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0 | BioInfer.d0.s0 | [
{
"id": "BioInfer.d0.s0__text",
"type": "Sentence",
"text": [
"alpha-catenin inhibits beta-catenin signaling by preventing formation of a beta-catenin*T-cell factor*DNA complex."
],
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0,
114
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]
}
] | [
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],
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88,
101
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],
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{
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"alpha-catenin"
],
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0,
13
]
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{
"id": "BioInfer.d0.s0.e2",
"type": "Individual_protein",
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"beta-catenin"
],
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23,
35
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{
"id": "BioInfer.d0.s0.e3",
"type": "Individual_protein",
"text": [
"beta-catenin"
],
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[
75,
87
]
],
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] | [] | [] | [
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] |
1 | BioInfer.d1.s0 | [
{
"id": "BioInfer.d1.s0__text",
"type": "Sentence",
"text": [
"A binary complex of birch profilin and skeletal muscle actin could be isolated by gel chromatography."
],
"offsets": [
[
0,
101
]
]
}
] | [
{
"id": "BioInfer.d1.s0.e0",
"type": "Individual_protein",
"text": [
"profilin"
],
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26,
34
]
],
"normalized": []
},
{
"id": "BioInfer.d1.s0.e1",
"type": "Individual_protein",
"text": [
"skeletal muscle actin"
],
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[
39,
60
]
],
"normalized": []
}
] | [] | [] | [
{
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] |
2 | BioInfer.d1.s1 | [
{
"id": "BioInfer.d1.s1__text",
"type": "Sentence",
"text": [
"Birch profilin increased the critical concentration required for muscle and brain actin polymerization in a concentration-dependent manner, supporting the notion of the formation of a heterologous complex between the plant protein and animal actin."
],
"offsets": [
[
0,
248
]
]
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] | [
{
"id": "BioInfer.d1.s1.e0",
"type": "Individual_protein",
"text": [
"brain actin"
],
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76,
87
]
],
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{
"id": "BioInfer.d1.s1.e1",
"type": "Individual_protein",
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6,
14
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},
{
"id": "BioInfer.d1.s1.e2",
"type": "Individual_protein",
"text": [
"muscle",
"actin"
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65,
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82,
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{
"id": "BioInfer.d1.s1.e3",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
242,
247
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d1.s1.i0",
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{
"id": "BioInfer.d1.s1.i1",
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"arg2_id": "BioInfer.d1.s1.e2",
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{
"id": "BioInfer.d1.s1.i2",
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"arg1_id": "BioInfer.d1.s1.e1",
"arg2_id": "BioInfer.d1.s1.e3",
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}
] |
3 | BioInfer.d1.s2 | [
{
"id": "BioInfer.d1.s2__text",
"type": "Sentence",
"text": [
"Interaction of plant profilin with mammalian actin."
],
"offsets": [
[
0,
51
]
]
}
] | [
{
"id": "BioInfer.d1.s2.e0",
"type": "Individual_protein",
"text": [
"profilin"
],
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[
21,
29
]
],
"normalized": []
},
{
"id": "BioInfer.d1.s2.e1",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
45,
50
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d1.s2.i0",
"type": "PPI",
"arg1_id": "BioInfer.d1.s2.e0",
"arg2_id": "BioInfer.d1.s2.e1",
"normalized": []
}
] |
4 | BioInfer.d1.s3 | [
{
"id": "BioInfer.d1.s3__text",
"type": "Sentence",
"text": [
"In viscometric assays, the birch protein was seen to modulate actin filament formation analogous to animal profilin."
],
"offsets": [
[
0,
116
]
]
}
] | [
{
"id": "BioInfer.d1.s3.e0",
"type": "Individual_protein",
"text": [
"actin"
],
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62,
67
]
],
"normalized": []
},
{
"id": "BioInfer.d1.s3.e1",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
107,
115
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d1.s3.i0",
"type": "PPI",
"arg1_id": "BioInfer.d1.s3.e0",
"arg2_id": "BioInfer.d1.s3.e1",
"normalized": []
}
] |
5 | BioInfer.d1.s4 | [
{
"id": "BioInfer.d1.s4__text",
"type": "Sentence",
"text": [
"These data indicate that the actin-binding domains in plant and animal profilins are functionally highly conserved, although the overall sequence similarity is less than 25%."
],
"offsets": [
[
0,
174
]
]
}
] | [
{
"id": "BioInfer.d1.s4.e0",
"type": "Protein_family_or_group",
"text": [
"profilins"
],
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[
71,
80
]
],
"normalized": []
},
{
"id": "BioInfer.d1.s4.e1",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
29,
34
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d1.s4.i0",
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"arg2_id": "BioInfer.d1.s4.e1",
"normalized": []
}
] |
6 | BioInfer.d2.s0 | [
{
"id": "BioInfer.d2.s0__text",
"type": "Sentence",
"text": [
"Abnormal immunoreactivity in the tumor tissue was observed in 18 patients (34.0%) for E-cadherin, in 35 (66.0%) for alpha-catenin, in 20 (37.7%) for beta-catenin, and in 37 (69.8%) for gamma-catenin."
],
"offsets": [
[
0,
199
]
]
}
] | [
{
"id": "BioInfer.d2.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"alpha-catenin"
],
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116,
129
]
],
"normalized": []
},
{
"id": "BioInfer.d2.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"gamma-catenin"
],
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[
185,
198
]
],
"normalized": []
},
{
"id": "BioInfer.d2.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"E-cadherin"
],
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86,
96
]
],
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},
{
"id": "BioInfer.d2.s0.e3",
"type": "Gene/protein/RNA",
"text": [
"beta-catenin"
],
"offsets": [
[
149,
161
]
],
"normalized": []
}
] | [] | [] | [] |
7 | BioInfer.d3.s0 | [
{
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"type": "Sentence",
"text": [
"Absence of alpha-syntrophin leads to structurally aberrant neuromuscular synapses deficient in utrophin."
],
"offsets": [
[
0,
104
]
]
}
] | [
{
"id": "BioInfer.d3.s0.e0",
"type": "Individual_protein",
"text": [
"utrophin"
],
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[
95,
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],
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},
{
"id": "BioInfer.d3.s0.e1",
"type": "Individual_protein",
"text": [
"alpha-syntrophin"
],
"offsets": [
[
11,
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]
],
"normalized": []
}
] | [] | [] | [
{
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"normalized": []
}
] |
8 | BioInfer.d3.s1 | [
{
"id": "BioInfer.d3.s1__text",
"type": "Sentence",
"text": [
"Thus, alpha-syntrophin has an important role in synapse formation and in the organization of utrophin, acetylcholine receptor, and acetylcholinesterase at the neuromuscular synapse."
],
"offsets": [
[
0,
181
]
]
}
] | [
{
"id": "BioInfer.d3.s1.e0",
"type": "Individual_protein",
"text": [
"acetylcholine receptor"
],
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103,
125
]
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"normalized": []
},
{
"id": "BioInfer.d3.s1.e1",
"type": "Individual_protein",
"text": [
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],
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131,
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{
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6,
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]
],
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] | [] | [] | [
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}
] |
9 | BioInfer.d4.s0 | [
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"type": "Sentence",
"text": [
"Abundance of actin, talin, alpha 5 and beta 1 integrins, pp125 focal adhesion kinase, and alpha-catenin is not affected by the differential calreticulin expression."
],
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[
0,
164
]
]
}
] | [
{
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},
{
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140,
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{
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"text": [
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13,
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},
{
"id": "BioInfer.d4.s0.e3",
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46,
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{
"id": "BioInfer.d4.s0.e4",
"type": "Individual_protein",
"text": [
"pp125"
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57,
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],
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},
{
"id": "BioInfer.d4.s0.e5",
"type": "Individual_protein",
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39,
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{
"id": "BioInfer.d4.s0.e6",
"type": "Individual_protein",
"text": [
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20,
25
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},
{
"id": "BioInfer.d4.s0.e7",
"type": "Individual_protein",
"text": [
"focal adhesion kinase"
],
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63,
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] | [] | [] | [
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"id": "BioInfer.d4.s0.i3",
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}
] |
10 | BioInfer.d5.s0 | [
{
"id": "BioInfer.d5.s0__text",
"type": "Sentence",
"text": [
"Acanthamoeba actin and profilin can be cross-linked between glutamic acid 364 of actin and lysine 115 of profilin."
],
"offsets": [
[
0,
114
]
]
}
] | [
{
"id": "BioInfer.d5.s0.e0",
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"text": [
"actin"
],
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13,
18
]
],
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},
{
"id": "BioInfer.d5.s0.e1",
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]
],
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},
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"actin"
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],
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},
{
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"text": [
"profilin"
],
"offsets": [
[
105,
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]
],
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}
] | [] | [] | [
{
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"normalized": []
}
] |
11 | BioInfer.d5.s1 | [
{
"id": "BioInfer.d5.s1__text",
"type": "Sentence",
"text": [
"Acanthamoeba profilin was cross-linked to actin via a zero-length isopeptide bond using carbodiimide."
],
"offsets": [
[
0,
101
]
]
}
] | [
{
"id": "BioInfer.d5.s1.e0",
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13,
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]
],
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{
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"text": [
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],
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]
],
"normalized": []
}
] | [] | [] | [
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}
] |
12 | BioInfer.d5.s2 | [
{
"id": "BioInfer.d5.s2__text",
"type": "Sentence",
"text": [
"Since the NH2 terminus of profilin is blocked, Edman degradation gave only the sequence of the conjugated actin CNBr fragment beginning with Trp-356."
],
"offsets": [
[
0,
149
]
]
}
] | [
{
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26,
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},
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"text": [
"actin"
],
"offsets": [
[
106,
111
]
],
"normalized": []
}
] | [] | [] | [] |
13 | BioInfer.d6.s0 | [
{
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"type": "Sentence",
"text": [
"Acanthamoeba profilin affects the mechanical properties of nonfilamentous actin."
],
"offsets": [
[
0,
80
]
]
}
] | [
{
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"actin"
],
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[
74,
79
]
],
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},
{
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"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
13,
21
]
],
"normalized": []
}
] | [] | [] | [
{
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"arg2_id": "BioInfer.d6.s0.e1",
"normalized": []
}
] |
14 | BioInfer.d6.s1 | [
{
"id": "BioInfer.d6.s1__text",
"type": "Sentence",
"text": [
"In contrast, profilin had little effect on the rigidity and viscosity of actin filaments."
],
"offsets": [
[
0,
89
]
]
}
] | [
{
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],
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13,
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]
],
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},
{
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],
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]
],
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}
] | [] | [] | [
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"id": "BioInfer.d6.s1.i0",
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"arg1_id": "BioInfer.d6.s1.e0",
"arg2_id": "BioInfer.d6.s1.e1",
"normalized": []
}
] |
15 | BioInfer.d6.s2 | [
{
"id": "BioInfer.d6.s2__text",
"type": "Sentence",
"text": [
"We speculate that nonfilamentous actin and profilin, both of which form shear-sensitive structures, can be modeled as flocculant materials."
],
"offsets": [
[
0,
139
]
]
}
] | [
{
"id": "BioInfer.d6.s2.e0",
"type": "Gene/protein/RNA",
"text": [
"profilin"
],
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[
43,
51
]
],
"normalized": []
},
{
"id": "BioInfer.d6.s2.e1",
"type": "Gene/protein/RNA",
"text": [
"actin"
],
"offsets": [
[
33,
38
]
],
"normalized": []
}
] | [] | [] | [] |
16 | BioInfer.d7.s0 | [
{
"id": "BioInfer.d7.s0__text",
"type": "Sentence",
"text": [
"Acanthamoeba profilin has similar but weaker effects on muscle actin, requiring 5 to 10 times more profilin than with amoeba actin."
],
"offsets": [
[
0,
131
]
]
}
] | [
{
"id": "BioInfer.d7.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"profilin"
],
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[
99,
107
]
],
"normalized": []
},
{
"id": "BioInfer.d7.s0.e1",
"type": "Individual_protein",
"text": [
"muscle actin"
],
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56,
68
]
],
"normalized": []
},
{
"id": "BioInfer.d7.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"actin"
],
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[
125,
130
]
],
"normalized": []
},
{
"id": "BioInfer.d7.s0.e3",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
13,
21
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d7.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d7.s0.e1",
"arg2_id": "BioInfer.d7.s0.e3",
"normalized": []
}
] |
17 | BioInfer.d7.s1 | [
{
"id": "BioInfer.d7.s1__text",
"type": "Sentence",
"text": [
"Acanthamoeba profilin strongly inhibits in a concentration-dependent fashion the rate and extent of Acanthamoeba actin polymerization in 50 mM KCl."
],
"offsets": [
[
0,
147
]
]
}
] | [
{
"id": "BioInfer.d7.s1.e0",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
113,
118
]
],
"normalized": []
},
{
"id": "BioInfer.d7.s1.e1",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
13,
21
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d7.s1.i0",
"type": "PPI",
"arg1_id": "BioInfer.d7.s1.e0",
"arg2_id": "BioInfer.d7.s1.e1",
"normalized": []
}
] |
18 | BioInfer.d7.s2 | [
{
"id": "BioInfer.d7.s2__text",
"type": "Sentence",
"text": [
"Addition of profilin to polymerized actin causes it to depolymerize until a new steady-state, dependent on profilin concentration, is achieved."
],
"offsets": [
[
0,
143
]
]
}
] | [
{
"id": "BioInfer.d7.s2.e0",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
12,
20
]
],
"normalized": []
},
{
"id": "BioInfer.d7.s2.e1",
"type": "Individual_protein",
"text": [
"actin"
],
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36,
41
]
],
"normalized": []
},
{
"id": "BioInfer.d7.s2.e2",
"type": "Gene/protein/RNA",
"text": [
"profilin"
],
"offsets": [
[
107,
115
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d7.s2.i0",
"type": "PPI",
"arg1_id": "BioInfer.d7.s2.e0",
"arg2_id": "BioInfer.d7.s2.e1",
"normalized": []
}
] |
19 | BioInfer.d7.s3 | [
{
"id": "BioInfer.d7.s3__text",
"type": "Sentence",
"text": [
"Mechanism of action of Acanthamoeba profilin: demonstration of actin species specificity and regulation by micromolar concentrations of MgCl2."
],
"offsets": [
[
0,
142
]
]
}
] | [
{
"id": "BioInfer.d7.s3.e0",
"type": "Gene/protein/RNA",
"text": [
"profilin"
],
"offsets": [
[
36,
44
]
],
"normalized": []
},
{
"id": "BioInfer.d7.s3.e1",
"type": "Gene/protein/RNA",
"text": [
"actin"
],
"offsets": [
[
63,
68
]
],
"normalized": []
}
] | [] | [] | [] |
20 | BioInfer.d7.s4 | [
{
"id": "BioInfer.d7.s4__text",
"type": "Sentence",
"text": [
"MgCl2 strongly inhibits these effects of profilin, most likely by binding to the high-affinity divalent cation site on the actin."
],
"offsets": [
[
0,
129
]
]
}
] | [
{
"id": "BioInfer.d7.s4.e0",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
123,
128
]
],
"normalized": []
},
{
"id": "BioInfer.d7.s4.e1",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
41,
49
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d7.s4.i0",
"type": "PPI",
"arg1_id": "BioInfer.d7.s4.e0",
"arg2_id": "BioInfer.d7.s4.e1",
"normalized": []
}
] |
21 | BioInfer.d8.s0 | [
{
"id": "BioInfer.d8.s0__text",
"type": "Sentence",
"text": [
"Accordingly, beta-catenin is also found in these structures, again in the absence of alpha-catenin."
],
"offsets": [
[
0,
99
]
]
}
] | [
{
"id": "BioInfer.d8.s0.e0",
"type": "Individual_protein",
"text": [
"alpha-catenin"
],
"offsets": [
[
85,
98
]
],
"normalized": []
},
{
"id": "BioInfer.d8.s0.e1",
"type": "Individual_protein",
"text": [
"beta-catenin"
],
"offsets": [
[
13,
25
]
],
"normalized": []
}
] | [] | [] | [] |
22 | BioInfer.d8.s1 | [
{
"id": "BioInfer.d8.s1__text",
"type": "Sentence",
"text": [
"In addition to its presence in cell-cell adhesion sites, we have found beta-catenin, but not alpha-catenin, in the Z-discs of heart and skeletal striated muscles."
],
"offsets": [
[
0,
162
]
]
}
] | [
{
"id": "BioInfer.d8.s1.e0",
"type": "Individual_protein",
"text": [
"beta-catenin"
],
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[
71,
83
]
],
"normalized": []
},
{
"id": "BioInfer.d8.s1.e1",
"type": "Individual_protein",
"text": [
"alpha-catenin"
],
"offsets": [
[
93,
106
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d8.s1.i0",
"type": "PPI",
"arg1_id": "BioInfer.d8.s1.e0",
"arg2_id": "BioInfer.d8.s1.e1",
"normalized": []
}
] |
23 | BioInfer.d9.s0 | [
{
"id": "BioInfer.d9.s0__text",
"type": "Sentence",
"text": [
"A chimera consisting of the alpha-catenin-binding region of beta-catenin linked to the amino terminus of alpha-catenin 57-264 behaves as a monomer in solution, as expected, since beta-catenin binding disrupts the alpha-catenin dimer."
],
"offsets": [
[
0,
233
]
]
}
] | [
{
"id": "BioInfer.d9.s0.e0",
"type": "Individual_protein",
"text": [
"beta-catenin"
],
"offsets": [
[
60,
72
]
],
"normalized": []
},
{
"id": "BioInfer.d9.s0.e1",
"type": "Individual_protein",
"text": [
"beta-catenin"
],
"offsets": [
[
179,
191
]
],
"normalized": []
},
{
"id": "BioInfer.d9.s0.e2",
"type": "Individual_protein",
"text": [
"alpha-catenin 57-264"
],
"offsets": [
[
105,
125
]
],
"normalized": []
},
{
"id": "BioInfer.d9.s0.e3",
"type": "Individual_protein",
"text": [
"alpha-catenin"
],
"offsets": [
[
213,
226
]
],
"normalized": []
},
{
"id": "BioInfer.d9.s0.e4",
"type": "Individual_protein",
"text": [
"alpha-catenin"
],
"offsets": [
[
28,
41
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d9.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d9.s0.e0",
"arg2_id": "BioInfer.d9.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d9.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d9.s0.e0",
"arg2_id": "BioInfer.d9.s0.e4",
"normalized": []
},
{
"id": "BioInfer.d9.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d9.s0.e1",
"arg2_id": "BioInfer.d9.s0.e3",
"normalized": []
}
] |
24 | BioInfer.d10.s0 | [
{
"id": "BioInfer.d10.s0__text",
"type": "Sentence",
"text": [
"Acidic domain of the phosphoprotein (P) of vesicular stomatitis virus differentially interacts with homologous and heterologous nucleocapsid protein (N)."
],
"offsets": [
[
0,
153
]
]
}
] | [
{
"id": "BioInfer.d10.s0.e0",
"type": "Individual_protein",
"text": [
"nucleocapsid protein"
],
"offsets": [
[
128,
148
]
],
"normalized": []
},
{
"id": "BioInfer.d10.s0.e1",
"type": "Individual_protein",
"text": [
"phosphoprotein"
],
"offsets": [
[
21,
35
]
],
"normalized": []
},
{
"id": "BioInfer.d10.s0.e2",
"type": "Individual_protein",
"text": [
"P"
],
"offsets": [
[
37,
38
]
],
"normalized": []
},
{
"id": "BioInfer.d10.s0.e3",
"type": "Individual_protein",
"text": [
"N"
],
"offsets": [
[
150,
151
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d10.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d10.s0.e0",
"arg2_id": "BioInfer.d10.s0.e1",
"normalized": []
},
{
"id": "BioInfer.d10.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d10.s0.e0",
"arg2_id": "BioInfer.d10.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d10.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d10.s0.e1",
"arg2_id": "BioInfer.d10.s0.e3",
"normalized": []
},
{
"id": "BioInfer.d10.s0.i3",
"type": "PPI",
"arg1_id": "BioInfer.d10.s0.e2",
"arg2_id": "BioInfer.d10.s0.e3",
"normalized": []
}
] |
25 | BioInfer.d11.s0 | [
{
"id": "BioInfer.d11.s0__text",
"type": "Sentence",
"text": [
"A common feature of these talin-positive domains is the deep membrane infoldings, where bundles of actin filaments are inserted into the membrane."
],
"offsets": [
[
0,
146
]
]
}
] | [
{
"id": "BioInfer.d11.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"actin"
],
"offsets": [
[
99,
104
]
],
"normalized": []
},
{
"id": "BioInfer.d11.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"talin"
],
"offsets": [
[
26,
31
]
],
"normalized": []
}
] | [] | [] | [] |
26 | BioInfer.d12.s0 | [
{
"id": "BioInfer.d12.s0__text",
"type": "Sentence",
"text": [
"A core activity associated with the N terminus of the yeast RAD52 protein is revealed by RAD51 overexpression suppression of C-terminal rad52 truncation alleles."
],
"offsets": [
[
0,
161
]
]
}
] | [
{
"id": "BioInfer.d12.s0.e0",
"type": "Gene",
"text": [
"rad52"
],
"offsets": [
[
136,
141
]
],
"normalized": []
},
{
"id": "BioInfer.d12.s0.e1",
"type": "Individual_protein",
"text": [
"RAD51"
],
"offsets": [
[
89,
94
]
],
"normalized": []
},
{
"id": "BioInfer.d12.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"RAD52"
],
"offsets": [
[
60,
65
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d12.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d12.s0.e0",
"arg2_id": "BioInfer.d12.s0.e1",
"normalized": []
}
] |
27 | BioInfer.d14.s0 | [
{
"id": "BioInfer.d14.s0__text",
"type": "Sentence",
"text": [
"Actin-binding proteins such as profilin and gelsolin bind to phosphatidylinositol (PI) 4,5-bisphosphate (PI 4,5-P2) and regulate the concentration of monomeric actin."
],
"offsets": [
[
0,
166
]
]
}
] | [
{
"id": "BioInfer.d14.s0.e0",
"type": "Individual_protein",
"text": [
"gelsolin"
],
"offsets": [
[
44,
52
]
],
"normalized": []
},
{
"id": "BioInfer.d14.s0.e1",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
160,
165
]
],
"normalized": []
},
{
"id": "BioInfer.d14.s0.e2",
"type": "Protein_family_or_group",
"text": [
"Actin-binding proteins"
],
"offsets": [
[
0,
22
]
],
"normalized": []
},
{
"id": "BioInfer.d14.s0.e3",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
31,
39
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d14.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d14.s0.e0",
"arg2_id": "BioInfer.d14.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d14.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d14.s0.e1",
"arg2_id": "BioInfer.d14.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d14.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d14.s0.e2",
"arg2_id": "BioInfer.d14.s0.e3",
"normalized": []
}
] |
28 | BioInfer.d14.s1 | [
{
"id": "BioInfer.d14.s1__text",
"type": "Sentence",
"text": [
"These studies suggest that profilin and gelsolin may control the generation of 3-OH phosphorylated phosphoinositides, which in turn may regulate the actin polymerization."
],
"offsets": [
[
0,
170
]
]
}
] | [
{
"id": "BioInfer.d14.s1.e0",
"type": "Gene/protein/RNA",
"text": [
"profilin"
],
"offsets": [
[
27,
35
]
],
"normalized": []
},
{
"id": "BioInfer.d14.s1.e1",
"type": "Gene/protein/RNA",
"text": [
"actin"
],
"offsets": [
[
149,
154
]
],
"normalized": []
},
{
"id": "BioInfer.d14.s1.e2",
"type": "Gene/protein/RNA",
"text": [
"gelsolin"
],
"offsets": [
[
40,
48
]
],
"normalized": []
}
] | [] | [] | [] |
29 | BioInfer.d14.s2 | [
{
"id": "BioInfer.d14.s2__text",
"type": "Sentence",
"text": [
"This effect is specific to profilin and gelsolin because other cytoskeletal proteins such as tau or actin do not affect PI 3-kinase activity."
],
"offsets": [
[
0,
141
]
]
}
] | [
{
"id": "BioInfer.d14.s2.e0",
"type": "Gene/protein/RNA",
"text": [
"profilin"
],
"offsets": [
[
27,
35
]
],
"normalized": []
},
{
"id": "BioInfer.d14.s2.e1",
"type": "Individual_protein",
"text": [
"PI 3-kinase"
],
"offsets": [
[
120,
131
]
],
"normalized": []
},
{
"id": "BioInfer.d14.s2.e2",
"type": "Individual_protein",
"text": [
"tau"
],
"offsets": [
[
93,
96
]
],
"normalized": []
},
{
"id": "BioInfer.d14.s2.e3",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
100,
105
]
],
"normalized": []
},
{
"id": "BioInfer.d14.s2.e4",
"type": "Gene/protein/RNA",
"text": [
"gelsolin"
],
"offsets": [
[
40,
48
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d14.s2.i0",
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"arg1_id": "BioInfer.d14.s2.e1",
"arg2_id": "BioInfer.d14.s2.e2",
"normalized": []
},
{
"id": "BioInfer.d14.s2.i1",
"type": "PPI",
"arg1_id": "BioInfer.d14.s2.e1",
"arg2_id": "BioInfer.d14.s2.e3",
"normalized": []
}
] |
30 | BioInfer.d16.s0 | [
{
"id": "BioInfer.d16.s0__text",
"type": "Sentence",
"text": [
"Actin-depolymerizing factor (ADF) and cofilin define a family of actin-binding proteins essential for the rapid turnover of filamentous actin in vivo."
],
"offsets": [
[
0,
150
]
]
}
] | [
{
"id": "BioInfer.d16.s0.e0",
"type": "Individual_protein",
"text": [
"ADF"
],
"offsets": [
[
29,
32
]
],
"normalized": []
},
{
"id": "BioInfer.d16.s0.e1",
"type": "Individual_protein",
"text": [
"Actin-depolymerizing factor"
],
"offsets": [
[
0,
27
]
],
"normalized": []
},
{
"id": "BioInfer.d16.s0.e2",
"type": "Individual_protein",
"text": [
"cofilin"
],
"offsets": [
[
38,
45
]
],
"normalized": []
},
{
"id": "BioInfer.d16.s0.e3",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
136,
141
]
],
"normalized": []
},
{
"id": "BioInfer.d16.s0.e4",
"type": "Protein_family_or_group",
"text": [
"actin-binding proteins"
],
"offsets": [
[
65,
87
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d16.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d16.s0.e0",
"arg2_id": "BioInfer.d16.s0.e4",
"normalized": []
},
{
"id": "BioInfer.d16.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d16.s0.e1",
"arg2_id": "BioInfer.d16.s0.e4",
"normalized": []
},
{
"id": "BioInfer.d16.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d16.s0.e2",
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"normalized": []
},
{
"id": "BioInfer.d16.s0.i3",
"type": "PPI",
"arg1_id": "BioInfer.d16.s0.e3",
"arg2_id": "BioInfer.d16.s0.e4",
"normalized": []
}
] |
31 | BioInfer.d17.s0 | [
{
"id": "BioInfer.d17.s0__text",
"type": "Sentence",
"text": [
"Actin expression was reduced by 25-50%, relative to that of myosin heavy chain, in smooth muscle of KO mice, without any change in the relative distribution of the actin isoforms."
],
"offsets": [
[
0,
179
]
]
}
] | [
{
"id": "BioInfer.d17.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"Actin"
],
"offsets": [
[
0,
5
]
],
"normalized": []
},
{
"id": "BioInfer.d17.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"actin"
],
"offsets": [
[
164,
169
]
],
"normalized": []
},
{
"id": "BioInfer.d17.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"myosin heavy chain"
],
"offsets": [
[
60,
78
]
],
"normalized": []
}
] | [] | [] | [] |
32 | BioInfer.d17.s1 | [
{
"id": "BioInfer.d17.s1__text",
"type": "Sentence",
"text": [
"We conclude that the faster Vus of smooth muscle of the KO mouse is consistent with, but does not prove without further study, physiological regulation of the crossbridge cycle by calponin."
],
"offsets": [
[
0,
189
]
]
}
] | [
{
"id": "BioInfer.d17.s1.e0",
"type": "Gene/protein/RNA",
"text": [
"calponin"
],
"offsets": [
[
180,
188
]
],
"normalized": []
}
] | [] | [] | [] |
33 | BioInfer.d18.s0 | [
{
"id": "BioInfer.d18.s0__text",
"type": "Sentence",
"text": [
"Actin isoforms from different species were also compared, and the effect of profilin on the thermal stability of actin was studied."
],
"offsets": [
[
0,
131
]
]
}
] | [
{
"id": "BioInfer.d18.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"Actin"
],
"offsets": [
[
0,
5
]
],
"normalized": []
},
{
"id": "BioInfer.d18.s0.e1",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
113,
118
]
],
"normalized": []
},
{
"id": "BioInfer.d18.s0.e2",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
76,
84
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d18.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d18.s0.e1",
"arg2_id": "BioInfer.d18.s0.e2",
"normalized": []
}
] |
34 | BioInfer.d20.s0 | [
{
"id": "BioInfer.d20.s0__text",
"type": "Sentence",
"text": [
"Active, Ser133-phosphorylated CREB effects transcription of CRE-dependent genes via interaction with the 265-kDa co-activator protein CREB-binding-protein, CBP, which bridges the CRE/CREB complex to components of the basal transcriptional apparatus."
],
"offsets": [
[
0,
249
]
]
}
] | [
{
"id": "BioInfer.d20.s0.e0",
"type": "Individual_protein",
"text": [
"CREB-binding-protein"
],
"offsets": [
[
134,
154
]
],
"normalized": []
},
{
"id": "BioInfer.d20.s0.e1",
"type": "Individual_protein",
"text": [
"CREB"
],
"offsets": [
[
183,
187
]
],
"normalized": []
},
{
"id": "BioInfer.d20.s0.e2",
"type": "Individual_protein",
"text": [
"CREB"
],
"offsets": [
[
30,
34
]
],
"normalized": []
},
{
"id": "BioInfer.d20.s0.e3",
"type": "Individual_protein",
"text": [
"CBP"
],
"offsets": [
[
156,
159
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d20.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d20.s0.e0",
"arg2_id": "BioInfer.d20.s0.e1",
"normalized": []
},
{
"id": "BioInfer.d20.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d20.s0.e0",
"arg2_id": "BioInfer.d20.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d20.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d20.s0.e1",
"arg2_id": "BioInfer.d20.s0.e3",
"normalized": []
},
{
"id": "BioInfer.d20.s0.i3",
"type": "PPI",
"arg1_id": "BioInfer.d20.s0.e2",
"arg2_id": "BioInfer.d20.s0.e3",
"normalized": []
}
] |
35 | BioInfer.d21.s0 | [
{
"id": "BioInfer.d21.s0__text",
"type": "Sentence",
"text": [
"Actophorin and profilin have opposite effects on the rate of exchange of nucleotide bound to actin monomers."
],
"offsets": [
[
0,
108
]
]
}
] | [
{
"id": "BioInfer.d21.s0.e0",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
93,
98
]
],
"normalized": []
},
{
"id": "BioInfer.d21.s0.e1",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
15,
23
]
],
"normalized": []
},
{
"id": "BioInfer.d21.s0.e2",
"type": "Individual_protein",
"text": [
"Actophorin"
],
"offsets": [
[
0,
10
]
],
"normalized": []
}
] | [] | [] | [] |
36 | BioInfer.d24.s0 | [
{
"id": "BioInfer.d24.s0__text",
"type": "Sentence",
"text": [
"Addition of EGTA (3 mM) to the extracellular media completely inhibited the cleavage of actin-binding protein, talin, and pp60src in response to A23187 (1 microM)."
],
"offsets": [
[
0,
163
]
]
}
] | [
{
"id": "BioInfer.d24.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"pp60src"
],
"offsets": [
[
122,
129
]
],
"normalized": []
},
{
"id": "BioInfer.d24.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"actin-binding protein"
],
"offsets": [
[
88,
109
]
],
"normalized": []
},
{
"id": "BioInfer.d24.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"talin"
],
"offsets": [
[
111,
116
]
],
"normalized": []
}
] | [] | [] | [] |
37 | BioInfer.d25.s0 | [
{
"id": "BioInfer.d25.s0__text",
"type": "Sentence",
"text": [
"Adherens junction proteins (N-cadherin, E-cadherin, alpha-catenin, beta-catenin, plakoglobin, and actin) and the proliferation marker Ki-67 were localized in the cultures by fluorescence microscopy, and in vitro wound healing was compared."
],
"offsets": [
[
0,
239
]
]
}
] | [
{
"id": "BioInfer.d25.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"plakoglobin"
],
"offsets": [
[
81,
92
]
],
"normalized": []
},
{
"id": "BioInfer.d25.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"E-cadherin"
],
"offsets": [
[
40,
50
]
],
"normalized": []
},
{
"id": "BioInfer.d25.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"alpha-catenin"
],
"offsets": [
[
52,
65
]
],
"normalized": []
},
{
"id": "BioInfer.d25.s0.e3",
"type": "Gene/protein/RNA",
"text": [
"N-cadherin"
],
"offsets": [
[
28,
38
]
],
"normalized": []
},
{
"id": "BioInfer.d25.s0.e4",
"type": "Gene/protein/RNA",
"text": [
"Ki-67"
],
"offsets": [
[
134,
139
]
],
"normalized": []
},
{
"id": "BioInfer.d25.s0.e5",
"type": "Gene/protein/RNA",
"text": [
"actin"
],
"offsets": [
[
98,
103
]
],
"normalized": []
},
{
"id": "BioInfer.d25.s0.e6",
"type": "Gene/protein/RNA",
"text": [
"beta-catenin"
],
"offsets": [
[
67,
79
]
],
"normalized": []
}
] | [] | [] | [] |
38 | BioInfer.d26.s0 | [
{
"id": "BioInfer.d26.s0__text",
"type": "Sentence",
"text": [
"A distinct modulating domain in glucocorticoid receptor monomers in the repression of activity of the transcription factor AP-1."
],
"offsets": [
[
0,
128
]
]
}
] | [
{
"id": "BioInfer.d26.s0.e0",
"type": "Individual_protein",
"text": [
"AP-1"
],
"offsets": [
[
123,
127
]
],
"normalized": []
},
{
"id": "BioInfer.d26.s0.e1",
"type": "Individual_protein",
"text": [
"glucocorticoid receptor"
],
"offsets": [
[
32,
55
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d26.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d26.s0.e0",
"arg2_id": "BioInfer.d26.s0.e1",
"normalized": []
}
] |
39 | BioInfer.d27.s0 | [
{
"id": "BioInfer.d27.s0__text",
"type": "Sentence",
"text": [
"ADP-ribosylation of actin at Arg 177 by Clostridium perfringens iota toxin increased the nucleotide dissociation rate from 2.2 x 10(-3) s-1 to 4.5 x 10(-3) s-1 without affecting the profilin-induced stimulation of nucleotide exchange."
],
"offsets": [
[
0,
234
]
]
}
] | [
{
"id": "BioInfer.d27.s0.e0",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
20,
25
]
],
"normalized": []
},
{
"id": "BioInfer.d27.s0.e1",
"type": "Individual_protein",
"text": [
"iota toxin"
],
"offsets": [
[
64,
74
]
],
"normalized": []
},
{
"id": "BioInfer.d27.s0.e2",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
182,
190
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d27.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d27.s0.e0",
"arg2_id": "BioInfer.d27.s0.e1",
"normalized": []
},
{
"id": "BioInfer.d27.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d27.s0.e1",
"arg2_id": "BioInfer.d27.s0.e2",
"normalized": []
}
] |
40 | BioInfer.d27.s1 | [
{
"id": "BioInfer.d27.s1__text",
"type": "Sentence",
"text": [
"In contrast, ADP-ribosylation of actin at Arg95/Arg372 induced by turkey erythrocyte transferase decreased the nucleotide dissociation rate to 1.5 x 10(3) s-1 and inhibited the profilin-induced stimulation of nucleotide exchange."
],
"offsets": [
[
0,
229
]
]
}
] | [
{
"id": "BioInfer.d27.s1.e0",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
177,
185
]
],
"normalized": []
},
{
"id": "BioInfer.d27.s1.e1",
"type": "Individual_protein",
"text": [
"erythrocyte transferase"
],
"offsets": [
[
73,
96
]
],
"normalized": []
},
{
"id": "BioInfer.d27.s1.e2",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
33,
38
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d27.s1.i0",
"type": "PPI",
"arg1_id": "BioInfer.d27.s1.e1",
"arg2_id": "BioInfer.d27.s1.e2",
"normalized": []
}
] |
41 | BioInfer.d28.s0 | [
{
"id": "BioInfer.d28.s0__text",
"type": "Sentence",
"text": [
"After 24 or 48 hours of shear, staining for VE-cadherin, alpha-catenin, and beta-catenin was intense and peripheral, forming a band of \"dashes\" (adherens plaques) that colocalized with the ends of stress fibers that inserted along the lateral membranes of cells."
],
"offsets": [
[
0,
262
]
]
}
] | [
{
"id": "BioInfer.d28.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"beta-catenin"
],
"offsets": [
[
76,
88
]
],
"normalized": []
},
{
"id": "BioInfer.d28.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"VE-cadherin"
],
"offsets": [
[
44,
55
]
],
"normalized": []
},
{
"id": "BioInfer.d28.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"alpha-catenin"
],
"offsets": [
[
57,
70
]
],
"normalized": []
}
] | [] | [] | [] |
42 | BioInfer.d28.s1 | [
{
"id": "BioInfer.d28.s1__text",
"type": "Sentence",
"text": [
"Cells were fixed and stained with antibodies to vascular endothelial (VE) cadherin, alpha-catenin, beta-catenin, or plakoglobin."
],
"offsets": [
[
0,
128
]
]
}
] | [
{
"id": "BioInfer.d28.s1.e0",
"type": "Gene/protein/RNA",
"text": [
"vascular endothelial",
"cadherin"
],
"offsets": [
[
48,
68
],
[
74,
82
]
],
"normalized": []
},
{
"id": "BioInfer.d28.s1.e1",
"type": "Gene/protein/RNA",
"text": [
"beta-catenin"
],
"offsets": [
[
99,
111
]
],
"normalized": []
},
{
"id": "BioInfer.d28.s1.e2",
"type": "Gene/protein/RNA",
"text": [
"alpha-catenin"
],
"offsets": [
[
84,
97
]
],
"normalized": []
},
{
"id": "BioInfer.d28.s1.e3",
"type": "Gene/protein/RNA",
"text": [
"plakoglobin"
],
"offsets": [
[
116,
127
]
],
"normalized": []
}
] | [] | [] | [] |
43 | BioInfer.d29.s0 | [
{
"id": "BioInfer.d29.s0__text",
"type": "Sentence",
"text": [
"After digestion of the 60 kDa fragment with cyanogen bromide, the N-terminal 21-amino acid sequence of one of the resulting peptides was found to show sequence similarity to a region near the actin-binding site (amino acid residues 260-281) of yeast fimbrin."
],
"offsets": [
[
0,
258
]
]
}
] | [
{
"id": "BioInfer.d29.s0.e0",
"type": "Individual_protein",
"text": [
"fimbrin"
],
"offsets": [
[
250,
257
]
],
"normalized": []
},
{
"id": "BioInfer.d29.s0.e1",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
192,
197
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d29.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d29.s0.e0",
"arg2_id": "BioInfer.d29.s0.e1",
"normalized": []
}
] |
44 | BioInfer.d30.s0 | [
{
"id": "BioInfer.d30.s0__text",
"type": "Sentence",
"text": [
"After elution of the three actin-binding proteins, actin and profilin were recovered from the DNase I column with 2 M urea solution."
],
"offsets": [
[
0,
132
]
]
}
] | [
{
"id": "BioInfer.d30.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"actin"
],
"offsets": [
[
51,
56
]
],
"normalized": []
},
{
"id": "BioInfer.d30.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"DNase I"
],
"offsets": [
[
94,
101
]
],
"normalized": []
},
{
"id": "BioInfer.d30.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"actin-binding proteins"
],
"offsets": [
[
27,
49
]
],
"normalized": []
},
{
"id": "BioInfer.d30.s0.e3",
"type": "Gene/protein/RNA",
"text": [
"profilin"
],
"offsets": [
[
61,
69
]
],
"normalized": []
}
] | [] | [] | [] |
45 | BioInfer.d31.s0 | [
{
"id": "BioInfer.d31.s0__text",
"type": "Sentence",
"text": [
"After in vitro labelling of isolated rat liver nuclei, the following ADP-ribosylated and unmodified histones were identified by HPLC and gel electrophoresis: histone H1(0), four histone H1 subfractions, histone H2A.1, histone H2A.2, oxidized histone H2A.2, histone H2A.X, histone H2A.Z, histone H2B, three histone H3 variants and histone H4."
],
"offsets": [
[
0,
341
]
]
}
] | [
{
"id": "BioInfer.d31.s0.e0",
"type": "Protein_family_or_group",
"text": [
"histone"
],
"offsets": [
[
330,
337
]
],
"normalized": []
},
{
"id": "BioInfer.d31.s0.e1",
"type": "Protein_family_or_group",
"text": [
"histone"
],
"offsets": [
[
306,
313
]
],
"normalized": []
},
{
"id": "BioInfer.d31.s0.e2",
"type": "Protein_family_or_group",
"text": [
"histone"
],
"offsets": [
[
158,
165
]
],
"normalized": []
},
{
"id": "BioInfer.d31.s0.e3",
"type": "Protein_family_or_group",
"text": [
"histone"
],
"offsets": [
[
218,
225
]
],
"normalized": []
},
{
"id": "BioInfer.d31.s0.e4",
"type": "Protein_family_or_group",
"text": [
"histone"
],
"offsets": [
[
203,
210
]
],
"normalized": []
},
{
"id": "BioInfer.d31.s0.e5",
"type": "Protein_family_or_group",
"text": [
"histone"
],
"offsets": [
[
178,
185
]
],
"normalized": []
},
{
"id": "BioInfer.d31.s0.e6",
"type": "Protein_family_or_group",
"text": [
"histone"
],
"offsets": [
[
257,
264
]
],
"normalized": []
},
{
"id": "BioInfer.d31.s0.e7",
"type": "Protein_family_or_group",
"text": [
"histone"
],
"offsets": [
[
287,
294
]
],
"normalized": []
},
{
"id": "BioInfer.d31.s0.e8",
"type": "Protein_family_or_group",
"text": [
"histone"
],
"offsets": [
[
272,
279
]
],
"normalized": []
},
{
"id": "BioInfer.d31.s0.e9",
"type": "Individual_protein",
"text": [
"H3"
],
"offsets": [
[
314,
316
]
],
"normalized": []
},
{
"id": "BioInfer.d31.s0.e10",
"type": "Individual_protein",
"text": [
"H2B"
],
"offsets": [
[
295,
298
]
],
"normalized": []
},
{
"id": "BioInfer.d31.s0.e11",
"type": "Individual_protein",
"text": [
"H4"
],
"offsets": [
[
338,
340
]
],
"normalized": []
},
{
"id": "BioInfer.d31.s0.e12",
"type": "Protein_family_or_group",
"text": [
"histone"
],
"offsets": [
[
242,
249
]
],
"normalized": []
},
{
"id": "BioInfer.d31.s0.e13",
"type": "Individual_protein",
"text": [
"H2A.1"
],
"offsets": [
[
211,
216
]
],
"normalized": []
},
{
"id": "BioInfer.d31.s0.e14",
"type": "Individual_protein",
"text": [
"H1"
],
"offsets": [
[
186,
188
]
],
"normalized": []
},
{
"id": "BioInfer.d31.s0.e15",
"type": "Individual_protein",
"text": [
"H1(0)"
],
"offsets": [
[
166,
171
]
],
"normalized": []
},
{
"id": "BioInfer.d31.s0.e16",
"type": "Gene/protein/RNA",
"text": [
"histones"
],
"offsets": [
[
100,
108
]
],
"normalized": []
},
{
"id": "BioInfer.d31.s0.e17",
"type": "Individual_protein",
"text": [
"H2A.Z"
],
"offsets": [
[
280,
285
]
],
"normalized": []
},
{
"id": "BioInfer.d31.s0.e18",
"type": "Individual_protein",
"text": [
"H2A.X"
],
"offsets": [
[
265,
270
]
],
"normalized": []
},
{
"id": "BioInfer.d31.s0.e19",
"type": "Individual_protein",
"text": [
"H2A.2"
],
"offsets": [
[
250,
255
]
],
"normalized": []
},
{
"id": "BioInfer.d31.s0.e20",
"type": "Individual_protein",
"text": [
"H2A.2"
],
"offsets": [
[
226,
231
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d31.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d31.s0.e0",
"arg2_id": "BioInfer.d31.s0.e11",
"normalized": []
},
{
"id": "BioInfer.d31.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d31.s0.e1",
"arg2_id": "BioInfer.d31.s0.e9",
"normalized": []
},
{
"id": "BioInfer.d31.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d31.s0.e2",
"arg2_id": "BioInfer.d31.s0.e15",
"normalized": []
},
{
"id": "BioInfer.d31.s0.i3",
"type": "PPI",
"arg1_id": "BioInfer.d31.s0.e3",
"arg2_id": "BioInfer.d31.s0.e20",
"normalized": []
},
{
"id": "BioInfer.d31.s0.i4",
"type": "PPI",
"arg1_id": "BioInfer.d31.s0.e4",
"arg2_id": "BioInfer.d31.s0.e13",
"normalized": []
},
{
"id": "BioInfer.d31.s0.i5",
"type": "PPI",
"arg1_id": "BioInfer.d31.s0.e5",
"arg2_id": "BioInfer.d31.s0.e14",
"normalized": []
},
{
"id": "BioInfer.d31.s0.i6",
"type": "PPI",
"arg1_id": "BioInfer.d31.s0.e6",
"arg2_id": "BioInfer.d31.s0.e18",
"normalized": []
},
{
"id": "BioInfer.d31.s0.i7",
"type": "PPI",
"arg1_id": "BioInfer.d31.s0.e7",
"arg2_id": "BioInfer.d31.s0.e10",
"normalized": []
},
{
"id": "BioInfer.d31.s0.i8",
"type": "PPI",
"arg1_id": "BioInfer.d31.s0.e8",
"arg2_id": "BioInfer.d31.s0.e17",
"normalized": []
},
{
"id": "BioInfer.d31.s0.i9",
"type": "PPI",
"arg1_id": "BioInfer.d31.s0.e12",
"arg2_id": "BioInfer.d31.s0.e19",
"normalized": []
}
] |
46 | BioInfer.d32.s0 | [
{
"id": "BioInfer.d32.s0__text",
"type": "Sentence",
"text": [
"A further outcome of this study is that the actin filament core bundles in microvilli of chicken pigment epithelial cells are presumed to contain a crosslinking protein, which is not immunologically related to either villin, fimbrin or myosin I of the intestinal brush border."
],
"offsets": [
[
0,
276
]
]
}
] | [
{
"id": "BioInfer.d32.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"myosin I"
],
"offsets": [
[
236,
244
]
],
"normalized": []
},
{
"id": "BioInfer.d32.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"fimbrin"
],
"offsets": [
[
225,
232
]
],
"normalized": []
},
{
"id": "BioInfer.d32.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"actin"
],
"offsets": [
[
44,
49
]
],
"normalized": []
},
{
"id": "BioInfer.d32.s0.e3",
"type": "Gene/protein/RNA",
"text": [
"villin"
],
"offsets": [
[
217,
223
]
],
"normalized": []
}
] | [] | [] | [] |
47 | BioInfer.d33.s0 | [
{
"id": "BioInfer.d33.s0__text",
"type": "Sentence",
"text": [
"A highly significant correlation was observed between the loss of expression of E-cadherin, alpha-catenin and gamma-catenin, but not beta-catenin, with increased TNM stage (p <0.05)."
],
"offsets": [
[
0,
182
]
]
}
] | [
{
"id": "BioInfer.d33.s0.e0",
"type": "Individual_protein",
"text": [
"alpha-catenin"
],
"offsets": [
[
92,
105
]
],
"normalized": []
},
{
"id": "BioInfer.d33.s0.e1",
"type": "Individual_protein",
"text": [
"E-cadherin"
],
"offsets": [
[
80,
90
]
],
"normalized": []
},
{
"id": "BioInfer.d33.s0.e2",
"type": "Individual_protein",
"text": [
"beta-catenin"
],
"offsets": [
[
133,
145
]
],
"normalized": []
},
{
"id": "BioInfer.d33.s0.e3",
"type": "Individual_protein",
"text": [
"gamma-catenin"
],
"offsets": [
[
110,
123
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d33.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d33.s0.e0",
"arg2_id": "BioInfer.d33.s0.e1",
"normalized": []
},
{
"id": "BioInfer.d33.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d33.s0.e0",
"arg2_id": "BioInfer.d33.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d33.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d33.s0.e0",
"arg2_id": "BioInfer.d33.s0.e3",
"normalized": []
},
{
"id": "BioInfer.d33.s0.i3",
"type": "PPI",
"arg1_id": "BioInfer.d33.s0.e1",
"arg2_id": "BioInfer.d33.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d33.s0.i4",
"type": "PPI",
"arg1_id": "BioInfer.d33.s0.e1",
"arg2_id": "BioInfer.d33.s0.e3",
"normalized": []
},
{
"id": "BioInfer.d33.s0.i5",
"type": "PPI",
"arg1_id": "BioInfer.d33.s0.e2",
"arg2_id": "BioInfer.d33.s0.e3",
"normalized": []
}
] |
48 | BioInfer.d33.s1 | [
{
"id": "BioInfer.d33.s1__text",
"type": "Sentence",
"text": [
"Loss of normal surface E-cadherin, alpha-catenin, beta-catenin and gamma-catenin expression was found in 52/68 (76.4%) tumors, 57/68 (83.8%) tumors, 54/68 (79.4%) tumors and 54/68 (79.4%) tumors (p <0.001)."
],
"offsets": [
[
0,
206
]
]
}
] | [
{
"id": "BioInfer.d33.s1.e0",
"type": "Gene/protein/RNA",
"text": [
"beta-catenin"
],
"offsets": [
[
50,
62
]
],
"normalized": []
},
{
"id": "BioInfer.d33.s1.e1",
"type": "Gene/protein/RNA",
"text": [
"E-cadherin"
],
"offsets": [
[
23,
33
]
],
"normalized": []
},
{
"id": "BioInfer.d33.s1.e2",
"type": "Gene/protein/RNA",
"text": [
"gamma-catenin"
],
"offsets": [
[
67,
80
]
],
"normalized": []
},
{
"id": "BioInfer.d33.s1.e3",
"type": "Gene/protein/RNA",
"text": [
"alpha-catenin"
],
"offsets": [
[
35,
48
]
],
"normalized": []
}
] | [] | [] | [] |
49 | BioInfer.d33.s2 | [
{
"id": "BioInfer.d33.s2__text",
"type": "Sentence",
"text": [
"MATERIALS AND METHODS: We used an avidin-biotin immunoperoxidase technique to examine the cellular localization of alpha-catenin, beta-catenin, gamma-catenin and E-cadherin in 68 TCC and 14 normal bladder biopsies."
],
"offsets": [
[
0,
214
]
]
}
] | [
{
"id": "BioInfer.d33.s2.e0",
"type": "Gene/protein/RNA",
"text": [
"avidin"
],
"offsets": [
[
34,
40
]
],
"normalized": []
},
{
"id": "BioInfer.d33.s2.e1",
"type": "Gene/protein/RNA",
"text": [
"beta-catenin"
],
"offsets": [
[
130,
142
]
],
"normalized": []
},
{
"id": "BioInfer.d33.s2.e2",
"type": "Gene/protein/RNA",
"text": [
"alpha-catenin"
],
"offsets": [
[
115,
128
]
],
"normalized": []
},
{
"id": "BioInfer.d33.s2.e3",
"type": "Gene/protein/RNA",
"text": [
"E-cadherin"
],
"offsets": [
[
162,
172
]
],
"normalized": []
},
{
"id": "BioInfer.d33.s2.e4",
"type": "Gene/protein/RNA",
"text": [
"gamma-catenin"
],
"offsets": [
[
144,
157
]
],
"normalized": []
}
] | [] | [] | [] |
50 | BioInfer.d33.s3 | [
{
"id": "BioInfer.d33.s3__text",
"type": "Sentence",
"text": [
"RESULTS: E-cadherin, alpha-catenin, beta-catenin and gamma-catenin were expressed in a normal membranous pattern in all normal bladder epithelium specimens."
],
"offsets": [
[
0,
156
]
]
}
] | [
{
"id": "BioInfer.d33.s3.e0",
"type": "Gene/protein/RNA",
"text": [
"alpha-catenin"
],
"offsets": [
[
21,
34
]
],
"normalized": []
},
{
"id": "BioInfer.d33.s3.e1",
"type": "Gene/protein/RNA",
"text": [
"gamma-catenin"
],
"offsets": [
[
53,
66
]
],
"normalized": []
},
{
"id": "BioInfer.d33.s3.e2",
"type": "Gene/protein/RNA",
"text": [
"E-cadherin"
],
"offsets": [
[
9,
19
]
],
"normalized": []
},
{
"id": "BioInfer.d33.s3.e3",
"type": "Gene/protein/RNA",
"text": [
"beta-catenin"
],
"offsets": [
[
36,
48
]
],
"normalized": []
}
] | [] | [] | [] |
51 | BioInfer.d34.s0 | [
{
"id": "BioInfer.d34.s0__text",
"type": "Sentence",
"text": [
"AIMS: To investigate the disturbance of intercellular adhesion in adenoid cystic carcinoma (ACC), we examined the ultrastructural localization of E-cadherin (E-cad), alpha-catenin (alpha-cat) and beta-catenin (beta-cat) in ACC, and compared it with that in the normal labial gland."
],
"offsets": [
[
0,
281
]
]
}
] | [
{
"id": "BioInfer.d34.s0.e0",
"type": "Individual_protein",
"text": [
"E-cadherin"
],
"offsets": [
[
146,
156
]
],
"normalized": []
},
{
"id": "BioInfer.d34.s0.e1",
"type": "Individual_protein",
"text": [
"beta-catenin"
],
"offsets": [
[
196,
208
]
],
"normalized": []
},
{
"id": "BioInfer.d34.s0.e2",
"type": "Individual_protein",
"text": [
"alpha-catenin"
],
"offsets": [
[
166,
179
]
],
"normalized": []
},
{
"id": "BioInfer.d34.s0.e3",
"type": "Individual_protein",
"text": [
"beta-cat"
],
"offsets": [
[
210,
218
]
],
"normalized": []
},
{
"id": "BioInfer.d34.s0.e4",
"type": "Individual_protein",
"text": [
"alpha-cat"
],
"offsets": [
[
181,
190
]
],
"normalized": []
},
{
"id": "BioInfer.d34.s0.e5",
"type": "Individual_protein",
"text": [
"E-cad"
],
"offsets": [
[
158,
163
]
],
"normalized": []
}
] | [] | [] | [] |
52 | BioInfer.d35.s0 | [
{
"id": "BioInfer.d35.s0__text",
"type": "Sentence",
"text": [
"Aip1p interacts with cofilin to disassemble actin filaments."
],
"offsets": [
[
0,
60
]
]
}
] | [
{
"id": "BioInfer.d35.s0.e0",
"type": "Individual_protein",
"text": [
"Aip1p"
],
"offsets": [
[
0,
5
]
],
"normalized": []
},
{
"id": "BioInfer.d35.s0.e1",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
44,
49
]
],
"normalized": []
},
{
"id": "BioInfer.d35.s0.e2",
"type": "Individual_protein",
"text": [
"cofilin"
],
"offsets": [
[
21,
28
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d35.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d35.s0.e0",
"arg2_id": "BioInfer.d35.s0.e1",
"normalized": []
},
{
"id": "BioInfer.d35.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d35.s0.e0",
"arg2_id": "BioInfer.d35.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d35.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d35.s0.e1",
"arg2_id": "BioInfer.d35.s0.e2",
"normalized": []
}
] |
53 | BioInfer.d35.s1 | [
{
"id": "BioInfer.d35.s1__text",
"type": "Sentence",
"text": [
"Aip1p localizes to cortical actin patches in yeast cells, and this localization is disrupted by specific actin and cofilin mutations."
],
"offsets": [
[
0,
133
]
]
}
] | [
{
"id": "BioInfer.d35.s1.e0",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
28,
33
]
],
"normalized": []
},
{
"id": "BioInfer.d35.s1.e1",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
105,
110
]
],
"normalized": []
},
{
"id": "BioInfer.d35.s1.e2",
"type": "Individual_protein",
"text": [
"Aip1p"
],
"offsets": [
[
0,
5
]
],
"normalized": []
},
{
"id": "BioInfer.d35.s1.e3",
"type": "Individual_protein",
"text": [
"cofilin"
],
"offsets": [
[
115,
122
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d35.s1.i0",
"type": "PPI",
"arg1_id": "BioInfer.d35.s1.e0",
"arg2_id": "BioInfer.d35.s1.e1",
"normalized": []
},
{
"id": "BioInfer.d35.s1.i1",
"type": "PPI",
"arg1_id": "BioInfer.d35.s1.e0",
"arg2_id": "BioInfer.d35.s1.e2",
"normalized": []
},
{
"id": "BioInfer.d35.s1.i2",
"type": "PPI",
"arg1_id": "BioInfer.d35.s1.e0",
"arg2_id": "BioInfer.d35.s1.e3",
"normalized": []
}
] |
54 | BioInfer.d35.s2 | [
{
"id": "BioInfer.d35.s2__text",
"type": "Sentence",
"text": [
"A two-hybrid-based approach using cofilin and actin mutants identified residues necessary for the interaction of actin, cofilin, and Aip1p in an apparent ternary complex."
],
"offsets": [
[
0,
170
]
]
}
] | [
{
"id": "BioInfer.d35.s2.e0",
"type": "Gene/protein/RNA",
"text": [
"actin"
],
"offsets": [
[
46,
51
]
],
"normalized": []
},
{
"id": "BioInfer.d35.s2.e1",
"type": "Gene/protein/RNA",
"text": [
"cofilin"
],
"offsets": [
[
34,
41
]
],
"normalized": []
},
{
"id": "BioInfer.d35.s2.e2",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
113,
118
]
],
"normalized": []
},
{
"id": "BioInfer.d35.s2.e3",
"type": "Individual_protein",
"text": [
"cofilin"
],
"offsets": [
[
120,
127
]
],
"normalized": []
},
{
"id": "BioInfer.d35.s2.e4",
"type": "Individual_protein",
"text": [
"Aip1p"
],
"offsets": [
[
133,
138
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d35.s2.i0",
"type": "PPI",
"arg1_id": "BioInfer.d35.s2.e2",
"arg2_id": "BioInfer.d35.s2.e3",
"normalized": []
},
{
"id": "BioInfer.d35.s2.i1",
"type": "PPI",
"arg1_id": "BioInfer.d35.s2.e2",
"arg2_id": "BioInfer.d35.s2.e4",
"normalized": []
},
{
"id": "BioInfer.d35.s2.i2",
"type": "PPI",
"arg1_id": "BioInfer.d35.s2.e3",
"arg2_id": "BioInfer.d35.s2.e4",
"normalized": []
}
] |
55 | BioInfer.d35.s3 | [
{
"id": "BioInfer.d35.s3__text",
"type": "Sentence",
"text": [
"Here, we report that Aip1p also interacts with the ubiquitous actin depolymerizing factor cofilin."
],
"offsets": [
[
0,
98
]
]
}
] | [
{
"id": "BioInfer.d35.s3.e0",
"type": "Individual_protein",
"text": [
"actin depolymerizing factor"
],
"offsets": [
[
62,
89
]
],
"normalized": []
},
{
"id": "BioInfer.d35.s3.e1",
"type": "Individual_protein",
"text": [
"cofilin"
],
"offsets": [
[
90,
97
]
],
"normalized": []
},
{
"id": "BioInfer.d35.s3.e2",
"type": "Individual_protein",
"text": [
"Aip1p"
],
"offsets": [
[
21,
26
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d35.s3.i0",
"type": "PPI",
"arg1_id": "BioInfer.d35.s3.e0",
"arg2_id": "BioInfer.d35.s3.e1",
"normalized": []
},
{
"id": "BioInfer.d35.s3.i1",
"type": "PPI",
"arg1_id": "BioInfer.d35.s3.e1",
"arg2_id": "BioInfer.d35.s3.e2",
"normalized": []
}
] |
56 | BioInfer.d35.s4 | [
{
"id": "BioInfer.d35.s4__text",
"type": "Sentence",
"text": [
"We conclude that Aip1p is a cofilin-associated protein that enhances the filament disassembly activity of cofilin and restricts cofilin localization to cortical actin patches."
],
"offsets": [
[
0,
175
]
]
}
] | [
{
"id": "BioInfer.d35.s4.e0",
"type": "Individual_protein",
"text": [
"cofilin"
],
"offsets": [
[
106,
113
]
],
"normalized": []
},
{
"id": "BioInfer.d35.s4.e1",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
161,
166
]
],
"normalized": []
},
{
"id": "BioInfer.d35.s4.e2",
"type": "Individual_protein",
"text": [
"Aip1p"
],
"offsets": [
[
17,
22
]
],
"normalized": []
},
{
"id": "BioInfer.d35.s4.e3",
"type": "Individual_protein",
"text": [
"cofilin"
],
"offsets": [
[
128,
135
]
],
"normalized": []
},
{
"id": "BioInfer.d35.s4.e4",
"type": "Individual_protein",
"text": [
"cofilin"
],
"offsets": [
[
28,
35
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d35.s4.i0",
"type": "PPI",
"arg1_id": "BioInfer.d35.s4.e0",
"arg2_id": "BioInfer.d35.s4.e2",
"normalized": []
},
{
"id": "BioInfer.d35.s4.i1",
"type": "PPI",
"arg1_id": "BioInfer.d35.s4.e1",
"arg2_id": "BioInfer.d35.s4.e2",
"normalized": []
},
{
"id": "BioInfer.d35.s4.i2",
"type": "PPI",
"arg1_id": "BioInfer.d35.s4.e1",
"arg2_id": "BioInfer.d35.s4.e3",
"normalized": []
},
{
"id": "BioInfer.d35.s4.i3",
"type": "PPI",
"arg1_id": "BioInfer.d35.s4.e2",
"arg2_id": "BioInfer.d35.s4.e4",
"normalized": []
}
] |
57 | BioInfer.d36.s0 | [
{
"id": "BioInfer.d36.s0__text",
"type": "Sentence",
"text": [
"A LIMK2 mutant with replacement of threonine 505 by valine abolished LIMK2 activities for cofilin phosphorylation and actin cytoskeletal changes, whereas replacement by glutamate enhanced the protein kinase activity and stress fiber formation by LIMK2."
],
"offsets": [
[
0,
252
]
]
}
] | [
{
"id": "BioInfer.d36.s0.e0",
"type": "Individual_protein",
"text": [
"protein kinase"
],
"offsets": [
[
192,
206
]
],
"normalized": []
},
{
"id": "BioInfer.d36.s0.e1",
"type": "Individual_protein",
"text": [
"LIMK2"
],
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[
246,
251
]
],
"normalized": []
},
{
"id": "BioInfer.d36.s0.e2",
"type": "Individual_protein",
"text": [
"cofilin"
],
"offsets": [
[
90,
97
]
],
"normalized": []
},
{
"id": "BioInfer.d36.s0.e3",
"type": "Individual_protein",
"text": [
"LIMK2"
],
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[
2,
7
]
],
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},
{
"id": "BioInfer.d36.s0.e4",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
118,
123
]
],
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},
{
"id": "BioInfer.d36.s0.e5",
"type": "Individual_protein",
"text": [
"LIMK2"
],
"offsets": [
[
69,
74
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d36.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d36.s0.e0",
"arg2_id": "BioInfer.d36.s0.e1",
"normalized": []
},
{
"id": "BioInfer.d36.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d36.s0.e2",
"arg2_id": "BioInfer.d36.s0.e3",
"normalized": []
},
{
"id": "BioInfer.d36.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d36.s0.e2",
"arg2_id": "BioInfer.d36.s0.e5",
"normalized": []
},
{
"id": "BioInfer.d36.s0.i3",
"type": "PPI",
"arg1_id": "BioInfer.d36.s0.e3",
"arg2_id": "BioInfer.d36.s0.e4",
"normalized": []
},
{
"id": "BioInfer.d36.s0.i4",
"type": "PPI",
"arg1_id": "BioInfer.d36.s0.e4",
"arg2_id": "BioInfer.d36.s0.e5",
"normalized": []
}
] |
58 | BioInfer.d37.s0 | [
{
"id": "BioInfer.d37.s0__text",
"type": "Sentence",
"text": [
"All of the experimental data were quantitatively accounted for on the basis of a 1:1 complex between profilin and monomeric actin with a Kr between 4 and 9 microM, the same value obtained previously in the absence of MgCl2."
],
"offsets": [
[
0,
223
]
]
}
] | [
{
"id": "BioInfer.d37.s0.e0",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
101,
109
]
],
"normalized": []
},
{
"id": "BioInfer.d37.s0.e1",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
124,
129
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d37.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d37.s0.e0",
"arg2_id": "BioInfer.d37.s0.e1",
"normalized": []
}
] |
59 | BioInfer.d37.s1 | [
{
"id": "BioInfer.d37.s1__text",
"type": "Sentence",
"text": [
"The interaction of Acanthamoeba actin and Acanthamoeba profilin was evaluated as a function of ionic conditions."
],
"offsets": [
[
0,
112
]
]
}
] | [
{
"id": "BioInfer.d37.s1.e0",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
32,
37
]
],
"normalized": []
},
{
"id": "BioInfer.d37.s1.e1",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
55,
63
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d37.s1.i0",
"type": "PPI",
"arg1_id": "BioInfer.d37.s1.e0",
"arg2_id": "BioInfer.d37.s1.e1",
"normalized": []
}
] |
60 | BioInfer.d39.s0 | [
{
"id": "BioInfer.d39.s0__text",
"type": "Sentence",
"text": [
"Although binding patterns of different sera were not identical, almost all sera caused IgG binding to platelet components of 87-90 kD, 140 kD (identified as vinculin) and 220-240 kD (tentatively identified as talin and actin-binding protein)."
],
"offsets": [
[
0,
242
]
]
}
] | [
{
"id": "BioInfer.d39.s0.e0",
"type": "Individual_protein",
"text": [
"IgG"
],
"offsets": [
[
87,
90
]
],
"normalized": []
},
{
"id": "BioInfer.d39.s0.e1",
"type": "Individual_protein",
"text": [
"actin-binding protein"
],
"offsets": [
[
219,
240
]
],
"normalized": []
},
{
"id": "BioInfer.d39.s0.e2",
"type": "Individual_protein",
"text": [
"talin"
],
"offsets": [
[
209,
214
]
],
"normalized": []
},
{
"id": "BioInfer.d39.s0.e3",
"type": "Individual_protein",
"text": [
"vinculin"
],
"offsets": [
[
157,
165
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d39.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d39.s0.e0",
"arg2_id": "BioInfer.d39.s0.e1",
"normalized": []
},
{
"id": "BioInfer.d39.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d39.s0.e0",
"arg2_id": "BioInfer.d39.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d39.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d39.s0.e0",
"arg2_id": "BioInfer.d39.s0.e3",
"normalized": []
}
] |
61 | BioInfer.d41.s0 | [
{
"id": "BioInfer.d41.s0__text",
"type": "Sentence",
"text": [
"Although profilin released actin at the appropriate time to stimulate actin assembly during exposure to chemoattractants, the concentration of profilin in PMN was insufficient to explain the high unpolymerized actin content in unstimulated PMN and the quantity of actin released from profilin too small to account for the large shifts from unpolymerized to polymerized actin associated with maximal chemoattractant stimulation."
],
"offsets": [
[
0,
427
]
]
}
] | [
{
"id": "BioInfer.d41.s0.e0",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
9,
17
]
],
"normalized": []
},
{
"id": "BioInfer.d41.s0.e1",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
264,
269
]
],
"normalized": []
},
{
"id": "BioInfer.d41.s0.e2",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
70,
75
]
],
"normalized": []
},
{
"id": "BioInfer.d41.s0.e3",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
27,
32
]
],
"normalized": []
},
{
"id": "BioInfer.d41.s0.e4",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
210,
215
]
],
"normalized": []
},
{
"id": "BioInfer.d41.s0.e5",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
143,
151
]
],
"normalized": []
},
{
"id": "BioInfer.d41.s0.e6",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
369,
374
]
],
"normalized": []
},
{
"id": "BioInfer.d41.s0.e7",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
284,
292
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d41.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d41.s0.e0",
"arg2_id": "BioInfer.d41.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d41.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d41.s0.e0",
"arg2_id": "BioInfer.d41.s0.e3",
"normalized": []
},
{
"id": "BioInfer.d41.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d41.s0.e1",
"arg2_id": "BioInfer.d41.s0.e6",
"normalized": []
},
{
"id": "BioInfer.d41.s0.i3",
"type": "PPI",
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"arg2_id": "BioInfer.d41.s0.e7",
"normalized": []
},
{
"id": "BioInfer.d41.s0.i4",
"type": "PPI",
"arg1_id": "BioInfer.d41.s0.e2",
"arg2_id": "BioInfer.d41.s0.e3",
"normalized": []
},
{
"id": "BioInfer.d41.s0.i5",
"type": "PPI",
"arg1_id": "BioInfer.d41.s0.e4",
"arg2_id": "BioInfer.d41.s0.e5",
"normalized": []
}
] |
62 | BioInfer.d41.s1 | [
{
"id": "BioInfer.d41.s1__text",
"type": "Sentence",
"text": [
"Determination of the total profilin and actin concentrations in PMN revealed that the molar ratio of profilin to actin was 1 to 5.2."
],
"offsets": [
[
0,
132
]
]
}
] | [
{
"id": "BioInfer.d41.s1.e0",
"type": "Gene/protein/RNA",
"text": [
"actin"
],
"offsets": [
[
40,
45
]
],
"normalized": []
},
{
"id": "BioInfer.d41.s1.e1",
"type": "Gene/protein/RNA",
"text": [
"actin"
],
"offsets": [
[
113,
118
]
],
"normalized": []
},
{
"id": "BioInfer.d41.s1.e2",
"type": "Gene/protein/RNA",
"text": [
"profilin"
],
"offsets": [
[
27,
35
]
],
"normalized": []
},
{
"id": "BioInfer.d41.s1.e3",
"type": "Gene/protein/RNA",
"text": [
"profilin"
],
"offsets": [
[
101,
109
]
],
"normalized": []
}
] | [] | [] | [] |
63 | BioInfer.d41.s2 | [
{
"id": "BioInfer.d41.s2__text",
"type": "Sentence",
"text": [
"We examined the role of the actin monomer sequestering protein, profilin, in the regulation of PMN actin filament assembly during chemoattractant stimulation using a Triton extraction method."
],
"offsets": [
[
0,
191
]
]
}
] | [
{
"id": "BioInfer.d41.s2.e0",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
64,
72
]
],
"normalized": []
},
{
"id": "BioInfer.d41.s2.e1",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
28,
33
]
],
"normalized": []
},
{
"id": "BioInfer.d41.s2.e2",
"type": "Individual_protein",
"text": [
"PMN actin"
],
"offsets": [
[
95,
104
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d41.s2.i0",
"type": "PPI",
"arg1_id": "BioInfer.d41.s2.e0",
"arg2_id": "BioInfer.d41.s2.e1",
"normalized": []
},
{
"id": "BioInfer.d41.s2.i1",
"type": "PPI",
"arg1_id": "BioInfer.d41.s2.e0",
"arg2_id": "BioInfer.d41.s2.e2",
"normalized": []
}
] |
64 | BioInfer.d43.s0 | [
{
"id": "BioInfer.d43.s0__text",
"type": "Sentence",
"text": [
"Although co-localization of glucokinase with actin filaments was not clearly demonstrated in the pancreatic beta-cell line MIN6, islet glucokinase was found to be present in both the nucleus and the cytoplasm, though predominantly in the nucleus."
],
"offsets": [
[
0,
246
]
]
}
] | [
{
"id": "BioInfer.d43.s0.e0",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
45,
50
]
],
"normalized": []
},
{
"id": "BioInfer.d43.s0.e1",
"type": "Individual_protein",
"text": [
"glucokinase"
],
"offsets": [
[
28,
39
]
],
"normalized": []
},
{
"id": "BioInfer.d43.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"islet glucokinase"
],
"offsets": [
[
129,
146
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d43.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d43.s0.e0",
"arg2_id": "BioInfer.d43.s0.e1",
"normalized": []
}
] |
65 | BioInfer.d43.s1 | [
{
"id": "BioInfer.d43.s1__text",
"type": "Sentence",
"text": [
"A portion of glucokinase appeared to be co-localized with actin filaments in the cytoplasm of cultured rat hepatocytes incubated with 25 mM glucose."
],
"offsets": [
[
0,
148
]
]
}
] | [
{
"id": "BioInfer.d43.s1.e0",
"type": "Individual_protein",
"text": [
"glucokinase"
],
"offsets": [
[
13,
24
]
],
"normalized": []
},
{
"id": "BioInfer.d43.s1.e1",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
58,
63
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d43.s1.i0",
"type": "PPI",
"arg1_id": "BioInfer.d43.s1.e0",
"arg2_id": "BioInfer.d43.s1.e1",
"normalized": []
}
] |
66 | BioInfer.d43.s2 | [
{
"id": "BioInfer.d43.s2__text",
"type": "Sentence",
"text": [
"Co-localization of glucokinase with actin filaments."
],
"offsets": [
[
0,
52
]
]
}
] | [
{
"id": "BioInfer.d43.s2.e0",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
36,
41
]
],
"normalized": []
},
{
"id": "BioInfer.d43.s2.e1",
"type": "Individual_protein",
"text": [
"glucokinase"
],
"offsets": [
[
19,
30
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d43.s2.i0",
"type": "PPI",
"arg1_id": "BioInfer.d43.s2.e0",
"arg2_id": "BioInfer.d43.s2.e1",
"normalized": []
}
] |
67 | BioInfer.d43.s3 | [
{
"id": "BioInfer.d43.s3__text",
"type": "Sentence",
"text": [
"When liver- or islet-type glucokinase was transiently expressed in COS-7 cells, the expressed glucokinase was also co-localized with actin filaments in the cytoplasm of these transfected cells."
],
"offsets": [
[
0,
193
]
]
}
] | [
{
"id": "BioInfer.d43.s3.e0",
"type": "Gene/protein/RNA",
"text": [
"islet-type glucokinase"
],
"offsets": [
[
15,
37
]
],
"normalized": []
},
{
"id": "BioInfer.d43.s3.e1",
"type": "Individual_protein",
"text": [
"glucokinase"
],
"offsets": [
[
94,
105
]
],
"normalized": []
},
{
"id": "BioInfer.d43.s3.e2",
"type": "Gene/protein/RNA",
"text": [
"liver-",
"type glucokinase"
],
"offsets": [
[
5,
11
],
[
21,
37
]
],
"normalized": []
},
{
"id": "BioInfer.d43.s3.e3",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
133,
138
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d43.s3.i0",
"type": "PPI",
"arg1_id": "BioInfer.d43.s3.e1",
"arg2_id": "BioInfer.d43.s3.e3",
"normalized": []
}
] |
68 | BioInfer.d44.s0 | [
{
"id": "BioInfer.d44.s0__text",
"type": "Sentence",
"text": [
"Although neither activation of BCK1 (MEKK) by the dominant BCK1-20 mutation nor increased dosage of MKK1 (MEK) or MPK1 (MAP kinase) mimicked PKC1 as a glc7-10 dosage suppressor, extra copies of genes encoding upstream components of the Pkc1p pathway such as ROM2, RHO2, HCS77/WSC1/SLG1 and MID2 also suppressed glc7-10 effectively."
],
"offsets": [
[
0,
331
]
]
}
] | [
{
"id": "BioInfer.d44.s0.e0",
"type": "Gene",
"text": [
"BCK1"
],
"offsets": [
[
31,
35
]
],
"normalized": []
},
{
"id": "BioInfer.d44.s0.e1",
"type": "Gene",
"text": [
"MKK1"
],
"offsets": [
[
100,
104
]
],
"normalized": []
},
{
"id": "BioInfer.d44.s0.e2",
"type": "Gene",
"text": [
"BCK1-20"
],
"offsets": [
[
59,
66
]
],
"normalized": []
},
{
"id": "BioInfer.d44.s0.e3",
"type": "Gene",
"text": [
"HCS77"
],
"offsets": [
[
270,
275
]
],
"normalized": []
},
{
"id": "BioInfer.d44.s0.e4",
"type": "Individual_protein",
"text": [
"Pkc1p"
],
"offsets": [
[
236,
241
]
],
"normalized": []
},
{
"id": "BioInfer.d44.s0.e5",
"type": "Gene",
"text": [
"WSC1"
],
"offsets": [
[
276,
280
]
],
"normalized": []
},
{
"id": "BioInfer.d44.s0.e6",
"type": "Gene",
"text": [
"MID2"
],
"offsets": [
[
290,
294
]
],
"normalized": []
},
{
"id": "BioInfer.d44.s0.e7",
"type": "Gene",
"text": [
"RHO2"
],
"offsets": [
[
264,
268
]
],
"normalized": []
},
{
"id": "BioInfer.d44.s0.e8",
"type": "Gene",
"text": [
"MPK1"
],
"offsets": [
[
114,
118
]
],
"normalized": []
},
{
"id": "BioInfer.d44.s0.e9",
"type": "Gene",
"text": [
"ROM2"
],
"offsets": [
[
258,
262
]
],
"normalized": []
},
{
"id": "BioInfer.d44.s0.e10",
"type": "Gene",
"text": [
"glc7-10"
],
"offsets": [
[
311,
318
]
],
"normalized": []
},
{
"id": "BioInfer.d44.s0.e11",
"type": "Gene",
"text": [
"glc7-10"
],
"offsets": [
[
151,
158
]
],
"normalized": []
},
{
"id": "BioInfer.d44.s0.e12",
"type": "Gene",
"text": [
"PKC1"
],
"offsets": [
[
141,
145
]
],
"normalized": []
},
{
"id": "BioInfer.d44.s0.e13",
"type": "Gene",
"text": [
"SLG1"
],
"offsets": [
[
281,
285
]
],
"normalized": []
},
{
"id": "BioInfer.d44.s0.e14",
"type": "DNA_family_or_group",
"text": [
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71 | BioInfer.d49.s0 | [
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72 | BioInfer.d49.s1 | [
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73 | BioInfer.d49.s2 | [
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75 | BioInfer.d49.s4 | [
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76 | BioInfer.d50.s0 | [
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"arg1_id": "BioInfer.d52.s2.e1",
"arg2_id": "BioInfer.d52.s2.e2",
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},
{
"id": "BioInfer.d52.s2.i4",
"type": "PPI",
"arg1_id": "BioInfer.d52.s2.e1",
"arg2_id": "BioInfer.d52.s2.e3",
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},
{
"id": "BioInfer.d52.s2.i5",
"type": "PPI",
"arg1_id": "BioInfer.d52.s2.e2",
"arg2_id": "BioInfer.d52.s2.e3",
"normalized": []
}
] |
81 | BioInfer.d52.s3 | [
{
"id": "BioInfer.d52.s3__text",
"type": "Sentence",
"text": [
"This implies that Munc18-2 function in apical membrane trafficking involves aspects independent of the syntaxin 3 interaction."
],
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[
0,
126
]
]
}
] | [
{
"id": "BioInfer.d52.s3.e0",
"type": "Gene/protein/RNA",
"text": [
"syntaxin 3"
],
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[
103,
113
]
],
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},
{
"id": "BioInfer.d52.s3.e1",
"type": "Gene/protein/RNA",
"text": [
"Munc18-2"
],
"offsets": [
[
18,
26
]
],
"normalized": []
}
] | [] | [] | [] |
82 | BioInfer.d53.s0 | [
{
"id": "BioInfer.d53.s0__text",
"type": "Sentence",
"text": [
"Analyses of beta-catenin or E-cadherin immunoprecipitates from BMMC lysate revealed that alpha-catenin, beta-catenin, and E-cadherin were co-precipitated, suggesting that E-cadherin and catenins form a complex in mast cells."
],
"offsets": [
[
0,
224
]
]
}
] | [
{
"id": "BioInfer.d53.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"E-cadherin"
],
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[
28,
38
]
],
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},
{
"id": "BioInfer.d53.s0.e1",
"type": "Individual_protein",
"text": [
"beta-catenin"
],
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[
104,
116
]
],
"normalized": []
},
{
"id": "BioInfer.d53.s0.e2",
"type": "Individual_protein",
"text": [
"catenins"
],
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[
186,
194
]
],
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},
{
"id": "BioInfer.d53.s0.e3",
"type": "Individual_protein",
"text": [
"E-cadherin"
],
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[
171,
181
]
],
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},
{
"id": "BioInfer.d53.s0.e4",
"type": "Gene/protein/RNA",
"text": [
"beta-catenin"
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12,
24
]
],
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},
{
"id": "BioInfer.d53.s0.e5",
"type": "Individual_protein",
"text": [
"alpha-catenin"
],
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[
89,
102
]
],
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},
{
"id": "BioInfer.d53.s0.e6",
"type": "Individual_protein",
"text": [
"E-cadherin"
],
"offsets": [
[
122,
132
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d53.s0.i0",
"type": "PPI",
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"arg2_id": "BioInfer.d53.s0.e5",
"normalized": []
},
{
"id": "BioInfer.d53.s0.i1",
"type": "PPI",
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"arg2_id": "BioInfer.d53.s0.e6",
"normalized": []
},
{
"id": "BioInfer.d53.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d53.s0.e2",
"arg2_id": "BioInfer.d53.s0.e3",
"normalized": []
},
{
"id": "BioInfer.d53.s0.i3",
"type": "PPI",
"arg1_id": "BioInfer.d53.s0.e5",
"arg2_id": "BioInfer.d53.s0.e6",
"normalized": []
}
] |
83 | BioInfer.d55.s0 | [
{
"id": "BioInfer.d55.s0__text",
"type": "Sentence",
"text": [
"Analysis of profilin: actin crystals reveals an extensive intermolecular network, rather than a discrete \"monomeric complex\", comprising stacked actin ribbons held in place by columns of profilin molecules, wedged in between neighboring actin subunits and running perpendicular to the ribbons."
],
"offsets": [
[
0,
293
]
]
}
] | [
{
"id": "BioInfer.d55.s0.e0",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
12,
20
]
],
"normalized": []
},
{
"id": "BioInfer.d55.s0.e1",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
187,
195
]
],
"normalized": []
},
{
"id": "BioInfer.d55.s0.e2",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
145,
150
]
],
"normalized": []
},
{
"id": "BioInfer.d55.s0.e3",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
22,
27
]
],
"normalized": []
},
{
"id": "BioInfer.d55.s0.e4",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
237,
242
]
],
"normalized": []
}
] | [] | [] | [] |
84 | BioInfer.d55.s1 | [
{
"id": "BioInfer.d55.s1__text",
"type": "Sentence",
"text": [
"Molecular packing in profilin: actin crystals and its implications."
],
"offsets": [
[
0,
67
]
]
}
] | [
{
"id": "BioInfer.d55.s1.e0",
"type": "Individual_protein",
"text": [
"profilin"
],
"offsets": [
[
21,
29
]
],
"normalized": []
},
{
"id": "BioInfer.d55.s1.e1",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
31,
36
]
],
"normalized": []
}
] | [] | [] | [] |
85 | BioInfer.d56.s0 | [
{
"id": "BioInfer.d56.s0__text",
"type": "Sentence",
"text": [
"Analysis of changes in state suggests that SIR1 protein has a role in the establishment but not the maintenance of repression of silent mating type genes, whereas SIR2, SIR3, and SIR4 are required for maintenance."
],
"offsets": [
[
0,
213
]
]
}
] | [
{
"id": "BioInfer.d56.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"SIR2"
],
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163,
167
]
],
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},
{
"id": "BioInfer.d56.s0.e1",
"type": "Gene/protein/RNA",
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"SIR4"
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179,
183
]
],
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},
{
"id": "BioInfer.d56.s0.e2",
"type": "Gene/protein/RNA",
"text": [
"SIR1"
],
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43,
47
]
],
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},
{
"id": "BioInfer.d56.s0.e3",
"type": "Gene/protein/RNA",
"text": [
"SIR3"
],
"offsets": [
[
169,
173
]
],
"normalized": []
}
] | [] | [] | [] |
86 | BioInfer.d57.s0 | [
{
"id": "BioInfer.d57.s0__text",
"type": "Sentence",
"text": [
"Analysis of the formation of the calf spleen complex in the presence of varying concentrations of divalent cations gave evidence for the presence of a high-affinity divalent-cation-binding site on the spleen actin (beta, gamma) which appears to regulate the interaction with profilin."
],
"offsets": [
[
0,
284
]
]
}
] | [
{
"id": "BioInfer.d57.s0.e0",
"type": "Individual_protein",
"text": [
"profilin"
],
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275,
283
]
],
"normalized": []
},
{
"id": "BioInfer.d57.s0.e1",
"type": "Individual_protein",
"text": [
"spleen actin",
"gamma"
],
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[
201,
213
],
[
221,
226
]
],
"normalized": []
},
{
"id": "BioInfer.d57.s0.e2",
"type": "Individual_protein",
"text": [
"spleen actin",
"beta"
],
"offsets": [
[
201,
213
],
[
215,
219
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d57.s0.i0",
"type": "PPI",
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"arg2_id": "BioInfer.d57.s0.e1",
"normalized": []
},
{
"id": "BioInfer.d57.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d57.s0.e0",
"arg2_id": "BioInfer.d57.s0.e2",
"normalized": []
}
] |
87 | BioInfer.d57.s1 | [
{
"id": "BioInfer.d57.s1__text",
"type": "Sentence",
"text": [
"The interaction between calf spleen profilin and actin depends critically on the status of the C-terminus of the actin, and in the case of profilin, the C-terminus is of great importance for the physiochemical behaviour of the protein."
],
"offsets": [
[
0,
235
]
]
}
] | [
{
"id": "BioInfer.d57.s1.e0",
"type": "Gene/protein/RNA",
"text": [
"profilin"
],
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139,
147
]
],
"normalized": []
},
{
"id": "BioInfer.d57.s1.e1",
"type": "Individual_protein",
"text": [
"actin"
],
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113,
118
]
],
"normalized": []
},
{
"id": "BioInfer.d57.s1.e2",
"type": "Individual_protein",
"text": [
"spleen",
"actin"
],
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[
29,
35
],
[
49,
54
]
],
"normalized": []
},
{
"id": "BioInfer.d57.s1.e3",
"type": "Individual_protein",
"text": [
"spleen profilin"
],
"offsets": [
[
29,
44
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d57.s1.i0",
"type": "PPI",
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"arg2_id": "BioInfer.d57.s1.e2",
"normalized": []
},
{
"id": "BioInfer.d57.s1.i1",
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"arg2_id": "BioInfer.d57.s1.e3",
"normalized": []
},
{
"id": "BioInfer.d57.s1.i2",
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"arg1_id": "BioInfer.d57.s1.e2",
"arg2_id": "BioInfer.d57.s1.e3",
"normalized": []
}
] |
88 | BioInfer.d58.s0 | [
{
"id": "BioInfer.d58.s0__text",
"type": "Sentence",
"text": [
"Analysis of the u.v. absorbance and far-u.v. circular dichroism spectra of profilin and actin did not reveal any major changes in the conformation of the proteins accompanying the modifications at the C-terminal ends."
],
"offsets": [
[
0,
217
]
]
}
] | [
{
"id": "BioInfer.d58.s0.e0",
"type": "Gene/protein/RNA",
"text": [
"profilin"
],
"offsets": [
[
75,
83
]
],
"normalized": []
},
{
"id": "BioInfer.d58.s0.e1",
"type": "Gene/protein/RNA",
"text": [
"actin"
],
"offsets": [
[
88,
93
]
],
"normalized": []
}
] | [] | [] | [] |
89 | BioInfer.d59.s0 | [
{
"id": "BioInfer.d59.s0__text",
"type": "Sentence",
"text": [
"Analysis of this product by peptide mapping (Sutoh (1982) Biochemistry 21, 3654-3661) showed that cofilin was cross-linked with the N-terminal segment of actin containing residues 1-12."
],
"offsets": [
[
0,
185
]
]
}
] | [
{
"id": "BioInfer.d59.s0.e0",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
154,
159
]
],
"normalized": []
},
{
"id": "BioInfer.d59.s0.e1",
"type": "Individual_protein",
"text": [
"cofilin"
],
"offsets": [
[
98,
105
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d59.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d59.s0.e0",
"arg2_id": "BioInfer.d59.s0.e1",
"normalized": []
}
] |
90 | BioInfer.d59.s1 | [
{
"id": "BioInfer.d59.s1__text",
"type": "Sentence",
"text": [
"Purification of cofilin, a 21,000 molecular weight actin-binding protein, from porcine kidney and identification of the cofilin-binding site in the actin sequence."
],
"offsets": [
[
0,
163
]
]
}
] | [
{
"id": "BioInfer.d59.s1.e0",
"type": "Individual_protein",
"text": [
"actin"
],
"offsets": [
[
148,
153
]
],
"normalized": []
},
{
"id": "BioInfer.d59.s1.e1",
"type": "Individual_protein",
"text": [
"cofilin"
],
"offsets": [
[
120,
127
]
],
"normalized": []
},
{
"id": "BioInfer.d59.s1.e2",
"type": "Protein_family_or_group",
"text": [
"actin-binding protein"
],
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[
51,
72
]
],
"normalized": []
},
{
"id": "BioInfer.d59.s1.e3",
"type": "Individual_protein",
"text": [
"cofilin"
],
"offsets": [
[
16,
23
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d59.s1.i0",
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"arg2_id": "BioInfer.d59.s1.e1",
"normalized": []
},
{
"id": "BioInfer.d59.s1.i1",
"type": "PPI",
"arg1_id": "BioInfer.d59.s1.e2",
"arg2_id": "BioInfer.d59.s1.e3",
"normalized": []
}
] |
91 | BioInfer.d60.s0 | [
{
"id": "BioInfer.d60.s0__text",
"type": "Sentence",
"text": [
"Analysis of V3, a hamster equivalent of SCID, indicates that the protein level increases of RAD51 and RAD52 from G0 to G1/S/G2 do not require DNA-PK."
],
"offsets": [
[
0,
149
]
]
}
] | [
{
"id": "BioInfer.d60.s0.e0",
"type": "Individual_protein",
"text": [
"DNA-PK"
],
"offsets": [
[
142,
148
]
],
"normalized": []
},
{
"id": "BioInfer.d60.s0.e1",
"type": "Gene",
"text": [
"RAD51"
],
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[
92,
97
]
],
"normalized": []
},
{
"id": "BioInfer.d60.s0.e2",
"type": "Gene",
"text": [
"RAD52"
],
"offsets": [
[
102,
107
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d60.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d60.s0.e0",
"arg2_id": "BioInfer.d60.s0.e1",
"normalized": []
},
{
"id": "BioInfer.d60.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d60.s0.e0",
"arg2_id": "BioInfer.d60.s0.e2",
"normalized": []
}
] |
92 | BioInfer.d60.s1 | [
{
"id": "BioInfer.d60.s1__text",
"type": "Sentence",
"text": [
"In this study, cell cycle-dependent expression of human and rodent RAD51 and RAD52 proteins was monitored using two approaches."
],
"offsets": [
[
0,
127
]
]
}
] | [
{
"id": "BioInfer.d60.s1.e0",
"type": "Gene/protein/RNA",
"text": [
"RAD52"
],
"offsets": [
[
77,
82
]
],
"normalized": []
},
{
"id": "BioInfer.d60.s1.e1",
"type": "Gene/protein/RNA",
"text": [
"RAD51"
],
"offsets": [
[
67,
72
]
],
"normalized": []
}
] | [] | [] | [] |
93 | BioInfer.d61.s0 | [
{
"id": "BioInfer.d61.s0__text",
"type": "Sentence",
"text": [
"Analysis of various truncated alpha-catenin molecules revealed that amino-terminal residues 48-163 are able to bind to beta-catenin and plakoglobin."
],
"offsets": [
[
0,
148
]
]
}
] | [
{
"id": "BioInfer.d61.s0.e0",
"type": "Individual_protein",
"text": [
"plakoglobin"
],
"offsets": [
[
136,
147
]
],
"normalized": []
},
{
"id": "BioInfer.d61.s0.e1",
"type": "Individual_protein",
"text": [
"beta-catenin"
],
"offsets": [
[
119,
131
]
],
"normalized": []
},
{
"id": "BioInfer.d61.s0.e2",
"type": "Individual_protein",
"text": [
"alpha-catenin"
],
"offsets": [
[
30,
43
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d61.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d61.s0.e0",
"arg2_id": "BioInfer.d61.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d61.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d61.s0.e1",
"arg2_id": "BioInfer.d61.s0.e2",
"normalized": []
}
] |
94 | BioInfer.d61.s1 | [
{
"id": "BioInfer.d61.s1__text",
"type": "Sentence",
"text": [
"Consistent with the observation that beta-catenin and plakoglobin bind to the same region of alpha-catenin, beta-catenin competed with the binding of plakoglobin to alpha-catenin and vice versa."
],
"offsets": [
[
0,
194
]
]
}
] | [
{
"id": "BioInfer.d61.s1.e0",
"type": "Individual_protein",
"text": [
"alpha-catenin"
],
"offsets": [
[
93,
106
]
],
"normalized": []
},
{
"id": "BioInfer.d61.s1.e1",
"type": "Individual_protein",
"text": [
"alpha-catenin"
],
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[
165,
178
]
],
"normalized": []
},
{
"id": "BioInfer.d61.s1.e2",
"type": "Individual_protein",
"text": [
"beta-catenin"
],
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[
108,
120
]
],
"normalized": []
},
{
"id": "BioInfer.d61.s1.e3",
"type": "Individual_protein",
"text": [
"plakoglobin"
],
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[
150,
161
]
],
"normalized": []
},
{
"id": "BioInfer.d61.s1.e4",
"type": "Individual_protein",
"text": [
"plakoglobin"
],
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[
54,
65
]
],
"normalized": []
},
{
"id": "BioInfer.d61.s1.e5",
"type": "Individual_protein",
"text": [
"beta-catenin"
],
"offsets": [
[
37,
49
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d61.s1.i0",
"type": "PPI",
"arg1_id": "BioInfer.d61.s1.e0",
"arg2_id": "BioInfer.d61.s1.e4",
"normalized": []
},
{
"id": "BioInfer.d61.s1.i1",
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"arg1_id": "BioInfer.d61.s1.e0",
"arg2_id": "BioInfer.d61.s1.e5",
"normalized": []
},
{
"id": "BioInfer.d61.s1.i2",
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"arg2_id": "BioInfer.d61.s1.e2",
"normalized": []
},
{
"id": "BioInfer.d61.s1.i3",
"type": "PPI",
"arg1_id": "BioInfer.d61.s1.e1",
"arg2_id": "BioInfer.d61.s1.e3",
"normalized": []
}
] |
95 | BioInfer.d61.s2 | [
{
"id": "BioInfer.d61.s2__text",
"type": "Sentence",
"text": [
"Using an in vitro assay system involving bacterially expressed proteins, we localized a region in alpha-catenin required for molecular interaction with beta-catenin and plakoglobin."
],
"offsets": [
[
0,
181
]
]
}
] | [
{
"id": "BioInfer.d61.s2.e0",
"type": "Individual_protein",
"text": [
"beta-catenin"
],
"offsets": [
[
152,
164
]
],
"normalized": []
},
{
"id": "BioInfer.d61.s2.e1",
"type": "Individual_protein",
"text": [
"plakoglobin"
],
"offsets": [
[
169,
180
]
],
"normalized": []
},
{
"id": "BioInfer.d61.s2.e2",
"type": "Individual_protein",
"text": [
"alpha-catenin"
],
"offsets": [
[
98,
111
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d61.s2.i0",
"type": "PPI",
"arg1_id": "BioInfer.d61.s2.e0",
"arg2_id": "BioInfer.d61.s2.e2",
"normalized": []
},
{
"id": "BioInfer.d61.s2.i1",
"type": "PPI",
"arg1_id": "BioInfer.d61.s2.e1",
"arg2_id": "BioInfer.d61.s2.e2",
"normalized": []
}
] |
96 | BioInfer.d61.s3 | [
{
"id": "BioInfer.d61.s3__text",
"type": "Sentence",
"text": [
"When transfected into L cells expressing E-cadherin, the amino-terminal region of alpha-catenin (from residue 1 to 226) formed complexes with beta-catenin supporting the in vitro binding experiment results."
],
"offsets": [
[
0,
206
]
]
}
] | [
{
"id": "BioInfer.d61.s3.e0",
"type": "Individual_protein",
"text": [
"alpha-catenin"
],
"offsets": [
[
82,
95
]
],
"normalized": []
},
{
"id": "BioInfer.d61.s3.e1",
"type": "Gene/protein/RNA",
"text": [
"E-cadherin"
],
"offsets": [
[
41,
51
]
],
"normalized": []
},
{
"id": "BioInfer.d61.s3.e2",
"type": "Individual_protein",
"text": [
"beta-catenin"
],
"offsets": [
[
142,
154
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d61.s3.i0",
"type": "PPI",
"arg1_id": "BioInfer.d61.s3.e0",
"arg2_id": "BioInfer.d61.s3.e2",
"normalized": []
}
] |
97 | BioInfer.d62.s0 | [
{
"id": "BioInfer.d62.s0__text",
"type": "Sentence",
"text": [
"An assembly of the UL5 and UL52 subunits retains both enzymic activities, and the UL8 protein has been implicated in modulating these functions, facilitating efficient nuclear uptake of the complex and interacting with other viral DNA replication proteins."
],
"offsets": [
[
0,
256
]
]
}
] | [
{
"id": "BioInfer.d62.s0.e0",
"type": "Individual_protein",
"text": [
"UL52"
],
"offsets": [
[
27,
31
]
],
"normalized": []
},
{
"id": "BioInfer.d62.s0.e1",
"type": "Individual_protein",
"text": [
"UL5"
],
"offsets": [
[
19,
22
]
],
"normalized": []
},
{
"id": "BioInfer.d62.s0.e2",
"type": "Individual_protein",
"text": [
"UL8"
],
"offsets": [
[
82,
85
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d62.s0.i0",
"type": "PPI",
"arg1_id": "BioInfer.d62.s0.e0",
"arg2_id": "BioInfer.d62.s0.e1",
"normalized": []
},
{
"id": "BioInfer.d62.s0.i1",
"type": "PPI",
"arg1_id": "BioInfer.d62.s0.e0",
"arg2_id": "BioInfer.d62.s0.e2",
"normalized": []
},
{
"id": "BioInfer.d62.s0.i2",
"type": "PPI",
"arg1_id": "BioInfer.d62.s0.e1",
"arg2_id": "BioInfer.d62.s0.e2",
"normalized": []
}
] |
98 | BioInfer.d62.s1 | [
{
"id": "BioInfer.d62.s1__text",
"type": "Sentence",
"text": [
"Deletion mutants of the herpes simplex virus type 1 UL8 protein: effect on DNA synthesis and ability to interact with and influence the intracellular localization of the UL5 and UL52 proteins."
],
"offsets": [
[
0,
192
]
]
}
] | [
{
"id": "BioInfer.d62.s1.e0",
"type": "Individual_protein",
"text": [
"UL52"
],
"offsets": [
[
178,
182
]
],
"normalized": []
},
{
"id": "BioInfer.d62.s1.e1",
"type": "Individual_protein",
"text": [
"UL5"
],
"offsets": [
[
170,
173
]
],
"normalized": []
},
{
"id": "BioInfer.d62.s1.e2",
"type": "Individual_protein",
"text": [
"UL8"
],
"offsets": [
[
52,
55
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d62.s1.i0",
"type": "PPI",
"arg1_id": "BioInfer.d62.s1.e0",
"arg2_id": "BioInfer.d62.s1.e2",
"normalized": []
},
{
"id": "BioInfer.d62.s1.i1",
"type": "PPI",
"arg1_id": "BioInfer.d62.s1.e1",
"arg2_id": "BioInfer.d62.s1.e2",
"normalized": []
}
] |
99 | BioInfer.d62.s2 | [
{
"id": "BioInfer.d62.s2__text",
"type": "Sentence",
"text": [
"The herpes simplex virus type 1 (HSV-1) helicase-primase, an essential component of the viral DNA replication machinery, is a trimeric complex of the virus-coded UL5, UL8, and UL52 proteins."
],
"offsets": [
[
0,
190
]
]
}
] | [
{
"id": "BioInfer.d62.s2.e0",
"type": "Protein_complex",
"text": [
"helicase-primase"
],
"offsets": [
[
40,
56
]
],
"normalized": []
},
{
"id": "BioInfer.d62.s2.e1",
"type": "Individual_protein",
"text": [
"UL5"
],
"offsets": [
[
162,
165
]
],
"normalized": []
},
{
"id": "BioInfer.d62.s2.e2",
"type": "Individual_protein",
"text": [
"UL8"
],
"offsets": [
[
167,
170
]
],
"normalized": []
},
{
"id": "BioInfer.d62.s2.e3",
"type": "Individual_protein",
"text": [
"UL52"
],
"offsets": [
[
176,
180
]
],
"normalized": []
}
] | [] | [] | [
{
"id": "BioInfer.d62.s2.i0",
"type": "PPI",
"arg1_id": "BioInfer.d62.s2.e0",
"arg2_id": "BioInfer.d62.s2.e1",
"normalized": []
},
{
"id": "BioInfer.d62.s2.i1",
"type": "PPI",
"arg1_id": "BioInfer.d62.s2.e0",
"arg2_id": "BioInfer.d62.s2.e2",
"normalized": []
},
{
"id": "BioInfer.d62.s2.i2",
"type": "PPI",
"arg1_id": "BioInfer.d62.s2.e0",
"arg2_id": "BioInfer.d62.s2.e3",
"normalized": []
},
{
"id": "BioInfer.d62.s2.i3",
"type": "PPI",
"arg1_id": "BioInfer.d62.s2.e1",
"arg2_id": "BioInfer.d62.s2.e2",
"normalized": []
},
{
"id": "BioInfer.d62.s2.i4",
"type": "PPI",
"arg1_id": "BioInfer.d62.s2.e1",
"arg2_id": "BioInfer.d62.s2.e3",
"normalized": []
},
{
"id": "BioInfer.d62.s2.i5",
"type": "PPI",
"arg1_id": "BioInfer.d62.s2.e2",
"arg2_id": "BioInfer.d62.s2.e3",
"normalized": []
}
] |
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Dataset Card for BioInfer
A corpus targeted at protein, gene, and RNA relationships which serves as a resource for the development of information extraction systems and their components such as parsers and domain analyzers. Currently, the corpus contains 1100 sentences from abstracts of biomedical research articles annotated for relationships, named entities, as well as syntactic dependencies.
Citation Information
@article{pyysalo2007bioinfer,
title = {BioInfer: a corpus for information extraction in the biomedical domain},
author = {
Pyysalo, Sampo and Ginter, Filip and Heimonen, Juho and Bj{"o}rne, Jari
and Boberg, Jorma and J{"a}rvinen, Jouni and Salakoski, Tapio
},
year = 2007,
journal = {BMC bioinformatics},
publisher = {BioMed Central},
volume = 8,
number = 1,
pages = {1--24}
}
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