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BigScience Biomedical Datasets 148

[ { "id": "BioInfer.d607.s1__text", "type": "Sentence", "text": [ "The previous investigation (Abe et al. (1989) J. Biochem. 106, 696-702) suggested that cofilin is deeply involved in the regulation of actin assembly in developing skeletal muscle." ], "offsets": [ [ 0, 180 ] ] } ]

[ { "id": "BioInfer.d607.s1.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 135, 140 ] ], "normalized": [] }, { "id": "BioInfer.d607.s1.e1", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 87, 94 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d607.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d607.s1.e0", "arg2_id": "BioInfer.d607.s1.e1", "normalized": [] } ]

[ { "id": "BioInfer.d608.s0__text", "type": "Sentence", "text": [ "The E-cadherin-associated proteins alpha-catenin and beta-catenin were not significantly affected by treatment with TPA." ], "offsets": [ [ 0, 120 ] ] } ]

[ { "id": "BioInfer.d608.s0.e0", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 35, 48 ] ], "normalized": [] }, { "id": "BioInfer.d608.s0.e1", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 53, 65 ] ], "normalized": [] }, { "id": "BioInfer.d608.s0.e2", "type": "Individual_protein", "text": [ "TPA" ], "offsets": [ [ 116, 119 ] ], "normalized": [] }, { "id": "BioInfer.d608.s0.e3", "type": "Individual_protein", "text": [ "E-cadherin" ], "offsets": [ [ 4, 14 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d608.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d608.s0.e0", "arg2_id": "BioInfer.d608.s0.e3", "normalized": [] }, { "id": "BioInfer.d608.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d608.s0.e1", "arg2_id": "BioInfer.d608.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d609.s0__text", "type": "Sentence", "text": [ "The effects of two adhesion substrates (serum and laminin) and time in culture on the expression of genes encoding myosin heavy chain (MHC) isoforms and alpha-skeletal actin were analysed in myocytes isolated from adult rat heart and maintained in serum-free culture." ], "offsets": [ [ 0, 267 ] ] } ]

[ { "id": "BioInfer.d609.s0.e0", "type": "Individual_protein", "text": [ "laminin" ], "offsets": [ [ 50, 57 ] ], "normalized": [] }, { "id": "BioInfer.d609.s0.e1", "type": "Individual_protein", "text": [ "myosin heavy chain" ], "offsets": [ [ 115, 133 ] ], "normalized": [] }, { "id": "BioInfer.d609.s0.e2", "type": "Individual_protein", "text": [ "MHC" ], "offsets": [ [ 135, 138 ] ], "normalized": [] }, { "id": "BioInfer.d609.s0.e3", "type": "Individual_protein", "text": [ "alpha-skeletal actin" ], "offsets": [ [ 153, 173 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d609.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d609.s0.e0", "arg2_id": "BioInfer.d609.s0.e1", "normalized": [] }, { "id": "BioInfer.d609.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d609.s0.e0", "arg2_id": "BioInfer.d609.s0.e2", "normalized": [] }, { "id": "BioInfer.d609.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d609.s0.e0", "arg2_id": "BioInfer.d609.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d610.s0__text", "type": "Sentence", "text": [ "The enzyme showed hardly any activity below 50 degrees C but considerable activity at around 60 degrees C against myofibrils, digesting myosin heavy chain, actin and tropomyosin." ], "offsets": [ [ 0, 178 ] ] } ]

[ { "id": "BioInfer.d610.s0.e0", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 156, 161 ] ], "normalized": [] }, { "id": "BioInfer.d610.s0.e1", "type": "Gene/protein/RNA", "text": [ "tropomyosin" ], "offsets": [ [ 166, 177 ] ], "normalized": [] }, { "id": "BioInfer.d610.s0.e2", "type": "Gene/protein/RNA", "text": [ "myosin heavy chain" ], "offsets": [ [ 136, 154 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d611.s0__text", "type": "Sentence", "text": [ "The existence of this pathway helps to explain some of the effects of LIM kinase and cofilin in the control of actin dynamics." ], "offsets": [ [ 0, 126 ] ] } ]

[ { "id": "BioInfer.d611.s0.e0", "type": "Individual_protein", "text": [ "LIM kinase" ], "offsets": [ [ 70, 80 ] ], "normalized": [] }, { "id": "BioInfer.d611.s0.e1", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 85, 92 ] ], "normalized": [] }, { "id": "BioInfer.d611.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 111, 116 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d611.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d611.s0.e0", "arg2_id": "BioInfer.d611.s0.e2", "normalized": [] }, { "id": "BioInfer.d611.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d611.s0.e1", "arg2_id": "BioInfer.d611.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d612.s0__text", "type": "Sentence", "text": [ "The expression of APC, alpha-catenin and beta-catenin also was decreased in HT29 cells, with a translocation of APC into the nucleus." ], "offsets": [ [ 0, 133 ] ] } ]

[ { "id": "BioInfer.d612.s0.e0", "type": "Gene/protein/RNA", "text": [ "APC" ], "offsets": [ [ 18, 21 ] ], "normalized": [] }, { "id": "BioInfer.d612.s0.e1", "type": "Gene/protein/RNA", "text": [ "beta-catenin" ], "offsets": [ [ 41, 53 ] ], "normalized": [] }, { "id": "BioInfer.d612.s0.e2", "type": "Gene/protein/RNA", "text": [ "alpha-catenin" ], "offsets": [ [ 23, 36 ] ], "normalized": [] }, { "id": "BioInfer.d612.s0.e3", "type": "Gene/protein/RNA", "text": [ "APC" ], "offsets": [ [ 112, 115 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d613.s0__text", "type": "Sentence", "text": [ "The findings suggest that M1 muscarinic receptors are involved in muscarinic receptor-mediated enhancement of IL-2 production in Jurkat cells and that the transcription factor AP-1 and pathways via mitogen-activated protein kinase (MAPK)/extracellular signal regulated protein kinase and c-Jun N-terminal kinase, but not via p38 MAPK, may be involved in the muscarinic receptor-mediated enhancement of IL-2 production." ], "offsets": [ [ 0, 418 ] ] } ]

[ { "id": "BioInfer.d613.s0.e0", "type": "Individual_protein", "text": [ "IL-2" ], "offsets": [ [ 110, 114 ] ], "normalized": [] }, { "id": "BioInfer.d613.s0.e1", "type": "Individual_protein", "text": [ "M1" ], "offsets": [ [ 26, 28 ] ], "normalized": [] }, { "id": "BioInfer.d613.s0.e2", "type": "Protein_family_or_group", "text": [ "muscarinic receptors" ], "offsets": [ [ 29, 49 ] ], "normalized": [] }, { "id": "BioInfer.d613.s0.e3", "type": "Individual_protein", "text": [ "c-Jun N-terminal kinase" ], "offsets": [ [ 288, 311 ] ], "normalized": [] }, { "id": "BioInfer.d613.s0.e4", "type": "Individual_protein", "text": [ "IL-2" ], "offsets": [ [ 402, 406 ] ], "normalized": [] }, { "id": "BioInfer.d613.s0.e5", "type": "Individual_protein", "text": [ "muscarinic receptor" ], "offsets": [ [ 358, 377 ] ], "normalized": [] }, { "id": "BioInfer.d613.s0.e6", "type": "Individual_protein", "text": [ "muscarinic receptor" ], "offsets": [ [ 66, 85 ] ], "normalized": [] }, { "id": "BioInfer.d613.s0.e7", "type": "Protein_family_or_group", "text": [ "MAPK" ], "offsets": [ [ 329, 333 ] ], "normalized": [] }, { "id": "BioInfer.d613.s0.e8", "type": "Individual_protein", "text": [ "extracellular signal regulated protein kinase" ], "offsets": [ [ 238, 283 ] ], "normalized": [] }, { "id": "BioInfer.d613.s0.e9", "type": "Individual_protein", "text": [ "MAPK" ], "offsets": [ [ 232, 236 ] ], "normalized": [] }, { "id": "BioInfer.d613.s0.e10", "type": "Individual_protein", "text": [ "AP-1" ], "offsets": [ [ 176, 180 ] ], "normalized": [] }, { "id": "BioInfer.d613.s0.e11", "type": "Individual_protein", "text": [ "p38" ], "offsets": [ [ 325, 328 ] ], "normalized": [] }, { "id": "BioInfer.d613.s0.e12", "type": "Individual_protein", "text": [ "mitogen-activated protein kinase" ], "offsets": [ [ 198, 230 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d613.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d613.s0.e0", "arg2_id": "BioInfer.d613.s0.e1", "normalized": [] }, { "id": "BioInfer.d613.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d613.s0.e0", "arg2_id": "BioInfer.d613.s0.e6", "normalized": [] }, { "id": "BioInfer.d613.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d613.s0.e1", "arg2_id": "BioInfer.d613.s0.e2", "normalized": [] }, { "id": "BioInfer.d613.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d613.s0.e3", "arg2_id": "BioInfer.d613.s0.e4", "normalized": [] }, { "id": "BioInfer.d613.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d613.s0.e4", "arg2_id": "BioInfer.d613.s0.e5", "normalized": [] }, { "id": "BioInfer.d613.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d613.s0.e4", "arg2_id": "BioInfer.d613.s0.e8", "normalized": [] }, { "id": "BioInfer.d613.s0.i6", "type": "PPI", "arg1_id": "BioInfer.d613.s0.e4", "arg2_id": "BioInfer.d613.s0.e9", "normalized": [] }, { "id": "BioInfer.d613.s0.i7", "type": "PPI", "arg1_id": "BioInfer.d613.s0.e4", "arg2_id": "BioInfer.d613.s0.e10", "normalized": [] }, { "id": "BioInfer.d613.s0.i8", "type": "PPI", "arg1_id": "BioInfer.d613.s0.e4", "arg2_id": "BioInfer.d613.s0.e11", "normalized": [] }, { "id": "BioInfer.d613.s0.i9", "type": "PPI", "arg1_id": "BioInfer.d613.s0.e4", "arg2_id": "BioInfer.d613.s0.e12", "normalized": [] }, { "id": "BioInfer.d613.s0.i10", "type": "PPI", "arg1_id": "BioInfer.d613.s0.e7", "arg2_id": "BioInfer.d613.s0.e11", "normalized": [] } ]

[ { "id": "BioInfer.d614.s0__text", "type": "Sentence", "text": [ "The gene RVS167 therefore could be implicated in cytoskeletal reorganization in response to environmental stresses and could act in the budding site selection mechanism." ], "offsets": [ [ 0, 169 ] ] } ]

[ { "id": "BioInfer.d614.s0.e0", "type": "Gene/protein/RNA", "text": [ "RVS167" ], "offsets": [ [ 9, 15 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d615.s0__text", "type": "Sentence", "text": [ "The gene for the human CREB binding protein, the transcriptional coactivator CBP, is included in the RT1 cosmid, and mutations in CBP have recently been identified in nondeleted RTS patients." ], "offsets": [ [ 0, 191 ] ] } ]

[ { "id": "BioInfer.d615.s0.e0", "type": "Individual_protein", "text": [ "CBP" ], "offsets": [ [ 77, 80 ] ], "normalized": [] }, { "id": "BioInfer.d615.s0.e1", "type": "Gene/protein/RNA", "text": [ "CBP" ], "offsets": [ [ 130, 133 ] ], "normalized": [] }, { "id": "BioInfer.d615.s0.e2", "type": "Individual_protein", "text": [ "CREB binding protein" ], "offsets": [ [ 23, 43 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d616.s0__text", "type": "Sentence", "text": [ "The genes considered are those for 5S, 5.8S and 18S rRNA, actin I, profilins Ia/b and II, myosins IB, IC and II, and calmodulin." ], "offsets": [ [ 0, 128 ] ] } ]

[ { "id": "BioInfer.d616.s0.e0", "type": "Gene/protein/RNA", "text": [ "5.8S", "rRNA" ], "offsets": [ [ 39, 43 ], [ 52, 56 ] ], "normalized": [] }, { "id": "BioInfer.d616.s0.e1", "type": "Gene/protein/RNA", "text": [ "5S", "rRNA" ], "offsets": [ [ 35, 37 ], [ 52, 56 ] ], "normalized": [] }, { "id": "BioInfer.d616.s0.e2", "type": "Gene/protein/RNA", "text": [ "18S rRNA" ], "offsets": [ [ 48, 56 ] ], "normalized": [] }, { "id": "BioInfer.d616.s0.e3", "type": "Gene/protein/RNA", "text": [ "profilins Ia" ], "offsets": [ [ 67, 79 ] ], "normalized": [] }, { "id": "BioInfer.d616.s0.e4", "type": "Gene/protein/RNA", "text": [ "myosins", "IC" ], "offsets": [ [ 90, 97 ], [ 102, 104 ] ], "normalized": [] }, { "id": "BioInfer.d616.s0.e5", "type": "Gene/protein/RNA", "text": [ "actin I" ], "offsets": [ [ 58, 65 ] ], "normalized": [] }, { "id": "BioInfer.d616.s0.e6", "type": "Gene/protein/RNA", "text": [ "profilins", "II" ], "offsets": [ [ 67, 76 ], [ 86, 88 ] ], "normalized": [] }, { "id": "BioInfer.d616.s0.e7", "type": "Gene/protein/RNA", "text": [ "myosins", "II" ], "offsets": [ [ 90, 97 ], [ 109, 111 ] ], "normalized": [] }, { "id": "BioInfer.d616.s0.e8", "type": "Gene/protein/RNA", "text": [ "profilins I", "b" ], "offsets": [ [ 67, 78 ], [ 80, 81 ] ], "normalized": [] }, { "id": "BioInfer.d616.s0.e9", "type": "Gene/protein/RNA", "text": [ "myosins IB" ], "offsets": [ [ 90, 100 ] ], "normalized": [] }, { "id": "BioInfer.d616.s0.e10", "type": "Gene/protein/RNA", "text": [ "calmodulin" ], "offsets": [ [ 117, 127 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d617.s0__text", "type": "Sentence", "text": [ "The head domain of talin thus binds to integrins to form a link to the actin cytoskeleton and can thus regulate integrin function." ], "offsets": [ [ 0, 130 ] ] } ]

[ { "id": "BioInfer.d617.s0.e0", "type": "Individual_protein", "text": [ "integrins" ], "offsets": [ [ 39, 48 ] ], "normalized": [] }, { "id": "BioInfer.d617.s0.e1", "type": "Individual_protein", "text": [ "talin" ], "offsets": [ [ 19, 24 ] ], "normalized": [] }, { "id": "BioInfer.d617.s0.e2", "type": "Individual_protein", "text": [ "integrin" ], "offsets": [ [ 112, 120 ] ], "normalized": [] }, { "id": "BioInfer.d617.s0.e3", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 71, 76 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d617.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d617.s0.e0", "arg2_id": "BioInfer.d617.s0.e1", "normalized": [] }, { "id": "BioInfer.d617.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d617.s0.e0", "arg2_id": "BioInfer.d617.s0.e3", "normalized": [] }, { "id": "BioInfer.d617.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d617.s0.e1", "arg2_id": "BioInfer.d617.s0.e2", "normalized": [] }, { "id": "BioInfer.d617.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d617.s0.e1", "arg2_id": "BioInfer.d617.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d618.s0__text", "type": "Sentence", "text": [ "The herpes simplex virus helicase-primase complex, a heterotrimer of the UL5, UL8, and UL52 proteins, displays a single predominant site of primer synthesis on phi X174 virion DNA (Tenney, D. J., Hurlburt, W. W., Micheletti, P. M., Bifano, M., and Hamatake, R. K. (1994) J. Biol. Chem. 269, 5030-5035)." ], "offsets": [ [ 0, 302 ] ] } ]

[ { "id": "BioInfer.d618.s0.e0", "type": "Individual_protein", "text": [ "UL5" ], "offsets": [ [ 73, 76 ] ], "normalized": [] }, { "id": "BioInfer.d618.s0.e1", "type": "Protein_complex", "text": [ "helicase-primase" ], "offsets": [ [ 25, 41 ] ], "normalized": [] }, { "id": "BioInfer.d618.s0.e2", "type": "Individual_protein", "text": [ "UL8" ], "offsets": [ [ 78, 81 ] ], "normalized": [] }, { "id": "BioInfer.d618.s0.e3", "type": "Individual_protein", "text": [ "UL52" ], "offsets": [ [ 87, 91 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d618.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d618.s0.e0", "arg2_id": "BioInfer.d618.s0.e1", "normalized": [] }, { "id": "BioInfer.d618.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d618.s0.e0", "arg2_id": "BioInfer.d618.s0.e2", "normalized": [] }, { "id": "BioInfer.d618.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d618.s0.e0", "arg2_id": "BioInfer.d618.s0.e3", "normalized": [] }, { "id": "BioInfer.d618.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d618.s0.e1", "arg2_id": "BioInfer.d618.s0.e2", "normalized": [] }, { "id": "BioInfer.d618.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d618.s0.e1", "arg2_id": "BioInfer.d618.s0.e3", "normalized": [] }, { "id": "BioInfer.d618.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d618.s0.e2", "arg2_id": "BioInfer.d618.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d620.s0__text", "type": "Sentence", "text": [ "The herpes simplex virus type-1 DNA helicase-primase is a heterotrimer encoded by the UL5, UL8, and UL52 genes." ], "offsets": [ [ 0, 111 ] ] } ]

[ { "id": "BioInfer.d620.s0.e0", "type": "Gene", "text": [ "UL8" ], "offsets": [ [ 91, 94 ] ], "normalized": [] }, { "id": "BioInfer.d620.s0.e1", "type": "Gene", "text": [ "UL52" ], "offsets": [ [ 100, 104 ] ], "normalized": [] }, { "id": "BioInfer.d620.s0.e2", "type": "Individual_protein", "text": [ "DNA helicase-primase" ], "offsets": [ [ 32, 52 ] ], "normalized": [] }, { "id": "BioInfer.d620.s0.e3", "type": "Gene", "text": [ "UL5" ], "offsets": [ [ 86, 89 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d620.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d620.s0.e0", "arg2_id": "BioInfer.d620.s0.e2", "normalized": [] }, { "id": "BioInfer.d620.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d620.s0.e1", "arg2_id": "BioInfer.d620.s0.e2", "normalized": [] }, { "id": "BioInfer.d620.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d620.s0.e2", "arg2_id": "BioInfer.d620.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d621.s0__text", "type": "Sentence", "text": [ "The Herpes simplex virus type 1 primosome consists of three subunits that are the products of the UL5, UL8, and UL52 genes." ], "offsets": [ [ 0, 123 ] ] } ]

[ { "id": "BioInfer.d621.s0.e0", "type": "Gene", "text": [ "UL5" ], "offsets": [ [ 98, 101 ] ], "normalized": [] }, { "id": "BioInfer.d621.s0.e1", "type": "Individual_protein", "text": [ "primosome" ], "offsets": [ [ 32, 41 ] ], "normalized": [] }, { "id": "BioInfer.d621.s0.e2", "type": "Gene", "text": [ "UL8" ], "offsets": [ [ 103, 106 ] ], "normalized": [] }, { "id": "BioInfer.d621.s0.e3", "type": "Gene", "text": [ "UL52" ], "offsets": [ [ 112, 116 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d621.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d621.s0.e0", "arg2_id": "BioInfer.d621.s0.e1", "normalized": [] }, { "id": "BioInfer.d621.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d621.s0.e0", "arg2_id": "BioInfer.d621.s0.e2", "normalized": [] }, { "id": "BioInfer.d621.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d621.s0.e0", "arg2_id": "BioInfer.d621.s0.e3", "normalized": [] }, { "id": "BioInfer.d621.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d621.s0.e1", "arg2_id": "BioInfer.d621.s0.e2", "normalized": [] }, { "id": "BioInfer.d621.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d621.s0.e1", "arg2_id": "BioInfer.d621.s0.e3", "normalized": [] }, { "id": "BioInfer.d621.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d621.s0.e2", "arg2_id": "BioInfer.d621.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d622.s0__text", "type": "Sentence", "text": [ "The herpes simplex virus type-1 UL5, UL8, and UL52 genes encode an essential heterotrimeric DNA helicase-primase that is responsible for concomitant DNA unwinding and primer synthesis at the viral DNA replication fork." ], "offsets": [ [ 0, 218 ] ] } ]

[ { "id": "BioInfer.d622.s0.e0", "type": "Gene", "text": [ "UL8" ], "offsets": [ [ 37, 40 ] ], "normalized": [] }, { "id": "BioInfer.d622.s0.e1", "type": "Gene", "text": [ "UL5" ], "offsets": [ [ 32, 35 ] ], "normalized": [] }, { "id": "BioInfer.d622.s0.e2", "type": "Gene", "text": [ "UL52" ], "offsets": [ [ 46, 50 ] ], "normalized": [] }, { "id": "BioInfer.d622.s0.e3", "type": "Individual_protein", "text": [ "DNA helicase-primase" ], "offsets": [ [ 92, 112 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d623.s0__text", "type": "Sentence", "text": [ "The higher affinity of vaccinia profilin for polyphosphoinositides (Kd = 0.2-8.5 microM) than for actin or poly(L-proline) and the concentration of vaccinia profilin expressed in infected HeLa cells (approximately 20 microM) suggest that vaccinia profilin binds preferentially to PIP and PIP2 in vivo." ], "offsets": [ [ 0, 301 ] ] } ]

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[ { "id": "BioInfer.d623.s1__text", "type": "Sentence", "text": [ "We expressed in Escherichia coli the vaccinia virus gene for a protein similar to vertebrate profilins, purified the recombinant viral profilin, and characterized its interactions with actin and polyphosphoinositides." ], "offsets": [ [ 0, 217 ] ] } ]

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[ { "id": "BioInfer.d624.s0__text", "type": "Sentence", "text": [ "The high recombination levels seen in rad5 and rad18 mutants is dependent on the RAD1, RAD51, RAD52, and RAD5 genes." ], "offsets": [ [ 0, 116 ] ] } ]

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[ { "id": "BioInfer.d625.s0__text", "type": "Sentence", "text": [ "The hyperproliferative response observed in the gastric mucosa is secondary to this initial insult and is associated with increased expression of cyclin D1, the cyclin dependent kinase inhibitor p16ink4a and of p53 and decreased expression of the cyclin dependent kinase inhibitor p27kip1." ], "offsets": [ [ 0, 289 ] ] } ]

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[ { "id": "BioInfer.d627.s0__text", "type": "Sentence", "text": [ "The influence of these collagens on cell morphology and the distribution pattern of actin, vimentin, talin, and vinculin was analyzed by light microscopy, conventional electron microscopy, immunofluorescence, and immunogold labeling after lysis-squirting." ], "offsets": [ [ 0, 255 ] ] } ]

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[ { "id": "BioInfer.d628.s0__text", "type": "Sentence", "text": [ "The inhibitory effects of rapamycin on bombesin-stimulated cell cycle progression did not involve accumulation of the cyclin-dependent kinase inhibitor p27(kip1) but a striking inhibition of the expression of cyclin D1." ], "offsets": [ [ 0, 219 ] ] } ]

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[ { "id": "BioInfer.d628.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d628.s0.e0", "arg2_id": "BioInfer.d628.s0.e2", "normalized": [] }, { "id": "BioInfer.d628.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d628.s0.e0", "arg2_id": "BioInfer.d628.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d629.s0__text", "type": "Sentence", "text": [ "The interaction between the human respiratory syncytial virus phosphoprotein (P) and nucleocapsid (N) protein has been investigated using the two hybrid system in yeast and in tissue culture cells." ], "offsets": [ [ 0, 197 ] ] } ]

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[ { "id": "BioInfer.d629.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d629.s0.e0", "arg2_id": "BioInfer.d629.s0.e2", "normalized": [] }, { "id": "BioInfer.d629.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d629.s0.e0", "arg2_id": "BioInfer.d629.s0.e3", "normalized": [] }, { "id": "BioInfer.d629.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d629.s0.e1", "arg2_id": "BioInfer.d629.s0.e2", "normalized": [] }, { "id": "BioInfer.d629.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d629.s0.e1", "arg2_id": "BioInfer.d629.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d631.s0__text", "type": "Sentence", "text": [ "The interaction of bovine respiratory syncytial virus (BRSV) phosphoprotein (P) with nucleocapsid (N) and large polymerase (L) proteins was investigated using an intracellular BRSV-CAT minigenome replication system." ], "offsets": [ [ 0, 215 ] ] } ]

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[ { "id": "BioInfer.d632.s0__text", "type": "Sentence", "text": [ "The interactions of actin with thymosin beta 4, actobindin and profilin are compared." ], "offsets": [ [ 0, 85 ] ] } ]

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[ { "id": "BioInfer.d633.s0__text", "type": "Sentence", "text": [ "The intracellular molecules calmodulin and profilin actively regulate actin-based motility and participate in the signaling pathways used to steer growth cones." ], "offsets": [ [ 0, 160 ] ] } ]

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[ { "id": "BioInfer.d634.s0__text", "type": "Sentence", "text": [ "The involvement of the death adaptor proteins FADD/MORT1, TRADD, and RIP and the apoptosis-initiating caspases-8 and -10 in death signaling by the two death-inducing TRAIL receptors 1 and 2 (TRAIL-R1 and TRAIL-R2) are controversial." ], "offsets": [ [ 0, 232 ] ] } ]

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[ { "id": "BioInfer.d635.s0__text", "type": "Sentence", "text": [ "Their abilities to store lipids and express desmin intermediate filaments, alpha-smooth muscle actin, and smooth muscle myosin heavy chain in contractile filaments in vitro illustrate similarities among the pulmonary LF, the hepatic lipocyte, and the contractile interstitial cell, which contribute to the repair reaction in the lung after pulmonary injury." ], "offsets": [ [ 0, 357 ] ] } ]

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[ { "id": "BioInfer.d636.s0__text", "type": "Sentence", "text": [ "The isolated intestinal microvillus cytoskeleton (core) consists of four major proteins: actin, villin, fimbrin and brush border myosin-I." ], "offsets": [ [ 0, 138 ] ] } ]

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[ { "id": "BioInfer.d637.s0__text", "type": "Sentence", "text": [ "The junctional multidomain protein AF-6 is a binding partner of the Rap1A GTPase and associates with the actin cytoskeletal regulator profilin." ], "offsets": [ [ 0, 143 ] ] } ]

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[ { "id": "BioInfer.d637.s1__text", "type": "Sentence", "text": [ "To our knowledge, AF-6 is the only integral component in cell-cell junctions discovered thus far that interacts with profilin and thus could modulate actin modeling proximal to adhesion complexes." ], "offsets": [ [ 0, 196 ] ] } ]

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[ { "id": "BioInfer.d638.s0__text", "type": "Sentence", "text": [ "The long repeats, which are interdigitated between the PRRs, increased the frequency with which actin-based motility occurred by a mechanism independent of the PRRs, VASP, and profilin." ], "offsets": [ [ 0, 185 ] ] } ]

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[ { "id": "BioInfer.d638.s1__text", "type": "Sentence", "text": [ "The tandem repeat domain in the Listeria monocytogenes ActA protein controls the rate of actin-based motility, the percentage of moving bacteria, and the localization of vasodilator-stimulated phosphoprotein and profilin." ], "offsets": [ [ 0, 221 ] ] } ]

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[ { "id": "BioInfer.d639.s0__text", "type": "Sentence", "text": [ "The main inhibitory action of p27, a cyclin-dependent kinase inhibitor (CDKI), arises from its binding with the cyclin E/cyclin-dependent kinase 2 (Cdk2) complex that results in G(1)-S arrest." ], "offsets": [ [ 0, 192 ] ] } ]

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[ { "id": "BioInfer.d640.s0__text", "type": "Sentence", "text": [ "The majority of cortical thymomas showed diffuse and homogenous membrane immunoreactivity for these molecules (88 per cent for E-CD; 86 per cent for alpha-catenin; 91 per cent for beta-catenin) and the remaining cases showed heterogeneous immunoreactivity, whereas almost all mixed and medullary thymomas revealed decreased expression or were negative." ], "offsets": [ [ 0, 352 ] ] } ]

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[ { "id": "BioInfer.d641.s0__text", "type": "Sentence", "text": [ "The majority of the aromatic residues in profilin are exposed to solvent and lie in either of two hydrophobic patches, neither of which takes part in an interface with actin." ], "offsets": [ [ 0, 174 ] ] } ]

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[ { "id": "BioInfer.d644.s0__text", "type": "Sentence", "text": [ "The microvillus cytoskeleton, isolated from chicken intestinal epithelial cell brush borders, is known to contain five major protein components, the 110,000-dalton polypeptide, villin (95,000 daltons), fimbrin (68,000 daltons), actin (43,000 daltons), and calmodulin (17,000 daltons)." ], "offsets": [ [ 0, 284 ] ] } ]

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[ { "id": "BioInfer.d645.s0__text", "type": "Sentence", "text": [ "The monomeric actin-binding protein, profilin, is a key regulator of actin-filament dynamics in animal cells and it has recently been identified in plants as a pollen allergen." ], "offsets": [ [ 0, 176 ] ] } ]

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[ { "id": "BioInfer.d646.s0__text", "type": "Sentence", "text": [ "The most significant finding was the re-expression of E-cadherin, alpha-catenin, and beta-catenin, and increased down-regulation of gamma-catenin, in metastatic lesions." ], "offsets": [ [ 0, 169 ] ] } ]

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[ { "id": "BioInfer.d647.s0__text", "type": "Sentence", "text": [ "The most striking difference was in the relative preference for acetylation of histone H4 versus acetylation of histone H3: with the purified acetylase, histone H4 in nucleosomes was acetylated to a much greater extent than was histone H3, whereas the reverse preference was found with the endogenous acetylase(s)." ], "offsets": [ [ 0, 314 ] ] } ]

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[ { "id": "BioInfer.d648.s0__text", "type": "Sentence", "text": [ "The multifunctional protein profilin is one of the most abundant proteins in the cytoplasm and is thought to regulate actin assembly and the phosphoinositide signaling pathway." ], "offsets": [ [ 0, 176 ] ] } ]

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[ { "id": "BioInfer.d649.s0__text", "type": "Sentence", "text": [ "The muscle-related genes included actin, tropomyosin, troponin I, myosin regulatory light chain, myosin light chain kinase, myosin heavy chain, calmodulin, calponin, calcium vector protein, creatine kinase, muscle LIM protein, and SH3-binding glutamate-rich protein, suggesting that vertebrate skeletal and smooth muscle-type genes are simultaneously expressed in the amphioxus notochord." ], "offsets": [ [ 0, 388 ] ] } ]

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[ { "id": "BioInfer.d650.s0__text", "type": "Sentence", "text": [ "The mutants ranged in affinity, from those that only weakly affected polymerization of actin to one that bound actin more strongly than wild-type profilin." ], "offsets": [ [ 0, 155 ] ] } ]

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[ { "id": "BioInfer.d650.s1__text", "type": "Sentence", "text": [ "The role of profilin in actin polymerization and nucleotide exchange." ], "offsets": [ [ 0, 69 ] ] } ]

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[ { "id": "BioInfer.d650.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d650.s1.e0", "arg2_id": "BioInfer.d650.s1.e1", "normalized": [] } ]

[ { "id": "BioInfer.d650.s2__text", "type": "Sentence", "text": [ "With profilins, whose sequestering activity was low, the concentration of free actin monomers observed at steady-state of polymerization [Afree], was close to that seen with actin alone ([Acc], critical concentration of polymerization)." ], "offsets": [ [ 0, 236 ] ] } ]

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[ { "id": "BioInfer.d651.s0__text", "type": "Sentence", "text": [ "The neoplastic cells were positive for vimentin, Factor-XIIIa, alpha-smooth muscle actin and CD34, but negative for desmin, calponin, high molecular weight caldesmon, smooth muscle myosin heavy chain, collagen type IV, laminin and S-100 protein." ], "offsets": [ [ 0, 245 ] ] } ]

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[ { "id": "BioInfer.d652.s0__text", "type": "Sentence", "text": [ "The N-terminal talin polypeptide eventually disrupted actin stress fibres whereas the C-terminal polypeptide was without effect." ], "offsets": [ [ 0, 128 ] ] } ]

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[ { "id": "BioInfer.d652.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d652.s0.e0", "arg2_id": "BioInfer.d652.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d652.s1__text", "type": "Sentence", "text": [ "The Pro1176 to Thr substitution found in talin from Wistar-Furth rats does not destroy the capacity of this region of the protein to bind actin or vinculin." ], "offsets": [ [ 0, 156 ] ] } ]

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[ { "id": "BioInfer.d653.s0__text", "type": "Sentence", "text": [ "The nucleotide sequences of nucleocapsid (N), phosphoprotein (P), matrix (M), fusion (F), and large protein (L) genes were partly determined for 19 wild strains of measles virus (MV) isolated over the past 10 years in Japan (nucleotide position N: 1301-1700, P: 1751-2190, M: 3571-4057, F: 6621-7210, L: 10381-11133) and also for a MV strain obtained from a patient with subacute sclerosing panencephalitis (SSPE) who had natural measles in 1980." ], "offsets": [ [ 0, 446 ] ] } ]

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[ { "id": "BioInfer.d654.s0__text", "type": "Sentence", "text": [ "The observed in vivo expression patterns of alpha-catenin, beta-catenin, and plakoglobin suggest that these proteins are directly linked with the developmental regulation of cell junctions, as cardiac cells become stably committed and phenotypically differentiated to eventually form a mature myocardium." ], "offsets": [ [ 0, 304 ] ] } ]

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[ { "id": "BioInfer.d654.s1__text", "type": "Sentence", "text": [ "This study details the expression patterns of alpha-catenin, beta-catenin, and gamma-catenin, during definition of the cardiac cell population as distinct compartments in the anterior regions of the chick embryo between stages 5 and 9." ], "offsets": [ [ 0, 235 ] ] } ]

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[ { "id": "BioInfer.d656.s0__text", "type": "Sentence", "text": [ "The p120cas gene encodes a protein tyrosine kinase substrate that associates with the cell-cell adhesion protein complex containing E-cadherin and its cytoplasmic cofactors alpha-catenin, beta-catenin, and plakoglobin." ], "offsets": [ [ 0, 218 ] ] } ]

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[ { "id": "BioInfer.d657.s0__text", "type": "Sentence", "text": [ "p27 binds to and inhibits complexes formed by cyclin E-cdk2, cyclin A-cdk2, and cyclin D-cdk4." ], "offsets": [ [ 0, 94 ] ] } ]

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[ { "id": "BioInfer.d658.s0__text", "type": "Sentence", "text": [ "The phosphoprotein was identified as cofilin, an actin-binding protein, and the activation-induced changes in its intracellular distribution have been described elsewhere (Suzuki et al., 1995, J Biol Chem 270:19551-19556)." ], "offsets": [ [ 0, 222 ] ] } ]

[ { "id": "BioInfer.d658.s0.e0", "type": "Protein_family_or_group", "text": [ "actin-binding protein" ], "offsets": [ [ 49, 70 ] ], "normalized": [] }, { "id": "BioInfer.d658.s0.e1", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 37, 44 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d658.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d658.s0.e0", "arg2_id": "BioInfer.d658.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d659.s0__text", "type": "Sentence", "text": [ "The polycystic kidney disease 1 gene product mediates protein kinase C alpha-dependent and c-Jun N-terminal kinase-dependent activation of the transcription factor AP-1." ], "offsets": [ [ 0, 169 ] ] } ]

[ { "id": "BioInfer.d659.s0.e0", "type": "Individual_protein", "text": [ "protein kinase C alpha" ], "offsets": [ [ 54, 76 ] ], "normalized": [] }, { "id": "BioInfer.d659.s0.e1", "type": "Individual_protein", "text": [ "c-Jun N-terminal kinase" ], "offsets": [ [ 91, 114 ] ], "normalized": [] }, { "id": "BioInfer.d659.s0.e2", "type": "Gene", "text": [ "polycystic kidney disease 1" ], "offsets": [ [ 4, 31 ] ], "normalized": [] }, { "id": "BioInfer.d659.s0.e3", "type": "Individual_protein", "text": [ "AP-1" ], "offsets": [ [ 164, 168 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d659.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d659.s0.e0", "arg2_id": "BioInfer.d659.s0.e3", "normalized": [] }, { "id": "BioInfer.d659.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d659.s0.e1", "arg2_id": "BioInfer.d659.s0.e3", "normalized": [] }, { "id": "BioInfer.d659.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d659.s0.e2", "arg2_id": "BioInfer.d659.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d662.s0__text", "type": "Sentence", "text": [ "The posttranslational metabolism of myosin heavy chain (MHC) and actin was regulated in parallel with the total contractile protein pool." ], "offsets": [ [ 0, 137 ] ] } ]

[ { "id": "BioInfer.d662.s0.e0", "type": "Individual_protein", "text": [ "myosin heavy chain" ], "offsets": [ [ 36, 54 ] ], "normalized": [] }, { "id": "BioInfer.d662.s0.e1", "type": "Individual_protein", "text": [ "MHC" ], "offsets": [ [ 56, 59 ] ], "normalized": [] }, { "id": "BioInfer.d662.s0.e2", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 65, 70 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d663.s0__text", "type": "Sentence", "text": [ "The potentiating effect of insulin appears to involve increases in the expression of cyclin E and decreases in the expression of the cyclin-dependent kinase inhibitor p27(Kip1)." ], "offsets": [ [ 0, 177 ] ] } ]

[ { "id": "BioInfer.d663.s0.e0", "type": "Protein_family_or_group", "text": [ "cyclin-dependent kinase inhibitor" ], "offsets": [ [ 133, 166 ] ], "normalized": [] }, { "id": "BioInfer.d663.s0.e1", "type": "Individual_protein", "text": [ "Kip1" ], "offsets": [ [ 171, 175 ] ], "normalized": [] }, { "id": "BioInfer.d663.s0.e2", "type": "Individual_protein", "text": [ "cyclin E" ], "offsets": [ [ 85, 93 ] ], "normalized": [] }, { "id": "BioInfer.d663.s0.e3", "type": "Individual_protein", "text": [ "insulin" ], "offsets": [ [ 27, 34 ] ], "normalized": [] }, { "id": "BioInfer.d663.s0.e4", "type": "Individual_protein", "text": [ "p27" ], "offsets": [ [ 167, 170 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d663.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d663.s0.e0", "arg2_id": "BioInfer.d663.s0.e1", "normalized": [] }, { "id": "BioInfer.d663.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d663.s0.e0", "arg2_id": "BioInfer.d663.s0.e4", "normalized": [] }, { "id": "BioInfer.d663.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d663.s0.e1", "arg2_id": "BioInfer.d663.s0.e3", "normalized": [] }, { "id": "BioInfer.d663.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d663.s0.e2", "arg2_id": "BioInfer.d663.s0.e3", "normalized": [] }, { "id": "BioInfer.d663.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d663.s0.e3", "arg2_id": "BioInfer.d663.s0.e4", "normalized": [] } ]

[ { "id": "BioInfer.d665.s0__text", "type": "Sentence", "text": [ "The presence, in varying quantities, of myosin heavy chain and actin isoforms of smooth muscle type in the different vessels reflected their degree of differentiation." ], "offsets": [ [ 0, 167 ] ] } ]

[ { "id": "BioInfer.d665.s0.e0", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 63, 68 ] ], "normalized": [] }, { "id": "BioInfer.d665.s0.e1", "type": "Gene/protein/RNA", "text": [ "myosin heavy chain" ], "offsets": [ [ 40, 58 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d666.s0__text", "type": "Sentence", "text": [ "The present study was designed to determine if cholesterol feeding results in alterations in the isoforms of actin and/or myosin heavy chain in gallbladder smooth muscle." ], "offsets": [ [ 0, 170 ] ] } ]

[ { "id": "BioInfer.d666.s0.e0", "type": "Gene/protein/RNA", "text": [ "myosin heavy chain" ], "offsets": [ [ 122, 140 ] ], "normalized": [] }, { "id": "BioInfer.d666.s0.e1", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 109, 114 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d667.s0__text", "type": "Sentence", "text": [ "The primary purpose of this study was to determine the relationship between myosin heavy chain (MHC) and actin contents and maximum isometric tetanic force (Po) in mouse extensor digitorum longus (EDL) muscles following eccentric contraction-induced injury." ], "offsets": [ [ 0, 257 ] ] } ]

[ { "id": "BioInfer.d667.s0.e0", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 105, 110 ] ], "normalized": [] }, { "id": "BioInfer.d667.s0.e1", "type": "Individual_protein", "text": [ "MHC" ], "offsets": [ [ 96, 99 ] ], "normalized": [] }, { "id": "BioInfer.d667.s0.e2", "type": "Individual_protein", "text": [ "myosin heavy chain" ], "offsets": [ [ 76, 94 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d668.s0__text", "type": "Sentence", "text": [ "The procedure allows for the simultaneous quantification of myosin heavy chain, myosin light chain, phosphorylatable myosin light chain and actin from as little as 50 mg of tissue." ], "offsets": [ [ 0, 180 ] ] } ]

[ { "id": "BioInfer.d668.s0.e0", "type": "Gene/protein/RNA", "text": [ "phosphorylatable myosin light chain" ], "offsets": [ [ 100, 135 ] ], "normalized": [] }, { "id": "BioInfer.d668.s0.e1", "type": "Gene/protein/RNA", "text": [ "myosin heavy chain" ], "offsets": [ [ 60, 78 ] ], "normalized": [] }, { "id": "BioInfer.d668.s0.e2", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 140, 145 ] ], "normalized": [] }, { "id": "BioInfer.d668.s0.e3", "type": "Gene/protein/RNA", "text": [ "myosin light chain" ], "offsets": [ [ 80, 98 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d669.s0__text", "type": "Sentence", "text": [ "The product of UL38 has been shown to be essential for capsid assembly, but no role has previously been assigned to the product of UL18." ], "offsets": [ [ 0, 136 ] ] } ]

[ { "id": "BioInfer.d669.s0.e0", "type": "Gene/protein/RNA", "text": [ "UL38" ], "offsets": [ [ 15, 19 ] ], "normalized": [] }, { "id": "BioInfer.d669.s0.e1", "type": "Gene/protein/RNA", "text": [ "UL18" ], "offsets": [ [ 131, 135 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d670.s0__text", "type": "Sentence", "text": [ "The products of the yeast mismatch repair genes MSH2 and MSH3 participate in the inhibition of genetic recombination between homeologous (divergent) DNA sequences." ], "offsets": [ [ 0, 163 ] ] } ]

[ { "id": "BioInfer.d670.s0.e0", "type": "Gene/protein/RNA", "text": [ "MSH2" ], "offsets": [ [ 48, 52 ] ], "normalized": [] }, { "id": "BioInfer.d670.s0.e1", "type": "Gene/protein/RNA", "text": [ "MSH3" ], "offsets": [ [ 57, 61 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d670.s1__text", "type": "Sentence", "text": [ "These results suggest that MSH2 and MSH3 can function differentially to control homeologous exchanges." ], "offsets": [ [ 0, 102 ] ] } ]

[ { "id": "BioInfer.d670.s1.e0", "type": "Gene/protein/RNA", "text": [ "MSH2" ], "offsets": [ [ 27, 31 ] ], "normalized": [] }, { "id": "BioInfer.d670.s1.e1", "type": "Gene/protein/RNA", "text": [ "MSH3" ], "offsets": [ [ 36, 40 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d671.s0__text", "type": "Sentence", "text": [ "The prominent 125 A transverse stripping pattern characteristic of the actin cross-bridges in a bundle is also absent in hair borders suggesting fimbrin as the component that gives rise to the transverse stripes." ], "offsets": [ [ 0, 212 ] ] } ]

[ { "id": "BioInfer.d671.s0.e0", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 71, 76 ] ], "normalized": [] }, { "id": "BioInfer.d671.s0.e1", "type": "Gene/protein/RNA", "text": [ "fimbrin" ], "offsets": [ [ 145, 152 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d672.s0__text", "type": "Sentence", "text": [ "The proposed LNYV genomic map is 3'-N-4a-4b-M-G-L-5', where N is the nucleocapsid protein gene; 4a and 4b are two genes, one of which codes for the proposed phosphoprotein P and the other for a putative protein of unknown function; M is the proposed matrix protein gene; G is the proposed glycoprotein gene; and L is the proposed transcriptase gene." ], "offsets": [ [ 0, 349 ] ] } ]

[ { "id": "BioInfer.d672.s0.e0", "type": "Gene", "text": [ "4b" ], "offsets": [ [ 103, 105 ] ], "normalized": [] }, { "id": "BioInfer.d672.s0.e1", "type": "Gene/protein/RNA", "text": [ "G" ], "offsets": [ [ 46, 47 ] ], "normalized": [] }, { "id": "BioInfer.d672.s0.e2", "type": "Gene/protein/RNA", "text": [ "L" ], "offsets": [ [ 48, 49 ] ], "normalized": [] }, { "id": "BioInfer.d672.s0.e3", "type": "Gene/protein/RNA", "text": [ "4b" ], "offsets": [ [ 41, 43 ] ], "normalized": [] }, { "id": "BioInfer.d672.s0.e4", "type": "Gene/protein/RNA", "text": [ "M" ], "offsets": [ [ 44, 45 ] ], "normalized": [] }, { "id": "BioInfer.d672.s0.e5", "type": "Gene/protein/RNA", "text": [ "N" ], "offsets": [ [ 36, 37 ] ], "normalized": [] }, { "id": "BioInfer.d672.s0.e6", "type": "Gene/protein/RNA", "text": [ "4a" ], "offsets": [ [ 38, 40 ] ], "normalized": [] }, { "id": "BioInfer.d672.s0.e7", "type": "Gene", "text": [ "G" ], "offsets": [ [ 271, 272 ] ], "normalized": [] }, { "id": "BioInfer.d672.s0.e8", "type": "Gene", "text": [ "L" ], "offsets": [ [ 312, 313 ] ], "normalized": [] }, { "id": "BioInfer.d672.s0.e9", "type": "Gene", "text": [ "N" ], "offsets": [ [ 60, 61 ] ], "normalized": [] }, { "id": "BioInfer.d672.s0.e10", "type": "Individual_protein", "text": [ "P" ], "offsets": [ [ 172, 173 ] ], "normalized": [] }, { "id": "BioInfer.d672.s0.e11", "type": "Gene", "text": [ "M" ], "offsets": [ [ 232, 233 ] ], "normalized": [] }, { "id": "BioInfer.d672.s0.e12", "type": "Individual_protein", "text": [ "transcriptase" ], "offsets": [ [ 330, 343 ] ], "normalized": [] }, { "id": "BioInfer.d672.s0.e13", "type": "Individual_protein", "text": [ "glycoprotein" ], "offsets": [ [ 289, 301 ] ], "normalized": [] }, { "id": "BioInfer.d672.s0.e14", "type": "Individual_protein", "text": [ "nucleocapsid protein" ], "offsets": [ [ 69, 89 ] ], "normalized": [] }, { "id": "BioInfer.d672.s0.e15", "type": "Individual_protein", "text": [ "phosphoprotein" ], "offsets": [ [ 157, 171 ] ], "normalized": [] }, { "id": "BioInfer.d672.s0.e16", "type": "Gene", "text": [ "4a" ], "offsets": [ [ 96, 98 ] ], "normalized": [] }, { "id": "BioInfer.d672.s0.e17", "type": "Individual_protein", "text": [ "matrix protein" ], "offsets": [ [ 250, 264 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d672.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d672.s0.e0", "arg2_id": "BioInfer.d672.s0.e10", "normalized": [] }, { "id": "BioInfer.d672.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d672.s0.e10", "arg2_id": "BioInfer.d672.s0.e15", "normalized": [] }, { "id": "BioInfer.d672.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d672.s0.e10", "arg2_id": "BioInfer.d672.s0.e16", "normalized": [] } ]

[ { "id": "BioInfer.d673.s0__text", "type": "Sentence", "text": [ "The protein profilin binds to both actin and the head groups of poly)phosphoinositide)s and may regulate both actin assembly and the phosphoinositide signaling pathway." ], "offsets": [ [ 0, 168 ] ] } ]

[ { "id": "BioInfer.d673.s0.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 35, 40 ] ], "normalized": [] }, { "id": "BioInfer.d673.s0.e1", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 12, 20 ] ], "normalized": [] }, { "id": "BioInfer.d673.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 110, 115 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d673.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d673.s0.e0", "arg2_id": "BioInfer.d673.s0.e1", "normalized": [] }, { "id": "BioInfer.d673.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d673.s0.e1", "arg2_id": "BioInfer.d673.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d674.s0__text", "type": "Sentence", "text": [ "The protein has the two conserved domains identified as actin and phosphatidylinositol 4,5-biphosphate (PIP2) binding sites found in members of the cofilin family." ], "offsets": [ [ 0, 163 ] ] } ]

[ { "id": "BioInfer.d674.s0.e0", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 148, 155 ] ], "normalized": [] }, { "id": "BioInfer.d674.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 56, 61 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d674.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d674.s0.e0", "arg2_id": "BioInfer.d674.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d675.s0__text", "type": "Sentence", "text": [ "The proteins encoded by MRS5 and MRS11, which display 35%, sequence identity are both located in the mitochondrial intermembrane space." ], "offsets": [ [ 0, 135 ] ] } ]

[ { "id": "BioInfer.d675.s0.e0", "type": "Gene", "text": [ "MRS5" ], "offsets": [ [ 24, 28 ] ], "normalized": [] }, { "id": "BioInfer.d675.s0.e1", "type": "Gene", "text": [ "MRS11" ], "offsets": [ [ 33, 38 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d675.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d675.s0.e0", "arg2_id": "BioInfer.d675.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d676.s0__text", "type": "Sentence", "text": [ "The proximity of the semi-conserved actin-binding site and the binding pocket characteristic of plant profilins suggests that epitopes encompassing both features are responsible for the cross-reactivity of antibodies between human and plant profilins thought to be responsible for type I allergies." ], "offsets": [ [ 0, 298 ] ] } ]

[ { "id": "BioInfer.d676.s0.e0", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 36, 41 ] ], "normalized": [] }, { "id": "BioInfer.d676.s0.e1", "type": "Gene/protein/RNA", "text": [ "profilins" ], "offsets": [ [ 102, 111 ] ], "normalized": [] }, { "id": "BioInfer.d676.s0.e2", "type": "Individual_protein", "text": [ "profilins" ], "offsets": [ [ 241, 250 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d678.s0__text", "type": "Sentence", "text": [ "The radioresistant N10 and parental KB cell lines were examined for the expression of human DNA repair genes which were related to the repair of radiation-induced DNA damage by northern blot analysis using five kinds of DNA probes (XRCC1, XRCC3, XRCC5, RAD51, RAD52)." ], "offsets": [ [ 0, 267 ] ] } ]

[ { "id": "BioInfer.d678.s0.e0", "type": "Gene/protein/RNA", "text": [ "XRCC5" ], "offsets": [ [ 246, 251 ] ], "normalized": [] }, { "id": "BioInfer.d678.s0.e1", "type": "Gene/protein/RNA", "text": [ "XRCC1" ], "offsets": [ [ 232, 237 ] ], "normalized": [] }, { "id": "BioInfer.d678.s0.e2", "type": "Gene/protein/RNA", "text": [ "RAD52" ], "offsets": [ [ 260, 265 ] ], "normalized": [] }, { "id": "BioInfer.d678.s0.e3", "type": "Gene/protein/RNA", "text": [ "XRCC3" ], "offsets": [ [ 239, 244 ] ], "normalized": [] }, { "id": "BioInfer.d678.s0.e4", "type": "Gene/protein/RNA", "text": [ "RAD51" ], "offsets": [ [ 253, 258 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d680.s0__text", "type": "Sentence", "text": [ "There are only 14 non-conservative substitutions in the two myosin heavy chains, three of which are located in the secondary actin-binding loop and flanking regions and others correspond to residues so far not assigned a functional role, including two residues in the proximal S2 domain." ], "offsets": [ [ 0, 287 ] ] } ]

[ { "id": "BioInfer.d680.s0.e0", "type": "Individual_protein", "text": [ "myosin heavy chains" ], "offsets": [ [ 60, 79 ] ], "normalized": [] }, { "id": "BioInfer.d680.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 125, 130 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d680.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d680.s0.e0", "arg2_id": "BioInfer.d680.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d682.s0__text", "type": "Sentence", "text": [ "The recombinant material is similar to authentic profilin from Acanthamoeba-based on fluorescence monitored urea denaturation, circular dichroism, actin-nucleotide exchange rate and the Kd for rabbit skeletal actin." ], "offsets": [ [ 0, 215 ] ] } ]

[ { "id": "BioInfer.d682.s0.e0", "type": "Individual_protein", "text": [ "skeletal actin" ], "offsets": [ [ 200, 214 ] ], "normalized": [] }, { "id": "BioInfer.d682.s0.e1", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 147, 152 ] ], "normalized": [] }, { "id": "BioInfer.d682.s0.e2", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 49, 57 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d682.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d682.s0.e0", "arg2_id": "BioInfer.d682.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d683.s0__text", "type": "Sentence", "text": [ "The recombinant material is similar to authentic human platelet profilin based on the measured Kd for rabbit skeletal muscle actin." ], "offsets": [ [ 0, 131 ] ] } ]

[ { "id": "BioInfer.d683.s0.e0", "type": "Individual_protein", "text": [ "skeletal muscle actin" ], "offsets": [ [ 109, 130 ] ], "normalized": [] }, { "id": "BioInfer.d683.s0.e1", "type": "Individual_protein", "text": [ "platelet profilin" ], "offsets": [ [ 55, 72 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d683.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d683.s0.e0", "arg2_id": "BioInfer.d683.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d685.s0__text", "type": "Sentence", "text": [ "The resulting beta-catenin product is unable to bind alpha-catenin that is responsible for actin filament binding and organization." ], "offsets": [ [ 0, 131 ] ] } ]

[ { "id": "BioInfer.d685.s0.e0", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 14, 26 ] ], "normalized": [] }, { "id": "BioInfer.d685.s0.e1", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 53, 66 ] ], "normalized": [] }, { "id": "BioInfer.d685.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 91, 96 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d686.s0__text", "type": "Sentence", "text": [ "The results clearly showed that the mutated cofilin possessing KTLKK instead of KKRKK did not translocate into the nuclei in response to heat shock whereas a recombinant cofilin with the unaltered sequence of KKRKK responded to heat shock and formed intranuclear rods together with actin." ], "offsets": [ [ 0, 288 ] ] } ]

[ { "id": "BioInfer.d686.s0.e0", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 170, 177 ] ], "normalized": [] }, { "id": "BioInfer.d686.s0.e1", "type": "Gene/protein/RNA", "text": [ "cofilin" ], "offsets": [ [ 44, 51 ] ], "normalized": [] }, { "id": "BioInfer.d686.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 282, 287 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d686.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d686.s0.e0", "arg2_id": "BioInfer.d686.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d688.s0__text", "type": "Sentence", "text": [ "The results indicate that (a) plakoglobin and beta-catenin differ in their nuclear translocation and complexing with LEF-1 and vinculin; (b) LEF-1-dependent transactivation is preferentially driven by beta-catenin; and (c) the cytoplasmic partners of beta-catenin, cadherin and alpha-catenin, can sequester it to the cytoplasm and inhibit its transcriptional activity." ], "offsets": [ [ 0, 368 ] ] } ]

[ { "id": "BioInfer.d688.s0.e0", "type": "Individual_protein", "text": [ "LEF-1" ], "offsets": [ [ 141, 146 ] ], "normalized": [] }, { "id": "BioInfer.d688.s0.e1", "type": "Individual_protein", "text": [ "LEF-1" ], "offsets": [ [ 117, 122 ] ], "normalized": [] }, { "id": "BioInfer.d688.s0.e2", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 278, 291 ] ], "normalized": [] }, { "id": "BioInfer.d688.s0.e3", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 251, 263 ] ], "normalized": [] }, { "id": "BioInfer.d688.s0.e4", "type": "Individual_protein", "text": [ "vinculin" ], "offsets": [ [ 127, 135 ] ], "normalized": [] }, { "id": "BioInfer.d688.s0.e5", "type": "Individual_protein", "text": [ "plakoglobin" ], "offsets": [ [ 30, 41 ] ], "normalized": [] }, { "id": "BioInfer.d688.s0.e6", "type": "Individual_protein", "text": [ "cadherin" ], "offsets": [ [ 265, 273 ] ], "normalized": [] }, { "id": "BioInfer.d688.s0.e7", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 201, 213 ] ], "normalized": [] }, { "id": "BioInfer.d688.s0.e8", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 46, 58 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d692.s0__text", "type": "Sentence", "text": [ "The Schizosaccharomyces pombe rhp51+, rad22+ and rhp54+ genes are homologous to RAD51, RAD52 and RAD54 respectively, which are indispensable in the recombinational repair of double-strand breaks (DSBs) in Saccharomyces cerevisiae." ], "offsets": [ [ 0, 230 ] ] } ]

[ { "id": "BioInfer.d692.s0.e0", "type": "Gene", "text": [ "rhp54+" ], "offsets": [ [ 49, 55 ] ], "normalized": [] }, { "id": "BioInfer.d692.s0.e1", "type": "Gene", "text": [ "RAD54" ], "offsets": [ [ 97, 102 ] ], "normalized": [] }, { "id": "BioInfer.d692.s0.e2", "type": "Gene", "text": [ "RAD51" ], "offsets": [ [ 80, 85 ] ], "normalized": [] }, { "id": "BioInfer.d692.s0.e3", "type": "Gene", "text": [ "rad22+" ], "offsets": [ [ 38, 44 ] ], "normalized": [] }, { "id": "BioInfer.d692.s0.e4", "type": "Gene", "text": [ "rhp51+" ], "offsets": [ [ 30, 36 ] ], "normalized": [] }, { "id": "BioInfer.d692.s0.e5", "type": "Gene", "text": [ "RAD52" ], "offsets": [ [ 87, 92 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d692.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d692.s0.e0", "arg2_id": "BioInfer.d692.s0.e1", "normalized": [] }, { "id": "BioInfer.d692.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d692.s0.e2", "arg2_id": "BioInfer.d692.s0.e4", "normalized": [] }, { "id": "BioInfer.d692.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d692.s0.e3", "arg2_id": "BioInfer.d692.s0.e5", "normalized": [] } ]

[ { "id": "BioInfer.d693.s0__text", "type": "Sentence", "text": [ "These cells have both alpha-catenin and beta-catenin, display unusual expression of N-cadherin, and have the typical fibroblastic phenotype of transformed cells." ], "offsets": [ [ 0, 161 ] ] } ]

[ { "id": "BioInfer.d693.s0.e0", "type": "Gene/protein/RNA", "text": [ "beta-catenin" ], "offsets": [ [ 40, 52 ] ], "normalized": [] }, { "id": "BioInfer.d693.s0.e1", "type": "Gene/protein/RNA", "text": [ "alpha-catenin" ], "offsets": [ [ 22, 35 ] ], "normalized": [] }, { "id": "BioInfer.d693.s0.e2", "type": "Gene/protein/RNA", "text": [ "N-cadherin" ], "offsets": [ [ 84, 94 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d694.s0__text", "type": "Sentence", "text": [ "These data strongly suggest that the head, neck, and tail domains of all myosin heavy chains, and light chains at least of class II myosins, have coevolved and are likely to be functionally interdependent, consistent with biochemical evidence showing that regulated actin-dependent MgATPase activity of Dictyostelium myosin II requires isoform specific interactions between the heavy chain head and tail and light chains." ], "offsets": [ [ 0, 421 ] ] } ]

[ { "id": "BioInfer.d694.s0.e0", "type": "Protein_family_or_group", "text": [ "class II myosins" ], "offsets": [ [ 123, 139 ] ], "normalized": [] }, { "id": "BioInfer.d694.s0.e1", "type": "Individual_protein", "text": [ "myosin II" ], "offsets": [ [ 317, 326 ] ], "normalized": [] }, { "id": "BioInfer.d694.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 266, 271 ] ], "normalized": [] }, { "id": "BioInfer.d694.s0.e3", "type": "Individual_protein", "text": [ "MgATPase" ], "offsets": [ [ 282, 290 ] ], "normalized": [] }, { "id": "BioInfer.d694.s0.e4", "type": "Protein_family_or_group", "text": [ "myosin heavy chains" ], "offsets": [ [ 73, 92 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d694.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d694.s0.e0", "arg2_id": "BioInfer.d694.s0.e1", "normalized": [] }, { "id": "BioInfer.d694.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d694.s0.e0", "arg2_id": "BioInfer.d694.s0.e4", "normalized": [] }, { "id": "BioInfer.d694.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d694.s0.e1", "arg2_id": "BioInfer.d694.s0.e2", "normalized": [] }, { "id": "BioInfer.d694.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d694.s0.e1", "arg2_id": "BioInfer.d694.s0.e3", "normalized": [] }, { "id": "BioInfer.d694.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d694.s0.e1", "arg2_id": "BioInfer.d694.s0.e4", "normalized": [] } ]

[ { "id": "BioInfer.d695.s0__text", "type": "Sentence", "text": [ "These data suggest that nuclear profilin can mediate a stimulus-response action on the actin cytoskeleton which is somehow linked to a phosphoinositide-signaling cascade." ], "offsets": [ [ 0, 170 ] ] } ]

[ { "id": "BioInfer.d695.s0.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 87, 92 ] ], "normalized": [] }, { "id": "BioInfer.d695.s0.e1", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 32, 40 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d695.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d695.s0.e0", "arg2_id": "BioInfer.d695.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d696.s0__text", "type": "Sentence", "text": [ "These differences in contractile protein profiles between single and cultured cells were collaborated with the observation of cells using immunofluorescence microscope with responsible antibodies to isoforms of myosin heavy chain, actin and tropomyosin." ], "offsets": [ [ 0, 253 ] ] } ]

[ { "id": "BioInfer.d696.s0.e0", "type": "Gene/protein/RNA", "text": [ "tropomyosin" ], "offsets": [ [ 241, 252 ] ], "normalized": [] }, { "id": "BioInfer.d696.s0.e1", "type": "Gene/protein/RNA", "text": [ "myosin heavy chain" ], "offsets": [ [ 211, 229 ] ], "normalized": [] }, { "id": "BioInfer.d696.s0.e2", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 231, 236 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d697.s0__text", "type": "Sentence", "text": [ "These findings reveal striking differences between S. cerevisiae and vertebrates in the functions of RAD51 and RAD52." ], "offsets": [ [ 0, 117 ] ] } ]

[ { "id": "BioInfer.d697.s0.e0", "type": "Gene/protein/RNA", "text": [ "RAD51" ], "offsets": [ [ 101, 106 ] ], "normalized": [] }, { "id": "BioInfer.d697.s0.e1", "type": "Gene/protein/RNA", "text": [ "RAD52" ], "offsets": [ [ 111, 116 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d699.s0__text", "type": "Sentence", "text": [ "These genes were designated UL5, UL8, UL9, UL42, and UL52 and were predicted to encode proteins with molecular weights of, respectively, 99,000, 80,000, 94,000, 51,000, and 114,000." ], "offsets": [ [ 0, 181 ] ] } ]

[ { "id": "BioInfer.d699.s0.e0", "type": "Gene/protein/RNA", "text": [ "UL5" ], "offsets": [ [ 28, 31 ] ], "normalized": [] }, { "id": "BioInfer.d699.s0.e1", "type": "Gene/protein/RNA", "text": [ "UL9" ], "offsets": [ [ 38, 41 ] ], "normalized": [] }, { "id": "BioInfer.d699.s0.e2", "type": "Gene/protein/RNA", "text": [ "UL8" ], "offsets": [ [ 33, 36 ] ], "normalized": [] }, { "id": "BioInfer.d699.s0.e3", "type": "Gene/protein/RNA", "text": [ "UL52" ], "offsets": [ [ 53, 57 ] ], "normalized": [] }, { "id": "BioInfer.d699.s0.e4", "type": "Gene/protein/RNA", "text": [ "UL42" ], "offsets": [ [ 43, 47 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d700.s0__text", "type": "Sentence", "text": [ "These increases were specific; DNA, total protein, lactic dehydrogenase, profilin, and actin depolymerizing factor levels were unchanged in the overexpressing cells." ], "offsets": [ [ 0, 165 ] ] } ]

[ { "id": "BioInfer.d700.s0.e0", "type": "Gene/protein/RNA", "text": [ "profilin" ], "offsets": [ [ 73, 81 ] ], "normalized": [] }, { "id": "BioInfer.d700.s0.e1", "type": "Gene/protein/RNA", "text": [ "actin depolymerizing factor" ], "offsets": [ [ 87, 114 ] ], "normalized": [] }, { "id": "BioInfer.d700.s0.e2", "type": "Gene/protein/RNA", "text": [ "lactic dehydrogenase" ], "offsets": [ [ 51, 71 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d701.s0__text", "type": "Sentence", "text": [ "These observations demonstrate that cardiac development in man, in contrast to rodent heart, is characterized by an up-regulation of the skeletal actin gene, the expression of which does not change in hypertrophied and failing hearts, and suggest that the actin and myosin heavy chain families are independently regulated in human heart." ], "offsets": [ [ 0, 337 ] ] } ]

[ { "id": "BioInfer.d701.s0.e0", "type": "Gene/protein/RNA", "text": [ "skeletal actin" ], "offsets": [ [ 137, 151 ] ], "normalized": [] }, { "id": "BioInfer.d701.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 256, 261 ] ], "normalized": [] }, { "id": "BioInfer.d701.s0.e2", "type": "Individual_protein", "text": [ "myosin heavy chain" ], "offsets": [ [ 266, 284 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d701.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d701.s0.e1", "arg2_id": "BioInfer.d701.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d702.s0__text", "type": "Sentence", "text": [ "These phenotypes are similar to those of the mutant of PFY1, which encodes profilin, an actin-binding protein." ], "offsets": [ [ 0, 110 ] ] } ]

[ { "id": "BioInfer.d702.s0.e0", "type": "Gene", "text": [ "PFY1" ], "offsets": [ [ 55, 59 ] ], "normalized": [] }, { "id": "BioInfer.d702.s0.e1", "type": "Protein_family_or_group", "text": [ "actin-binding protein" ], "offsets": [ [ 88, 109 ] ], "normalized": [] }, { "id": "BioInfer.d702.s0.e2", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 75, 83 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d702.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d702.s0.e0", "arg2_id": "BioInfer.d702.s0.e2", "normalized": [] }, { "id": "BioInfer.d702.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d702.s0.e1", "arg2_id": "BioInfer.d702.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d704.s0__text", "type": "Sentence", "text": [ "These proteins each have a verprolin-homology (V) domain, cofilin-homology (C) domain and an acidic (A) region at the C-terminus, through which they activate the Arp2/3 complex, leading to rapid actin polymerization." ], "offsets": [ [ 0, 216 ] ] } ]

[ { "id": "BioInfer.d704.s0.e0", "type": "Gene/protein/RNA", "text": [ "verprolin" ], "offsets": [ [ 27, 36 ] ], "normalized": [] }, { "id": "BioInfer.d704.s0.e1", "type": "Individual_protein", "text": [ "Arp2" ], "offsets": [ [ 162, 166 ] ], "normalized": [] }, { "id": "BioInfer.d704.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 195, 200 ] ], "normalized": [] }, { "id": "BioInfer.d704.s0.e3", "type": "Gene/protein/RNA", "text": [ "cofilin" ], "offsets": [ [ 58, 65 ] ], "normalized": [] }, { "id": "BioInfer.d704.s0.e4", "type": "Individual_protein", "text": [ "Arp", "3" ], "offsets": [ [ 162, 165 ], [ 167, 168 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d704.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d704.s0.e1", "arg2_id": "BioInfer.d704.s0.e2", "normalized": [] }, { "id": "BioInfer.d704.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d704.s0.e1", "arg2_id": "BioInfer.d704.s0.e4", "normalized": [] }, { "id": "BioInfer.d704.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d704.s0.e2", "arg2_id": "BioInfer.d704.s0.e4", "normalized": [] } ]

[ { "id": "BioInfer.d705.s0__text", "type": "Sentence", "text": [ "The sequence of the inhibitory region is similar to that of a beta-hairpin region of the actin-binding protein profilin." ], "offsets": [ [ 0, 120 ] ] } ]

[ { "id": "BioInfer.d705.s0.e0", "type": "Protein_family_or_group", "text": [ "actin-binding protein" ], "offsets": [ [ 89, 110 ] ], "normalized": [] }, { "id": "BioInfer.d705.s0.e1", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 111, 119 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d705.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d705.s0.e0", "arg2_id": "BioInfer.d705.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d706.s0__text", "type": "Sentence", "text": [ "The sequences of the predicted HMP-1, HMP-2, and HMR-1 proteins are related to the cell adhesion proteins alpha-catenin, beta-catenin/Armadillo, and classical cadherin, respectively." ], "offsets": [ [ 0, 182 ] ] } ]

[ { "id": "BioInfer.d706.s0.e0", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 121, 133 ] ], "normalized": [] }, { "id": "BioInfer.d706.s0.e1", "type": "Protein_family_or_group", "text": [ "cell adhesion proteins" ], "offsets": [ [ 83, 105 ] ], "normalized": [] }, { "id": "BioInfer.d706.s0.e2", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 106, 119 ] ], "normalized": [] }, { "id": "BioInfer.d706.s0.e3", "type": "Individual_protein", "text": [ "classical cadherin" ], "offsets": [ [ 149, 167 ] ], "normalized": [] }, { "id": "BioInfer.d706.s0.e4", "type": "Individual_protein", "text": [ "HMP-2" ], "offsets": [ [ 38, 43 ] ], "normalized": [] }, { "id": "BioInfer.d706.s0.e5", "type": "Individual_protein", "text": [ "HMR-1" ], "offsets": [ [ 49, 54 ] ], "normalized": [] }, { "id": "BioInfer.d706.s0.e6", "type": "Individual_protein", "text": [ "Armadillo" ], "offsets": [ [ 134, 143 ] ], "normalized": [] }, { "id": "BioInfer.d706.s0.e7", "type": "Individual_protein", "text": [ "HMP-1" ], "offsets": [ [ 31, 36 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d706.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d706.s0.e0", "arg2_id": "BioInfer.d706.s0.e1", "normalized": [] }, { "id": "BioInfer.d706.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d706.s0.e0", "arg2_id": "BioInfer.d706.s0.e4", "normalized": [] }, { "id": "BioInfer.d706.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d706.s0.e1", "arg2_id": "BioInfer.d706.s0.e2", "normalized": [] }, { "id": "BioInfer.d706.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d706.s0.e1", "arg2_id": "BioInfer.d706.s0.e3", "normalized": [] }, { "id": "BioInfer.d706.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d706.s0.e1", "arg2_id": "BioInfer.d706.s0.e6", "normalized": [] }, { "id": "BioInfer.d706.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d706.s0.e2", "arg2_id": "BioInfer.d706.s0.e7", "normalized": [] }, { "id": "BioInfer.d706.s0.i6", "type": "PPI", "arg1_id": "BioInfer.d706.s0.e3", "arg2_id": "BioInfer.d706.s0.e5", "normalized": [] }, { "id": "BioInfer.d706.s0.i7", "type": "PPI", "arg1_id": "BioInfer.d706.s0.e4", "arg2_id": "BioInfer.d706.s0.e6", "normalized": [] } ]

[ { "id": "BioInfer.d707.s0__text", "type": "Sentence", "text": [ "These regions also interact with the physiologically relevant ligands of profilin, actin and proline-rich peptides." ], "offsets": [ [ 0, 115 ] ] } ]

[ { "id": "BioInfer.d707.s0.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 83, 88 ] ], "normalized": [] }, { "id": "BioInfer.d707.s0.e1", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 73, 81 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d709.s0__text", "type": "Sentence", "text": [ "These results indicate that phosphorylation of LIM-kinase by ROCK and consequently increased phosphorylation of cofilin by LIM-kinase contribute to Rho-induced reorganization of the actin cytoskeleton." ], "offsets": [ [ 0, 201 ] ] } ]

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[ { "id": "BioInfer.d713.s0__text", "type": "Sentence", "text": [ "These results suggest that LIMK2 functions downstream of the Rho-ROCK signalling pathway and plays a role in reorganization of actin filaments and membrane structures, by phosphorylating cofilin/ADF proteins." ], "offsets": [ [ 0, 208 ] ] } ]

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[ { "id": "BioInfer.d713.s1__text", "type": "Sentence", "text": [ "We report here that LIMK1 and LIMK2 phosphorylate both cofilin and actin-depolymerizing factor (ADF) specifically at Ser-3 and exhibit partially distinct substrate specificity when tested using site-directed cofilin mutants as substrates." ], "offsets": [ [ 0, 238 ] ] } ]

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[ { "id": "BioInfer.d714.s0__text", "type": "Sentence", "text": [ "These results suggest that the heptapeptide sequence is specific for the interaction with actin and, therefore, may constitute part of the actin-binding domain of cofilin." ], "offsets": [ [ 0, 171 ] ] } ]

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[ { "id": "BioInfer.d716.s0__text", "type": "Sentence", "text": [ "The serine phosphatases PP1 and PP2A associate with and activate the actin-binding protein cofilin in human T lymphocytes." ], "offsets": [ [ 0, 122 ] ] } ]

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[ { "id": "BioInfer.d718.s0__text", "type": "Sentence", "text": [ "These two proteins were identified as the phosphorylated and non-phosphorylated forms of the pH-sensitive actin-depolymerizing protein, cofilin, by sequencing of peptide fragments and immunoblotting with a monoclonal antibody specific for cofilin." ], "offsets": [ [ 0, 247 ] ] } ]

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