Datasets:

bigbio

/

bioinfer

like 3

[ { "id": "BioInfer.d232.s1__text", "type": "Sentence", "text": [ "We find that heterozygotes for actin (Act88F) or myosin heavy chain (Mhc36B) null alleles have complex myofibrillar defects, whereas Mhc36B-/+; Act88F-/+ double heterozygotes have nearly normal myofibrils." ], "offsets": [ [ 0, 205 ] ] } ]

[ { "id": "BioInfer.d232.s1.e0", "type": "Gene/protein/RNA", "text": [ "Act88F" ], "offsets": [ [ 144, 150 ] ], "normalized": [] }, { "id": "BioInfer.d232.s1.e1", "type": "Individual_protein", "text": [ "Mhc36B" ], "offsets": [ [ 69, 75 ] ], "normalized": [] }, { "id": "BioInfer.d232.s1.e2", "type": "Individual_protein", "text": [ "myosin heavy chain" ], "offsets": [ [ 49, 67 ] ], "normalized": [] }, { "id": "BioInfer.d232.s1.e3", "type": "Individual_protein", "text": [ "Act88F" ], "offsets": [ [ 38, 44 ] ], "normalized": [] }, { "id": "BioInfer.d232.s1.e4", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 31, 36 ] ], "normalized": [] }, { "id": "BioInfer.d232.s1.e5", "type": "Gene/protein/RNA", "text": [ "Mhc36B" ], "offsets": [ [ 133, 139 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d233.s0__text", "type": "Sentence", "text": [ "Germline mutations in several members of these families, MSH2, MSH6, MLH1, and PMS2, but not MSH3, are responsible for hereditary non-polyposis colorectal cancer." ], "offsets": [ [ 0, 162 ] ] } ]

[ { "id": "BioInfer.d233.s0.e0", "type": "Gene/protein/RNA", "text": [ "MSH3" ], "offsets": [ [ 93, 97 ] ], "normalized": [] }, { "id": "BioInfer.d233.s0.e1", "type": "Gene/protein/RNA", "text": [ "MSH6" ], "offsets": [ [ 63, 67 ] ], "normalized": [] }, { "id": "BioInfer.d233.s0.e2", "type": "Gene/protein/RNA", "text": [ "MLH1" ], "offsets": [ [ 69, 73 ] ], "normalized": [] }, { "id": "BioInfer.d233.s0.e3", "type": "Gene/protein/RNA", "text": [ "MSH2" ], "offsets": [ [ 57, 61 ] ], "normalized": [] }, { "id": "BioInfer.d233.s0.e4", "type": "Gene/protein/RNA", "text": [ "PMS2" ], "offsets": [ [ 79, 83 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d234.s0__text", "type": "Sentence", "text": [ "Glutathione S-transferase pull-down performed with Tax deletion mutants and peptide competition have localized the site in Tax critical for binding CBP/p300 to a highly protease-sensitive region around amino acid residues 81 to 95 (81QRTSKTLKVLTPPIT95) which lies between the domains previously proposed to be important for CREB binding and Tax subunit dimerization." ], "offsets": [ [ 0, 366 ] ] } ]

[ { "id": "BioInfer.d234.s0.e0", "type": "Individual_protein", "text": [ "p300" ], "offsets": [ [ 152, 156 ] ], "normalized": [] }, { "id": "BioInfer.d234.s0.e1", "type": "Individual_protein", "text": [ "Tax" ], "offsets": [ [ 123, 126 ] ], "normalized": [] }, { "id": "BioInfer.d234.s0.e2", "type": "Individual_protein", "text": [ "CBP" ], "offsets": [ [ 148, 151 ] ], "normalized": [] }, { "id": "BioInfer.d234.s0.e3", "type": "Individual_protein", "text": [ "CREB" ], "offsets": [ [ 324, 328 ] ], "normalized": [] }, { "id": "BioInfer.d234.s0.e4", "type": "Gene/protein/RNA", "text": [ "Glutathione S-transferase" ], "offsets": [ [ 0, 25 ] ], "normalized": [] }, { "id": "BioInfer.d234.s0.e5", "type": "Individual_protein", "text": [ "Tax" ], "offsets": [ [ 341, 344 ] ], "normalized": [] }, { "id": "BioInfer.d234.s0.e6", "type": "Gene/protein/RNA", "text": [ "Tax" ], "offsets": [ [ 51, 54 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d236.s0__text", "type": "Sentence", "text": [ "Hence, we conclude that in its dimeric form, which is used in actin and lipid binding, talin is a dumbbell-shaped molecule built of two antiparallel subunits." ], "offsets": [ [ 0, 158 ] ] } ]

[ { "id": "BioInfer.d236.s0.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 62, 67 ] ], "normalized": [] }, { "id": "BioInfer.d236.s0.e1", "type": "Individual_protein", "text": [ "talin" ], "offsets": [ [ 87, 92 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d236.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d236.s0.e0", "arg2_id": "BioInfer.d236.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d236.s1__text", "type": "Sentence", "text": [ "The talin dimer, which is crucial for actin and lipid binding, is built of a backbone containing the 200 kDa rod portions, at both ends of which a 47 kDa globular domain is attached." ], "offsets": [ [ 0, 182 ] ] } ]

[ { "id": "BioInfer.d236.s1.e0", "type": "Individual_protein", "text": [ "talin" ], "offsets": [ [ 4, 9 ] ], "normalized": [] }, { "id": "BioInfer.d236.s1.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 38, 43 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d236.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d236.s1.e0", "arg2_id": "BioInfer.d236.s1.e1", "normalized": [] } ]

[ { "id": "BioInfer.d237.s0__text", "type": "Sentence", "text": [ "Here, specific interactions between human RAD51 and RAD52 proteins are demonstrated both in vivo, using the yeast two-hybrid system and immunoprecipitation of insect cells co-infected with RAD51 and RAD52 recombinant viruses, and in vitro, using affinity chromatography with purified recombinant proteins." ], "offsets": [ [ 0, 305 ] ] } ]

[ { "id": "BioInfer.d237.s0.e0", "type": "Gene/protein/RNA", "text": [ "RAD52" ], "offsets": [ [ 199, 204 ] ], "normalized": [] }, { "id": "BioInfer.d237.s0.e1", "type": "Gene/protein/RNA", "text": [ "RAD51" ], "offsets": [ [ 189, 194 ] ], "normalized": [] }, { "id": "BioInfer.d237.s0.e2", "type": "Gene", "text": [ "RAD52" ], "offsets": [ [ 52, 57 ] ], "normalized": [] }, { "id": "BioInfer.d237.s0.e3", "type": "Gene", "text": [ "RAD51" ], "offsets": [ [ 42, 47 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d237.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d237.s0.e2", "arg2_id": "BioInfer.d237.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d237.s1__text", "type": "Sentence", "text": [ "Interaction of the yeast RAD51 and RAD52 proteins plays a crucial role in yeast DNA homologous recombination and DNA double-strand break repair." ], "offsets": [ [ 0, 144 ] ] } ]

[ { "id": "BioInfer.d237.s1.e0", "type": "Individual_protein", "text": [ "RAD51" ], "offsets": [ [ 25, 30 ] ], "normalized": [] }, { "id": "BioInfer.d237.s1.e1", "type": "Individual_protein", "text": [ "RAD52" ], "offsets": [ [ 35, 40 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d237.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d237.s1.e0", "arg2_id": "BioInfer.d237.s1.e1", "normalized": [] } ]

[ { "id": "BioInfer.d237.s2__text", "type": "Sentence", "text": [ "Specific interactions between the human RAD51 and RAD52 proteins." ], "offsets": [ [ 0, 65 ] ] } ]

[ { "id": "BioInfer.d237.s2.e0", "type": "Individual_protein", "text": [ "RAD52" ], "offsets": [ [ 50, 55 ] ], "normalized": [] }, { "id": "BioInfer.d237.s2.e1", "type": "Individual_protein", "text": [ "RAD51" ], "offsets": [ [ 40, 45 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d237.s2.i0", "type": "PPI", "arg1_id": "BioInfer.d237.s2.e0", "arg2_id": "BioInfer.d237.s2.e1", "normalized": [] } ]

[ { "id": "BioInfer.d237.s3__text", "type": "Sentence", "text": [ "The RAD51-interacting region (amino acids 291-330) of the human RAD52 protein shows no homology with the yeast RAD52 protein, indicating that the interaction between RAD51 and RAD52 is species-specific." ], "offsets": [ [ 0, 202 ] ] } ]

[ { "id": "BioInfer.d237.s3.e0", "type": "Individual_protein", "text": [ "RAD52" ], "offsets": [ [ 111, 116 ] ], "normalized": [] }, { "id": "BioInfer.d237.s3.e1", "type": "Individual_protein", "text": [ "RAD52" ], "offsets": [ [ 64, 69 ] ], "normalized": [] }, { "id": "BioInfer.d237.s3.e2", "type": "Individual_protein", "text": [ "RAD51" ], "offsets": [ [ 166, 171 ] ], "normalized": [] }, { "id": "BioInfer.d237.s3.e3", "type": "Individual_protein", "text": [ "RAD52" ], "offsets": [ [ 176, 181 ] ], "normalized": [] }, { "id": "BioInfer.d237.s3.e4", "type": "Individual_protein", "text": [ "RAD51" ], "offsets": [ [ 4, 9 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d237.s3.i0", "type": "PPI", "arg1_id": "BioInfer.d237.s3.e0", "arg2_id": "BioInfer.d237.s3.e1", "normalized": [] }, { "id": "BioInfer.d237.s3.i1", "type": "PPI", "arg1_id": "BioInfer.d237.s3.e1", "arg2_id": "BioInfer.d237.s3.e4", "normalized": [] }, { "id": "BioInfer.d237.s3.i2", "type": "PPI", "arg1_id": "BioInfer.d237.s3.e2", "arg2_id": "BioInfer.d237.s3.e3", "normalized": [] } ]

[ { "id": "BioInfer.d237.s4__text", "type": "Sentence", "text": [ "These results suggest that RAD52 may modulate the catalytic activities of RAD51 protein such as homologous pairing and strand exchange through a direct physical interaction." ], "offsets": [ [ 0, 173 ] ] } ]

[ { "id": "BioInfer.d237.s4.e0", "type": "Gene", "text": [ "RAD52" ], "offsets": [ [ 27, 32 ] ], "normalized": [] }, { "id": "BioInfer.d237.s4.e1", "type": "Gene", "text": [ "RAD51" ], "offsets": [ [ 74, 79 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d237.s4.i0", "type": "PPI", "arg1_id": "BioInfer.d237.s4.e0", "arg2_id": "BioInfer.d237.s4.e1", "normalized": [] } ]

[ { "id": "BioInfer.d238.s0__text", "type": "Sentence", "text": [ "Here we demonstrate that accessory receptor triggering induces the transient association of cofilin with the actin cytoskeleton." ], "offsets": [ [ 0, 128 ] ] } ]

[ { "id": "BioInfer.d238.s0.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 109, 114 ] ], "normalized": [] }, { "id": "BioInfer.d238.s0.e1", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 92, 99 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d238.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d238.s0.e0", "arg2_id": "BioInfer.d238.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d238.s1__text", "type": "Sentence", "text": [ "Recently, we have shown that the small actin-depolymerizing protein cofilin represents a component of a co-stimulatory signaling pathway in human T cells." ], "offsets": [ [ 0, 154 ] ] } ]

[ { "id": "BioInfer.d238.s1.e0", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 68, 75 ] ], "normalized": [] }, { "id": "BioInfer.d238.s1.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 39, 44 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d238.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d238.s1.e0", "arg2_id": "BioInfer.d238.s1.e1", "normalized": [] } ]

[ { "id": "BioInfer.d238.s2__text", "type": "Sentence", "text": [ "These results suggest that cofilin provides an as yet missing link between functionally crucial T cell surface receptors and rearrangements of the actin cytoskeleton." ], "offsets": [ [ 0, 166 ] ] } ]

[ { "id": "BioInfer.d238.s2.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 147, 152 ] ], "normalized": [] }, { "id": "BioInfer.d238.s2.e1", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 27, 34 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d238.s2.i0", "type": "PPI", "arg1_id": "BioInfer.d238.s2.e0", "arg2_id": "BioInfer.d238.s2.e1", "normalized": [] } ]

[ { "id": "BioInfer.d239.s0__text", "type": "Sentence", "text": [ "Here we demonstrate that growth arrest and differentiation of NT2/D1 cells induced by HMBA involve increased expression of the cyclin-dependent kinase inhibitor p27, enhanced association of p27 with cyclin E/CDK2 complexes and suppression of kinase activity associated to cyclin E/CDK2 (but not to cyclin D3/CDK4)." ], "offsets": [ [ 0, 314 ] ] } ]

[ { "id": "BioInfer.d239.s0.e0", "type": "Individual_protein", "text": [ "CDK4" ], "offsets": [ [ 308, 312 ] ], "normalized": [] }, { "id": "BioInfer.d239.s0.e1", "type": "Individual_protein", "text": [ "p27" ], "offsets": [ [ 161, 164 ] ], "normalized": [] }, { "id": "BioInfer.d239.s0.e2", "type": "Individual_protein", "text": [ "CDK2" ], "offsets": [ [ 281, 285 ] ], "normalized": [] }, { "id": "BioInfer.d239.s0.e3", "type": "Protein_family_or_group", "text": [ "cyclin-dependent kinase inhibitor" ], "offsets": [ [ 127, 160 ] ], "normalized": [] }, { "id": "BioInfer.d239.s0.e4", "type": "Individual_protein", "text": [ "cyclin E" ], "offsets": [ [ 272, 280 ] ], "normalized": [] }, { "id": "BioInfer.d239.s0.e5", "type": "Individual_protein", "text": [ "CDK2" ], "offsets": [ [ 208, 212 ] ], "normalized": [] }, { "id": "BioInfer.d239.s0.e6", "type": "Individual_protein", "text": [ "cyclin D3" ], "offsets": [ [ 298, 307 ] ], "normalized": [] }, { "id": "BioInfer.d239.s0.e7", "type": "Individual_protein", "text": [ "cyclin E" ], "offsets": [ [ 199, 207 ] ], "normalized": [] }, { "id": "BioInfer.d239.s0.e8", "type": "Individual_protein", "text": [ "p27" ], "offsets": [ [ 190, 193 ] ], "normalized": [] }, { "id": "BioInfer.d239.s0.e9", "type": "Protein_family_or_group", "text": [ "kinase" ], "offsets": [ [ 242, 248 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d239.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d239.s0.e0", "arg2_id": "BioInfer.d239.s0.e6", "normalized": [] }, { "id": "BioInfer.d239.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d239.s0.e0", "arg2_id": "BioInfer.d239.s0.e9", "normalized": [] }, { "id": "BioInfer.d239.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d239.s0.e1", "arg2_id": "BioInfer.d239.s0.e3", "normalized": [] }, { "id": "BioInfer.d239.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d239.s0.e2", "arg2_id": "BioInfer.d239.s0.e4", "normalized": [] }, { "id": "BioInfer.d239.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d239.s0.e2", "arg2_id": "BioInfer.d239.s0.e9", "normalized": [] }, { "id": "BioInfer.d239.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d239.s0.e4", "arg2_id": "BioInfer.d239.s0.e9", "normalized": [] }, { "id": "BioInfer.d239.s0.i6", "type": "PPI", "arg1_id": "BioInfer.d239.s0.e5", "arg2_id": "BioInfer.d239.s0.e7", "normalized": [] }, { "id": "BioInfer.d239.s0.i7", "type": "PPI", "arg1_id": "BioInfer.d239.s0.e5", "arg2_id": "BioInfer.d239.s0.e8", "normalized": [] }, { "id": "BioInfer.d239.s0.i8", "type": "PPI", "arg1_id": "BioInfer.d239.s0.e6", "arg2_id": "BioInfer.d239.s0.e9", "normalized": [] }, { "id": "BioInfer.d239.s0.i9", "type": "PPI", "arg1_id": "BioInfer.d239.s0.e7", "arg2_id": "BioInfer.d239.s0.e8", "normalized": [] } ]

[ { "id": "BioInfer.d240.s0__text", "type": "Sentence", "text": [ "Here we demonstrate that type XIII collagen is concentrated in cultured skin fibroblasts and several other human mesenchymal cell lines in the focal adhesions at the ends of actin stress fibers, co-localizing with the known focal adhesion components talin and vinculin." ], "offsets": [ [ 0, 269 ] ] } ]

[ { "id": "BioInfer.d240.s0.e0", "type": "Individual_protein", "text": [ "type XIII collagen" ], "offsets": [ [ 25, 43 ] ], "normalized": [] }, { "id": "BioInfer.d240.s0.e1", "type": "Individual_protein", "text": [ "talin" ], "offsets": [ [ 250, 255 ] ], "normalized": [] }, { "id": "BioInfer.d240.s0.e2", "type": "Individual_protein", "text": [ "vinculin" ], "offsets": [ [ 260, 268 ] ], "normalized": [] }, { "id": "BioInfer.d240.s0.e3", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 174, 179 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d240.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d240.s0.e0", "arg2_id": "BioInfer.d240.s0.e1", "normalized": [] }, { "id": "BioInfer.d240.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d240.s0.e0", "arg2_id": "BioInfer.d240.s0.e2", "normalized": [] }, { "id": "BioInfer.d240.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d240.s0.e0", "arg2_id": "BioInfer.d240.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d241.s0__text", "type": "Sentence", "text": [ "Here, we describe proline-rich proteins involved in regulating actin polymerization and classify them according to their role in recruiting profilin to the membrane." ], "offsets": [ [ 0, 165 ] ] } ]

[ { "id": "BioInfer.d241.s0.e0", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 63, 68 ] ], "normalized": [] }, { "id": "BioInfer.d241.s0.e1", "type": "Gene/protein/RNA", "text": [ "profilin" ], "offsets": [ [ 140, 148 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d242.s0__text", "type": "Sentence", "text": [ "Here we describe the TNF-dependent activation of acid SMase (A-SMase) through the p55 TNF receptor-associated proteins TRADD and FADD." ], "offsets": [ [ 0, 134 ] ] } ]

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[ { "id": "BioInfer.d242.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d242.s0.e0", "arg2_id": "BioInfer.d242.s0.e3", "normalized": [] }, { "id": "BioInfer.d242.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d242.s0.e0", "arg2_id": "BioInfer.d242.s0.e5", "normalized": [] }, { "id": "BioInfer.d242.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d242.s0.e0", "arg2_id": "BioInfer.d242.s0.e6", "normalized": [] }, { "id": "BioInfer.d242.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d242.s0.e1", "arg2_id": "BioInfer.d242.s0.e3", "normalized": [] }, { "id": "BioInfer.d242.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d242.s0.e1", "arg2_id": "BioInfer.d242.s0.e5", "normalized": [] }, { "id": "BioInfer.d242.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d242.s0.e1", "arg2_id": "BioInfer.d242.s0.e6", "normalized": [] }, { "id": "BioInfer.d242.s0.i6", "type": "PPI", "arg1_id": "BioInfer.d242.s0.e2", "arg2_id": "BioInfer.d242.s0.e5", "normalized": [] }, { "id": "BioInfer.d242.s0.i7", "type": "PPI", "arg1_id": "BioInfer.d242.s0.e2", "arg2_id": "BioInfer.d242.s0.e6", "normalized": [] }, { "id": "BioInfer.d242.s0.i8", "type": "PPI", "arg1_id": "BioInfer.d242.s0.e3", "arg2_id": "BioInfer.d242.s0.e4", "normalized": [] } ]

[ { "id": "BioInfer.d242.s1__text", "type": "Sentence", "text": [ "TNF receptor death domain-associated proteins TRADD and FADD signal activation of acid sphingomyelinase." ], "offsets": [ [ 0, 104 ] ] } ]

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[ { "id": "BioInfer.d242.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d242.s1.e0", "arg2_id": "BioInfer.d242.s1.e1", "normalized": [] }, { "id": "BioInfer.d242.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d242.s1.e0", "arg2_id": "BioInfer.d242.s1.e3", "normalized": [] }, { "id": "BioInfer.d242.s1.i2", "type": "PPI", "arg1_id": "BioInfer.d242.s1.e1", "arg2_id": "BioInfer.d242.s1.e2", "normalized": [] }, { "id": "BioInfer.d242.s1.i3", "type": "PPI", "arg1_id": "BioInfer.d242.s1.e2", "arg2_id": "BioInfer.d242.s1.e3", "normalized": [] } ]

[ { "id": "BioInfer.d243.s0__text", "type": "Sentence", "text": [ "Here, we designed a genetic screen for mutant strains defective for filamentous growth (dfg) to identify novel targets of the filamentation signaling pathway, and we thereby identified 16 different genes, CDC39, STE12, TEC1, WHI3, NAB1, DBR1, CDC55, SRV2, TPM1, SPA2, BNI1, DFG5, DFG9, DFG10, BUD8 and DFG16, mutations that block filamentous growth." ], "offsets": [ [ 0, 349 ] ] } ]

[ { "id": "BioInfer.d243.s0.e0", "type": "Gene/protein/RNA", "text": [ "BUD8" ], "offsets": [ [ 293, 297 ] ], "normalized": [] }, { "id": "BioInfer.d243.s0.e1", "type": "Gene/protein/RNA", "text": [ "TEC1" ], "offsets": [ [ 219, 223 ] ], "normalized": [] }, { "id": "BioInfer.d243.s0.e2", "type": "Gene/protein/RNA", "text": [ "CDC39" ], "offsets": [ [ 205, 210 ] ], "normalized": [] }, { "id": "BioInfer.d243.s0.e3", "type": "Gene/protein/RNA", "text": [ "NAB1" ], "offsets": [ [ 231, 235 ] ], "normalized": [] }, { "id": "BioInfer.d243.s0.e4", "type": "Gene/protein/RNA", "text": [ "STE12" ], "offsets": [ [ 212, 217 ] ], "normalized": [] }, { "id": "BioInfer.d243.s0.e5", "type": "Gene/protein/RNA", "text": [ "CDC55" ], "offsets": [ [ 243, 248 ] ], "normalized": [] }, { "id": "BioInfer.d243.s0.e6", "type": "Gene/protein/RNA", "text": [ "WHI3" ], "offsets": [ [ 225, 229 ] ], "normalized": [] }, { "id": "BioInfer.d243.s0.e7", "type": "Gene/protein/RNA", "text": [ "TPM1" ], "offsets": [ [ 256, 260 ] ], "normalized": [] }, { "id": "BioInfer.d243.s0.e8", "type": "Gene/protein/RNA", "text": [ "DBR1" ], "offsets": [ [ 237, 241 ] ], "normalized": [] }, { "id": "BioInfer.d243.s0.e9", "type": "Gene/protein/RNA", "text": [ "BNI1" ], "offsets": [ [ 268, 272 ] ], "normalized": [] }, { "id": "BioInfer.d243.s0.e10", "type": "Gene/protein/RNA", "text": [ "DFG10" ], "offsets": [ [ 286, 291 ] ], "normalized": [] }, { "id": "BioInfer.d243.s0.e11", "type": "Gene/protein/RNA", "text": [ "DFG16" ], "offsets": [ [ 302, 307 ] ], "normalized": [] }, { "id": "BioInfer.d243.s0.e12", "type": "Gene/protein/RNA", "text": [ "DFG9" ], "offsets": [ [ 280, 284 ] ], "normalized": [] }, { "id": "BioInfer.d243.s0.e13", "type": "Gene/protein/RNA", "text": [ "SPA2" ], "offsets": [ [ 262, 266 ] ], "normalized": [] }, { "id": "BioInfer.d243.s0.e14", "type": "Gene/protein/RNA", "text": [ "SRV2" ], "offsets": [ [ 250, 254 ] ], "normalized": [] }, { "id": "BioInfer.d243.s0.e15", "type": "Gene/protein/RNA", "text": [ "DFG5" ], "offsets": [ [ 274, 278 ] ], "normalized": [] } ]

[]

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[ { "id": "BioInfer.d244.s0__text", "type": "Sentence", "text": [ "Here, we have detected a polypeptide in rat rod outer segments that is recognized by myosin heavy chain antibodies and was found to possess other characteristics of conventional non-muscle myosin heavy chain: it comigrates in SDS-PAGE with non-muscle myosin heavy chain; it associates with the cytoskeleton of rod outer segments in an ATP-sensitive manner; and it binds to purified actin filaments in the absence of ATP." ], "offsets": [ [ 0, 420 ] ] } ]

[ { "id": "BioInfer.d244.s0.e0", "type": "Gene/protein/RNA", "text": [ "non-muscle myosin heavy chain" ], "offsets": [ [ 240, 269 ] ], "normalized": [] }, { "id": "BioInfer.d244.s0.e1", "type": "Gene/protein/RNA", "text": [ "myosin heavy chain" ], "offsets": [ [ 85, 103 ] ], "normalized": [] }, { "id": "BioInfer.d244.s0.e2", "type": "Individual_protein", "text": [ "non-muscle myosin heavy chain" ], "offsets": [ [ 178, 207 ] ], "normalized": [] }, { "id": "BioInfer.d244.s0.e3", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 382, 387 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d244.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d244.s0.e2", "arg2_id": "BioInfer.d244.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d245.s0__text", "type": "Sentence", "text": [ "Here we have now identified the reciprocal complementary binding site in alpha-catenin which mediates its interaction with beta-catenin and plakoglobin." ], "offsets": [ [ 0, 152 ] ] } ]

[ { "id": "BioInfer.d245.s0.e0", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 73, 86 ] ], "normalized": [] }, { "id": "BioInfer.d245.s0.e1", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 123, 135 ] ], "normalized": [] }, { "id": "BioInfer.d245.s0.e2", "type": "Individual_protein", "text": [ "plakoglobin" ], "offsets": [ [ 140, 151 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d245.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d245.s0.e0", "arg2_id": "BioInfer.d245.s0.e1", "normalized": [] }, { "id": "BioInfer.d245.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d245.s0.e0", "arg2_id": "BioInfer.d245.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d245.s1__text", "type": "Sentence", "text": [ "It is well established that the cytoplasmic domain of E-cadherin binds either beta-catenin or plakoglobin, which both can assemble alpha-catenin into the complex." ], "offsets": [ [ 0, 162 ] ] } ]

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[ { "id": "BioInfer.d245.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d245.s1.e0", "arg2_id": "BioInfer.d245.s1.e1", "normalized": [] }, { "id": "BioInfer.d245.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d245.s1.e0", "arg2_id": "BioInfer.d245.s1.e3", "normalized": [] }, { "id": "BioInfer.d245.s1.i2", "type": "PPI", "arg1_id": "BioInfer.d245.s1.e1", "arg2_id": "BioInfer.d245.s1.e2", "normalized": [] }, { "id": "BioInfer.d245.s1.i3", "type": "PPI", "arg1_id": "BioInfer.d245.s1.e1", "arg2_id": "BioInfer.d245.s1.e3", "normalized": [] }, { "id": "BioInfer.d245.s1.i4", "type": "PPI", "arg1_id": "BioInfer.d245.s1.e2", "arg2_id": "BioInfer.d245.s1.e3", "normalized": [] } ]

[ { "id": "BioInfer.d245.s2__text", "type": "Sentence", "text": [ "Recently we have identified an alpha-catenin binding site in beta-catenin and plakoglobin and postulated, based on sequence analysis, that these protein-protein interactions are mediated by a hydrophobic interaction mechanism." ], "offsets": [ [ 0, 226 ] ] } ]

[ { "id": "BioInfer.d245.s2.e0", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 31, 44 ] ], "normalized": [] }, { "id": "BioInfer.d245.s2.e1", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 61, 73 ] ], "normalized": [] }, { "id": "BioInfer.d245.s2.e2", "type": "Individual_protein", "text": [ "plakoglobin" ], "offsets": [ [ 78, 89 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d245.s2.i0", "type": "PPI", "arg1_id": "BioInfer.d245.s2.e0", "arg2_id": "BioInfer.d245.s2.e1", "normalized": [] }, { "id": "BioInfer.d245.s2.i1", "type": "PPI", "arg1_id": "BioInfer.d245.s2.e0", "arg2_id": "BioInfer.d245.s2.e2", "normalized": [] } ]

[ { "id": "BioInfer.d246.s0__text", "type": "Sentence", "text": [ "Here we identify a pathway for the regulation of cofilin, a ubiquitous actin-binding protein that is essential for effective depolymerization of actin filaments." ], "offsets": [ [ 0, 161 ] ] } ]

[ { "id": "BioInfer.d246.s0.e0", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 49, 56 ] ], "normalized": [] }, { "id": "BioInfer.d246.s0.e1", "type": "Protein_family_or_group", "text": [ "actin-binding protein" ], "offsets": [ [ 71, 92 ] ], "normalized": [] }, { "id": "BioInfer.d246.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 145, 150 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d246.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d246.s0.e0", "arg2_id": "BioInfer.d246.s0.e1", "normalized": [] }, { "id": "BioInfer.d246.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d246.s0.e0", "arg2_id": "BioInfer.d246.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d246.s1__text", "type": "Sentence", "text": [ "Our results define a mechanism for the regulation of cofilin and hence of actin dynamics in vivo." ], "offsets": [ [ 0, 97 ] ] } ]

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[]

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[ { "id": "BioInfer.d246.s2__text", "type": "Sentence", "text": [ "Phosphorylation by LIM-kinase 1 inactivates cofilin, leading to accumulation of actin filaments." ], "offsets": [ [ 0, 96 ] ] } ]

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[]

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[ { "id": "BioInfer.d246.s2.i0", "type": "PPI", "arg1_id": "BioInfer.d246.s2.e0", "arg2_id": "BioInfer.d246.s2.e1", "normalized": [] }, { "id": "BioInfer.d246.s2.i1", "type": "PPI", "arg1_id": "BioInfer.d246.s2.e0", "arg2_id": "BioInfer.d246.s2.e2", "normalized": [] }, { "id": "BioInfer.d246.s2.i2", "type": "PPI", "arg1_id": "BioInfer.d246.s2.e1", "arg2_id": "BioInfer.d246.s2.e2", "normalized": [] } ]

[ { "id": "BioInfer.d246.s3__text", "type": "Sentence", "text": [ "Regulation of actin dynamics through phosphorylation of cofilin by LIM-kinase." ], "offsets": [ [ 0, 78 ] ] } ]

[ { "id": "BioInfer.d246.s3.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 14, 19 ] ], "normalized": [] }, { "id": "BioInfer.d246.s3.e1", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 56, 63 ] ], "normalized": [] }, { "id": "BioInfer.d246.s3.e2", "type": "Individual_protein", "text": [ "LIM-kinase" ], "offsets": [ [ 67, 77 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d246.s3.i0", "type": "PPI", "arg1_id": "BioInfer.d246.s3.e0", "arg2_id": "BioInfer.d246.s3.e1", "normalized": [] }, { "id": "BioInfer.d246.s3.i1", "type": "PPI", "arg1_id": "BioInfer.d246.s3.e0", "arg2_id": "BioInfer.d246.s3.e2", "normalized": [] }, { "id": "BioInfer.d246.s3.i2", "type": "PPI", "arg1_id": "BioInfer.d246.s3.e1", "arg2_id": "BioInfer.d246.s3.e2", "normalized": [] } ]

[ { "id": "BioInfer.d247.s0__text", "type": "Sentence", "text": [ "Here, we prepared a profilin mutant (H119E) defective in actin binding, but retaining the ability to bind to other proteins." ], "offsets": [ [ 0, 124 ] ] } ]

[ { "id": "BioInfer.d247.s0.e0", "type": "Individual_protein", "text": [ "profilin", "H119E" ], "offsets": [ [ 20, 28 ], [ 37, 42 ] ], "normalized": [] }, { "id": "BioInfer.d247.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 57, 62 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d247.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d247.s0.e0", "arg2_id": "BioInfer.d247.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d247.s1__text", "type": "Sentence", "text": [ "The essential role of profilin in the assembly of actin for microspike formation." ], "offsets": [ [ 0, 81 ] ] } ]

[ { "id": "BioInfer.d247.s1.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 50, 55 ] ], "normalized": [] }, { "id": "BioInfer.d247.s1.e1", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 22, 30 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d247.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d247.s1.e0", "arg2_id": "BioInfer.d247.s1.e1", "normalized": [] } ]

[ { "id": "BioInfer.d247.s2__text", "type": "Sentence", "text": [ "These findings provide the first evidence that profilin is a key molecule linking a signaling network to rapid actin polymerization in microspike formation." ], "offsets": [ [ 0, 156 ] ] } ]

[ { "id": "BioInfer.d247.s2.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 111, 116 ] ], "normalized": [] }, { "id": "BioInfer.d247.s2.e1", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 47, 55 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d247.s2.i0", "type": "PPI", "arg1_id": "BioInfer.d247.s2.e0", "arg2_id": "BioInfer.d247.s2.e1", "normalized": [] } ]

[ { "id": "BioInfer.d247.s3__text", "type": "Sentence", "text": [ "This mutant profilin I suppresses actin polymerization in microspike formation induced by N-WASP, the essential factor in microspike formation." ], "offsets": [ [ 0, 143 ] ] } ]

[ { "id": "BioInfer.d247.s3.e0", "type": "Individual_protein", "text": [ "profilin I" ], "offsets": [ [ 12, 22 ] ], "normalized": [] }, { "id": "BioInfer.d247.s3.e1", "type": "Individual_protein", "text": [ "N-WASP" ], "offsets": [ [ 90, 96 ] ], "normalized": [] }, { "id": "BioInfer.d247.s3.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 34, 39 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d247.s3.i0", "type": "PPI", "arg1_id": "BioInfer.d247.s3.e0", "arg2_id": "BioInfer.d247.s3.e1", "normalized": [] }, { "id": "BioInfer.d247.s3.i1", "type": "PPI", "arg1_id": "BioInfer.d247.s3.e0", "arg2_id": "BioInfer.d247.s3.e2", "normalized": [] }, { "id": "BioInfer.d247.s3.i2", "type": "PPI", "arg1_id": "BioInfer.d247.s3.e1", "arg2_id": "BioInfer.d247.s3.e2", "normalized": [] } ]

[ { "id": "BioInfer.d248.s0__text", "type": "Sentence", "text": [ "Here we report that p120 associates with a complex containing E-cadherin, alpha-catenin, beta-catenin, and plakoglobin." ], "offsets": [ [ 0, 119 ] ] } ]

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[ { "id": "BioInfer.d249.s0__text", "type": "Sentence", "text": [ "Here we report the functional importance of profilin in various actin-mediated morphological changes using H119E mutant profilin I, which is deficient only in actin binding." ], "offsets": [ [ 0, 173 ] ] } ]

[ { "id": "BioInfer.d249.s0.e0", "type": "Individual_protein", "text": [ "H119E", "profilin I" ], "offsets": [ [ 107, 112 ], [ 120, 130 ] ], "normalized": [] }, { "id": "BioInfer.d249.s0.e1", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 44, 52 ] ], "normalized": [] }, { "id": "BioInfer.d249.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 64, 69 ] ], "normalized": [] }, { "id": "BioInfer.d249.s0.e3", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 159, 164 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d249.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d249.s0.e0", "arg2_id": "BioInfer.d249.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d250.s0__text", "type": "Sentence", "text": [ "Here we show that cdc12p is a member of a family of proteins including Drosophila diaphanous, Saccharomyces cerevisiae BNI1, and S. pombe fus1, which are involved in cytokinesis or other actin-mediated processes." ], "offsets": [ [ 0, 212 ] ] } ]

[ { "id": "BioInfer.d250.s0.e0", "type": "Individual_protein", "text": [ "cdc12p" ], "offsets": [ [ 18, 24 ] ], "normalized": [] }, { "id": "BioInfer.d250.s0.e1", "type": "Individual_protein", "text": [ "fus1" ], "offsets": [ [ 138, 142 ] ], "normalized": [] }, { "id": "BioInfer.d250.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 187, 192 ] ], "normalized": [] }, { "id": "BioInfer.d250.s0.e3", "type": "Individual_protein", "text": [ "BNI1" ], "offsets": [ [ 119, 123 ] ], "normalized": [] }, { "id": "BioInfer.d250.s0.e4", "type": "Individual_protein", "text": [ "diaphanous" ], "offsets": [ [ 82, 92 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d251.s0__text", "type": "Sentence", "text": [ "Here, we show that EID-1 is a potent inhibitor of differentiation and link this activity to its ability to inhibit p300 (and the highly related molecule, CREB-binding protein, or CBP) histone acetylation activity." ], "offsets": [ [ 0, 213 ] ] } ]

[ { "id": "BioInfer.d251.s0.e0", "type": "Individual_protein", "text": [ "p300" ], "offsets": [ [ 115, 119 ] ], "normalized": [] }, { "id": "BioInfer.d251.s0.e1", "type": "Protein_family_or_group", "text": [ "histone" ], "offsets": [ [ 184, 191 ] ], "normalized": [] }, { "id": "BioInfer.d251.s0.e2", "type": "Individual_protein", "text": [ "CREB-binding protein" ], "offsets": [ [ 154, 174 ] ], "normalized": [] }, { "id": "BioInfer.d251.s0.e3", "type": "Individual_protein", "text": [ "CBP" ], "offsets": [ [ 179, 182 ] ], "normalized": [] }, { "id": "BioInfer.d251.s0.e4", "type": "Individual_protein", "text": [ "EID-1" ], "offsets": [ [ 19, 24 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d251.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d251.s0.e0", "arg2_id": "BioInfer.d251.s0.e1", "normalized": [] }, { "id": "BioInfer.d251.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d251.s0.e0", "arg2_id": "BioInfer.d251.s0.e2", "normalized": [] }, { "id": "BioInfer.d251.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d251.s0.e0", "arg2_id": "BioInfer.d251.s0.e3", "normalized": [] }, { "id": "BioInfer.d251.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d251.s0.e1", "arg2_id": "BioInfer.d251.s0.e2", "normalized": [] }, { "id": "BioInfer.d251.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d251.s0.e1", "arg2_id": "BioInfer.d251.s0.e3", "normalized": [] }, { "id": "BioInfer.d251.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d251.s0.e1", "arg2_id": "BioInfer.d251.s0.e4", "normalized": [] } ]

[ { "id": "BioInfer.d252.s0__text", "type": "Sentence", "text": [ "Here we show that the N-terminal domain of ActA binds one actin monomer, in a profilin-like fashion, and Arp2/3 complex and mimics the C-terminal domain of WASp family proteins in catalyzing filament barbed end branching by Arp2/3 complex." ], "offsets": [ [ 0, 239 ] ] } ]

[ { "id": "BioInfer.d252.s0.e0", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 78, 86 ] ], "normalized": [] }, { "id": "BioInfer.d252.s0.e1", "type": "Individual_protein", "text": [ "Arp2" ], "offsets": [ [ 105, 109 ] ], "normalized": [] }, { "id": "BioInfer.d252.s0.e2", "type": "Individual_protein", "text": [ "Arp2" ], "offsets": [ [ 224, 228 ] ], "normalized": [] }, { "id": "BioInfer.d252.s0.e3", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 58, 63 ] ], "normalized": [] }, { "id": "BioInfer.d252.s0.e4", "type": "Individual_protein", "text": [ "Arp", "3" ], "offsets": [ [ 105, 108 ], [ 110, 111 ] ], "normalized": [] }, { "id": "BioInfer.d252.s0.e5", "type": "Individual_protein", "text": [ "Arp", "3" ], "offsets": [ [ 224, 227 ], [ 229, 230 ] ], "normalized": [] }, { "id": "BioInfer.d252.s0.e6", "type": "Individual_protein", "text": [ "WASp" ], "offsets": [ [ 156, 160 ] ], "normalized": [] }, { "id": "BioInfer.d252.s0.e7", "type": "Individual_protein", "text": [ "ActA" ], "offsets": [ [ 43, 47 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d252.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d252.s0.e0", "arg2_id": "BioInfer.d252.s0.e7", "normalized": [] }, { "id": "BioInfer.d252.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d252.s0.e1", "arg2_id": "BioInfer.d252.s0.e4", "normalized": [] }, { "id": "BioInfer.d252.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d252.s0.e1", "arg2_id": "BioInfer.d252.s0.e7", "normalized": [] }, { "id": "BioInfer.d252.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d252.s0.e2", "arg2_id": "BioInfer.d252.s0.e5", "normalized": [] }, { "id": "BioInfer.d252.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d252.s0.e3", "arg2_id": "BioInfer.d252.s0.e7", "normalized": [] }, { "id": "BioInfer.d252.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d252.s0.e4", "arg2_id": "BioInfer.d252.s0.e7", "normalized": [] } ]

[ { "id": "BioInfer.d254.s0__text", "type": "Sentence", "text": [ "Here, we show that the x-ray sensitivity of rad55 and rad57 mutant strains is suppressible by overexpression of RAD51 or RAD52." ], "offsets": [ [ 0, 127 ] ] } ]

[ { "id": "BioInfer.d254.s0.e0", "type": "Gene", "text": [ "rad57" ], "offsets": [ [ 54, 59 ] ], "normalized": [] }, { "id": "BioInfer.d254.s0.e1", "type": "Individual_protein", "text": [ "RAD51" ], "offsets": [ [ 112, 117 ] ], "normalized": [] }, { "id": "BioInfer.d254.s0.e2", "type": "Gene", "text": [ "rad55" ], "offsets": [ [ 44, 49 ] ], "normalized": [] }, { "id": "BioInfer.d254.s0.e3", "type": "Individual_protein", "text": [ "RAD52" ], "offsets": [ [ 121, 126 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d255.s0__text", "type": "Sentence", "text": [ "alpha-SNAP binds to predicted alpha-helical coiled-coil regions of syntaxin and SNAP-25, shown previously to be engaged in their direct interaction." ], "offsets": [ [ 0, 148 ] ] } ]

[ { "id": "BioInfer.d255.s0.e0", "type": "Individual_protein", "text": [ "syntaxin" ], "offsets": [ [ 67, 75 ] ], "normalized": [] }, { "id": "BioInfer.d255.s0.e1", "type": "Individual_protein", "text": [ "alpha-SNAP" ], "offsets": [ [ 0, 10 ] ], "normalized": [] }, { "id": "BioInfer.d255.s0.e2", "type": "Individual_protein", "text": [ "SNAP-25" ], "offsets": [ [ 80, 87 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d255.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d255.s0.e0", "arg2_id": "BioInfer.d255.s0.e1", "normalized": [] }, { "id": "BioInfer.d255.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d255.s0.e0", "arg2_id": "BioInfer.d255.s0.e2", "normalized": [] }, { "id": "BioInfer.d255.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d255.s0.e1", "arg2_id": "BioInfer.d255.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d256.s0__text", "type": "Sentence", "text": [ "Here, we sought to determine the spatial distributions of E-cadherin, alpha-catenin, beta-catenin, and plakoglobin, and whether different complexes of these proteins accumulate at steady state in polarized Madin-Darby canine kidney cells." ], "offsets": [ [ 0, 238 ] ] } ]

[ { "id": "BioInfer.d256.s0.e0", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 85, 97 ] ], "normalized": [] }, { "id": "BioInfer.d256.s0.e1", "type": "Individual_protein", "text": [ "E-cadherin" ], "offsets": [ [ 58, 68 ] ], "normalized": [] }, { "id": "BioInfer.d256.s0.e2", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 70, 83 ] ], "normalized": [] }, { "id": "BioInfer.d256.s0.e3", "type": "Individual_protein", "text": [ "plakoglobin" ], "offsets": [ [ 103, 114 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d257.s0__text", "type": "Sentence", "text": [ "Herpes simplex virus type 1 encodes a heterotrimeric helicase-primase complex that is composed of the products of the UL5, UL52, and UL8 genes." ], "offsets": [ [ 0, 143 ] ] } ]

[ { "id": "BioInfer.d257.s0.e0", "type": "Gene", "text": [ "UL52" ], "offsets": [ [ 123, 127 ] ], "normalized": [] }, { "id": "BioInfer.d257.s0.e1", "type": "Protein_complex", "text": [ "helicase-primase" ], "offsets": [ [ 53, 69 ] ], "normalized": [] }, { "id": "BioInfer.d257.s0.e2", "type": "Gene", "text": [ "UL5" ], "offsets": [ [ 118, 121 ] ], "normalized": [] }, { "id": "BioInfer.d257.s0.e3", "type": "Gene", "text": [ "UL8" ], "offsets": [ [ 133, 136 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d257.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d257.s0.e0", "arg2_id": "BioInfer.d257.s0.e1", "normalized": [] }, { "id": "BioInfer.d257.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d257.s0.e0", "arg2_id": "BioInfer.d257.s0.e2", "normalized": [] }, { "id": "BioInfer.d257.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d257.s0.e0", "arg2_id": "BioInfer.d257.s0.e3", "normalized": [] }, { "id": "BioInfer.d257.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d257.s0.e1", "arg2_id": "BioInfer.d257.s0.e2", "normalized": [] }, { "id": "BioInfer.d257.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d257.s0.e1", "arg2_id": "BioInfer.d257.s0.e3", "normalized": [] }, { "id": "BioInfer.d257.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d257.s0.e2", "arg2_id": "BioInfer.d257.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d258.s0__text", "type": "Sentence", "text": [ "Herpes simplex virus type 1 expresses a heterotrimeric helicase-primase, the subunits of which are encoded by the viral UL5, UL8 and UL52 genes." ], "offsets": [ [ 0, 144 ] ] } ]

[ { "id": "BioInfer.d258.s0.e0", "type": "Gene", "text": [ "UL8" ], "offsets": [ [ 125, 128 ] ], "normalized": [] }, { "id": "BioInfer.d258.s0.e1", "type": "Gene", "text": [ "UL5" ], "offsets": [ [ 120, 123 ] ], "normalized": [] }, { "id": "BioInfer.d258.s0.e2", "type": "Protein_complex", "text": [ "helicase-primase" ], "offsets": [ [ 55, 71 ] ], "normalized": [] }, { "id": "BioInfer.d258.s0.e3", "type": "Gene", "text": [ "UL52" ], "offsets": [ [ 133, 137 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d258.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d258.s0.e0", "arg2_id": "BioInfer.d258.s0.e2", "normalized": [] }, { "id": "BioInfer.d258.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d258.s0.e1", "arg2_id": "BioInfer.d258.s0.e2", "normalized": [] }, { "id": "BioInfer.d258.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d258.s0.e2", "arg2_id": "BioInfer.d258.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d258.s1__text", "type": "Sentence", "text": [ "The interactions of the UL52 protein with the UL8 and UL5 proteins were analysed by using the yeast two-hybrid system." ], "offsets": [ [ 0, 118 ] ] } ]

[ { "id": "BioInfer.d258.s1.e0", "type": "Individual_protein", "text": [ "UL5" ], "offsets": [ [ 54, 57 ] ], "normalized": [] }, { "id": "BioInfer.d258.s1.e1", "type": "Individual_protein", "text": [ "UL8" ], "offsets": [ [ 46, 49 ] ], "normalized": [] }, { "id": "BioInfer.d258.s1.e2", "type": "Individual_protein", "text": [ "UL52" ], "offsets": [ [ 24, 28 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d258.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d258.s1.e0", "arg2_id": "BioInfer.d258.s1.e2", "normalized": [] }, { "id": "BioInfer.d258.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d258.s1.e1", "arg2_id": "BioInfer.d258.s1.e2", "normalized": [] } ]

[ { "id": "BioInfer.d258.s2__text", "type": "Sentence", "text": [ "Two-hybrid analysis of the interaction between the UL52 and UL8 subunits of the herpes simplex virus type 1 helicase-primase." ], "offsets": [ [ 0, 125 ] ] } ]

[ { "id": "BioInfer.d258.s2.e0", "type": "Protein_complex", "text": [ "helicase-primase" ], "offsets": [ [ 108, 124 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d259.s0__text", "type": "Sentence", "text": [ "Herpes simplex virus type 1 (HSV-1) encodes a helicase-primase that consists of the products of the UL5, UL8, and UL52 genes (Crute, J. J., Tsurumi, T., Zhu, L., Weller, S. K., Olivo, P. D., Challberg, M. D., Mocarski, E. S. and Lehman, I. R. (1989) Proc. Natl. Acad. Sci. U. S. A. 86, 2186-2189)." ], "offsets": [ [ 0, 297 ] ] } ]

[ { "id": "BioInfer.d259.s0.e0", "type": "Gene", "text": [ "UL8" ], "offsets": [ [ 105, 108 ] ], "normalized": [] }, { "id": "BioInfer.d259.s0.e1", "type": "Gene", "text": [ "UL52" ], "offsets": [ [ 114, 118 ] ], "normalized": [] }, { "id": "BioInfer.d259.s0.e2", "type": "Protein_complex", "text": [ "helicase-primase" ], "offsets": [ [ 46, 62 ] ], "normalized": [] }, { "id": "BioInfer.d259.s0.e3", "type": "Gene", "text": [ "UL5" ], "offsets": [ [ 100, 103 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d259.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d259.s0.e0", "arg2_id": "BioInfer.d259.s0.e1", "normalized": [] }, { "id": "BioInfer.d259.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d259.s0.e0", "arg2_id": "BioInfer.d259.s0.e2", "normalized": [] }, { "id": "BioInfer.d259.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d259.s0.e0", "arg2_id": "BioInfer.d259.s0.e3", "normalized": [] }, { "id": "BioInfer.d259.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d259.s0.e1", "arg2_id": "BioInfer.d259.s0.e2", "normalized": [] }, { "id": "BioInfer.d259.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d259.s0.e1", "arg2_id": "BioInfer.d259.s0.e3", "normalized": [] }, { "id": "BioInfer.d259.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d259.s0.e2", "arg2_id": "BioInfer.d259.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d260.s0__text", "type": "Sentence", "text": [ "Herpes simplex virus type 1 (HSV-1) encodes a helicase-primase that consists of three polypeptides encoded by the UL5, UL8, and UL52 genes (Crute, J.J., Tsurumi, T., Zhu, L., Weller, S.K., Olivo, P.D., Challberg, M.D., Mocarski, E.S., and Lehman, I.R. (1989) Proc. Natl." ], "offsets": [ [ 0, 270 ] ] } ]

[ { "id": "BioInfer.d260.s0.e0", "type": "Individual_protein", "text": [ "helicase-primase" ], "offsets": [ [ 46, 62 ] ], "normalized": [] }, { "id": "BioInfer.d260.s0.e1", "type": "Gene", "text": [ "UL8" ], "offsets": [ [ 119, 122 ] ], "normalized": [] }, { "id": "BioInfer.d260.s0.e2", "type": "Gene", "text": [ "UL5" ], "offsets": [ [ 114, 117 ] ], "normalized": [] }, { "id": "BioInfer.d260.s0.e3", "type": "Gene", "text": [ "UL52" ], "offsets": [ [ 128, 132 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d260.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d260.s0.e0", "arg2_id": "BioInfer.d260.s0.e1", "normalized": [] }, { "id": "BioInfer.d260.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d260.s0.e0", "arg2_id": "BioInfer.d260.s0.e2", "normalized": [] }, { "id": "BioInfer.d260.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d260.s0.e0", "arg2_id": "BioInfer.d260.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d261.s0__text", "type": "Sentence", "text": [ "Herpes simplex virus type 1 (HSV-1) encodes a heterotrimeric helicase-primase composed of the products of the three DNA replication-specific genes UL5, UL8, and UL52 (Crute, J. J., and Lehman, I. R. (1991) J. Biol. Chem. 266, 4484-4488)." ], "offsets": [ [ 0, 237 ] ] } ]

[ { "id": "BioInfer.d261.s0.e0", "type": "Gene", "text": [ "UL8" ], "offsets": [ [ 152, 155 ] ], "normalized": [] }, { "id": "BioInfer.d261.s0.e1", "type": "Protein_complex", "text": [ "helicase-primase" ], "offsets": [ [ 61, 77 ] ], "normalized": [] }, { "id": "BioInfer.d261.s0.e2", "type": "Gene", "text": [ "UL5" ], "offsets": [ [ 147, 150 ] ], "normalized": [] }, { "id": "BioInfer.d261.s0.e3", "type": "Gene", "text": [ "UL52" ], "offsets": [ [ 161, 165 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d262.s0__text", "type": "Sentence", "text": [ "HGF/SF treatment of LoVo reduced the amount of alpha-catenin complexed with E-cadherin more markedly than in L-10, but in both cell lines this reduction was not accompanied by increased tyrosine phosphorylation of beta-catenin, suggesting the presence of a mechanism other than phosphorylation for release from cell-cell adhesion during cell motility." ], "offsets": [ [ 0, 351 ] ] } ]

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[ { "id": "BioInfer.d263.s0__text", "type": "Sentence", "text": [ "High levels of profilin suppress the lethality caused by overproduction of actin in yeast cells." ], "offsets": [ [ 0, 96 ] ] } ]

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[ { "id": "BioInfer.d263.s1__text", "type": "Sentence", "text": [ "In contrast, overexpression of the profilin gene, PFY1, encoding an actin-binding protein, leads to no very obvious phenotype." ], "offsets": [ [ 0, 126 ] ] } ]

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[ { "id": "BioInfer.d263.s2__text", "type": "Sentence", "text": [ "Interestingly, profilin overproduction can compensate for the deleterious effects of too much actin in a profilin concentration-dependent manner." ], "offsets": [ [ 0, 145 ] ] } ]

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[ { "id": "BioInfer.d264.s0__text", "type": "Sentence", "text": [ "Histone H3 showed at least seven sites of acetylation, histone H2B.1 had six sites and histone H4 had five sites." ], "offsets": [ [ 0, 113 ] ] } ]

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[ { "id": "BioInfer.d264.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d264.s0.e0", "arg2_id": "BioInfer.d264.s0.e4", "normalized": [] }, { "id": "BioInfer.d264.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d264.s0.e1", "arg2_id": "BioInfer.d264.s0.e5", "normalized": [] }, { "id": "BioInfer.d264.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d264.s0.e2", "arg2_id": "BioInfer.d264.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d266.s0__text", "type": "Sentence", "text": [ "However, although expression of Ras alone will not induce G1 CDK activity or S phase, coexpression of Ras with Myc allows the generation of cyclin E-dependent kinase activity and the induction of S phase, coincident with the loss of the p27 cyclin-dependent kinase inhibitor (CKI)." ], "offsets": [ [ 0, 281 ] ] } ]

[ { "id": "BioInfer.d266.s0.e0", "type": "Protein_family_or_group", "text": [ "cyclin-dependent kinase inhibitor" ], "offsets": [ [ 241, 274 ] ], "normalized": [] }, { "id": "BioInfer.d266.s0.e1", "type": "Protein_family_or_group", "text": [ "CKI" ], "offsets": [ [ 276, 279 ] ], "normalized": [] }, { "id": "BioInfer.d266.s0.e2", "type": "Individual_protein", "text": [ "Myc" ], "offsets": [ [ 111, 114 ] ], "normalized": [] }, { "id": "BioInfer.d266.s0.e3", "type": "Individual_protein", "text": [ "Ras" ], "offsets": [ [ 102, 105 ] ], "normalized": [] }, { "id": "BioInfer.d266.s0.e4", "type": "Individual_protein", "text": [ "CDK" ], "offsets": [ [ 61, 64 ] ], "normalized": [] }, { "id": "BioInfer.d266.s0.e5", "type": "Individual_protein", "text": [ "Ras" ], "offsets": [ [ 32, 35 ] ], "normalized": [] }, { "id": "BioInfer.d266.s0.e6", "type": "Individual_protein", "text": [ "p27" ], "offsets": [ [ 237, 240 ] ], "normalized": [] }, { "id": "BioInfer.d266.s0.e7", "type": "Individual_protein", "text": [ "cyclin E-dependent kinase" ], "offsets": [ [ 140, 165 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d266.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d266.s0.e0", "arg2_id": "BioInfer.d266.s0.e6", "normalized": [] }, { "id": "BioInfer.d266.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d266.s0.e1", "arg2_id": "BioInfer.d266.s0.e6", "normalized": [] }, { "id": "BioInfer.d266.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d266.s0.e2", "arg2_id": "BioInfer.d266.s0.e3", "normalized": [] }, { "id": "BioInfer.d266.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d266.s0.e2", "arg2_id": "BioInfer.d266.s0.e7", "normalized": [] }, { "id": "BioInfer.d266.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d266.s0.e3", "arg2_id": "BioInfer.d266.s0.e7", "normalized": [] }, { "id": "BioInfer.d266.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d266.s0.e4", "arg2_id": "BioInfer.d266.s0.e5", "normalized": [] }, { "id": "BioInfer.d266.s0.i6", "type": "PPI", "arg1_id": "BioInfer.d266.s0.e6", "arg2_id": "BioInfer.d266.s0.e7", "normalized": [] } ]

[ { "id": "BioInfer.d267.s0__text", "type": "Sentence", "text": [ "However, a number of mammalian DNA repair proteins lack NLS clusters; these proteins include ERCC1, ERCC2 (XPD), mouse RAD51, and the HHR23B/p58 and HHR23A subunits of XPC." ], "offsets": [ [ 0, 172 ] ] } ]

[ { "id": "BioInfer.d267.s0.e0", "type": "Protein_complex", "text": [ "XPC" ], "offsets": [ [ 168, 171 ] ], "normalized": [] }, { "id": "BioInfer.d267.s0.e1", "type": "Individual_protein", "text": [ "XPD" ], "offsets": [ [ 107, 110 ] ], "normalized": [] }, { "id": "BioInfer.d267.s0.e2", "type": "Individual_protein", "text": [ "HHR23B" ], "offsets": [ [ 134, 140 ] ], "normalized": [] }, { "id": "BioInfer.d267.s0.e3", "type": "Individual_protein", "text": [ "p58" ], "offsets": [ [ 141, 144 ] ], "normalized": [] }, { "id": "BioInfer.d267.s0.e4", "type": "Individual_protein", "text": [ "HHR23A" ], "offsets": [ [ 149, 155 ] ], "normalized": [] }, { "id": "BioInfer.d267.s0.e5", "type": "Gene/protein/RNA", "text": [ "ERCC1" ], "offsets": [ [ 93, 98 ] ], "normalized": [] }, { "id": "BioInfer.d267.s0.e6", "type": "Individual_protein", "text": [ "ERCC2" ], "offsets": [ [ 100, 105 ] ], "normalized": [] }, { "id": "BioInfer.d267.s0.e7", "type": "Gene/protein/RNA", "text": [ "RAD51" ], "offsets": [ [ 119, 124 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d267.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d267.s0.e0", "arg2_id": "BioInfer.d267.s0.e2", "normalized": [] }, { "id": "BioInfer.d267.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d267.s0.e0", "arg2_id": "BioInfer.d267.s0.e3", "normalized": [] }, { "id": "BioInfer.d267.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d267.s0.e0", "arg2_id": "BioInfer.d267.s0.e4", "normalized": [] }, { "id": "BioInfer.d267.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d267.s0.e2", "arg2_id": "BioInfer.d267.s0.e3", "normalized": [] }, { "id": "BioInfer.d267.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d267.s0.e2", "arg2_id": "BioInfer.d267.s0.e4", "normalized": [] }, { "id": "BioInfer.d267.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d267.s0.e3", "arg2_id": "BioInfer.d267.s0.e4", "normalized": [] } ]

[ { "id": "BioInfer.d267.s1__text", "type": "Sentence", "text": [ "NLS-less S.cerevisiae proteins include both RAD51 and RAD52 that function in the recombination and in the repair of double-strand breaks as well as the RAD23 and HRR25 molecules." ], "offsets": [ [ 0, 178 ] ] } ]

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[ { "id": "BioInfer.d268.s0__text", "type": "Sentence", "text": [ "However, disassembly of the actin cytoskeleton using Latrunculin-A does not alter verprolin's location, indicating that verprolin establishes and maintains its location independent of the actin cytoskeleton." ], "offsets": [ [ 0, 207 ] ] } ]

[ { "id": "BioInfer.d268.s0.e0", "type": "Individual_protein", "text": [ "verprolin" ], "offsets": [ [ 120, 129 ] ], "normalized": [] }, { "id": "BioInfer.d268.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 188, 193 ] ], "normalized": [] }, { "id": "BioInfer.d268.s0.e2", "type": "Individual_protein", "text": [ "verprolin" ], "offsets": [ [ 82, 91 ] ], "normalized": [] }, { "id": "BioInfer.d268.s0.e3", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 28, 33 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d268.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d268.s0.e0", "arg2_id": "BioInfer.d268.s0.e1", "normalized": [] }, { "id": "BioInfer.d268.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d268.s0.e2", "arg2_id": "BioInfer.d268.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d268.s1__text", "type": "Sentence", "text": [ "Using the two-hybrid system, we show that verprolin binds actin." ], "offsets": [ [ 0, 64 ] ] } ]

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[ { "id": "BioInfer.d268.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d268.s1.e0", "arg2_id": "BioInfer.d268.s1.e1", "normalized": [] } ]

[ { "id": "BioInfer.d269.s0__text", "type": "Sentence", "text": [ "However, immunofluorescence staining revealed a similar organisation of actin microfilaments, talin and phosphotyrosyl-containing proteins on both substrates." ], "offsets": [ [ 0, 158 ] ] } ]

[ { "id": "BioInfer.d269.s0.e0", "type": "Gene/protein/RNA", "text": [ "talin" ], "offsets": [ [ 94, 99 ] ], "normalized": [] }, { "id": "BioInfer.d269.s0.e1", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 72, 77 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d270.s0__text", "type": "Sentence", "text": [ "However, increases were also selective in nature, with increases in certain individual proteins, including actin (twofold to threefold), vimentin (2.5-fold to sevenfold), tropomyosin (threefold to sixfold), and myosin heavy chain, far exceeding overall increases in cellular protein content (20-40%)." ], "offsets": [ [ 0, 300 ] ] } ]

[ { "id": "BioInfer.d270.s0.e0", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 107, 112 ] ], "normalized": [] }, { "id": "BioInfer.d270.s0.e1", "type": "Gene/protein/RNA", "text": [ "tropomyosin" ], "offsets": [ [ 171, 182 ] ], "normalized": [] }, { "id": "BioInfer.d270.s0.e2", "type": "Gene/protein/RNA", "text": [ "vimentin" ], "offsets": [ [ 137, 145 ] ], "normalized": [] }, { "id": "BioInfer.d270.s0.e3", "type": "Gene/protein/RNA", "text": [ "myosin heavy chain" ], "offsets": [ [ 211, 229 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d272.s0__text", "type": "Sentence", "text": [ "However, once initiated, the synthesis of muscle tropomyosin mRNA continued in the presence of cycloheximide, while the expression of muscle actin, myosin heavy chain, and myogenin mRNA was abolished." ], "offsets": [ [ 0, 200 ] ] } ]

[ { "id": "BioInfer.d272.s0.e0", "type": "Gene/protein/RNA", "text": [ "muscle", "myosin heavy chain" ], "offsets": [ [ 134, 140 ], [ 148, 166 ] ], "normalized": [] }, { "id": "BioInfer.d272.s0.e1", "type": "Gene/protein/RNA", "text": [ "muscle tropomyosin" ], "offsets": [ [ 42, 60 ] ], "normalized": [] }, { "id": "BioInfer.d272.s0.e2", "type": "Gene/protein/RNA", "text": [ "muscle", "myogenin" ], "offsets": [ [ 134, 140 ], [ 172, 180 ] ], "normalized": [] }, { "id": "BioInfer.d272.s0.e3", "type": "Gene/protein/RNA", "text": [ "muscle actin" ], "offsets": [ [ 134, 146 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d272.s1__text", "type": "Sentence", "text": [ "These results suggest that muscle-specific processing of tropomyosin transcripts can continue to occur in the absence of myogenin expression unlike the expression of muscle actin and myosin heavy chain mRNAs." ], "offsets": [ [ 0, 208 ] ] } ]

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[ { "id": "BioInfer.d272.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d272.s1.e1", "arg2_id": "BioInfer.d272.s1.e3", "normalized": [] } ]

[ { "id": "BioInfer.d274.s0__text", "type": "Sentence", "text": [ "However, similar to utrophin, alpha-syntrophin is only present at the neuromuscular junction in mdx mouse muscle in which dystrophin is absent." ], "offsets": [ [ 0, 143 ] ] } ]

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[ { "id": "BioInfer.d274.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d274.s0.e0", "arg2_id": "BioInfer.d274.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d274.s1__text", "type": "Sentence", "text": [ "Identification of alpha-syntrophin binding to syntrophin triplet, dystrophin, and utrophin." ], "offsets": [ [ 0, 91 ] ] } ]

[ { "id": "BioInfer.d274.s1.e0", "type": "Individual_protein", "text": [ "alpha-syntrophin" ], "offsets": [ [ 18, 34 ] ], "normalized": [] }, { "id": "BioInfer.d274.s1.e1", "type": "Individual_protein", "text": [ "dystrophin" ], "offsets": [ [ 66, 76 ] ], "normalized": [] }, { "id": "BioInfer.d274.s1.e2", "type": "Individual_protein", "text": [ "syntrophin triplet" ], "offsets": [ [ 46, 64 ] ], "normalized": [] }, { "id": "BioInfer.d274.s1.e3", "type": "Individual_protein", "text": [ "utrophin" ], "offsets": [ [ 82, 90 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d274.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d274.s1.e0", "arg2_id": "BioInfer.d274.s1.e1", "normalized": [] }, { "id": "BioInfer.d274.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d274.s1.e0", "arg2_id": "BioInfer.d274.s1.e2", "normalized": [] }, { "id": "BioInfer.d274.s1.i2", "type": "PPI", "arg1_id": "BioInfer.d274.s1.e0", "arg2_id": "BioInfer.d274.s1.e3", "normalized": [] } ]

[ { "id": "BioInfer.d275.s0__text", "type": "Sentence", "text": [ "However, smooth muscle contents of actin (26.0 +/- 1.8 vs. 19.1 +/- 2.2 micrograms/mg wet wt) and myosin heavy chain (5.5 +/- 0.4 vs. 2.0 +/- 0.3 microgram/mg wet wt) were greater (P < 0.04) in myometrium from late-pregnant vs. nonpregnant ewes." ], "offsets": [ [ 0, 245 ] ] } ]

[ { "id": "BioInfer.d275.s0.e0", "type": "Gene/protein/RNA", "text": [ "myosin heavy chain" ], "offsets": [ [ 98, 116 ] ], "normalized": [] }, { "id": "BioInfer.d275.s0.e1", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 35, 40 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d276.s0__text", "type": "Sentence", "text": [ "However, some proteins (e.g., profilin) and other agents (e.g., cytochalasin D) that bind to actin are affected by the presence of fluorescent labels, making actin intrinsic fluorescence potentially useful in investigating the interaction of these agents with actin, and in validating data obtained using labeled actin." ], "offsets": [ [ 0, 319 ] ] } ]

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[ { "id": "BioInfer.d278.s0__text", "type": "Sentence", "text": [ "However, these rod structures were not observed in response to TSH, forskolin, or TPA, suggesting that dephosphorylation of cofilin correlates with the reorganization of actin microfilaments but not with the nuclear transport of cofilin." ], "offsets": [ [ 0, 237 ] ] } ]

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[ { "id": "BioInfer.d278.s1__text", "type": "Sentence", "text": [ "This suggests that dephosphorylation of cofilin and destrin/ADF by TSH could be implicated in the disruption of actin-containing stress fibers and in the reorganization of microfilaments induced by this hormone." ], "offsets": [ [ 0, 211 ] ] } ]

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[ { "id": "BioInfer.d279.s0__text", "type": "Sentence", "text": [ "However, upon treatment with DMSO, cytoplasmic actin filaments were disrupted and intranuclear rod structures containing cofilin and actin were apparently larger and thicker in cells overexpressing cofilin than in normal cells." ], "offsets": [ [ 0, 227 ] ] } ]

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[ { "id": "BioInfer.d279.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d279.s0.e1", "arg2_id": "BioInfer.d279.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d279.s1__text", "type": "Sentence", "text": [ "In cultured cells, cofilin, as well as ADF, translocates from the cytoplasm into the nucleus together with actin and forms rod-like structures in response to heat shock or dimethylsulfoxide (DMSO) treatment." ], "offsets": [ [ 0, 207 ] ] } ]

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[ { "id": "BioInfer.d279.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d279.s1.e0", "arg2_id": "BioInfer.d279.s1.e1", "normalized": [] }, { "id": "BioInfer.d279.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d279.s1.e1", "arg2_id": "BioInfer.d279.s1.e2", "normalized": [] } ]

[ { "id": "BioInfer.d279.s2__text", "type": "Sentence", "text": [ "Stimulus-dependent disorganization of actin filaments induced by overexpression of cofilin in C2 myoblasts." ], "offsets": [ [ 0, 107 ] ] } ]

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[ { "id": "BioInfer.d279.s2.i0", "type": "PPI", "arg1_id": "BioInfer.d279.s2.e0", "arg2_id": "BioInfer.d279.s2.e1", "normalized": [] } ]

[ { "id": "BioInfer.d280.s0__text", "type": "Sentence", "text": [ "However, when all of the four proteins (E-cadherin, alpha-catenin, beta-catenin, and gamma-catenin) were analysed as one group, a significant association was seen between reduction in immunoreactivity of at least one of these four proteins and the presence of metastases." ], "offsets": [ [ 0, 271 ] ] } ]

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[ { "id": "BioInfer.d280.s1__text", "type": "Sentence", "text": [ "Reduced or absent immunoreactivity in the tumour tissue was seen in 63 (70.0 per cent) for alpha-catenin, in 50 (55.6 per cent) for beta-catenin, and in 50 (55.6 per cent) for gamma-catenin." ], "offsets": [ [ 0, 190 ] ] } ]

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[ { "id": "BioInfer.d281.s0__text", "type": "Sentence", "text": [ "Human profilins are multifunctional, single-domain proteins which directly link the actin microfilament system to a variety of signalling pathways via two spatially distinct binding sites." ], "offsets": [ [ 0, 188 ] ] } ]

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[ { "id": "BioInfer.d281.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d281.s0.e0", "arg2_id": "BioInfer.d281.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d282.s0__text", "type": "Sentence", "text": [ "Human platelet P-235, a talin-like actin binding protein, binds selectively to mixed lipid bilayers." ], "offsets": [ [ 0, 100 ] ] } ]

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[ { "id": "BioInfer.d282.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d282.s0.e0", "arg2_id": "BioInfer.d282.s0.e1", "normalized": [] }, { "id": "BioInfer.d282.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d282.s0.e1", "arg2_id": "BioInfer.d282.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d283.s0__text", "type": "Sentence", "text": [ "Human platelets contain profilin, a potential regulator of actin polymerisability." ], "offsets": [ [ 0, 82 ] ] } ]

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[ { "id": "BioInfer.d283.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d283.s0.e0", "arg2_id": "BioInfer.d283.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d284.s0__text", "type": "Sentence", "text": [ "Hypertonicity provoked Fyn-dependent tyrosine phosphorylation in beta-catenin, alpha-catenin, and p120(Cas) and caused the dissociation of beta-catenin from the contacts." ], "offsets": [ [ 0, 170 ] ] } ]

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[ { "id": "BioInfer.d285.s0__text", "type": "Sentence", "text": [ "Immediately after synthesis, E-cadherin, beta-catenin, and plakoglobin cosedimented as complexes." ], "offsets": [ [ 0, 97 ] ] } ]

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[ { "id": "BioInfer.d285.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d285.s0.e0", "arg2_id": "BioInfer.d285.s0.e1", "normalized": [] }, { "id": "BioInfer.d285.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d285.s0.e0", "arg2_id": "BioInfer.d285.s0.e2", "normalized": [] }, { "id": "BioInfer.d285.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d285.s0.e1", "arg2_id": "BioInfer.d285.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d285.s1__text", "type": "Sentence", "text": [ "alpha-Catenin was not associated with these complexes after synthesis, but a subpopulation of alpha-catenin joined the complex at a time coincident with the arrival of E-cadherin at the plasma membrane." ], "offsets": [ [ 0, 202 ] ] } ]

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[ { "id": "BioInfer.d285.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d285.s1.e0", "arg2_id": "BioInfer.d285.s1.e1", "normalized": [] } ]

[ { "id": "BioInfer.d287.s0__text", "type": "Sentence", "text": [ "Immunocytochemical localisation of actin and profilin in the generative cell of angiosperm pollen: TEM studies on high-pressure frozen and freeze-substituted Ledebouria socialis Roth (Hyacinthaceae)." ], "offsets": [ [ 0, 199 ] ] } ]

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[ { "id": "BioInfer.d287.s1__text", "type": "Sentence", "text": [ "We attribute the detection of actin and profilin to the applied cryomethods which yield a much better preservation of ultrastructure and antigenicity of delicate cytoskeletal constituents than conventional fixation techniques." ], "offsets": [ [ 0, 226 ] ] } ]

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[ { "id": "BioInfer.d288.s0__text", "type": "Sentence", "text": [ "Immunofluorescence experiments showed that, like Abp1p, cofilin is associated with the membrane actin cytoskeleton." ], "offsets": [ [ 0, 115 ] ] } ]

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[ { "id": "BioInfer.d288.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d288.s0.e0", "arg2_id": "BioInfer.d288.s0.e1", "normalized": [] }, { "id": "BioInfer.d288.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d288.s0.e1", "arg2_id": "BioInfer.d288.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d288.s1__text", "type": "Sentence", "text": [ "In this study, we demonstrate using viscosity, sedimentation, and actin assembly rate assays that yeast cofilin (16 kD) possesses all of these properties." ], "offsets": [ [ 0, 154 ] ] } ]

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[ { "id": "BioInfer.d288.s2__text", "type": "Sentence", "text": [ "The NH2-terminal 16kD of Abp1p, a 65-kD yeast protein identified by its ability to bind to actin filaments, is 23% identical to yeast cofilin." ], "offsets": [ [ 0, 142 ] ] } ]

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[ { "id": "BioInfer.d288.s3__text", "type": "Sentence", "text": [ "We have biochemically identified the Saccharomyces cerevisiae homologue of the mammalian actin binding protein cofilin." ], "offsets": [ [ 0, 119 ] ] } ]

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[ { "id": "BioInfer.d288.s3.i0", "type": "PPI", "arg1_id": "BioInfer.d288.s3.e0", "arg2_id": "BioInfer.d288.s3.e1", "normalized": [] } ]

[ { "id": "BioInfer.d289.s0__text", "type": "Sentence", "text": [ "Immunofluorescence microscopy of monolayers between 2 and 3 h post-TGF-beta1 showed that beta-catenin, plakoglobin, alpha-catenin, and cadherin-5 were colocalized both at the cell periphery and in newly formed bands that are perpendicular to the cell-cell border." ], "offsets": [ [ 0, 263 ] ] } ]

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[ { "id": "BioInfer.d291.s0__text", "type": "Sentence", "text": [ "Immunohistochemical identification and localization of actin and fimbrin in vestibular hair cells in the normal guinea pig and in a strain of the waltzing guinea pig." ], "offsets": [ [ 0, 166 ] ] } ]

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[ { "id": "BioInfer.d292.s0__text", "type": "Sentence", "text": [ "Immunohistochemical investigation of actin-anchoring proteins vinculin, talin and paxillin in rat brain following lesion: a moderate reaction, confined to the astroglia of brain tracts." ], "offsets": [ [ 0, 185 ] ] } ]

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[ { "id": "BioInfer.d293.s0__text", "type": "Sentence", "text": [ "Immunohistochemical studies showed a strong reactivity of most LAM cells for alpha-smooth muscle actin and smooth muscle myosin heavy chain and a weak to moderate reactivity of a lesser number of cells for desmin and nonmuscle myosin heavy chain II-B." ], "offsets": [ [ 0, 251 ] ] } ]

[ { "id": "BioInfer.d293.s0.e0", "type": "Gene/protein/RNA", "text": [ "desmin" ], "offsets": [ [ 206, 212 ] ], "normalized": [] }, { "id": "BioInfer.d293.s0.e1", "type": "Gene/protein/RNA", "text": [ "alpha-smooth muscle actin" ], "offsets": [ [ 77, 102 ] ], "normalized": [] }, { "id": "BioInfer.d293.s0.e2", "type": "Gene/protein/RNA", "text": [ "nonmuscle myosin heavy chain II-B" ], "offsets": [ [ 217, 250 ] ], "normalized": [] }, { "id": "BioInfer.d293.s0.e3", "type": "Gene/protein/RNA", "text": [ "smooth muscle myosin heavy chain" ], "offsets": [ [ 107, 139 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d294.s0__text", "type": "Sentence", "text": [ "Immunohistochemistry for a variety of cytokeratins (CKs) (8/18, 1/10, 7, and 20), epithelial membrane antigen (EMA), S-100 protein, vimentin CD34, type IV collagen, smooth muscle actin, smooth muscle myosin heavy chain, calponin, and glial fibrillary acid protein was performed." ], "offsets": [ [ 0, 278 ] ] } ]

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[ { "id": "BioInfer.d295.s0__text", "type": "Sentence", "text": [ "Immunohistochemistry revealed that arteries had three distinct populations of cells in respect to alpha-smooth muscle actin, smooth muscle myosin heavy chain and vimentin (staining intensities '-', '+' or '++' for each protein), but only two populations in respect to desmin ('-' and '+')." ], "offsets": [ [ 0, 289 ] ] } ]

[ { "id": "BioInfer.d295.s0.e0", "type": "Gene/protein/RNA", "text": [ "alpha-smooth muscle actin" ], "offsets": [ [ 98, 123 ] ], "normalized": [] }, { "id": "BioInfer.d295.s0.e1", "type": "Gene/protein/RNA", "text": [ "vimentin" ], "offsets": [ [ 162, 170 ] ], "normalized": [] }, { "id": "BioInfer.d295.s0.e2", "type": "Gene/protein/RNA", "text": [ "smooth muscle myosin heavy chain" ], "offsets": [ [ 125, 157 ] ], "normalized": [] }, { "id": "BioInfer.d295.s0.e3", "type": "Gene/protein/RNA", "text": [ "desmin" ], "offsets": [ [ 268, 274 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d296.s0__text", "type": "Sentence", "text": [ "Immunolocalization of E-cadherin (E-cad), alpha-catenin, beta-catenin, and CD44 has rarely been investigated in human cholangiocarcinoma (CC)." ], "offsets": [ [ 0, 142 ] ] } ]

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[ { "id": "BioInfer.d296.s1__text", "type": "Sentence", "text": [ "In CC, membranous expression of E-cad, alpha-catenin, and beta-catenin was the same or reduced when compared with non-cancerous bile ducts in the majority of CC." ], "offsets": [ [ 0, 161 ] ] } ]

[ { "id": "BioInfer.d296.s1.e0", "type": "Gene/protein/RNA", "text": [ "E-cad" ], "offsets": [ [ 32, 37 ] ], "normalized": [] }, { "id": "BioInfer.d296.s1.e1", "type": "Gene/protein/RNA", "text": [ "beta-catenin" ], "offsets": [ [ 58, 70 ] ], "normalized": [] }, { "id": "BioInfer.d296.s1.e2", "type": "Gene/protein/RNA", "text": [ "alpha-catenin" ], "offsets": [ [ 39, 52 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d296.s2__text", "type": "Sentence", "text": [ "In normal livers, E-cad, alpha-catenin and beta-catenin, but not CD44s, CD44v5, CD44v6, CD44v7-8, and CD44v10, were expressed at the cell membrane of normal intrahepatic bile ducts." ], "offsets": [ [ 0, 181 ] ] } ]

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[ { "id": "BioInfer.d296.s3__text", "type": "Sentence", "text": [ "We found that the down-regulation of E-cad, alpha-catenin, and beta-catenin expression significantly correlated with tumor high grade, but not with vascular invasion, metastasis, p53 expression, Ki-67 labeling, or c-erbB2 expression, except for beta-catenin, the down-regulation of which was associated with c-erbB2 down-regulation." ], "offsets": [ [ 0, 332 ] ] } ]

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[ { "id": "BioInfer.d297.s0__text", "type": "Sentence", "text": [ "Immunoprecipitation of alpha-catenin was increased in response to both doses of CdCl2, while the immunoprecipitation of beta-catenin was little changed by either cadmium dose." ], "offsets": [ [ 0, 175 ] ] } ]

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[ { "id": "BioInfer.d298.s0__text", "type": "Sentence", "text": [ "Immunoprecipitation of metabolically labeled proteins with HECD-1 revealed three bands corresponding to E-cadherin, alpha-catenin, and gamma-catenin and a 79-kDa band which was apparently smaller than that of normal beta-catenin, indicating truncated beta-catenin." ], "offsets": [ [ 0, 264 ] ] } ]

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[ { "id": "BioInfer.d299.s0__text", "type": "Sentence", "text": [ "Immunoprecipitations showed in both cell lines the presence of two different E-cadherin- catenin complexes, one composed of E-cadherin, alpha-catenin and beta-catenin, and the other of E-cadherin, alpha-catenin and plakoglobin." ], "offsets": [ [ 0, 227 ] ] } ]

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[ { "id": "BioInfer.d300.s0__text", "type": "Sentence", "text": [ "Immunoprecipitation with an E-cadherin mAb, which is known to co-precipitate the catenins, demonstrated that the three poorly differentiated cell lines expressing E-cadherin did not co-precipitate alpha-catenin, although all of the moderately-well differentiated cell lines expressed both alpha- and beta-catenin." ], "offsets": [ [ 0, 313 ] ] } ]

[ { "id": "BioInfer.d300.s0.e0", "type": "Individual_protein", "text": [ "E-cadherin" ], "offsets": [ [ 28, 38 ] ], "normalized": [] }, { "id": "BioInfer.d300.s0.e1", "type": "Gene/protein/RNA", "text": [ "beta-catenin" ], "offsets": [ [ 300, 312 ] ], "normalized": [] }, { "id": "BioInfer.d300.s0.e2", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 197, 210 ] ], "normalized": [] }, { "id": "BioInfer.d300.s0.e3", "type": "Gene/protein/RNA", "text": [ "alpha-", "catenin" ], "offsets": [ [ 289, 295 ], [ 305, 312 ] ], "normalized": [] }, { "id": "BioInfer.d300.s0.e4", "type": "Individual_protein", "text": [ "catenins" ], "offsets": [ [ 81, 89 ] ], "normalized": [] }, { "id": "BioInfer.d300.s0.e5", "type": "Individual_protein", "text": [ "E-cadherin" ], "offsets": [ [ 163, 173 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d300.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d300.s0.e0", "arg2_id": "BioInfer.d300.s0.e4", "normalized": [] }, { "id": "BioInfer.d300.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d300.s0.e2", "arg2_id": "BioInfer.d300.s0.e5", "normalized": [] } ]

[ { "id": "BioInfer.d301.s0__text", "type": "Sentence", "text": [ "Immunoreactive E-cadherin, alpha-catenin, beta-catenin, and gamma-catenin proteins in hepatocellular carcinoma: relationships with tumor grade, clinicopathologic parameters, and patients' survival." ], "offsets": [ [ 0, 197 ] ] } ]

[ { "id": "BioInfer.d301.s0.e0", "type": "Gene/protein/RNA", "text": [ "E-cadherin" ], "offsets": [ [ 15, 25 ] ], "normalized": [] }, { "id": "BioInfer.d301.s0.e1", "type": "Gene/protein/RNA", "text": [ "beta-catenin" ], "offsets": [ [ 42, 54 ] ], "normalized": [] }, { "id": "BioInfer.d301.s0.e2", "type": "Gene/protein/RNA", "text": [ "alpha-catenin" ], "offsets": [ [ 27, 40 ] ], "normalized": [] }, { "id": "BioInfer.d301.s0.e3", "type": "Gene/protein/RNA", "text": [ "gamma-catenin" ], "offsets": [ [ 60, 73 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d302.s0__text", "type": "Sentence", "text": [ "Immunoreactivity for pan-cadherin, E-cadherin, alpha-catenin, beta-catenin, and p120 was observed in all 15 specimens." ], "offsets": [ [ 0, 118 ] ] } ]

[ { "id": "BioInfer.d302.s0.e0", "type": "Gene/protein/RNA", "text": [ "alpha-catenin" ], "offsets": [ [ 47, 60 ] ], "normalized": [] }, { "id": "BioInfer.d302.s0.e1", "type": "Gene/protein/RNA", "text": [ "pan-cadherin" ], "offsets": [ [ 21, 33 ] ], "normalized": [] }, { "id": "BioInfer.d302.s0.e2", "type": "Gene/protein/RNA", "text": [ "p120" ], "offsets": [ [ 80, 84 ] ], "normalized": [] }, { "id": "BioInfer.d302.s0.e3", "type": "Gene/protein/RNA", "text": [ "E-cadherin" ], "offsets": [ [ 35, 45 ] ], "normalized": [] }, { "id": "BioInfer.d302.s0.e4", "type": "Gene/protein/RNA", "text": [ "beta-catenin" ], "offsets": [ [ 62, 74 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d304.s0__text", "type": "Sentence", "text": [ "Impact of profilin on actin-bound nucleotide exchange and actin polymerization dynamics." ], "offsets": [ [ 0, 88 ] ] } ]

[ { "id": "BioInfer.d304.s0.e0", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 10, 18 ] ], "normalized": [] }, { "id": "BioInfer.d304.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 22, 27 ] ], "normalized": [] }, { "id": "BioInfer.d304.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 58, 63 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d304.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d304.s0.e0", "arg2_id": "BioInfer.d304.s0.e2", "normalized": [] } ]