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BigScience Biomedical Datasets 123

[ { "id": "BioInfer.d144.s0__text", "type": "Sentence", "text": [ "Coexpression of the A8R and A23R genes in Escherichia coli was required for in vitro activity." ], "offsets": [ [ 0, 94 ] ] } ]

[ { "id": "BioInfer.d144.s0.e0", "type": "Gene", "text": [ "A23R" ], "offsets": [ [ 28, 32 ] ], "normalized": [] }, { "id": "BioInfer.d144.s0.e1", "type": "Gene", "text": [ "A8R" ], "offsets": [ [ 20, 23 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d144.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d144.s0.e0", "arg2_id": "BioInfer.d144.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d144.s1__text", "type": "Sentence", "text": [ "Expression of the A8R and A23R genes occurred between 1 and 5 h after vaccinia virus infection and was not prevented by an inhibitor of DNA replication, consistent with a role for VITF-3 in specifically regulating intermediate transcription in vivo." ], "offsets": [ [ 0, 249 ] ] } ]

[ { "id": "BioInfer.d144.s1.e0", "type": "Gene/protein/RNA", "text": [ "A23R" ], "offsets": [ [ 26, 30 ] ], "normalized": [] }, { "id": "BioInfer.d144.s1.e1", "type": "Gene/protein/RNA", "text": [ "VITF-3" ], "offsets": [ [ 180, 186 ] ], "normalized": [] }, { "id": "BioInfer.d144.s1.e2", "type": "Gene/protein/RNA", "text": [ "A8R" ], "offsets": [ [ 18, 21 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d144.s2__text", "type": "Sentence", "text": [ "We found that the 34- and 45-kDa polypeptides encoded by vaccinia virus ORFs A8R and A23R, respectively, were necessary to reconstitute transcription of a template with an intermediate stage promoter." ], "offsets": [ [ 0, 200 ] ] } ]

[ { "id": "BioInfer.d144.s2.e0", "type": "Gene/protein/RNA", "text": [ "A8R" ], "offsets": [ [ 77, 80 ] ], "normalized": [] }, { "id": "BioInfer.d144.s2.e1", "type": "Gene/protein/RNA", "text": [ "A23R" ], "offsets": [ [ 85, 89 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d147.s0__text", "type": "Sentence", "text": [ "Cofilin was identified by peptide sequencing, and cofilin recruitment and Listeria tail length were found to be pH-dependent, in agreement with its recently reported role in enhancing actin filament turnover." ], "offsets": [ [ 0, 208 ] ] } ]

[ { "id": "BioInfer.d147.s0.e0", "type": "Individual_protein", "text": [ "Cofilin" ], "offsets": [ [ 0, 7 ] ], "normalized": [] }, { "id": "BioInfer.d147.s0.e1", "type": "Gene/protein/RNA", "text": [ "cofilin" ], "offsets": [ [ 50, 57 ] ], "normalized": [] }, { "id": "BioInfer.d147.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 184, 189 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d147.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d147.s0.e0", "arg2_id": "BioInfer.d147.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d148.s0__text", "type": "Sentence", "text": [ "Compared with control and contralateral kidneys, the ligated kidneys displayed a dynamic expression of mRNAs for many apoptosis-related molecules, which included an up to threefold increase for Fas, Fas ligand, TNF-R1, TRAIL, TRADD, RIP, and caspase-8, and an up to twofold increase for FADD and FAP, but there was little change for FAF." ], "offsets": [ [ 0, 337 ] ] } ]

[ { "id": "BioInfer.d148.s0.e0", "type": "Gene/protein/RNA", "text": [ "caspase-8" ], "offsets": [ [ 242, 251 ] ], "normalized": [] }, { "id": "BioInfer.d148.s0.e1", "type": "Gene/protein/RNA", "text": [ "TRAIL" ], "offsets": [ [ 219, 224 ] ], "normalized": [] }, { "id": "BioInfer.d148.s0.e2", "type": "Gene/protein/RNA", "text": [ "FAP" ], "offsets": [ [ 296, 299 ] ], "normalized": [] }, { "id": "BioInfer.d148.s0.e3", "type": "Gene/protein/RNA", "text": [ "RIP" ], "offsets": [ [ 233, 236 ] ], "normalized": [] }, { "id": "BioInfer.d148.s0.e4", "type": "Gene/protein/RNA", "text": [ "TNF-R1" ], "offsets": [ [ 211, 217 ] ], "normalized": [] }, { "id": "BioInfer.d148.s0.e5", "type": "Gene/protein/RNA", "text": [ "Fas" ], "offsets": [ [ 194, 197 ] ], "normalized": [] }, { "id": "BioInfer.d148.s0.e6", "type": "Gene/protein/RNA", "text": [ "TRADD" ], "offsets": [ [ 226, 231 ] ], "normalized": [] }, { "id": "BioInfer.d148.s0.e7", "type": "Gene/protein/RNA", "text": [ "Fas ligand" ], "offsets": [ [ 199, 209 ] ], "normalized": [] }, { "id": "BioInfer.d148.s0.e8", "type": "Gene/protein/RNA", "text": [ "FAF" ], "offsets": [ [ 333, 336 ] ], "normalized": [] }, { "id": "BioInfer.d148.s0.e9", "type": "Gene/protein/RNA", "text": [ "FADD" ], "offsets": [ [ 287, 291 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d148.s1__text", "type": "Sentence", "text": [ "To detect the expression of apoptosis-related molecules, ribonuclease protection assay was used with specific antisense RNA probes for Fas, Fas ligand, TNFR-1, TRAIL, FADD, TRADD, RIP, FAF, FAP, and caspase-8." ], "offsets": [ [ 0, 209 ] ] } ]

[ { "id": "BioInfer.d148.s1.e0", "type": "Gene/protein/RNA", "text": [ "TRAIL" ], "offsets": [ [ 160, 165 ] ], "normalized": [] }, { "id": "BioInfer.d148.s1.e1", "type": "Gene/protein/RNA", "text": [ "ribonuclease" ], "offsets": [ [ 57, 69 ] ], "normalized": [] }, { "id": "BioInfer.d148.s1.e2", "type": "Gene/protein/RNA", "text": [ "FAF" ], "offsets": [ [ 185, 188 ] ], "normalized": [] }, { "id": "BioInfer.d148.s1.e3", "type": "Gene/protein/RNA", "text": [ "FAP" ], "offsets": [ [ 190, 193 ] ], "normalized": [] }, { "id": "BioInfer.d148.s1.e4", "type": "Gene/protein/RNA", "text": [ "TRADD" ], "offsets": [ [ 173, 178 ] ], "normalized": [] }, { "id": "BioInfer.d148.s1.e5", "type": "Gene/protein/RNA", "text": [ "RIP" ], "offsets": [ [ 180, 183 ] ], "normalized": [] }, { "id": "BioInfer.d148.s1.e6", "type": "Gene/protein/RNA", "text": [ "caspase-8" ], "offsets": [ [ 199, 208 ] ], "normalized": [] }, { "id": "BioInfer.d148.s1.e7", "type": "Gene/protein/RNA", "text": [ "FADD" ], "offsets": [ [ 167, 171 ] ], "normalized": [] }, { "id": "BioInfer.d148.s1.e8", "type": "Gene/protein/RNA", "text": [ "Fas ligand" ], "offsets": [ [ 140, 150 ] ], "normalized": [] }, { "id": "BioInfer.d148.s1.e9", "type": "Gene/protein/RNA", "text": [ "TNFR-1" ], "offsets": [ [ 152, 158 ] ], "normalized": [] }, { "id": "BioInfer.d148.s1.e10", "type": "Gene/protein/RNA", "text": [ "Fas" ], "offsets": [ [ 135, 138 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d149.s0__text", "type": "Sentence", "text": [ "Complete gene sequences for the nucleocapsid protein (N) and phosphoprotein (P/V) have been determined and recombinant N and V proteins produced in baculovirus." ], "offsets": [ [ 0, 160 ] ] } ]

[ { "id": "BioInfer.d149.s0.e0", "type": "Individual_protein", "text": [ "N" ], "offsets": [ [ 54, 55 ] ], "normalized": [] }, { "id": "BioInfer.d149.s0.e1", "type": "Individual_protein", "text": [ "V" ], "offsets": [ [ 79, 80 ] ], "normalized": [] }, { "id": "BioInfer.d149.s0.e2", "type": "Gene/protein/RNA", "text": [ "V" ], "offsets": [ [ 125, 126 ] ], "normalized": [] }, { "id": "BioInfer.d149.s0.e3", "type": "Individual_protein", "text": [ "P" ], "offsets": [ [ 77, 78 ] ], "normalized": [] }, { "id": "BioInfer.d149.s0.e4", "type": "Gene/protein/RNA", "text": [ "N" ], "offsets": [ [ 119, 120 ] ], "normalized": [] }, { "id": "BioInfer.d149.s0.e5", "type": "Individual_protein", "text": [ "phosphoprotein" ], "offsets": [ [ 61, 75 ] ], "normalized": [] }, { "id": "BioInfer.d149.s0.e6", "type": "Individual_protein", "text": [ "nucleocapsid protein" ], "offsets": [ [ 32, 52 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d149.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d149.s0.e1", "arg2_id": "BioInfer.d149.s0.e5", "normalized": [] }, { "id": "BioInfer.d149.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d149.s0.e3", "arg2_id": "BioInfer.d149.s0.e5", "normalized": [] } ]

[ { "id": "BioInfer.d150.s0__text", "type": "Sentence", "text": [ "CONCLUSIONS: The expression of alpha-catenin, beta-catenin, and gamma-catenin is related to histological type and differentiation in NSCLC, although catenins have no independent prognostic value." ], "offsets": [ [ 0, 195 ] ] } ]

[ { "id": "BioInfer.d150.s0.e0", "type": "Gene/protein/RNA", "text": [ "catenins" ], "offsets": [ [ 149, 157 ] ], "normalized": [] }, { "id": "BioInfer.d150.s0.e1", "type": "Gene/protein/RNA", "text": [ "beta-catenin" ], "offsets": [ [ 46, 58 ] ], "normalized": [] }, { "id": "BioInfer.d150.s0.e2", "type": "Gene/protein/RNA", "text": [ "gamma-catenin" ], "offsets": [ [ 64, 77 ] ], "normalized": [] }, { "id": "BioInfer.d150.s0.e3", "type": "Gene/protein/RNA", "text": [ "alpha-catenin" ], "offsets": [ [ 31, 44 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d150.s1__text", "type": "Sentence", "text": [ "Reduced expression of alpha-catenin, beta-catenin, and gamma-catenin is associated with high cell proliferative activity and poor differentiation in non-small cell lung cancer." ], "offsets": [ [ 0, 176 ] ] } ]

[ { "id": "BioInfer.d150.s1.e0", "type": "Gene/protein/RNA", "text": [ "gamma-catenin" ], "offsets": [ [ 55, 68 ] ], "normalized": [] }, { "id": "BioInfer.d150.s1.e1", "type": "Gene/protein/RNA", "text": [ "alpha-catenin" ], "offsets": [ [ 22, 35 ] ], "normalized": [] }, { "id": "BioInfer.d150.s1.e2", "type": "Gene/protein/RNA", "text": [ "beta-catenin" ], "offsets": [ [ 37, 49 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d151.s0__text", "type": "Sentence", "text": [ "CONCLUSIONS: These results suggest the cooperative modulation of the actin cytoskeleton by cofilin and Aip1." ], "offsets": [ [ 0, 108 ] ] } ]

[ { "id": "BioInfer.d151.s0.e0", "type": "Individual_protein", "text": [ "Aip1" ], "offsets": [ [ 103, 107 ] ], "normalized": [] }, { "id": "BioInfer.d151.s0.e1", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 91, 98 ] ], "normalized": [] }, { "id": "BioInfer.d151.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 69, 74 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d151.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d151.s0.e0", "arg2_id": "BioInfer.d151.s0.e1", "normalized": [] }, { "id": "BioInfer.d151.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d151.s0.e0", "arg2_id": "BioInfer.d151.s0.e2", "normalized": [] }, { "id": "BioInfer.d151.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d151.s0.e1", "arg2_id": "BioInfer.d151.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d151.s1__text", "type": "Sentence", "text": [ "Immunofluorescence staining of a wild-type strain using anti-Aip1 antibodies revealed that Aip1 was distributed in cortical actin patches where cofilin was also co-localized." ], "offsets": [ [ 0, 174 ] ] } ]

[ { "id": "BioInfer.d151.s1.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 124, 129 ] ], "normalized": [] }, { "id": "BioInfer.d151.s1.e1", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 144, 151 ] ], "normalized": [] }, { "id": "BioInfer.d151.s1.e2", "type": "Individual_protein", "text": [ "Aip1" ], "offsets": [ [ 91, 95 ] ], "normalized": [] }, { "id": "BioInfer.d151.s1.e3", "type": "Gene/protein/RNA", "text": [ "Aip1" ], "offsets": [ [ 61, 65 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d151.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d151.s1.e0", "arg2_id": "BioInfer.d151.s1.e1", "normalized": [] }, { "id": "BioInfer.d151.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d151.s1.e0", "arg2_id": "BioInfer.d151.s1.e2", "normalized": [] } ]

[ { "id": "BioInfer.d153.s0__text", "type": "Sentence", "text": [ "Confluent calf pulmonary artery endothelial monolayers exposed to 95% oxygen for 1, 2, or 3 days exhibit a time-dependent increase in adherence to substratum, which closely parallels changes in actin cytoarchitecture and the distribution of focal contact proteins vinculin and talin." ], "offsets": [ [ 0, 283 ] ] } ]

[ { "id": "BioInfer.d153.s0.e0", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 194, 199 ] ], "normalized": [] }, { "id": "BioInfer.d153.s0.e1", "type": "Gene/protein/RNA", "text": [ "talin" ], "offsets": [ [ 277, 282 ] ], "normalized": [] }, { "id": "BioInfer.d153.s0.e2", "type": "Gene/protein/RNA", "text": [ "vinculin" ], "offsets": [ [ 264, 272 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d154.s0__text", "type": "Sentence", "text": [ "Conversely, inhibition of LIMK's activity by expressing a dominant negative construct, LIMK1-, or expression of the constitutively active S3A cofilin mutant induces loss of actin filaments at the phagocytic cup and also inhibits phagocytosis." ], "offsets": [ [ 0, 242 ] ] } ]

[ { "id": "BioInfer.d154.s0.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 173, 178 ] ], "normalized": [] }, { "id": "BioInfer.d154.s0.e1", "type": "Individual_protein", "text": [ "LIMK" ], "offsets": [ [ 26, 30 ] ], "normalized": [] }, { "id": "BioInfer.d154.s0.e2", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 142, 149 ] ], "normalized": [] }, { "id": "BioInfer.d154.s0.e3", "type": "Individual_protein", "text": [ "LIMK1-" ], "offsets": [ [ 87, 93 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d154.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d154.s0.e0", "arg2_id": "BioInfer.d154.s0.e1", "normalized": [] }, { "id": "BioInfer.d154.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d154.s0.e0", "arg2_id": "BioInfer.d154.s0.e2", "normalized": [] }, { "id": "BioInfer.d154.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d154.s0.e0", "arg2_id": "BioInfer.d154.s0.e3", "normalized": [] }, { "id": "BioInfer.d154.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d154.s0.e1", "arg2_id": "BioInfer.d154.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d155.s0__text", "type": "Sentence", "text": [ "Co-precipitation experiments using whole cell lysates indicate that the mutant form of alpha-catenin binds beta-catenin and plakoglobin, and can form a structural complex with E-cadherin via these interactions." ], "offsets": [ [ 0, 210 ] ] } ]

[ { "id": "BioInfer.d155.s0.e0", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 87, 100 ] ], "normalized": [] }, { "id": "BioInfer.d155.s0.e1", "type": "Individual_protein", "text": [ "E-cadherin" ], "offsets": [ [ 176, 186 ] ], "normalized": [] }, { "id": "BioInfer.d155.s0.e2", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 107, 119 ] ], "normalized": [] }, { "id": "BioInfer.d155.s0.e3", "type": "Individual_protein", "text": [ "plakoglobin" ], "offsets": [ [ 124, 135 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d155.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d155.s0.e0", "arg2_id": "BioInfer.d155.s0.e1", "normalized": [] }, { "id": "BioInfer.d155.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d155.s0.e0", "arg2_id": "BioInfer.d155.s0.e2", "normalized": [] }, { "id": "BioInfer.d155.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d155.s0.e0", "arg2_id": "BioInfer.d155.s0.e3", "normalized": [] }, { "id": "BioInfer.d155.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d155.s0.e1", "arg2_id": "BioInfer.d155.s0.e2", "normalized": [] }, { "id": "BioInfer.d155.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d155.s0.e1", "arg2_id": "BioInfer.d155.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d156.s0__text", "type": "Sentence", "text": [ "Coprecipitations revealed that transfected cadherin molecules are complexed with alpha-catenin and beta-catenin at plasma membranes." ], "offsets": [ [ 0, 132 ] ] } ]

[ { "id": "BioInfer.d156.s0.e0", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 99, 111 ] ], "normalized": [] }, { "id": "BioInfer.d156.s0.e1", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 81, 94 ] ], "normalized": [] }, { "id": "BioInfer.d156.s0.e2", "type": "Individual_protein", "text": [ "cadherin" ], "offsets": [ [ 43, 51 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d156.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d156.s0.e0", "arg2_id": "BioInfer.d156.s0.e1", "normalized": [] }, { "id": "BioInfer.d156.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d156.s0.e0", "arg2_id": "BioInfer.d156.s0.e2", "normalized": [] }, { "id": "BioInfer.d156.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d156.s0.e1", "arg2_id": "BioInfer.d156.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d157.s0__text", "type": "Sentence", "text": [ "Cotransfections with different combinations of these genes demonstrated that a subset of four of them, coding for the HSV helicase-primase complex (UL5, UL8, UL52) and the major DNA-binding protein (UL29), was already sufficient to mediate the helper effect." ], "offsets": [ [ 0, 258 ] ] } ]

[ { "id": "BioInfer.d157.s0.e0", "type": "Protein_complex", "text": [ "helicase-primase" ], "offsets": [ [ 122, 138 ] ], "normalized": [] }, { "id": "BioInfer.d157.s0.e1", "type": "Individual_protein", "text": [ "UL29" ], "offsets": [ [ 199, 203 ] ], "normalized": [] }, { "id": "BioInfer.d157.s0.e2", "type": "Individual_protein", "text": [ "UL52" ], "offsets": [ [ 158, 162 ] ], "normalized": [] }, { "id": "BioInfer.d157.s0.e3", "type": "Individual_protein", "text": [ "major DNA-binding protein" ], "offsets": [ [ 172, 197 ] ], "normalized": [] }, { "id": "BioInfer.d157.s0.e4", "type": "Individual_protein", "text": [ "UL5" ], "offsets": [ [ 148, 151 ] ], "normalized": [] }, { "id": "BioInfer.d157.s0.e5", "type": "Individual_protein", "text": [ "UL8" ], "offsets": [ [ 153, 156 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d157.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d157.s0.e0", "arg2_id": "BioInfer.d157.s0.e2", "normalized": [] }, { "id": "BioInfer.d157.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d157.s0.e0", "arg2_id": "BioInfer.d157.s0.e4", "normalized": [] }, { "id": "BioInfer.d157.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d157.s0.e0", "arg2_id": "BioInfer.d157.s0.e5", "normalized": [] }, { "id": "BioInfer.d157.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d157.s0.e2", "arg2_id": "BioInfer.d157.s0.e4", "normalized": [] }, { "id": "BioInfer.d157.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d157.s0.e2", "arg2_id": "BioInfer.d157.s0.e5", "normalized": [] }, { "id": "BioInfer.d157.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d157.s0.e4", "arg2_id": "BioInfer.d157.s0.e5", "normalized": [] } ]

[ { "id": "BioInfer.d158.s0__text", "type": "Sentence", "text": [ "Crystallization and preliminary crystallographic analysis of the N-terminal actin binding domain of human fimbrin." ], "offsets": [ [ 0, 114 ] ] } ]

[ { "id": "BioInfer.d158.s0.e0", "type": "Individual_protein", "text": [ "fimbrin" ], "offsets": [ [ 106, 113 ] ], "normalized": [] }, { "id": "BioInfer.d158.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 76, 81 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d158.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d158.s0.e0", "arg2_id": "BioInfer.d158.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d159.s0__text", "type": "Sentence", "text": [ "CV-1 cells were transfected with cloned genes from wild-type HPIV-3 encoding the large protein (L), phosphoprotein (P), and nucleocapsid protein (NP), alone or together, for the expression of biologically active proteins." ], "offsets": [ [ 0, 221 ] ] } ]

[ { "id": "BioInfer.d159.s0.e0", "type": "Individual_protein", "text": [ "L" ], "offsets": [ [ 96, 97 ] ], "normalized": [] }, { "id": "BioInfer.d159.s0.e1", "type": "Individual_protein", "text": [ "NP" ], "offsets": [ [ 146, 148 ] ], "normalized": [] }, { "id": "BioInfer.d159.s0.e2", "type": "Individual_protein", "text": [ "nucleocapsid protein" ], "offsets": [ [ 124, 144 ] ], "normalized": [] }, { "id": "BioInfer.d159.s0.e3", "type": "Individual_protein", "text": [ "large protein" ], "offsets": [ [ 81, 94 ] ], "normalized": [] }, { "id": "BioInfer.d159.s0.e4", "type": "Individual_protein", "text": [ "P" ], "offsets": [ [ 116, 117 ] ], "normalized": [] }, { "id": "BioInfer.d159.s0.e5", "type": "Individual_protein", "text": [ "phosphoprotein" ], "offsets": [ [ 100, 114 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d160.s0__text", "type": "Sentence", "text": [ "Cytoplasmic staining included stress fibers that colocalized with actin, probably as a consequence of the myosin heavy chain component of the fusion protein." ], "offsets": [ [ 0, 157 ] ] } ]

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[ { "id": "BioInfer.d161.s0__text", "type": "Sentence", "text": [ "Data from affinity chromatography, analytical ultracentrifugation, covalent cross-linking, and fluorescence anisotropy show that profilin, thymosin beta(4), and actin form a ternary complex." ], "offsets": [ [ 0, 190 ] ] } ]

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[ { "id": "BioInfer.d161.s1__text", "type": "Sentence", "text": [ "Experiments using a peptide that corresponds to the N-terminus of thymosin beta(4) (residues 6-22) confirm the presence of an extensive binding surface between actin and thymosin beta(4), and explain why thymosin beta(4) and profilin can bind simultaneously to actin." ], "offsets": [ [ 0, 267 ] ] } ]

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[ { "id": "BioInfer.d162.s0__text", "type": "Sentence", "text": [ "Data is presented to suggest that the G1 cyclin D1 and the cyclin-dependent kinase inhibitor p27KIP1 may be involved in subversion of the G1/S traverse by signaling pathways activated by HER-2 function." ], "offsets": [ [ 0, 202 ] ] } ]

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[ { "id": "BioInfer.d162.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d162.s0.e0", "arg2_id": "BioInfer.d162.s0.e2", "normalized": [] }, { "id": "BioInfer.d162.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d162.s0.e1", "arg2_id": "BioInfer.d162.s0.e2", "normalized": [] }, { "id": "BioInfer.d162.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d162.s0.e1", "arg2_id": "BioInfer.d162.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d163.s0__text", "type": "Sentence", "text": [ "Data presented here suggest that two of the repressed genes encode the proteins actin and myosin heavy chain." ], "offsets": [ [ 0, 109 ] ] } ]

[ { "id": "BioInfer.d163.s0.e0", "type": "Gene/protein/RNA", "text": [ "myosin heavy chain" ], "offsets": [ [ 90, 108 ] ], "normalized": [] }, { "id": "BioInfer.d163.s0.e1", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 80, 85 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d163.s1__text", "type": "Sentence", "text": [ "Selective repression of actin and myosin heavy chain expression during the programmed death of insect skeletal muscle." ], "offsets": [ [ 0, 118 ] ] } ]

[ { "id": "BioInfer.d163.s1.e0", "type": "Gene/protein/RNA", "text": [ "myosin heavy chain" ], "offsets": [ [ 34, 52 ] ], "normalized": [] }, { "id": "BioInfer.d163.s1.e1", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 24, 29 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d163.s2__text", "type": "Sentence", "text": [ "The reduction in actin and myosin heavy chain synthesis presumably plays a role in the rapid dissolution of the muscles." ], "offsets": [ [ 0, 120 ] ] } ]

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[ { "id": "BioInfer.d164.s0__text", "type": "Sentence", "text": [ "Death receptors belong to the TNF receptor family and are characterised by an intracellular death domain that serves to recruit adapter proteins such as TRADD and FADD and cysteine proteases such as Caspase-8." ], "offsets": [ [ 0, 209 ] ] } ]

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[ { "id": "BioInfer.d164.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d164.s0.e0", "arg2_id": "BioInfer.d164.s0.e2", "normalized": [] }, { "id": "BioInfer.d164.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d164.s0.e0", "arg2_id": "BioInfer.d164.s0.e3", "normalized": [] }, { "id": "BioInfer.d164.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d164.s0.e0", "arg2_id": "BioInfer.d164.s0.e4", "normalized": [] }, { "id": "BioInfer.d164.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d164.s0.e0", "arg2_id": "BioInfer.d164.s0.e5", "normalized": [] }, { "id": "BioInfer.d164.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d164.s0.e1", "arg2_id": "BioInfer.d164.s0.e4", "normalized": [] } ]

[ { "id": "BioInfer.d165.s0__text", "type": "Sentence", "text": [ "Deletion and overexpression studies demonstrate that SIR2, but not SIR1, SIR3 or SIR4, is required for this rDNA position effect." ], "offsets": [ [ 0, 129 ] ] } ]

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[ { "id": "BioInfer.d166.s0__text", "type": "Sentence", "text": [ "Deletion of both RAD50 and RAD51 produces a phenotype similar to that produced by deletion of RAD52." ], "offsets": [ [ 0, 100 ] ] } ]

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[ { "id": "BioInfer.d166.s1__text", "type": "Sentence", "text": [ "rad59 mutations completely abolished the ability to generate type II survivors, while rad50 mutations decreased the growth viability of type II survivors but did not completely eliminate their appearance." ], "offsets": [ [ 0, 204 ] ] } ]

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[ { "id": "BioInfer.d167.s0__text", "type": "Sentence", "text": [ "Deletion of SIR4 enhanced mURA3 and MET15 silencing, but deletion of SIR1 or SIR3 did not affect silencing, indicating that the mechanism of silencing differs from that at telomeres and silent mating loci." ], "offsets": [ [ 0, 205 ] ] } ]

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[ { "id": "BioInfer.d168.s0__text", "type": "Sentence", "text": [ "Demembranated stereociliary cores consisted primarily of protein bands corresponding to actin and fimbrin and several proteins ranging from 43 to 63 kDa." ], "offsets": [ [ 0, 153 ] ] } ]

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[ { "id": "BioInfer.d168.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d168.s0.e0", "arg2_id": "BioInfer.d168.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d169.s0__text", "type": "Sentence", "text": [ "Depending on the nature of the divalent cation, recombinant plant (birch) profilin exhibited two different modes of interaction with actin, like mammalian profilin." ], "offsets": [ [ 0, 164 ] ] } ]

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[ { "id": "BioInfer.d169.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d169.s0.e0", "arg2_id": "BioInfer.d169.s0.e1", "normalized": [] }, { "id": "BioInfer.d169.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d169.s0.e0", "arg2_id": "BioInfer.d169.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d169.s1__text", "type": "Sentence", "text": [ "In the presence of magnesium ions birch profilin promoted the polymerization of actin from A:Tbeta4." ], "offsets": [ [ 0, 100 ] ] } ]

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[ { "id": "BioInfer.d169.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d169.s1.e0", "arg2_id": "BioInfer.d169.s1.e1", "normalized": [] }, { "id": "BioInfer.d169.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d169.s1.e0", "arg2_id": "BioInfer.d169.s1.e3", "normalized": [] }, { "id": "BioInfer.d169.s1.i2", "type": "PPI", "arg1_id": "BioInfer.d169.s1.e1", "arg2_id": "BioInfer.d169.s1.e2", "normalized": [] }, { "id": "BioInfer.d169.s1.i3", "type": "PPI", "arg1_id": "BioInfer.d169.s1.e1", "arg2_id": "BioInfer.d169.s1.e3", "normalized": [] } ]

[ { "id": "BioInfer.d169.s2__text", "type": "Sentence", "text": [ "Recombinant plant (birch) profilin was analyzed for its ability to promote actin polymerization from the actin:thymosin beta4 and beta9 complex." ], "offsets": [ [ 0, 144 ] ] } ]

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[ { "id": "BioInfer.d169.s3__text", "type": "Sentence", "text": [ "These data indicated a negative co-operativity between the profilin and DNase I binding sites on actin." ], "offsets": [ [ 0, 103 ] ] } ]

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[ { "id": "BioInfer.d169.s3.i0", "type": "PPI", "arg1_id": "BioInfer.d169.s3.e0", "arg2_id": "BioInfer.d169.s3.e1", "normalized": [] }, { "id": "BioInfer.d169.s3.i1", "type": "PPI", "arg1_id": "BioInfer.d169.s3.e0", "arg2_id": "BioInfer.d169.s3.e2", "normalized": [] }, { "id": "BioInfer.d169.s3.i2", "type": "PPI", "arg1_id": "BioInfer.d169.s3.e1", "arg2_id": "BioInfer.d169.s3.e2", "normalized": [] } ]

[ { "id": "BioInfer.d170.s0__text", "type": "Sentence", "text": [ "Detection of a sequence involved in actin-binding and phosphoinositide-binding in the N-terminal side of cofilin." ], "offsets": [ [ 0, 113 ] ] } ]

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[ { "id": "BioInfer.d170.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d170.s0.e0", "arg2_id": "BioInfer.d170.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d170.s1__text", "type": "Sentence", "text": [ "The truncated cofilin molecules produced in E. coli were purified and examined for their actin-binding and PIP2-binding ability." ], "offsets": [ [ 0, 128 ] ] } ]

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[ { "id": "BioInfer.d171.s0__text", "type": "Sentence", "text": [ "Detection of loss of heterozygosity at RAD51, RAD52, RAD54 and BRCA1 and BRCA2 loci in breast cancer: pathological correlations." ], "offsets": [ [ 0, 128 ] ] } ]

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[ { "id": "BioInfer.d171.s1__text", "type": "Sentence", "text": [ "LOH was found in the RAD51 region in 32% of tumours, in the RAD52 region in 16%, in RAD54 in 20% and in the BRCA1 and BRCA2 regions in 49% and 44% respectively." ], "offsets": [ [ 0, 160 ] ] } ]

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[ { "id": "BioInfer.d171.s2__text", "type": "Sentence", "text": [ "We investigate allelic losses in microsatellites of the RAD51, RAD52, RAD54, BRCA1 and BRCA2 regions, and their correlations with nine pathologic parameters in 127 breast carcinomas." ], "offsets": [ [ 0, 182 ] ] } ]

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[ { "id": "BioInfer.d172.s0__text", "type": "Sentence", "text": [ "Developmental changes in actin and myosin heavy chain isoform expression in smooth muscle." ], "offsets": [ [ 0, 90 ] ] } ]

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[ { "id": "BioInfer.d173.s0__text", "type": "Sentence", "text": [ "Digestion of isolated myofibrils with alkaline proteinase resulted in the degradation of myosin heavy chain and actin." ], "offsets": [ [ 0, 118 ] ] } ]

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[ { "id": "BioInfer.d174.s0__text", "type": "Sentence", "text": [ "Direct binding of the verprolin-homology domain in N-WASP to actin is essential for cytoskeletal reorganization." ], "offsets": [ [ 0, 112 ] ] } ]

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[ { "id": "BioInfer.d174.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d174.s0.e0", "arg2_id": "BioInfer.d174.s0.e2", "normalized": [] }, { "id": "BioInfer.d174.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d174.s0.e1", "arg2_id": "BioInfer.d174.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d174.s1__text", "type": "Sentence", "text": [ "Recently, two mammalian proteins previously shown to regulate the actin cytoskeleton, Wiskott-Aldrich Syndrome Protein (WASP) and its homolog expressed in neurons (N-WASP), were found to possess short peptide motifs homologous to one part of verprolin." ], "offsets": [ [ 0, 252 ] ] } ]

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[ { "id": "BioInfer.d175.s0__text", "type": "Sentence", "text": [ "Discrete segments (70-150 amino acids) of PRT1 and TIF35 were found to be responsible for their binding to TIF34." ], "offsets": [ [ 0, 113 ] ] } ]

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[ { "id": "BioInfer.d175.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d175.s0.e0", "arg2_id": "BioInfer.d175.s0.e1", "normalized": [] }, { "id": "BioInfer.d175.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d175.s0.e1", "arg2_id": "BioInfer.d175.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d175.s1__text", "type": "Sentence", "text": [ "The PRT1, TIF34, GCD10, and SUI1 proteins of Saccharomyces cerevisiae were found previously to copurify with eukaryotic translation initiation factor 3 (eIF3) activity." ], "offsets": [ [ 0, 168 ] ] } ]

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[ { "id": "BioInfer.d177.s0__text", "type": "Sentence", "text": [ "Disruption of the RVS167 gene, which is homologous to END6/RVS161 and which is also required for correct actin localization, also blocks endocytosis." ], "offsets": [ [ 0, 149 ] ] } ]

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[ { "id": "BioInfer.d177.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d177.s0.e0", "arg2_id": "BioInfer.d177.s0.e3", "normalized": [] }, { "id": "BioInfer.d177.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d177.s0.e1", "arg2_id": "BioInfer.d177.s0.e3", "normalized": [] }, { "id": "BioInfer.d177.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d177.s0.e2", "arg2_id": "BioInfer.d177.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d178.s0__text", "type": "Sentence", "text": [ "DNA sequence analysis of the cdc3+ gene reveals that it encodes profilin, an actin-monomer-binding protein." ], "offsets": [ [ 0, 107 ] ] } ]

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[ { "id": "BioInfer.d178.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d178.s0.e0", "arg2_id": "BioInfer.d178.s0.e1", "normalized": [] }, { "id": "BioInfer.d178.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d178.s0.e0", "arg2_id": "BioInfer.d178.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d178.s1__text", "type": "Sentence", "text": [ "We attribute these effects to potential sequestration of actin monomers by profilin, when present in excess." ], "offsets": [ [ 0, 108 ] ] } ]

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[ { "id": "BioInfer.d178.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d178.s1.e0", "arg2_id": "BioInfer.d178.s1.e1", "normalized": [] } ]

[ { "id": "BioInfer.d179.s0__text", "type": "Sentence", "text": [ "Double mutants containing N-terminal domain deletions of both histone H3 and histone H4 were inviable." ], "offsets": [ [ 0, 102 ] ] } ]

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[ { "id": "BioInfer.d179.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d179.s0.e0", "arg2_id": "BioInfer.d179.s0.e3", "normalized": [] }, { "id": "BioInfer.d179.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d179.s0.e1", "arg2_id": "BioInfer.d179.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d180.s0__text", "type": "Sentence", "text": [ "DR3 signal transduction is mediated by a complex of intracellular signaling molecules including TRADD, TRAF2, FADD, and FLICE." ], "offsets": [ [ 0, 126 ] ] } ]

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[ { "id": "BioInfer.d180.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d180.s0.e0", "arg2_id": "BioInfer.d180.s0.e2", "normalized": [] }, { "id": "BioInfer.d180.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d180.s0.e0", "arg2_id": "BioInfer.d180.s0.e3", "normalized": [] }, { "id": "BioInfer.d180.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d180.s0.e0", "arg2_id": "BioInfer.d180.s0.e4", "normalized": [] }, { "id": "BioInfer.d180.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d180.s0.e2", "arg2_id": "BioInfer.d180.s0.e3", "normalized": [] }, { "id": "BioInfer.d180.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d180.s0.e2", "arg2_id": "BioInfer.d180.s0.e4", "normalized": [] }, { "id": "BioInfer.d180.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d180.s0.e3", "arg2_id": "BioInfer.d180.s0.e4", "normalized": [] } ]

[ { "id": "BioInfer.d181.s0__text", "type": "Sentence", "text": [ "During apoptotic process induced by the agents, expression of cyclin-dependent kinase inhibitors p21 and p27 increased, whereas expression of cyclin D1 decreased." ], "offsets": [ [ 0, 162 ] ] } ]

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[ { "id": "BioInfer.d181.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d181.s0.e0", "arg2_id": "BioInfer.d181.s0.e2", "normalized": [] }, { "id": "BioInfer.d181.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d181.s0.e1", "arg2_id": "BioInfer.d181.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d182.s0__text", "type": "Sentence", "text": [ "During incubation of whole myofibrils at 37 degrees C, myosin heavy chain, alpha actinin, actin and troponin T suffered degradation." ], "offsets": [ [ 0, 132 ] ] } ]

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[ { "id": "BioInfer.d183.s0__text", "type": "Sentence", "text": [ "Dynamic actin structures stabilized by profilin." ], "offsets": [ [ 0, 48 ] ] } ]

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[ { "id": "BioInfer.d183.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d183.s0.e0", "arg2_id": "BioInfer.d183.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d183.s1__text", "type": "Sentence", "text": [ "The distribution of actin filaments is altered by profilin overexpression." ], "offsets": [ [ 0, 74 ] ] } ]

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[ { "id": "BioInfer.d183.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d183.s1.e0", "arg2_id": "BioInfer.d183.s1.e1", "normalized": [] } ]

[ { "id": "BioInfer.d183.s2__text", "type": "Sentence", "text": [ "While parallel actin bundles crossing the cells are virtually absent in cells overexpressing profilin, the submembranous actin network of these cells is denser than in control cells." ], "offsets": [ [ 0, 182 ] ] } ]

[ { "id": "BioInfer.d183.s2.e0", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 121, 126 ] ], "normalized": [] }, { "id": "BioInfer.d183.s2.e1", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 15, 20 ] ], "normalized": [] }, { "id": "BioInfer.d183.s2.e2", "type": "Gene/protein/RNA", "text": [ "profilin" ], "offsets": [ [ 93, 101 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d184.s0__text", "type": "Sentence", "text": [ "Effects of profilin-annexin I association on some properties of both profilin and annexin I: modification of the inhibitory activity of profilin on actin polymerization and inhibition of the self-association of annexin I and its interactions with liposomes." ], "offsets": [ [ 0, 257 ] ] } ]

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[ { "id": "BioInfer.d187.s0__text", "type": "Sentence", "text": [ "Effects of single amino acid substitutions in the actin-binding site on the biological activity of bovine profilin I." ], "offsets": [ [ 0, 117 ] ] } ]

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[ { "id": "BioInfer.d187.s2__text", "type": "Sentence", "text": [ "These results emphasize the highly conserved biological function of profilins with low sequence homology, and correlate specifically their actin-binding capacity with cell motility and proliferation." ], "offsets": [ [ 0, 199 ] ] } ]

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[ { "id": "BioInfer.d188.s0__text", "type": "Sentence", "text": [ "Electrical stimulation of cardiocyte contraction did not enhance alpha-cardiac actin or myosin heavy chain (alpha+beta) mRNA transcript levels relative to 28S rRNA during the period of rapid growth that occurred over the first 48 hours." ], "offsets": [ [ 0, 236 ] ] } ]

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[ { "id": "BioInfer.d189.s0__text", "type": "Sentence", "text": [ "Elevation of cAMP induced morphologic alterations indicative of changes in the adhesive status of the macrophage, including cell rounding and disassembly of structures that represent points of contact with substrate containing actin and talin." ], "offsets": [ [ 0, 243 ] ] } ]

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[ { "id": "BioInfer.d190.s0__text", "type": "Sentence", "text": [ "END5 encodes a proline-rich protein (End5p or verprolin) required for a polarised cortical actin cytoskeleton and endocytosis [2,3]." ], "offsets": [ [ 0, 132 ] ] } ]

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[ { "id": "BioInfer.d191.s0__text", "type": "Sentence", "text": [ "Equine satellite cell clone SE-11 and ovine satellite cell clone I(1)were evaluated for expression of myosin heavy chain, myogenin, desmin, and muscle-specific actin over a 240 h period in culture." ], "offsets": [ [ 0, 197 ] ] } ]

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[ { "id": "BioInfer.d192.s0__text", "type": "Sentence", "text": [ "Essential domains of the PRP21 splicing factor are implicated in the binding to PRP9 and PRP11 proteins and are conserved through evolution." ], "offsets": [ [ 0, 140 ] ] } ]

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[ { "id": "BioInfer.d193.s0__text", "type": "Sentence", "text": [ "Evaluation of the binding of Acanthamoeba profilin to pyrene-labeled actin by fluorescence enhancement." ], "offsets": [ [ 0, 103 ] ] } ]

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[ { "id": "BioInfer.d195.s0__text", "type": "Sentence", "text": [ "Evidence for a conformational change in actin induced by fimbrin (N375) binding." ], "offsets": [ [ 0, 80 ] ] } ]

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[ { "id": "BioInfer.d197.s0__text", "type": "Sentence", "text": [ "Exclusion of cardiac myosin heavy chain and actin gene involvement in hypertrophic cardiomyopathy of several French families." ], "offsets": [ [ 0, 125 ] ] } ]

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[ { "id": "BioInfer.d199.s0__text", "type": "Sentence", "text": [ "Exposure of the cells to tumor promoter did, however, result in a loss of actin and talin-rich cell surface elaborations that resemble focal contact precursor structures." ], "offsets": [ [ 0, 170 ] ] } ]

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[ { "id": "BioInfer.d201.s0__text", "type": "Sentence", "text": [ "Expression of actin and myosin heavy chain genes in skeletal, cardiac and uterine muscles of young and old rats." ], "offsets": [ [ 0, 112 ] ] } ]

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[ { "id": "BioInfer.d202.s0__text", "type": "Sentence", "text": [ "Expression of alpha-catenin was generally weak and did not correlate with the expression of either beta-catenin or E-cadherin." ], "offsets": [ [ 0, 126 ] ] } ]

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[ { "id": "BioInfer.d207.s0__text", "type": "Sentence", "text": [ "Features studied were actin, microtubules, vinculin, and talin, using immunofluorescence, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and immunoblotting; permeability of the cell sheet; wound healing; and phagocytic capacity." ], "offsets": [ [ 0, 240 ] ] } ]

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[ { "id": "BioInfer.d208.s0__text", "type": "Sentence", "text": [ "Finally, both receptors can interact with FADD, TRADD, and RIP." ], "offsets": [ [ 0, 63 ] ] } ]

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[ { "id": "BioInfer.d208.s1__text", "type": "Sentence", "text": [ "Thus, both DR5 and DR4 use FADD, TRADD, and RIP in their signal transduction pathways, and FADD is the common mediator of apoptosis by all known death domain-containing receptors." ], "offsets": [ [ 0, 179 ] ] } ]

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[ { "id": "BioInfer.d209.s0__text", "type": "Sentence", "text": [ "Finally it was shown that the two isoforms of actin can be separated from each other in the absence of profilin also by chromatography on hydroxyapatite." ], "offsets": [ [ 0, 153 ] ] } ]

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[ { "id": "BioInfer.d210.s0__text", "type": "Sentence", "text": [ "Finally, we evaluated the acetylation of three putative PCAF substrates, histones H3 and H4 and the transcription factor p53, and have determined that histone H3 is significantly preferred over the histone H4 and p53 substrates." ], "offsets": [ [ 0, 228 ] ] } ]

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[ { "id": "BioInfer.d212.s0__text", "type": "Sentence", "text": [ "First, the C-terminal verprolin-cofilin-acidic domain was shown to be essential for the regulation of actin cytoskeleton." ], "offsets": [ [ 0, 121 ] ] } ]

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[ { "id": "BioInfer.d213.s0__text", "type": "Sentence", "text": [ "Fluorescent actin analogs with a high affinity for profilin in vitro exhibit an enhanced gradient of assembly in living cells." ], "offsets": [ [ 0, 126 ] ] } ]

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[ { "id": "BioInfer.d213.s1__text", "type": "Sentence", "text": [ "Three-dimensional fluorescence microscopy of the fluorescent analog of actin with a high affinity for profilin revealed that it incorporated into cortical cytoplasmic fibers and was also distributed diffusely in the non-cortical cytoplasm consistent with a bias of actin assembly near the surface of the cell." ], "offsets": [ [ 0, 309 ] ] } ]

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[ { "id": "BioInfer.d213.s2__text", "type": "Sentence", "text": [ "To test these models in living cells using imaging techniques, we prepared a new fluorescent analog of actin that bound profilin, a protein that interacts with phosphoinositides and actin-monomers in a mutually exclusive manner, with an order of magnitude greater affinity (Kd = 3.6 microM) than cys-374-labeled actin (Kd > 30 microM), yet retained the ability to inhibit DNase I." ], "offsets": [ [ 0, 380 ] ] } ]

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[ { "id": "BioInfer.d214.s0__text", "type": "Sentence", "text": [ "Fluorographic analysis showed that the specific activity of soluble actin was two to three times that of its particulate form and that soluble actin, cofilin, actin depolymerizing factor, and profilin were transported at similar rates in slow component b of axonal flow." ], "offsets": [ [ 0, 270 ] ] } ]

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[ { "id": "BioInfer.d214.s1__text", "type": "Sentence", "text": [ "Our data strongly support the view that the mobile form of actin in slow transport is soluble and that a substantial amount of this actin may travel as a complex with actin depolymerizing factor, cofilin, and profilin." ], "offsets": [ [ 0, 218 ] ] } ]

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[ { "id": "BioInfer.d214.s2__text", "type": "Sentence", "text": [ "We examined the axonal transport of actin and its monomer binding proteins, actin depolymerizing factor, cofilin, and profilin, in the chicken sciatic nerve following injection of [35S]methionine into the lumbar spinal cord." ], "offsets": [ [ 0, 224 ] ] } ]

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[ { "id": "BioInfer.d215.s0__text", "type": "Sentence", "text": [ "For example, it is associated with alpha-catenin and beta-catenin (Armadillo), and protected from trypsin digestion only in the presence of Ca2+, as is the case for many of classic cadherins." ], "offsets": [ [ 0, 191 ] ] } ]

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[ { "id": "BioInfer.d216.s0__text", "type": "Sentence", "text": [ "From an analysis of profilin mutants, whose actin cytoskeleton is disrupted, we found that E-APC also requires actin filaments to associate with adhesive cell membranes in the ovary." ], "offsets": [ [ 0, 182 ] ] } ]

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[ { "id": "BioInfer.d216.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d216.s0.e0", "arg2_id": "BioInfer.d216.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d218.s0__text", "type": "Sentence", "text": [ "From these observations it is concluded that (i) RAD52 is required for high levels of both gene conversions and reciprocal crossovers, (ii) that RAD51 is not required for intrachromosomal crossovers, and (iii) that RAD51 and RAD52 have different functions, or that RAD52 has functions in addition to those of the Rad51/Rad52 protein complex." ], "offsets": [ [ 0, 341 ] ] } ]

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[ { "id": "BioInfer.d222.s0__text", "type": "Sentence", "text": [ "Furthermore, a simultaneous expression of profilin, actin and extracellular matrix proteins was observed during the regeneration of rat liver, that is, all mRNAs of these proteins showed biphasic peaks around 6 h and 48 h after partial hepatectomy." ], "offsets": [ [ 0, 248 ] ] } ]

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[ { "id": "BioInfer.d222.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d222.s0.e0", "arg2_id": "BioInfer.d222.s0.e1", "normalized": [] }, { "id": "BioInfer.d222.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d222.s0.e0", "arg2_id": "BioInfer.d222.s0.e2", "normalized": [] }, { "id": "BioInfer.d222.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d222.s0.e1", "arg2_id": "BioInfer.d222.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d223.s0__text", "type": "Sentence", "text": [ "Furthermore, the deletion of SJL1 suppresses the temperature-sensitive growth defect of sac6, a mutant in yeast fimbrin, supporting a role for synaptojanin family members in actin function." ], "offsets": [ [ 0, 189 ] ] } ]

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[ { "id": "BioInfer.d224.s0__text", "type": "Sentence", "text": [ "Furthermore, this inactivating effect of calmodulin can be prevented by coexpressing a region of the cytoskeletal protein alpha-actinin2 known to interact with the CO region of NR1." ], "offsets": [ [ 0, 181 ] ] } ]

[ { "id": "BioInfer.d224.s0.e0", "type": "Individual_protein", "text": [ "calmodulin" ], "offsets": [ [ 41, 51 ] ], "normalized": [] }, { "id": "BioInfer.d224.s0.e1", "type": "Individual_protein", "text": [ "alpha-actinin2" ], "offsets": [ [ 122, 136 ] ], "normalized": [] }, { "id": "BioInfer.d224.s0.e2", "type": "Individual_protein", "text": [ "NR1" ], "offsets": [ [ 177, 180 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d224.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d224.s0.e0", "arg2_id": "BioInfer.d224.s0.e1", "normalized": [] }, { "id": "BioInfer.d224.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d224.s0.e1", "arg2_id": "BioInfer.d224.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d225.s0__text", "type": "Sentence", "text": [ "Further, PRP incubated with IL-6 showed a dose dependent increase in TXB2 and BTG secretion as measured by RIA and an increased incorporation of actin binding protein, talin, and myosin into the cytoskeletal core (triton insoluble residue) as shown by SDS-PAGE." ], "offsets": [ [ 0, 261 ] ] } ]

[ { "id": "BioInfer.d225.s0.e0", "type": "Individual_protein", "text": [ "BTG" ], "offsets": [ [ 78, 81 ] ], "normalized": [] }, { "id": "BioInfer.d225.s0.e1", "type": "Individual_protein", "text": [ "myosin" ], "offsets": [ [ 179, 185 ] ], "normalized": [] }, { "id": "BioInfer.d225.s0.e2", "type": "Individual_protein", "text": [ "TXB2" ], "offsets": [ [ 69, 73 ] ], "normalized": [] }, { "id": "BioInfer.d225.s0.e3", "type": "Individual_protein", "text": [ "talin" ], "offsets": [ [ 168, 173 ] ], "normalized": [] }, { "id": "BioInfer.d225.s0.e4", "type": "Protein_family_or_group", "text": [ "actin binding protein" ], "offsets": [ [ 145, 166 ] ], "normalized": [] }, { "id": "BioInfer.d225.s0.e5", "type": "Individual_protein", "text": [ "IL-6" ], "offsets": [ [ 28, 32 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d225.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d225.s0.e0", "arg2_id": "BioInfer.d225.s0.e5", "normalized": [] }, { "id": "BioInfer.d225.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d225.s0.e1", "arg2_id": "BioInfer.d225.s0.e3", "normalized": [] }, { "id": "BioInfer.d225.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d225.s0.e1", "arg2_id": "BioInfer.d225.s0.e4", "normalized": [] }, { "id": "BioInfer.d225.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d225.s0.e2", "arg2_id": "BioInfer.d225.s0.e5", "normalized": [] }, { "id": "BioInfer.d225.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d225.s0.e3", "arg2_id": "BioInfer.d225.s0.e4", "normalized": [] } ]

[ { "id": "BioInfer.d226.s0__text", "type": "Sentence", "text": [ "Further, we show that talin, a high molecular weight structural protein that links integrins to the actin cytoskeleton, is proteolytically cleaved in fetal, but not in neonatal melanocytes." ], "offsets": [ [ 0, 189 ] ] } ]

[ { "id": "BioInfer.d226.s0.e0", "type": "Individual_protein", "text": [ "integrins" ], "offsets": [ [ 83, 92 ] ], "normalized": [] }, { "id": "BioInfer.d226.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 100, 105 ] ], "normalized": [] }, { "id": "BioInfer.d226.s0.e2", "type": "Individual_protein", "text": [ "talin" ], "offsets": [ [ 22, 27 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d226.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d226.s0.e0", "arg2_id": "BioInfer.d226.s0.e1", "normalized": [] }, { "id": "BioInfer.d226.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d226.s0.e0", "arg2_id": "BioInfer.d226.s0.e2", "normalized": [] }, { "id": "BioInfer.d226.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d226.s0.e1", "arg2_id": "BioInfer.d226.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d226.s1__text", "type": "Sentence", "text": [ "Immunofluorescence microscopy of cells grown on fibronectin confirmed the presence of paxillin, talin, and vinculin at the ends of actin stress fibers at presumptive focal contacts in melanocytes." ], "offsets": [ [ 0, 196 ] ] } ]

[ { "id": "BioInfer.d226.s1.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 131, 136 ] ], "normalized": [] }, { "id": "BioInfer.d226.s1.e1", "type": "Individual_protein", "text": [ "vinculin" ], "offsets": [ [ 107, 115 ] ], "normalized": [] }, { "id": "BioInfer.d226.s1.e2", "type": "Gene/protein/RNA", "text": [ "fibronectin" ], "offsets": [ [ 48, 59 ] ], "normalized": [] }, { "id": "BioInfer.d226.s1.e3", "type": "Individual_protein", "text": [ "paxillin" ], "offsets": [ [ 86, 94 ] ], "normalized": [] }, { "id": "BioInfer.d226.s1.e4", "type": "Individual_protein", "text": [ "talin" ], "offsets": [ [ 96, 101 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d226.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d226.s1.e0", "arg2_id": "BioInfer.d226.s1.e1", "normalized": [] }, { "id": "BioInfer.d226.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d226.s1.e0", "arg2_id": "BioInfer.d226.s1.e3", "normalized": [] }, { "id": "BioInfer.d226.s1.i2", "type": "PPI", "arg1_id": "BioInfer.d226.s1.e0", "arg2_id": "BioInfer.d226.s1.e4", "normalized": [] } ]

[ { "id": "BioInfer.d227.s0__text", "type": "Sentence", "text": [ "Fusiform RPE, however, were not deficient in these proteins, expressing amounts of N-cadherin, alpha-catenin, beta-catenin, plakoglobin, p120, alpha-actinin and vinculin that were equivalent to epithelioid cells." ], "offsets": [ [ 0, 212 ] ] } ]

[ { "id": "BioInfer.d227.s0.e0", "type": "Gene/protein/RNA", "text": [ "alpha-actinin" ], "offsets": [ [ 143, 156 ] ], "normalized": [] }, { "id": "BioInfer.d227.s0.e1", "type": "Gene/protein/RNA", "text": [ "vinculin" ], "offsets": [ [ 161, 169 ] ], "normalized": [] }, { "id": "BioInfer.d227.s0.e2", "type": "Gene/protein/RNA", "text": [ "plakoglobin" ], "offsets": [ [ 124, 135 ] ], "normalized": [] }, { "id": "BioInfer.d227.s0.e3", "type": "Gene/protein/RNA", "text": [ "p120" ], "offsets": [ [ 137, 141 ] ], "normalized": [] }, { "id": "BioInfer.d227.s0.e4", "type": "Gene/protein/RNA", "text": [ "alpha-catenin" ], "offsets": [ [ 95, 108 ] ], "normalized": [] }, { "id": "BioInfer.d227.s0.e5", "type": "Gene/protein/RNA", "text": [ "beta-catenin" ], "offsets": [ [ 110, 122 ] ], "normalized": [] }, { "id": "BioInfer.d227.s0.e6", "type": "Gene/protein/RNA", "text": [ "N-cadherin" ], "offsets": [ [ 83, 93 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d229.s0__text", "type": "Sentence", "text": [ "Gel electrophoresis was used to measure changes in the relative amounts of actin or myosin and of myosin heavy chain (MHC) isoforms." ], "offsets": [ [ 0, 132 ] ] } ]

[ { "id": "BioInfer.d229.s0.e0", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 75, 80 ] ], "normalized": [] }, { "id": "BioInfer.d229.s0.e1", "type": "Individual_protein", "text": [ "myosin heavy chain" ], "offsets": [ [ 98, 116 ] ], "normalized": [] }, { "id": "BioInfer.d229.s0.e2", "type": "Gene/protein/RNA", "text": [ "myosin" ], "offsets": [ [ 84, 90 ] ], "normalized": [] }, { "id": "BioInfer.d229.s0.e3", "type": "Individual_protein", "text": [ "MHC" ], "offsets": [ [ 118, 121 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d230.s0__text", "type": "Sentence", "text": [ "Generation of these membrane microparticles was dependent on the presence of extracellular calcium and was accompanied by proteolytic degradation of the cytoskeletal proteins, actin binding protein (ABP), talin, and myosin heavy chain." ], "offsets": [ [ 0, 235 ] ] } ]

[ { "id": "BioInfer.d230.s0.e0", "type": "Protein_family_or_group", "text": [ "actin binding protein" ], "offsets": [ [ 176, 197 ] ], "normalized": [] }, { "id": "BioInfer.d230.s0.e1", "type": "Gene/protein/RNA", "text": [ "myosin heavy chain" ], "offsets": [ [ 216, 234 ] ], "normalized": [] }, { "id": "BioInfer.d230.s0.e2", "type": "Gene/protein/RNA", "text": [ "talin" ], "offsets": [ [ 205, 210 ] ], "normalized": [] }, { "id": "BioInfer.d230.s0.e3", "type": "Protein_family_or_group", "text": [ "ABP" ], "offsets": [ [ 199, 202 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d232.s0__text", "type": "Sentence", "text": [ "Genetic dissection of Drosophila myofibril formation: effects of actin and myosin heavy chain null alleles." ], "offsets": [ [ 0, 107 ] ] } ]

[ { "id": "BioInfer.d232.s0.e0", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 65, 70 ] ], "normalized": [] }, { "id": "BioInfer.d232.s0.e1", "type": "Gene/protein/RNA", "text": [ "myosin heavy chain" ], "offsets": [ [ 75, 93 ] ], "normalized": [] } ]

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