in the tumour tissue was seen in 63 (70.0 per cent) for alpha-catenin, in 50 (55.6 per cent) for beta-catenin, and in 50 (55.6 per cent) for gamma-catenin."
],
"offsets": [
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0,
190
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{
"id": "BioInfer.d280.s1.e0",
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"beta-catenin"
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132,
144
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"id": "BioInfer.d280.s1.e1",
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176,
189
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{
"id": "BioInfer.d280.s1.e2",
"type": "Gene/protein/RNA",
"text": [
"alpha-catenin"
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91,
104
]
],
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}
] | [] | [] | [] |
371 | BioInfer.d281.s0 | [
{
"id": "BioInfer.d281.s0__text",
"type": "Sentence",
"text": [
"Human profilins are multifunctional, single-domain proteins which directly link the actin microfilament system to a variety of signalling pathways via two spatially distinct binding sites."
],
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[
0,
188
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]
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] | [
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84,
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"id": "BioInfer.d281.s0.e1",
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"text": [
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6,
15
]
],
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}
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] |
372 | BioInfer.d282.s0 | [
{
"id": "BioInfer.d282.s0__text",
"type": "Sentence",
"text": [
"Human platelet P-235, a talin-like actin binding protein, binds selectively to mixed lipid bilayers."
],
"offsets": [
[
0,
100
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]
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] | [
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"id": "BioInfer.d282.s0.e0",
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35,
56
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6,
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"text": [
"talin"
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24,
29
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] |
373 | BioInfer.d283.s0 | [
{
"id": "BioInfer.d283.s0__text",
"type": "Sentence",
"text": [
"Human platelets contain profilin, a potential regulator of actin polymerisability."
],
"offsets": [
[
0,
82
]
]
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] | [
{
"id": "BioInfer.d283.s0.e0",
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{
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"text": [
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24,
32
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],
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}
] | [] | [] | [
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}
] |
374 | BioInfer.d284.s0 | [
{
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"text": [
"Hypertonicity provoked Fyn-dependent tyrosine phosphorylation in beta-catenin, alpha-catenin, and p120(Cas) and caused the dissociation of beta-catenin from the contacts."
],
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[
0,
170
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]
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] | [
{
"id": "BioInfer.d284.s0.e0",
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103,
106
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65,
77
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},
{
"id": "BioInfer.d284.s0.e2",
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98,
102
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},
{
"id": "BioInfer.d284.s0.e3",
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23,
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79,
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"id": "BioInfer.d284.s0.e5",
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139,
151
]
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}
] | [] | [] | [
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] |
375 | BioInfer.d285.s0 | [
{
"id": "BioInfer.d285.s0__text",
"type": "Sentence",
"text": [
"Immediately after synthesis, E-cadherin, beta-catenin, and plakoglobin cosedimented as complexes."
],
"offsets": [
[
0,
97
]
]
}
] | [
{
"id": "BioInfer.d285.s0.e0",
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],
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41,
53
]
],
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},
{
"id": "BioInfer.d285.s0.e1",
"type": "Individual_protein",
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59,
70
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},
{
"id": "BioInfer.d285.s0.e2",
"type": "Individual_protein",
"text": [
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],
"offsets": [
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29,
39
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],
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] | [] | [] | [
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] |
376 | BioInfer.d285.s1 | [
{
"id": "BioInfer.d285.s1__text",
"type": "Sentence",
"text": [
"alpha-Catenin was not associated with these complexes after synthesis, but a subpopulation of alpha-catenin joined the complex at a time coincident with the arrival of E-cadherin at the plasma membrane."
],
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0,
202
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]
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] | [
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168,
178
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94,
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0,
13
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],
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}
] | [] | [] | [
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377 | BioInfer.d287.s0 | [
{
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"type": "Sentence",
"text": [
"Immunocytochemical localisation of actin and profilin in the generative cell of angiosperm pollen: TEM studies on high-pressure frozen and freeze-substituted Ledebouria socialis Roth (Hyacinthaceae)."
],
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0,
199
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]
}
] | [
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35,
40
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],
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45,
53
]
],
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] | [] | [] | [] |
378 | BioInfer.d287.s1 | [
{
"id": "BioInfer.d287.s1__text",
"type": "Sentence",
"text": [
"We attribute the detection of actin and profilin to the applied cryomethods which yield a much better preservation of ultrastructure and antigenicity of delicate cytoskeletal constituents than conventional fixation techniques."
],
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[
0,
226
]
]
}
] | [
{
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30,
35
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40,
48
]
],
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}
] | [] | [] | [] |
379 | BioInfer.d288.s0 | [
{
"id": "BioInfer.d288.s0__text",
"type": "Sentence",
"text": [
"Immunofluorescence experiments showed that, like Abp1p, cofilin is associated with the membrane actin cytoskeleton."
],
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[
0,
115
]
]
}
] | [
{
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49,
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96,
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56,
63
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}
] | [] | [] | [
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] |
380 | BioInfer.d288.s1 | [
{
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"In this study, we demonstrate using viscosity, sedimentation, and actin assembly rate assays that yeast cofilin (16 kD) possesses all of these properties."
],
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0,
154
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104,
111
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66,
71
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] | [] | [] | [] |
381 | BioInfer.d288.s2 | [
{
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"text": [
"The NH2-terminal 16kD of Abp1p, a 65-kD yeast protein identified by its ability to bind to actin filaments, is 23% identical to yeast cofilin."
],
"offsets": [
[
0,
142
]
]
}
] | [
{
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] |
382 | BioInfer.d288.s3 | [
{
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"We have biochemically identified the Saccharomyces cerevisiae homologue of the mammalian actin binding protein cofilin."
],
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[
0,
119
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]
}
] | [
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383 | BioInfer.d289.s0 | [
{
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"text": [
"Immunofluorescence microscopy of monolayers between 2 and 3 h post-TGF-beta1 showed that beta-catenin, plakoglobin, alpha-catenin, and cadherin-5 were colocalized both at the cell periphery and in newly formed bands that are perpendicular to the cell-cell border."
],
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0,
263
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}
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67,
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135,
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}
] | [] | [] | [
{
"id": "BioInfer.d289.s0.i0",
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"arg1_id": "BioInfer.d289.s0.e1",
"arg2_id": "BioInfer.d289.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d289.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d289.s0.e1",
"arg2_id": "BioInfer.d289.s0.e3",
"normalized": []
},
{
"id": "BioInfer.d289.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d289.s0.e1",
"arg2_id": "BioInfer.d289.s0.e4",
"normalized": []
},
{
"id": "BioInfer.d289.s0.i3",
"type": "PPI",
"arg1_id": "BioInfer.d289.s0.e2",
"arg2_id": "BioInfer.d289.s0.e3",
"normalized": []
},
{
"id": "BioInfer.d289.s0.i4",
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"arg1_id": "BioInfer.d289.s0.e2",
"arg2_id": "BioInfer.d289.s0.e4",
"normalized": []
},
{
"id": "BioInfer.d289.s0.i5",
"type": "PPI",
"arg1_id": "BioInfer.d289.s0.e3",
"arg2_id": "BioInfer.d289.s0.e4",
"normalized": []
}
] |
384 | BioInfer.d291.s0 | [
{
"id": "BioInfer.d291.s0__text",
"type": "Sentence",
"text": [
"Immunohistochemical identification and localization of actin and fimbrin in vestibular hair cells in the normal guinea pig and in a strain of the waltzing guinea pig."
],
"offsets": [
[
0,
166
]
]
}
] | [
{
"id": "BioInfer.d291.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"actin"
],
"offsets": [
[
55,
60
]
],
"normalized": []
},
{
"id": "BioInfer.d291.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"fimbrin"
],
"offsets": [
[
65,
72
]
],
"normalized": []
}
] | [] | [] | [] |
385 | BioInfer.d292.s0 | [
{
"id": "BioInfer.d292.s0__text",
"type": "Sentence",
"text": [
"Immunohistochemical investigation of actin-anchoring proteins vinculin, talin and paxillin in rat brain following lesion: a moderate reaction, confined to the astroglia of brain tracts."
],
"offsets": [
[
0,
185
]
]
}
] | [
{
"id": "BioInfer.d292.s0.e0",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
37,
42
]
],
"normalized": []
},
{
"id": "BioInfer.d292.s0.e1",
"type": "Individual_protein",
"text": [
"paxillin"
],
"offsets": [
[
82,
90
]
],
"normalized": []
},
{
"id": "BioInfer.d292.s0.e2",
"type": "Individual_protein",
"text": [
"talin"
],
"offsets": [
[
72,
77
]
],
"normalized": []
},
{
"id": "BioInfer.d292.s0.e3",
"type": "Individual_protein",
"text": [
"vinculin"
],
"offsets": [
[
62,
70
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d292.s0.i0",
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"arg2_id": "BioInfer.d292.s0.e1",
"normalized": []
},
{
"id": "BioInfer.d292.s0.i1",
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"arg1_id": "BioInfer.d292.s0.e0",
"arg2_id": "BioInfer.d292.s0.e2",
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},
{
"id": "BioInfer.d292.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d292.s0.e0",
"arg2_id": "BioInfer.d292.s0.e3",
"normalized": []
}
] |
386 | BioInfer.d293.s0 | [
{
"id": "BioInfer.d293.s0__text",
"type": "Sentence",
"text": [
"Immunohistochemical studies showed a strong reactivity of most LAM cells for alpha-smooth muscle actin and smooth muscle myosin heavy chain and a weak to moderate reactivity of a lesser number of cells for desmin and nonmuscle myosin heavy chain II-B."
],
"offsets": [
[
0,
251
]
]
}
] | [
{
"id": "BioInfer.d293.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"desmin"
],
"offsets": [
[
206,
212
]
],
"normalized": []
},
{
"id": "BioInfer.d293.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"alpha-smooth muscle actin"
],
"offsets": [
[
77,
102
]
],
"normalized": []
},
{
"id": "BioInfer.d293.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"nonmuscle myosin heavy chain II-B"
],
"offsets": [
[
217,
250
]
],
"normalized": []
},
{
"id": "BioInfer.d293.s0.e3",
"type": "Gene/protein/RNA",
"text": [
"smooth muscle myosin heavy chain"
],
"offsets": [
[
107,
139
]
],
"normalized": []
}
] | [] | [] | [] |
387 | BioInfer.d294.s0 | [
{
"id": "BioInfer.d294.s0__text",
"type": "Sentence",
"text": [
"Immunohistochemistry for a variety of cytokeratins (CKs) (8/18, 1/10, 7, and 20), epithelial membrane antigen (EMA), S-100 protein, vimentin CD34, type IV collagen, smooth muscle actin, smooth muscle myosin heavy chain, calponin, and glial fibrillary acid protein was performed."
],
"offsets": [
[
0,
278
]
]
}
] | [
{
"id": "BioInfer.d294.s0.e0",
"type": "Individual_protein",
"text": [
"cytokeratins",
"1"
],
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[
38,
50
],
[
64,
65
]
],
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},
{
"id": "BioInfer.d294.s0.e1",
"type": "Individual_protein",
"text": [
"cytokeratins",
"8"
],
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[
38,
50
],
[
58,
59
]
],
"normalized": []
},
{
"id": "BioInfer.d294.s0.e2",
"type": "Individual_protein",
"text": [
"S-100"
],
"offsets": [
[
117,
122
]
],
"normalized": []
},
{
"id": "BioInfer.d294.s0.e3",
"type": "Gene/protein/RNA",
"text": [
"glial fibrillary acid protein"
],
"offsets": [
[
234,
263
]
],
"normalized": []
},
{
"id": "BioInfer.d294.s0.e4",
"type": "Individual_protein",
"text": [
"EMA"
],
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111,
114
]
],
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},
{
"id": "BioInfer.d294.s0.e5",
"type": "Individual_protein",
"text": [
"epithelial membrane antigen"
],
"offsets": [
[
82,
109
]
],
"normalized": []
},
{
"id": "BioInfer.d294.s0.e6",
"type": "Gene/protein/RNA",
"text": [
"type IV collagen"
],
"offsets": [
[
147,
163
]
],
"normalized": []
},
{
"id": "BioInfer.d294.s0.e7",
"type": "Gene/protein/RNA",
"text": [
"vimentin"
],
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[
132,
140
]
],
"normalized": []
},
{
"id": "BioInfer.d294.s0.e8",
"type": "Gene/protein/RNA",
"text": [
"smooth muscle myosin heavy chain"
],
"offsets": [
[
186,
218
]
],
"normalized": []
},
{
"id": "BioInfer.d294.s0.e9",
"type": "Gene/protein/RNA",
"text": [
"smooth muscle actin"
],
"offsets": [
[
165,
184
]
],
"normalized": []
},
{
"id": "BioInfer.d294.s0.e10",
"type": "Gene/protein/RNA",
"text": [
"CD34"
],
"offsets": [
[
141,
145
]
],
"normalized": []
},
{
"id": "BioInfer.d294.s0.e11",
"type": "Gene/protein/RNA",
"text": [
"cytokeratins",
"20"
],
"offsets": [
[
38,
50
],
[
77,
79
]
],
"normalized": []
},
{
"id": "BioInfer.d294.s0.e12",
"type": "Gene/protein/RNA",
"text": [
"cytokeratins",
"7"
],
"offsets": [
[
38,
50
],
[
70,
71
]
],
"normalized": []
},
{
"id": "BioInfer.d294.s0.e13",
"type": "Gene/protein/RNA",
"text": [
"calponin"
],
"offsets": [
[
220,
228
]
],
"normalized": []
},
{
"id": "BioInfer.d294.s0.e14",
"type": "Gene/protein/RNA",
"text": [
"CKs"
],
"offsets": [
[
52,
55
]
],
"normalized": []
},
{
"id": "BioInfer.d294.s0.e15",
"type": "Individual_protein",
"text": [
"cytokeratins",
"10"
],
"offsets": [
[
38,
50
],
[
66,
68
]
],
"normalized": []
},
{
"id": "BioInfer.d294.s0.e16",
"type": "Individual_protein",
"text": [
"cytokeratins",
"18"
],
"offsets": [
[
38,
50
],
[
60,
62
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d294.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d294.s0.e0",
"arg2_id": "BioInfer.d294.s0.e15",
"normalized": []
},
{
"id": "BioInfer.d294.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d294.s0.e1",
"arg2_id": "BioInfer.d294.s0.e16",
"normalized": []
}
] |
388 | BioInfer.d295.s0 | [
{
"id": "BioInfer.d295.s0__text",
"type": "Sentence",
"text": [
"Immunohistochemistry revealed that arteries had three distinct populations of cells in respect to alpha-smooth muscle actin, smooth muscle myosin heavy chain and vimentin (staining intensities '-', '+' or '++' for each protein), but only two populations in respect to desmin ('-' and '+')."
],
"offsets": [
[
0,
289
]
]
}
] | [
{
"id": "BioInfer.d295.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"alpha-smooth muscle actin"
],
"offsets": [
[
98,
123
]
],
"normalized": []
},
{
"id": "BioInfer.d295.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"vimentin"
],
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[
162,
170
]
],
"normalized": []
},
{
"id": "BioInfer.d295.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"smooth muscle myosin heavy chain"
],
"offsets": [
[
125,
157
]
],
"normalized": []
},
{
"id": "BioInfer.d295.s0.e3",
"type": "Gene/protein/RNA",
"text": [
"desmin"
],
"offsets": [
[
268,
274
]
],
"normalized": []
}
] | [] | [] | [] |
389 | BioInfer.d296.s0 | [
{
"id": "BioInfer.d296.s0__text",
"type": "Sentence",
"text": [
"Immunolocalization of E-cadherin (E-cad), alpha-catenin, beta-catenin, and CD44 has rarely been investigated in human cholangiocarcinoma (CC)."
],
"offsets": [
[
0,
142
]
]
}
] | [
{
"id": "BioInfer.d296.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"beta-catenin"
],
"offsets": [
[
57,
69
]
],
"normalized": []
},
{
"id": "BioInfer.d296.s0.e1",
"type": "Individual_protein",
"text": [
"E-cadherin"
],
"offsets": [
[
22,
32
]
],
"normalized": []
},
{
"id": "BioInfer.d296.s0.e2",
"type": "Individual_protein",
"text": [
"E-cad"
],
"offsets": [
[
34,
39
]
],
"normalized": []
},
{
"id": "BioInfer.d296.s0.e3",
"type": "Gene/protein/RNA",
"text": [
"alpha-catenin"
],
"offsets": [
[
42,
55
]
],
"normalized": []
},
{
"id": "BioInfer.d296.s0.e4",
"type": "Gene/protein/RNA",
"text": [
"CD44"
],
"offsets": [
[
75,
79
]
],
"normalized": []
}
] | [] | [] | [] |
390 | BioInfer.d296.s1 | [
{
"id": "BioInfer.d296.s1__text",
"type": "Sentence",
"text": [
"In CC, membranous expression of E-cad, alpha-catenin, and beta-catenin was the same or reduced when compared with non-cancerous bile ducts in the majority of CC."
],
"offsets": [
[
0,
161
]
]
}
] | [
{
"id": "BioInfer.d296.s1.e0",
"type": "Gene/protein/RNA",
"text": [
"E-cad"
],
"offsets": [
[
32,
37
]
],
"normalized": []
},
{
"id": "BioInfer.d296.s1.e1",
"type": "Gene/protein/RNA",
"text": [
"beta-catenin"
],
"offsets": [
[
58,
70
]
],
"normalized": []
},
{
"id": "BioInfer.d296.s1.e2",
"type": "Gene/protein/RNA",
"text": [
"alpha-catenin"
],
"offsets": [
[
39,
52
]
],
"normalized": []
}
] | [] | [] | [] |
391 | BioInfer.d296.s2 | [
{
"id": "BioInfer.d296.s2__text",
"type": "Sentence",
"text": [
"In normal livers, E-cad, alpha-catenin and beta-catenin, but not CD44s, CD44v5, CD44v6, CD44v7-8, and CD44v10, were expressed at the cell membrane of normal intrahepatic bile ducts."
],
"offsets": [
[
0,
181
]
]
}
] | [
{
"id": "BioInfer.d296.s2.e0",
"type": "Individual_protein",
"text": [
"beta-catenin"
],
"offsets": [
[
43,
55
]
],
"normalized": []
},
{
"id": "BioInfer.d296.s2.e1",
"type": "Individual_protein",
"text": [
"CD44s"
],
"offsets": [
[
65,
70
]
],
"normalized": []
},
{
"id": "BioInfer.d296.s2.e2",
"type": "Individual_protein",
"text": [
"CD44v10"
],
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[
102,
109
]
],
"normalized": []
},
{
"id": "BioInfer.d296.s2.e3",
"type": "Individual_protein",
"text": [
"CD44v6"
],
"offsets": [
[
80,
86
]
],
"normalized": []
},
{
"id": "BioInfer.d296.s2.e4",
"type": "Individual_protein",
"text": [
"E-cad"
],
"offsets": [
[
18,
23
]
],
"normalized": []
},
{
"id": "BioInfer.d296.s2.e5",
"type": "Individual_protein",
"text": [
"CD44v5"
],
"offsets": [
[
72,
78
]
],
"normalized": []
},
{
"id": "BioInfer.d296.s2.e6",
"type": "Individual_protein",
"text": [
"alpha-catenin"
],
"offsets": [
[
25,
38
]
],
"normalized": []
},
{
"id": "BioInfer.d296.s2.e7",
"type": "Individual_protein",
"text": [
"CD44v7-8"
],
"offsets": [
[
88,
96
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d296.s2.i0",
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"arg1_id": "BioInfer.d296.s2.e0",
"arg2_id": "BioInfer.d296.s2.e1",
"normalized": []
},
{
"id": "BioInfer.d296.s2.i1",
"type": "PPI",
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"arg2_id": "BioInfer.d296.s2.e2",
"normalized": []
},
{
"id": "BioInfer.d296.s2.i2",
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"arg2_id": "BioInfer.d296.s2.e3",
"normalized": []
},
{
"id": "BioInfer.d296.s2.i3",
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},
{
"id": "BioInfer.d296.s2.i4",
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},
{
"id": "BioInfer.d296.s2.i5",
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"normalized": []
},
{
"id": "BioInfer.d296.s2.i6",
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"arg2_id": "BioInfer.d296.s2.e7",
"normalized": []
},
{
"id": "BioInfer.d296.s2.i7",
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},
{
"id": "BioInfer.d296.s2.i8",
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},
{
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"arg2_id": "BioInfer.d296.s2.e4",
"normalized": []
},
{
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"normalized": []
},
{
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"normalized": []
},
{
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"arg2_id": "BioInfer.d296.s2.e6",
"normalized": []
},
{
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"normalized": []
},
{
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"normalized": []
},
{
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"arg2_id": "BioInfer.d296.s2.e7",
"normalized": []
},
{
"id": "BioInfer.d296.s2.i16",
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"normalized": []
},
{
"id": "BioInfer.d296.s2.i17",
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"arg1_id": "BioInfer.d296.s2.e6",
"arg2_id": "BioInfer.d296.s2.e7",
"normalized": []
}
] |
392 | BioInfer.d296.s3 | [
{
"id": "BioInfer.d296.s3__text",
"type": "Sentence",
"text": [
"We found that the down-regulation of E-cad, alpha-catenin, and beta-catenin expression significantly correlated with tumor high grade, but not with vascular invasion, metastasis, p53 expression, Ki-67 labeling, or c-erbB2 expression, except for beta-catenin, the down-regulation of which was associated with c-erbB2 down-regulation."
],
"offsets": [
[
0,
332
]
]
}
] | [
{
"id": "BioInfer.d296.s3.e0",
"type": "Individual_protein",
"text": [
"beta-catenin"
],
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[
245,
257
]
],
"normalized": []
},
{
"id": "BioInfer.d296.s3.e1",
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"text": [
"E-cad"
],
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[
37,
42
]
],
"normalized": []
},
{
"id": "BioInfer.d296.s3.e2",
"type": "Individual_protein",
"text": [
"beta-catenin"
],
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[
63,
75
]
],
"normalized": []
},
{
"id": "BioInfer.d296.s3.e3",
"type": "Individual_protein",
"text": [
"c-erbB2"
],
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[
214,
221
]
],
"normalized": []
},
{
"id": "BioInfer.d296.s3.e4",
"type": "Individual_protein",
"text": [
"p53"
],
"offsets": [
[
179,
182
]
],
"normalized": []
},
{
"id": "BioInfer.d296.s3.e5",
"type": "Individual_protein",
"text": [
"c-erbB2"
],
"offsets": [
[
308,
315
]
],
"normalized": []
},
{
"id": "BioInfer.d296.s3.e6",
"type": "Individual_protein",
"text": [
"alpha-catenin"
],
"offsets": [
[
44,
57
]
],
"normalized": []
},
{
"id": "BioInfer.d296.s3.e7",
"type": "Individual_protein",
"text": [
"Ki-67"
],
"offsets": [
[
195,
200
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d296.s3.i0",
"type": "PPI",
"arg1_id": "BioInfer.d296.s3.e0",
"arg2_id": "BioInfer.d296.s3.e5",
"normalized": []
},
{
"id": "BioInfer.d296.s3.i1",
"type": "PPI",
"arg1_id": "BioInfer.d296.s3.e1",
"arg2_id": "BioInfer.d296.s3.e3",
"normalized": []
},
{
"id": "BioInfer.d296.s3.i2",
"type": "PPI",
"arg1_id": "BioInfer.d296.s3.e1",
"arg2_id": "BioInfer.d296.s3.e4",
"normalized": []
},
{
"id": "BioInfer.d296.s3.i3",
"type": "PPI",
"arg1_id": "BioInfer.d296.s3.e2",
"arg2_id": "BioInfer.d296.s3.e3",
"normalized": []
},
{
"id": "BioInfer.d296.s3.i4",
"type": "PPI",
"arg1_id": "BioInfer.d296.s3.e2",
"arg2_id": "BioInfer.d296.s3.e4",
"normalized": []
},
{
"id": "BioInfer.d296.s3.i5",
"type": "PPI",
"arg1_id": "BioInfer.d296.s3.e3",
"arg2_id": "BioInfer.d296.s3.e6",
"normalized": []
},
{
"id": "BioInfer.d296.s3.i6",
"type": "PPI",
"arg1_id": "BioInfer.d296.s3.e4",
"arg2_id": "BioInfer.d296.s3.e6",
"normalized": []
}
] |
393 | BioInfer.d297.s0 | [
{
"id": "BioInfer.d297.s0__text",
"type": "Sentence",
"text": [
"Immunoprecipitation of alpha-catenin was increased in response to both doses of CdCl2, while the immunoprecipitation of beta-catenin was little changed by either cadmium dose."
],
"offsets": [
[
0,
175
]
]
}
] | [
{
"id": "BioInfer.d297.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"alpha-catenin"
],
"offsets": [
[
23,
36
]
],
"normalized": []
},
{
"id": "BioInfer.d297.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"beta-catenin"
],
"offsets": [
[
120,
132
]
],
"normalized": []
}
] | [] | [] | [] |
394 | BioInfer.d298.s0 | [
{
"id": "BioInfer.d298.s0__text",
"type": "Sentence",
"text": [
"Immunoprecipitation of metabolically labeled proteins with HECD-1 revealed three bands corresponding to E-cadherin, alpha-catenin, and gamma-catenin and a 79-kDa band which was apparently smaller than that of normal beta-catenin, indicating truncated beta-catenin."
],
"offsets": [
[
0,
264
]
]
}
] | [
{
"id": "BioInfer.d298.s0.e0",
"type": "Individual_protein",
"text": [
"beta-catenin"
],
"offsets": [
[
251,
263
]
],
"normalized": []
},
{
"id": "BioInfer.d298.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"beta-catenin"
],
"offsets": [
[
216,
228
]
],
"normalized": []
},
{
"id": "BioInfer.d298.s0.e2",
"type": "Individual_protein",
"text": [
"HECD-1"
],
"offsets": [
[
59,
65
]
],
"normalized": []
},
{
"id": "BioInfer.d298.s0.e3",
"type": "Individual_protein",
"text": [
"E-cadherin"
],
"offsets": [
[
104,
114
]
],
"normalized": []
},
{
"id": "BioInfer.d298.s0.e4",
"type": "Individual_protein",
"text": [
"alpha-catenin"
],
"offsets": [
[
116,
129
]
],
"normalized": []
},
{
"id": "BioInfer.d298.s0.e5",
"type": "Individual_protein",
"text": [
"gamma-catenin"
],
"offsets": [
[
135,
148
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d298.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d298.s0.e0",
"arg2_id": "BioInfer.d298.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d298.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d298.s0.e2",
"arg2_id": "BioInfer.d298.s0.e3",
"normalized": []
},
{
"id": "BioInfer.d298.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d298.s0.e2",
"arg2_id": "BioInfer.d298.s0.e4",
"normalized": []
},
{
"id": "BioInfer.d298.s0.i3",
"type": "PPI",
"arg1_id": "BioInfer.d298.s0.e2",
"arg2_id": "BioInfer.d298.s0.e5",
"normalized": []
}
] |
395 | BioInfer.d299.s0 | [
{
"id": "BioInfer.d299.s0__text",
"type": "Sentence",
"text": [
"Immunoprecipitations showed in both cell lines the presence of two different E-cadherin- catenin complexes, one composed of E-cadherin, alpha-catenin and beta-catenin, and the other of E-cadherin, alpha-catenin and plakoglobin."
],
"offsets": [
[
0,
227
]
]
}
] | [
{
"id": "BioInfer.d299.s0.e0",
"type": "Individual_protein",
"text": [
"beta-catenin"
],
"offsets": [
[
154,
166
]
],
"normalized": []
},
{
"id": "BioInfer.d299.s0.e1",
"type": "Individual_protein",
"text": [
"catenin"
],
"offsets": [
[
89,
96
]
],
"normalized": []
},
{
"id": "BioInfer.d299.s0.e2",
"type": "Individual_protein",
"text": [
"E-cadherin"
],
"offsets": [
[
77,
87
]
],
"normalized": []
},
{
"id": "BioInfer.d299.s0.e3",
"type": "Individual_protein",
"text": [
"E-cadherin"
],
"offsets": [
[
185,
195
]
],
"normalized": []
},
{
"id": "BioInfer.d299.s0.e4",
"type": "Individual_protein",
"text": [
"plakoglobin"
],
"offsets": [
[
215,
226
]
],
"normalized": []
},
{
"id": "BioInfer.d299.s0.e5",
"type": "Individual_protein",
"text": [
"alpha-catenin"
],
"offsets": [
[
197,
210
]
],
"normalized": []
},
{
"id": "BioInfer.d299.s0.e6",
"type": "Individual_protein",
"text": [
"E-cadherin"
],
"offsets": [
[
124,
134
]
],
"normalized": []
},
{
"id": "BioInfer.d299.s0.e7",
"type": "Individual_protein",
"text": [
"alpha-catenin"
],
"offsets": [
[
136,
149
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d299.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d299.s0.e0",
"arg2_id": "BioInfer.d299.s0.e6",
"normalized": []
},
{
"id": "BioInfer.d299.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d299.s0.e0",
"arg2_id": "BioInfer.d299.s0.e7",
"normalized": []
},
{
"id": "BioInfer.d299.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d299.s0.e1",
"arg2_id": "BioInfer.d299.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d299.s0.i3",
"type": "PPI",
"arg1_id": "BioInfer.d299.s0.e3",
"arg2_id": "BioInfer.d299.s0.e4",
"normalized": []
},
{
"id": "BioInfer.d299.s0.i4",
"type": "PPI",
"arg1_id": "BioInfer.d299.s0.e3",
"arg2_id": "BioInfer.d299.s0.e5",
"normalized": []
},
{
"id": "BioInfer.d299.s0.i5",
"type": "PPI",
"arg1_id": "BioInfer.d299.s0.e4",
"arg2_id": "BioInfer.d299.s0.e5",
"normalized": []
},
{
"id": "BioInfer.d299.s0.i6",
"type": "PPI",
"arg1_id": "BioInfer.d299.s0.e6",
"arg2_id": "BioInfer.d299.s0.e7",
"normalized": []
}
] |
396 | BioInfer.d300.s0 | [
{
"id": "BioInfer.d300.s0__text",
"type": "Sentence",
"text": [
"Immunoprecipitation with an E-cadherin mAb, which is known to co-precipitate the catenins, demonstrated that the three poorly differentiated cell lines expressing E-cadherin did not co-precipitate alpha-catenin, although all of the moderately-well differentiated cell lines expressed both alpha- and beta-catenin."
],
"offsets": [
[
0,
313
]
]
}
] | [
{
"id": "BioInfer.d300.s0.e0",
"type": "Individual_protein",
"text": [
"E-cadherin"
],
"offsets": [
[
28,
38
]
],
"normalized": []
},
{
"id": "BioInfer.d300.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"beta-catenin"
],
"offsets": [
[
300,
312
]
],
"normalized": []
},
{
"id": "BioInfer.d300.s0.e2",
"type": "Individual_protein",
"text": [
"alpha-catenin"
],
"offsets": [
[
197,
210
]
],
"normalized": []
},
{
"id": "BioInfer.d300.s0.e3",
"type": "Gene/protein/RNA",
"text": [
"alpha-",
"catenin"
],
"offsets": [
[
289,
295
],
[
305,
312
]
],
"normalized": []
},
{
"id": "BioInfer.d300.s0.e4",
"type": "Individual_protein",
"text": [
"catenins"
],
"offsets": [
[
81,
89
]
],
"normalized": []
},
{
"id": "BioInfer.d300.s0.e5",
"type": "Individual_protein",
"text": [
"E-cadherin"
],
"offsets": [
[
163,
173
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d300.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d300.s0.e0",
"arg2_id": "BioInfer.d300.s0.e4",
"normalized": []
},
{
"id": "BioInfer.d300.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d300.s0.e2",
"arg2_id": "BioInfer.d300.s0.e5",
"normalized": []
}
] |
397 | BioInfer.d301.s0 | [
{
"id": "BioInfer.d301.s0__text",
"type": "Sentence",
"text": [
"Immunoreactive E-cadherin, alpha-catenin, beta-catenin, and gamma-catenin proteins in hepatocellular carcinoma: relationships with tumor grade, clinicopathologic parameters, and patients' survival."
],
"offsets": [
[
0,
197
]
]
}
] | [
{
"id": "BioInfer.d301.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"E-cadherin"
],
"offsets": [
[
15,
25
]
],
"normalized": []
},
{
"id": "BioInfer.d301.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"beta-catenin"
],
"offsets": [
[
42,
54
]
],
"normalized": []
},
{
"id": "BioInfer.d301.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"alpha-catenin"
],
"offsets": [
[
27,
40
]
],
"normalized": []
},
{
"id": "BioInfer.d301.s0.e3",
"type": "Gene/protein/RNA",
"text": [
"gamma-catenin"
],
"offsets": [
[
60,
73
]
],
"normalized": []
}
] | [] | [] | [] |
398 | BioInfer.d302.s0 | [
{
"id": "BioInfer.d302.s0__text",
"type": "Sentence",
"text": [
"Immunoreactivity for pan-cadherin, E-cadherin, alpha-catenin, beta-catenin, and p120 was observed in all 15 specimens."
],
"offsets": [
[
0,
118
]
]
}
] | [
{
"id": "BioInfer.d302.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"alpha-catenin"
],
"offsets": [
[
47,
60
]
],
"normalized": []
},
{
"id": "BioInfer.d302.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"pan-cadherin"
],
"offsets": [
[
21,
33
]
],
"normalized": []
},
{
"id": "BioInfer.d302.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"p120"
],
"offsets": [
[
80,
84
]
],
"normalized": []
},
{
"id": "BioInfer.d302.s0.e3",
"type": "Gene/protein/RNA",
"text": [
"E-cadherin"
],
"offsets": [
[
35,
45
]
],
"normalized": []
},
{
"id": "BioInfer.d302.s0.e4",
"type": "Gene/protein/RNA",
"text": [
"beta-catenin"
],
"offsets": [
[
62,
74
]
],
"normalized": []
}
] | [] | [] | [] |
399 | BioInfer.d304.s0 | [
{
"id": "BioInfer.d304.s0__text",
"type": "Sentence",
"text": [
"Impact of profilin on actin-bound nucleotide exchange and actin polymerization dynamics."
],
"offsets": [
[
0,
88
]
]
}
] | [
{
"id": "BioInfer.d304.s0.e0",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
10,
18
]
],
"normalized": []
},
{
"id": "BioInfer.d304.s0.e1",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
22,
27
]
],
"normalized": []
},
{
"id": "BioInfer.d304.s0.e2",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
58,
63
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d304.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d304.s0.e0",
"arg2_id": "BioInfer.d304.s0.e2",
"normalized": []
}
] |
400 | BioInfer.d305.s0 | [
{
"id": "BioInfer.d305.s0__text",
"type": "Sentence",
"text": [
"In 50 mM KCl, high concentrations of Acanthamoeba profilin inhibit the elongation rate of muscle actin filaments measured directly by electron microscopy, but the effect is minimal in KCl with 2 MgCl2."
],
"offsets": [
[
0,
201
]
]
}
] | [
{
"id": "BioInfer.d305.s0.e0",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
50,
58
]
],
"normalized": []
},
{
"id": "BioInfer.d305.s0.e1",
"type": "Individual_protein",
"text": [
"muscle actin"
],
"offsets": [
[
90,
102
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d305.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d305.s0.e0",
"arg2_id": "BioInfer.d305.s0.e1",
"normalized": []
}
] |
401 | BioInfer.d306.s0 | [
{
"id": "BioInfer.d306.s0__text",
"type": "Sentence",
"text": [
"In a blot overlay experiment, purified 125I-labeled recombinant profilin bound not only to plant actin, but also to mammalian actin, demonstrating that cytoskeletal components from distantly related organisms with divergent primary structures can be compatible."
],
"offsets": [
[
0,
261
]
]
}
] | [
{
"id": "BioInfer.d306.s0.e0",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
64,
72
]
],
"normalized": []
},
{
"id": "BioInfer.d306.s0.e1",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
97,
102
]
],
"normalized": []
},
{
"id": "BioInfer.d306.s0.e2",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
126,
131
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d306.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d306.s0.e0",
"arg2_id": "BioInfer.d306.s0.e1",
"normalized": []
},
{
"id": "BioInfer.d306.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d306.s0.e0",
"arg2_id": "BioInfer.d306.s0.e2",
"normalized": []
}
] |
402 | BioInfer.d306.s1 | [
{
"id": "BioInfer.d306.s1__text",
"type": "Sentence",
"text": [
"cDNA cloning, heterologous expression, and actin-binding properties."
],
"offsets": [
[
0,
68
]
]
}
] | [
{
"id": "BioInfer.d306.s1.e0",
"type": "Gene/protein/RNA",
"text": [
"actin"
],
"offsets": [
[
43,
48
]
],
"normalized": []
}
] | [] | [] | [] |
403 | BioInfer.d307.s0 | [
{
"id": "BioInfer.d307.s0__text",
"type": "Sentence",
"text": [
"In Acanthamoeba actin polymerization is regulated, at least in part, by profilin, which binds to actin monomers, and by capping protein, which both nucleates polymerization and blocks monomer addition at the 'barbed' end of the filament."
],
"offsets": [
[
0,
237
]
]
}
] | [
{
"id": "BioInfer.d307.s0.e0",
"type": "Individual_protein",
"text": [
"capping protein"
],
"offsets": [
[
120,
135
]
],
"normalized": []
},
{
"id": "BioInfer.d307.s0.e1",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
97,
102
]
],
"normalized": []
},
{
"id": "BioInfer.d307.s0.e2",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
72,
80
]
],
"normalized": []
},
{
"id": "BioInfer.d307.s0.e3",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
16,
21
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d307.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d307.s0.e0",
"arg2_id": "BioInfer.d307.s0.e3",
"normalized": []
},
{
"id": "BioInfer.d307.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d307.s0.e1",
"arg2_id": "BioInfer.d307.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d307.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d307.s0.e2",
"arg2_id": "BioInfer.d307.s0.e3",
"normalized": []
}
] |
404 | BioInfer.d308.s0 | [
{
"id": "BioInfer.d308.s0__text",
"type": "Sentence",
"text": [
"In Acanthamoeba, the two isoforms of profilin may have specialized functions on the basis of their identical (approximately 10 microM) affinities for actin monomers and different affinities for PIP2."
],
"offsets": [
[
0,
199
]
]
}
] | [
{
"id": "BioInfer.d308.s0.e0",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
150,
155
]
],
"normalized": []
},
{
"id": "BioInfer.d308.s0.e1",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
37,
45
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d308.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d308.s0.e0",
"arg2_id": "BioInfer.d308.s0.e1",
"normalized": []
}
] |
405 | BioInfer.d309.s0 | [
{
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406 | BioInfer.d311.s0 | [
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407 | BioInfer.d312.s0 | [
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408 | BioInfer.d313.s0 | [
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409 | BioInfer.d314.s0 | [
{
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0,
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410 | BioInfer.d315.s0 | [
{
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0,
179
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411 | BioInfer.d316.s0 | [
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412 | BioInfer.d317.s0 | [
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0,
183
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] | [] | [] | [] |
413 | BioInfer.d319.s0 | [
{
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0,
108
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]
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414 | BioInfer.d320.s0 | [
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],
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0,
267
]
]
}
] | [
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] |
415 | BioInfer.d320.s1 | [
{
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],
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0,
241
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]
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] | [
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172,
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] |
416 | BioInfer.d321.s0 | [
{
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"type": "Sentence",
"text": [
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0,
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417 | BioInfer.d321.s1 | [
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418 | BioInfer.d322.s0 | [
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419 | BioInfer.d323.s0 | [
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420 | BioInfer.d324.s0 | [
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421 | BioInfer.d325.s0 | [
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0,
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422 | BioInfer.d327.s0 | [
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0,
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423 | BioInfer.d329.s0 | [
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0,
158
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424 | BioInfer.d330.s0 | [
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0,
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425 | BioInfer.d331.s0 | [
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0,
143
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426 | BioInfer.d332.s0 | [
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139
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427 | BioInfer.d332.s1 | [
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428 | BioInfer.d333.s0 | [
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429 | BioInfer.d334.s0 | [
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430 | BioInfer.d334.s1 | [
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102
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"text": [
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15,
25
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431 | BioInfer.d334.s2 | [
{
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"Our findings strongly suggest that in brain profilin I and profilin II complexes link the actin cytoskeleton and endocytic membrane flow, directing actin and clathrin assembly to distinct membrane domains."
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[
0,
205
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148,
153
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90,
95
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59,
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44,
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] |
432 | BioInfer.d335.s0 | [
{
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],
"offsets": [
[
0,
212
]
]
}
] | [
{
"id": "BioInfer.d335.s0.e0",
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171,
176
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},
{
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"type": "Individual_protein",
"text": [
"cofilin"
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44,
51
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{
"id": "BioInfer.d335.s0.e2",
"type": "Individual_protein",
"text": [
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91,
96
]
],
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}
] | [] | [] | [
{
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] |
433 | BioInfer.d335.s1 | [
{
"id": "BioInfer.d335.s1__text",
"type": "Sentence",
"text": [
"These results suggest that cofilin may be involved in dynamic reorganization of membranous actin cytoskeletons."
],
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[
0,
111
]
]
}
] | [
{
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91,
96
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},
{
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27,
34
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}
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}
] |
434 | BioInfer.d336.s0 | [
{
"id": "BioInfer.d336.s0__text",
"type": "Sentence",
"text": [
"In growth cones, myosin heavy chain B was most concentrated in the margin bordering the thickened, organelle-rich central region and the thin, actin-rich peripheral region."
],
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[
0,
172
]
]
}
] | [
{
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17,
37
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},
{
"id": "BioInfer.d336.s0.e1",
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143,
148
]
],
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}
] | [] | [] | [] |
435 | BioInfer.d336.s1 | [
{
"id": "BioInfer.d336.s1__text",
"type": "Sentence",
"text": [
"Myosin heavy chain A staining was dimmer and its colocalization with filamentous actin bundles in growth cones was less striking than that of myosin heavy chain B."
],
"offsets": [
[
0,
163
]
]
}
] | [
{
"id": "BioInfer.d336.s1.e0",
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"text": [
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81,
86
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},
{
"id": "BioInfer.d336.s1.e1",
"type": "Individual_protein",
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"Myosin heavy chain A"
],
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[
0,
20
]
],
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},
{
"id": "BioInfer.d336.s1.e2",
"type": "Individual_protein",
"text": [
"myosin heavy chain B"
],
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[
142,
162
]
],
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}
] | [] | [] | [
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}
] |
436 | BioInfer.d337.s0 | [
{
"id": "BioInfer.d337.s0__text",
"type": "Sentence",
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],
"offsets": [
[
0,
173
]
]
}
] | [
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82,
102
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112,
115
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] | [] | [] | [] |
437 | BioInfer.d338.s0 | [
{
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"type": "Sentence",
"text": [
"Inhibition of actin polymerization by a synthetic dodecapeptide patterned on the sequence around the actin-binding site of cofilin."
],
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[
0,
131
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]
}
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{
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14,
19
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101,
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123,
130
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] |
438 | BioInfer.d339.s0 | [
{
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"type": "Sentence",
"text": [
"Inhibition of actin polymerization in KCl was stronger than that of the parental profilin, and the Kd value of its interaction with rabbit skeletal muscle actin, as determined by falling ball viscometry, was smaller (mean value 0.5 x 10(-6) M, as compared to 1.9 x 10(-6) M for bovine profilin)."
],
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[
0,
295
]
]
}
] | [
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81,
89
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14,
19
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285,
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],
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139,
160
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}
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}
] |
439 | BioInfer.d340.s0 | [
{
"id": "BioInfer.d340.s0__text",
"type": "Sentence",
"text": [
"Inhibition of actomyosin subfragment 1 ATPase activity by analog peptides of the actin-binding site around the Cys(SH1) of myosin heavy chain."
],
"offsets": [
[
0,
142
]
]
}
] | [
{
"id": "BioInfer.d340.s0.e0",
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14,
24
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39,
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123,
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}
] |
440 | BioInfer.d342.s0 | [
{
"id": "BioInfer.d342.s0__text",
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"Inhibition of the interactions of cofilin, destrin, and deoxyribonuclease I with actin by phosphoinositides."
],
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[
0,
108
]
]
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{
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34,
41
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{
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56,
75
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43,
50
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],
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}
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}
] |
441 | BioInfer.d343.s0 | [
{
"id": "BioInfer.d343.s0__text",
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"text": [
"In higher plants, a large number of isoforms for the actin monomer-binding protein profilin have been identified, whereas other organisms express only few profilins."
],
"offsets": [
[
0,
165
]
]
}
] | [
{
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53,
58
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{
"id": "BioInfer.d343.s0.e1",
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155,
164
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],
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83,
91
]
],
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}
] | [] | [] | [
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] |
442 | BioInfer.d346.s0 | [
{
"id": "BioInfer.d346.s0__text",
"type": "Sentence",
"text": [
"In isolated hearts, PD 81,723 alone produced only a small stimulus to His bundle (S-H) interval prolongation of 1.5 to 4 msec, which was completely reversed by the A1 adenosine receptor antagonist 8-cyclopentyltheophylline and adenosine deaminase."
],
"offsets": [
[
0,
247
]
]
}
] | [
{
"id": "BioInfer.d346.s0.e0",
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227,
246
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],
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{
"id": "BioInfer.d346.s0.e1",
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"text": [
"A1 adenosine receptor"
],
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[
164,
185
]
],
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}
] | [] | [] | [] |
443 | BioInfer.d347.s0 | [
{
"id": "BioInfer.d347.s0__text",
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"text": [
"In localization studies with mammalian cells, all fusion proteins showed the localization expected for profilin in areas of high actin dynamics, such as leading lamellae and ruffles induced by epidermal growth factor."
],
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[
0,
217
]
]
}
] | [
{
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103,
111
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193,
216
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129,
134
]
],
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}
] | [] | [] | [] |
444 | BioInfer.d348.s0 | [
{
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"text": [
"In order to clarify cofilin-dependent regulation of actin assembly in muscle cells, cofilin tagged with fluorescence dyes was introduced into C2 myoblasts by a micro injection method."
],
"offsets": [
[
0,
183
]
]
}
] | [
{
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52,
57
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},
{
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20,
27
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{
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84,
91
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],
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}
] | [] | [] | [
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}
] |
445 | BioInfer.d348.s1 | [
{
"id": "BioInfer.d348.s1__text",
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"text": [
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],
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[
0,
132
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]
}
] | [
{
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15,
22
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{
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32,
35
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65,
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}
] |
446 | BioInfer.d348.s2 | [
{
"id": "BioInfer.d348.s2__text",
"type": "Sentence",
"text": [
"These results suggest that the subcellular distribution of cofilin as well as its interaction with actin in vivo is regulated by its phosphorylation and dephosphorylation."
],
"offsets": [
[
0,
171
]
]
}
] | [
{
"id": "BioInfer.d348.s2.e0",
"type": "Individual_protein",
"text": [
"actin"
],
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[
99,
104
]
],
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},
{
"id": "BioInfer.d348.s2.e1",
"type": "Individual_protein",
"text": [
"cofilin"
],
"offsets": [
[
59,
66
]
],
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}
] | [] | [] | [
{
"id": "BioInfer.d348.s2.i0",
"type": "PPI",
"arg1_id": "BioInfer.d348.s2.e0",
"arg2_id": "BioInfer.d348.s2.e1",
"normalized": []
}
] |
447 | BioInfer.d350.s0 | [
{
"id": "BioInfer.d350.s0__text",
"type": "Sentence",
"text": [
"In order to help explain the apparent beneficial effects of cyclin D1 over-expression, a number of closely associated cell cycle proteins have also been evaluated, including the cyclin dependent kinase inhibitor p27, which blocks the activating effects of cyclin D1."
],
"offsets": [
[
0,
266
]
]
}
] | [
{
"id": "BioInfer.d350.s0.e0",
"type": "Protein_family_or_group",
"text": [
"cyclin dependent kinase inhibitor"
],
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[
178,
211
]
],
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},
{
"id": "BioInfer.d350.s0.e1",
"type": "Individual_protein",
"text": [
"cyclin D1"
],
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256,
265
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],
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},
{
"id": "BioInfer.d350.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"cyclin D1"
],
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[
60,
69
]
],
"normalized": []
},
{
"id": "BioInfer.d350.s0.e3",
"type": "Individual_protein",
"text": [
"p27"
],
"offsets": [
[
212,
215
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d350.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d350.s0.e0",
"arg2_id": "BioInfer.d350.s0.e3",
"normalized": []
}
] |
448 | BioInfer.d351.s0 | [
{
"id": "BioInfer.d351.s0__text",
"type": "Sentence",
"text": [
"In reconstitution experiments, actin filaments incubated in EGTA with purified fimbrin and villin form smooth-sided bundles containing an apparently random number of filaments."
],
"offsets": [
[
0,
176
]
]
}
] | [
{
"id": "BioInfer.d351.s0.e0",
"type": "Individual_protein",
"text": [
"fimbrin"
],
"offsets": [
[
79,
86
]
],
"normalized": []
},
{
"id": "BioInfer.d351.s0.e1",
"type": "Individual_protein",
"text": [
"actin"
],
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[
31,
36
]
],
"normalized": []
},
{
"id": "BioInfer.d351.s0.e2",
"type": "Individual_protein",
"text": [
"villin"
],
"offsets": [
[
91,
97
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d351.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d351.s0.e0",
"arg2_id": "BioInfer.d351.s0.e1",
"normalized": []
},
{
"id": "BioInfer.d351.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d351.s0.e1",
"arg2_id": "BioInfer.d351.s0.e2",
"normalized": []
}
] |
449 | BioInfer.d352.s0 | [
{
"id": "BioInfer.d352.s0__text",
"type": "Sentence",
"text": [
"In resting leukocytes, beta2 integrins are constitutively linked to the actin cytoskeleton via the protein talin."
],
"offsets": [
[
0,
113
]
]
}
] | [
{
"id": "BioInfer.d352.s0.e0",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
72,
77
]
],
"normalized": []
},
{
"id": "BioInfer.d352.s0.e1",
"type": "Protein_family_or_group",
"text": [
"beta2 integrins"
],
"offsets": [
[
23,
38
]
],
"normalized": []
},
{
"id": "BioInfer.d352.s0.e2",
"type": "Individual_protein",
"text": [
"talin"
],
"offsets": [
[
107,
112
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d352.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d352.s0.e0",
"arg2_id": "BioInfer.d352.s0.e1",
"normalized": []
},
{
"id": "BioInfer.d352.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d352.s0.e0",
"arg2_id": "BioInfer.d352.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d352.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d352.s0.e1",
"arg2_id": "BioInfer.d352.s0.e2",
"normalized": []
}
] |
450 | BioInfer.d353.s0 | [
{
"id": "BioInfer.d353.s0__text",
"type": "Sentence",
"text": [
"In search for genes which might participate in chicken immunoglobulin gene conversion, we have identified chicken counterparts of the yeast RAD51, RAD52, and RAD54 genes."
],
"offsets": [
[
0,
170
]
]
}
] | [
{
"id": "BioInfer.d353.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"RAD54"
],
"offsets": [
[
158,
163
]
],
"normalized": []
},
{
"id": "BioInfer.d353.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"RAD51"
],
"offsets": [
[
140,
145
]
],
"normalized": []
},
{
"id": "BioInfer.d353.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"RAD52"
],
"offsets": [
[
147,
152
]
],
"normalized": []
},
{
"id": "BioInfer.d353.s0.e3",
"type": "Gene/protein/RNA",
"text": [
"immunoglobulin"
],
"offsets": [
[
55,
69
]
],
"normalized": []
}
] | [] | [] | [] |
451 | BioInfer.d354.s0 | [
{
"id": "BioInfer.d354.s0__text",
"type": "Sentence",
"text": [
"Insulin-like growth factor-I, actin, and myosin heavy chain messenger RNAs in skeletal muscle after an injection of growth hormone in subjects over 60 years old."
],
"offsets": [
[
0,
161
]
]
}
] | [
{
"id": "BioInfer.d354.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"actin"
],
"offsets": [
[
30,
35
]
],
"normalized": []
},
{
"id": "BioInfer.d354.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"Insulin-like growth factor-I"
],
"offsets": [
[
0,
28
]
],
"normalized": []
},
{
"id": "BioInfer.d354.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"myosin heavy chain"
],
"offsets": [
[
41,
59
]
],
"normalized": []
}
] | [] | [] | [] |
452 | BioInfer.d355.s0 | [
{
"id": "BioInfer.d355.s0__text",
"type": "Sentence",
"text": [
"Insulin-like growth factor I stimulates cardiac myosin heavy chain and actin synthesis in the awake rat."
],
"offsets": [
[
0,
104
]
]
}
] | [
{
"id": "BioInfer.d355.s0.e0",
"type": "Individual_protein",
"text": [
"cardiac myosin heavy chain"
],
"offsets": [
[
40,
66
]
],
"normalized": []
},
{
"id": "BioInfer.d355.s0.e1",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
71,
76
]
],
"normalized": []
},
{
"id": "BioInfer.d355.s0.e2",
"type": "Individual_protein",
"text": [
"Insulin-like growth factor I"
],
"offsets": [
[
0,
28
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d355.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d355.s0.e0",
"arg2_id": "BioInfer.d355.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d355.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d355.s0.e1",
"arg2_id": "BioInfer.d355.s0.e2",
"normalized": []
}
] |
453 | BioInfer.d355.s1 | [
{
"id": "BioInfer.d355.s1__text",
"type": "Sentence",
"text": [
"To determine the effect of insulin-like growth factor I (IGF-I) on cardiac contractile protein synthesis in vivo, we measured L-[ring-2, 6-3H]phenylalanine incorporation into myosin heavy chain and actin during intravenous infusions (4 h) of either saline or IGF-I (1 microgram. kg-1. min-1) in awake rats."
],
"offsets": [
[
0,
306
]
]
}
] | [
{
"id": "BioInfer.d355.s1.e0",
"type": "Gene/protein/RNA",
"text": [
"actin"
],
"offsets": [
[
198,
203
]
],
"normalized": []
},
{
"id": "BioInfer.d355.s1.e1",
"type": "Gene/protein/RNA",
"text": [
"myosin heavy chain"
],
"offsets": [
[
175,
193
]
],
"normalized": []
},
{
"id": "BioInfer.d355.s1.e2",
"type": "Individual_protein",
"text": [
"insulin-like growth factor I"
],
"offsets": [
[
27,
55
]
],
"normalized": []
},
{
"id": "BioInfer.d355.s1.e3",
"type": "Gene/protein/RNA",
"text": [
"IGF-I"
],
"offsets": [
[
259,
264
]
],
"normalized": []
},
{
"id": "BioInfer.d355.s1.e4",
"type": "Individual_protein",
"text": [
"IGF-I"
],
"offsets": [
[
57,
62
]
],
"normalized": []
}
] | [] | [] | [] |
454 | BioInfer.d356.s0 | [
{
"id": "BioInfer.d356.s0__text",
"type": "Sentence",
"text": [
"Integrating the actin and vimentin cytoskeletons."
],
"offsets": [
[
0,
49
]
]
}
] | [
{
"id": "BioInfer.d356.s0.e0",
"type": "Individual_protein",
"text": [
"vimentin"
],
"offsets": [
[
26,
34
]
],
"normalized": []
},
{
"id": "BioInfer.d356.s0.e1",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
16,
21
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d356.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d356.s0.e0",
"arg2_id": "BioInfer.d356.s0.e1",
"normalized": []
}
] |
455 | BioInfer.d357.s0 | [
{
"id": "BioInfer.d357.s0__text",
"type": "Sentence",
"text": [
"Integrin (beta) chains, for example, interact with actin-binding proteins (e.g. talin and filamin), which form mechanical links to the cytoskeleton."
],
"offsets": [
[
0,
148
]
]
}
] | [
{
"id": "BioInfer.d357.s0.e0",
"type": "Individual_protein",
"text": [
"Integrin",
"beta",
"chains"
],
"offsets": [
[
0,
8
],
[
10,
14
],
[
16,
22
]
],
"normalized": []
},
{
"id": "BioInfer.d357.s0.e1",
"type": "Protein_family_or_group",
"text": [
"actin-binding proteins"
],
"offsets": [
[
51,
73
]
],
"normalized": []
},
{
"id": "BioInfer.d357.s0.e2",
"type": "Individual_protein",
"text": [
"talin"
],
"offsets": [
[
80,
85
]
],
"normalized": []
},
{
"id": "BioInfer.d357.s0.e3",
"type": "Individual_protein",
"text": [
"filamin"
],
"offsets": [
[
90,
97
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d357.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d357.s0.e0",
"arg2_id": "BioInfer.d357.s0.e1",
"normalized": []
},
{
"id": "BioInfer.d357.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d357.s0.e1",
"arg2_id": "BioInfer.d357.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d357.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d357.s0.e1",
"arg2_id": "BioInfer.d357.s0.e3",
"normalized": []
}
] |
456 | BioInfer.d358.s0 | [
{
"id": "BioInfer.d358.s0__text",
"type": "Sentence",
"text": [
"Integrin binding may be promoted by disruption of links to the cytoskeleton, effected through depolymerisation of actin or cleavage of linking protein talin by calpain."
],
"offsets": [
[
0,
168
]
]
}
] | [
{
"id": "BioInfer.d358.s0.e0",
"type": "Individual_protein",
"text": [
"talin"
],
"offsets": [
[
151,
156
]
],
"normalized": []
},
{
"id": "BioInfer.d358.s0.e1",
"type": "Individual_protein",
"text": [
"calpain"
],
"offsets": [
[
160,
167
]
],
"normalized": []
},
{
"id": "BioInfer.d358.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"actin"
],
"offsets": [
[
114,
119
]
],
"normalized": []
},
{
"id": "BioInfer.d358.s0.e3",
"type": "Gene/protein/RNA",
"text": [
"Integrin"
],
"offsets": [
[
0,
8
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d358.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d358.s0.e0",
"arg2_id": "BioInfer.d358.s0.e1",
"normalized": []
}
] |
457 | BioInfer.d359.s0 | [
{
"id": "BioInfer.d359.s0__text",
"type": "Sentence",
"text": [
"Interaction between nucleocapsid protein (NP) and phosphoprotein (P) of human parainfluenza virus type 2: one of the two NP binding sites on P is essential for granule formation."
],
"offsets": [
[
0,
178
]
]
}
] | [
{
"id": "BioInfer.d359.s0.e0",
"type": "Individual_protein",
"text": [
"NP"
],
"offsets": [
[
42,
44
]
],
"normalized": []
},
{
"id": "BioInfer.d359.s0.e1",
"type": "Individual_protein",
"text": [
"NP"
],
"offsets": [
[
121,
123
]
],
"normalized": []
},
{
"id": "BioInfer.d359.s0.e2",
"type": "Individual_protein",
"text": [
"P"
],
"offsets": [
[
66,
67
]
],
"normalized": []
},
{
"id": "BioInfer.d359.s0.e3",
"type": "Individual_protein",
"text": [
"phosphoprotein"
],
"offsets": [
[
50,
64
]
],
"normalized": []
},
{
"id": "BioInfer.d359.s0.e4",
"type": "Individual_protein",
"text": [
"nucleocapsid protein"
],
"offsets": [
[
20,
40
]
],
"normalized": []
},
{
"id": "BioInfer.d359.s0.e5",
"type": "Individual_protein",
"text": [
"P"
],
"offsets": [
[
141,
142
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d359.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d359.s0.e0",
"arg2_id": "BioInfer.d359.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d359.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d359.s0.e0",
"arg2_id": "BioInfer.d359.s0.e3",
"normalized": []
},
{
"id": "BioInfer.d359.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d359.s0.e1",
"arg2_id": "BioInfer.d359.s0.e5",
"normalized": []
},
{
"id": "BioInfer.d359.s0.i3",
"type": "PPI",
"arg1_id": "BioInfer.d359.s0.e2",
"arg2_id": "BioInfer.d359.s0.e4",
"normalized": []
},
{
"id": "BioInfer.d359.s0.i4",
"type": "PPI",
"arg1_id": "BioInfer.d359.s0.e3",
"arg2_id": "BioInfer.d359.s0.e4",
"normalized": []
}
] |
458 | BioInfer.d360.s0 | [
{
"id": "BioInfer.d360.s0__text",
"type": "Sentence",
"text": [
"Interaction of Munc-18-2 with syntaxin 3 controls the association of apical SNAREs in epithelial cells."
],
"offsets": [
[
0,
103
]
]
}
] | [
{
"id": "BioInfer.d360.s0.e0",
"type": "Individual_protein",
"text": [
"Munc-18-2"
],
"offsets": [
[
15,
24
]
],
"normalized": []
},
{
"id": "BioInfer.d360.s0.e1",
"type": "Individual_protein",
"text": [
"syntaxin 3"
],
"offsets": [
[
30,
40
]
],
"normalized": []
},
{
"id": "BioInfer.d360.s0.e2",
"type": "Protein_family_or_group",
"text": [
"SNAREs"
],
"offsets": [
[
76,
82
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d360.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d360.s0.e0",
"arg2_id": "BioInfer.d360.s0.e1",
"normalized": []
},
{
"id": "BioInfer.d360.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d360.s0.e0",
"arg2_id": "BioInfer.d360.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d360.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d360.s0.e1",
"arg2_id": "BioInfer.d360.s0.e2",
"normalized": []
}
] |
459 | BioInfer.d360.s1 | [
{
"id": "BioInfer.d360.s1__text",
"type": "Sentence",
"text": [
"The quantity of the complex is reduced by treatment of Caco-2 cells with the alkylating agent N-ethylmaleimide which also has an inhibitory effect on the ability of Munc-18-2 to associate with syntaxin 3 in vitro."
],
"offsets": [
[
0,
213
]
]
}
] | [
{
"id": "BioInfer.d360.s1.e0",
"type": "Individual_protein",
"text": [
"Munc-18-2"
],
"offsets": [
[
165,
174
]
],
"normalized": []
},
{
"id": "BioInfer.d360.s1.e1",
"type": "Individual_protein",
"text": [
"syntaxin 3"
],
"offsets": [
[
193,
203
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d360.s1.i0",
"type": "PPI",
"arg1_id": "BioInfer.d360.s1.e0",
"arg2_id": "BioInfer.d360.s1.e1",
"normalized": []
}
] |
460 | BioInfer.d361.s0 | [
{
"id": "BioInfer.d361.s0__text",
"type": "Sentence",
"text": [
"Interactions of ADF/cofilin, Arp2/3 complex, capping protein and profilin in remodeling of branched actin filament networks."
],
"offsets": [
[
0,
124
]
]
}
] | [
{
"id": "BioInfer.d361.s0.e0",
"type": "Individual_protein",
"text": [
"Arp",
"3"
],
"offsets": [
[
29,
32
],
[
34,
35
]
],
"normalized": []
},
{
"id": "BioInfer.d361.s0.e1",
"type": "Individual_protein",
"text": [
"cofilin"
],
"offsets": [
[
20,
27
]
],
"normalized": []
},
{
"id": "BioInfer.d361.s0.e2",
"type": "Individual_protein",
"text": [
"ADF"
],
"offsets": [
[
16,
19
]
],
"normalized": []
},
{
"id": "BioInfer.d361.s0.e3",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
100,
105
]
],
"normalized": []
},
{
"id": "BioInfer.d361.s0.e4",
"type": "Individual_protein",
"text": [
"capping protein"
],
"offsets": [
[
45,
60
]
],
"normalized": []
},
{
"id": "BioInfer.d361.s0.e5",
"type": "Individual_protein",
"text": [
"Arp2"
],
"offsets": [
[
29,
33
]
],
"normalized": []
},
{
"id": "BioInfer.d361.s0.e6",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
65,
73
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d361.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d361.s0.e0",
"arg2_id": "BioInfer.d361.s0.e1",
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},
{
"id": "BioInfer.d361.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d361.s0.e0",
"arg2_id": "BioInfer.d361.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d361.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d361.s0.e0",
"arg2_id": "BioInfer.d361.s0.e3",
"normalized": []
},
{
"id": "BioInfer.d361.s0.i3",
"type": "PPI",
"arg1_id": "BioInfer.d361.s0.e0",
"arg2_id": "BioInfer.d361.s0.e4",
"normalized": []
},
{
"id": "BioInfer.d361.s0.i4",
"type": "PPI",
"arg1_id": "BioInfer.d361.s0.e0",
"arg2_id": "BioInfer.d361.s0.e5",
"normalized": []
},
{
"id": "BioInfer.d361.s0.i5",
"type": "PPI",
"arg1_id": "BioInfer.d361.s0.e0",
"arg2_id": "BioInfer.d361.s0.e6",
"normalized": []
},
{
"id": "BioInfer.d361.s0.i6",
"type": "PPI",
"arg1_id": "BioInfer.d361.s0.e1",
"arg2_id": "BioInfer.d361.s0.e3",
"normalized": []
},
{
"id": "BioInfer.d361.s0.i7",
"type": "PPI",
"arg1_id": "BioInfer.d361.s0.e1",
"arg2_id": "BioInfer.d361.s0.e4",
"normalized": []
},
{
"id": "BioInfer.d361.s0.i8",
"type": "PPI",
"arg1_id": "BioInfer.d361.s0.e1",
"arg2_id": "BioInfer.d361.s0.e5",
"normalized": []
},
{
"id": "BioInfer.d361.s0.i9",
"type": "PPI",
"arg1_id": "BioInfer.d361.s0.e1",
"arg2_id": "BioInfer.d361.s0.e6",
"normalized": []
},
{
"id": "BioInfer.d361.s0.i10",
"type": "PPI",
"arg1_id": "BioInfer.d361.s0.e2",
"arg2_id": "BioInfer.d361.s0.e3",
"normalized": []
},
{
"id": "BioInfer.d361.s0.i11",
"type": "PPI",
"arg1_id": "BioInfer.d361.s0.e2",
"arg2_id": "BioInfer.d361.s0.e4",
"normalized": []
},
{
"id": "BioInfer.d361.s0.i12",
"type": "PPI",
"arg1_id": "BioInfer.d361.s0.e2",
"arg2_id": "BioInfer.d361.s0.e5",
"normalized": []
},
{
"id": "BioInfer.d361.s0.i13",
"type": "PPI",
"arg1_id": "BioInfer.d361.s0.e2",
"arg2_id": "BioInfer.d361.s0.e6",
"normalized": []
},
{
"id": "BioInfer.d361.s0.i14",
"type": "PPI",
"arg1_id": "BioInfer.d361.s0.e3",
"arg2_id": "BioInfer.d361.s0.e4",
"normalized": []
},
{
"id": "BioInfer.d361.s0.i15",
"type": "PPI",
"arg1_id": "BioInfer.d361.s0.e3",
"arg2_id": "BioInfer.d361.s0.e5",
"normalized": []
},
{
"id": "BioInfer.d361.s0.i16",
"type": "PPI",
"arg1_id": "BioInfer.d361.s0.e3",
"arg2_id": "BioInfer.d361.s0.e6",
"normalized": []
},
{
"id": "BioInfer.d361.s0.i17",
"type": "PPI",
"arg1_id": "BioInfer.d361.s0.e4",
"arg2_id": "BioInfer.d361.s0.e5",
"normalized": []
},
{
"id": "BioInfer.d361.s0.i18",
"type": "PPI",
"arg1_id": "BioInfer.d361.s0.e4",
"arg2_id": "BioInfer.d361.s0.e6",
"normalized": []
},
{
"id": "BioInfer.d361.s0.i19",
"type": "PPI",
"arg1_id": "BioInfer.d361.s0.e5",
"arg2_id": "BioInfer.d361.s0.e6",
"normalized": []
}
] |
461 | BioInfer.d364.s0 | [
{
"id": "BioInfer.d364.s0__text",
"type": "Sentence",
"text": [
"In the ADE2 assay system, silencing depends completely upon the function of the SIR genes, known trans-acting regulators of the silent loci, and is sensitive to the gene dosage of two SIR genes, SIR1 and SIR4."
],
"offsets": [
[
0,
209
]
]
}
] | [
{
"id": "BioInfer.d364.s0.e0",
"type": "Gene",
"text": [
"SIR4"
],
"offsets": [
[
204,
208
]
],
"normalized": []
},
{
"id": "BioInfer.d364.s0.e1",
"type": "Gene",
"text": [
"SIR1"
],
"offsets": [
[
195,
199
]
],
"normalized": []
},
{
"id": "BioInfer.d364.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"SIR"
],
"offsets": [
[
80,
83
]
],
"normalized": []
},
{
"id": "BioInfer.d364.s0.e3",
"type": "Gene/protein/RNA",
"text": [
"ADE2"
],
"offsets": [
[
7,
11
]
],
"normalized": []
},
{
"id": "BioInfer.d364.s0.e4",
"type": "Gene",
"text": [
"SIR"
],
"offsets": [
[
184,
187
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d364.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d364.s0.e0",
"arg2_id": "BioInfer.d364.s0.e4",
"normalized": []
},
{
"id": "BioInfer.d364.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d364.s0.e1",
"arg2_id": "BioInfer.d364.s0.e4",
"normalized": []
}
] |
462 | BioInfer.d365.s0 | [
{
"id": "BioInfer.d365.s0__text",
"type": "Sentence",
"text": [
"In the basal layer, patches of brightly labeled cells were detected with antibodies to E-cadherin, beta-catenin, and gamma-catenin, but not with antibodies to P-cadherin, alpha-catenin, or with pan-desmocollin and pan-desmoglein antibodies."
],
"offsets": [
[
0,
240
]
]
}
] | [
{
"id": "BioInfer.d365.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"pan-desmoglein"
],
"offsets": [
[
214,
228
]
],
"normalized": []
},
{
"id": "BioInfer.d365.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"P-cadherin"
],
"offsets": [
[
159,
169
]
],
"normalized": []
},
{
"id": "BioInfer.d365.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"pan-desmocollin"
],
"offsets": [
[
194,
209
]
],
"normalized": []
},
{
"id": "BioInfer.d365.s0.e3",
"type": "Gene/protein/RNA",
"text": [
"gamma-catenin"
],
"offsets": [
[
117,
130
]
],
"normalized": []
},
{
"id": "BioInfer.d365.s0.e4",
"type": "Gene/protein/RNA",
"text": [
"E-cadherin"
],
"offsets": [
[
87,
97
]
],
"normalized": []
},
{
"id": "BioInfer.d365.s0.e5",
"type": "Gene/protein/RNA",
"text": [
"alpha-catenin"
],
"offsets": [
[
171,
184
]
],
"normalized": []
},
{
"id": "BioInfer.d365.s0.e6",
"type": "Gene/protein/RNA",
"text": [
"beta-catenin"
],
"offsets": [
[
99,
111
]
],
"normalized": []
}
] | [] | [] | [] |
463 | BioInfer.d366.s0 | [
{
"id": "BioInfer.d366.s0__text",
"type": "Sentence",
"text": [
"In the budding yeast Saccharomyces cerevisiae, the DNA damage-induced G2 arrest requires the checkpoint control genes RAD9, RAD17, RAD24, MEC1, MEC2 and MEC3."
],
"offsets": [
[
0,
158
]
]
}
] | [
{
"id": "BioInfer.d366.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"MEC2"
],
"offsets": [
[
144,
148
]
],
"normalized": []
},
{
"id": "BioInfer.d366.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"RAD17"
],
"offsets": [
[
124,
129
]
],
"normalized": []
},
{
"id": "BioInfer.d366.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"RAD24"
],
"offsets": [
[
131,
136
]
],
"normalized": []
},
{
"id": "BioInfer.d366.s0.e3",
"type": "Gene/protein/RNA",
"text": [
"RAD9"
],
"offsets": [
[
118,
122
]
],
"normalized": []
},
{
"id": "BioInfer.d366.s0.e4",
"type": "Gene/protein/RNA",
"text": [
"MEC3"
],
"offsets": [
[
153,
157
]
],
"normalized": []
},
{
"id": "BioInfer.d366.s0.e5",
"type": "Gene/protein/RNA",
"text": [
"MEC1"
],
"offsets": [
[
138,
142
]
],
"normalized": []
}
] | [] | [] | [] |
464 | BioInfer.d367.s0 | [
{
"id": "BioInfer.d367.s0__text",
"type": "Sentence",
"text": [
"In the cytoplasm, HBx was shown to stimulate the Ras-Raf-mitogen-activated protein kinase (MAP kinase) cascade, which is essential for activation of transcription factor AP-1."
],
"offsets": [
[
0,
175
]
]
}
] | [
{
"id": "BioInfer.d367.s0.e0",
"type": "Individual_protein",
"text": [
"Ras"
],
"offsets": [
[
49,
52
]
],
"normalized": []
},
{
"id": "BioInfer.d367.s0.e1",
"type": "Individual_protein",
"text": [
"MAP kinase"
],
"offsets": [
[
91,
101
]
],
"normalized": []
},
{
"id": "BioInfer.d367.s0.e2",
"type": "Individual_protein",
"text": [
"HBx"
],
"offsets": [
[
18,
21
]
],
"normalized": []
},
{
"id": "BioInfer.d367.s0.e3",
"type": "Individual_protein",
"text": [
"AP-1"
],
"offsets": [
[
170,
174
]
],
"normalized": []
},
{
"id": "BioInfer.d367.s0.e4",
"type": "Individual_protein",
"text": [
"mitogen-activated protein kinase"
],
"offsets": [
[
57,
89
]
],
"normalized": []
},
{
"id": "BioInfer.d367.s0.e5",
"type": "Individual_protein",
"text": [
"Raf"
],
"offsets": [
[
53,
56
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d367.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d367.s0.e0",
"arg2_id": "BioInfer.d367.s0.e1",
"normalized": []
},
{
"id": "BioInfer.d367.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d367.s0.e0",
"arg2_id": "BioInfer.d367.s0.e3",
"normalized": []
},
{
"id": "BioInfer.d367.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d367.s0.e0",
"arg2_id": "BioInfer.d367.s0.e4",
"normalized": []
},
{
"id": "BioInfer.d367.s0.i3",
"type": "PPI",
"arg1_id": "BioInfer.d367.s0.e0",
"arg2_id": "BioInfer.d367.s0.e5",
"normalized": []
},
{
"id": "BioInfer.d367.s0.i4",
"type": "PPI",
"arg1_id": "BioInfer.d367.s0.e1",
"arg2_id": "BioInfer.d367.s0.e3",
"normalized": []
},
{
"id": "BioInfer.d367.s0.i5",
"type": "PPI",
"arg1_id": "BioInfer.d367.s0.e1",
"arg2_id": "BioInfer.d367.s0.e4",
"normalized": []
},
{
"id": "BioInfer.d367.s0.i6",
"type": "PPI",
"arg1_id": "BioInfer.d367.s0.e1",
"arg2_id": "BioInfer.d367.s0.e5",
"normalized": []
},
{
"id": "BioInfer.d367.s0.i7",
"type": "PPI",
"arg1_id": "BioInfer.d367.s0.e3",
"arg2_id": "BioInfer.d367.s0.e4",
"normalized": []
},
{
"id": "BioInfer.d367.s0.i8",
"type": "PPI",
"arg1_id": "BioInfer.d367.s0.e3",
"arg2_id": "BioInfer.d367.s0.e5",
"normalized": []
},
{
"id": "BioInfer.d367.s0.i9",
"type": "PPI",
"arg1_id": "BioInfer.d367.s0.e4",
"arg2_id": "BioInfer.d367.s0.e5",
"normalized": []
}
] |
465 | BioInfer.d370.s0 | [
{
"id": "BioInfer.d370.s0__text",
"type": "Sentence",
"text": [
"In the present paper, using indirect immunofluorescence, we found that PMN adhesion to tumor necrosis factor-activated endothelial cells (EC) induced the disappearance from endothelial cell-to-cell contacts of adherens junction (AJ) components: vascular endothelial (VE)-cadherin, alpha-catenin, beta-catenin, and plakoglobin."
],
"offsets": [
[
0,
326
]
]
}
] | [
{
"id": "BioInfer.d370.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"plakoglobin"
],
"offsets": [
[
314,
325
]
],
"normalized": []
},
{
"id": "BioInfer.d370.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"beta-catenin"
],
"offsets": [
[
296,
308
]
],
"normalized": []
},
{
"id": "BioInfer.d370.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"alpha-catenin"
],
"offsets": [
[
281,
294
]
],
"normalized": []
},
{
"id": "BioInfer.d370.s0.e3",
"type": "Gene/protein/RNA",
"text": [
"vascular endothelial",
"cadherin"
],
"offsets": [
[
245,
265
],
[
271,
279
]
],
"normalized": []
},
{
"id": "BioInfer.d370.s0.e4",
"type": "Gene/protein/RNA",
"text": [
"tumor necrosis factor"
],
"offsets": [
[
87,
108
]
],
"normalized": []
}
] | [] | [] | [] |
466 | BioInfer.d372.s0 | [
{
"id": "BioInfer.d372.s0__text",
"type": "Sentence",
"text": [
"In these investigations, we determine that recruitment of a coactivator protein, CBP (the CREBbinding protein), to the CYBB or NCF2 promoter is the molecular mechanism of transcriptional activation by PU.1, IRF1, and ICSBP."
],
"offsets": [
[
0,
223
]
]
}
] | [
{
"id": "BioInfer.d372.s0.e0",
"type": "Gene",
"text": [
"NCF2"
],
"offsets": [
[
127,
131
]
],
"normalized": []
},
{
"id": "BioInfer.d372.s0.e1",
"type": "Individual_protein",
"text": [
"ICSBP"
],
"offsets": [
[
217,
222
]
],
"normalized": []
},
{
"id": "BioInfer.d372.s0.e2",
"type": "Individual_protein",
"text": [
"CREBbinding protein"
],
"offsets": [
[
90,
109
]
],
"normalized": []
},
{
"id": "BioInfer.d372.s0.e3",
"type": "Individual_protein",
"text": [
"PU.1"
],
"offsets": [
[
201,
205
]
],
"normalized": []
},
{
"id": "BioInfer.d372.s0.e4",
"type": "Individual_protein",
"text": [
"IRF1"
],
"offsets": [
[
207,
211
]
],
"normalized": []
},
{
"id": "BioInfer.d372.s0.e5",
"type": "Individual_protein",
"text": [
"CBP"
],
"offsets": [
[
81,
84
]
],
"normalized": []
},
{
"id": "BioInfer.d372.s0.e6",
"type": "Gene",
"text": [
"CYBB"
],
"offsets": [
[
119,
123
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d372.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d372.s0.e0",
"arg2_id": "BioInfer.d372.s0.e1",
"normalized": []
},
{
"id": "BioInfer.d372.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d372.s0.e0",
"arg2_id": "BioInfer.d372.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d372.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d372.s0.e0",
"arg2_id": "BioInfer.d372.s0.e3",
"normalized": []
},
{
"id": "BioInfer.d372.s0.i3",
"type": "PPI",
"arg1_id": "BioInfer.d372.s0.e0",
"arg2_id": "BioInfer.d372.s0.e4",
"normalized": []
},
{
"id": "BioInfer.d372.s0.i4",
"type": "PPI",
"arg1_id": "BioInfer.d372.s0.e0",
"arg2_id": "BioInfer.d372.s0.e5",
"normalized": []
},
{
"id": "BioInfer.d372.s0.i5",
"type": "PPI",
"arg1_id": "BioInfer.d372.s0.e1",
"arg2_id": "BioInfer.d372.s0.e6",
"normalized": []
},
{
"id": "BioInfer.d372.s0.i6",
"type": "PPI",
"arg1_id": "BioInfer.d372.s0.e2",
"arg2_id": "BioInfer.d372.s0.e6",
"normalized": []
},
{
"id": "BioInfer.d372.s0.i7",
"type": "PPI",
"arg1_id": "BioInfer.d372.s0.e3",
"arg2_id": "BioInfer.d372.s0.e6",
"normalized": []
},
{
"id": "BioInfer.d372.s0.i8",
"type": "PPI",
"arg1_id": "BioInfer.d372.s0.e4",
"arg2_id": "BioInfer.d372.s0.e6",
"normalized": []
},
{
"id": "BioInfer.d372.s0.i9",
"type": "PPI",
"arg1_id": "BioInfer.d372.s0.e5",
"arg2_id": "BioInfer.d372.s0.e6",
"normalized": []
}
] |
Subsets and Splits