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Knowledgator Engineering 126

[ { "id": "BioInfer.d43.s3__text", "type": "Sentence", "text": [ "When liver- or islet-type glucokinase was transiently expressed in COS-7 cells, the expressed glucokinase was also co-localized with actin filaments in the cytoplasm of these transfected cells." ], "offsets": [ [ 0, 193 ] ] } ]

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[ { "id": "BioInfer.d44.s0__text", "type": "Sentence", "text": [ "Although neither activation of BCK1 (MEKK) by the dominant BCK1-20 mutation nor increased dosage of MKK1 (MEK) or MPK1 (MAP kinase) mimicked PKC1 as a glc7-10 dosage suppressor, extra copies of genes encoding upstream components of the Pkc1p pathway such as ROM2, RHO2, HCS77/WSC1/SLG1 and MID2 also suppressed glc7-10 effectively." ], "offsets": [ [ 0, 331 ] ] } ]

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[ { "id": "BioInfer.d48.s0__text", "type": "Sentence", "text": [ "A major point of interest was to clarify whether rheological, high precision measurements can yield quantitative information about the influence of talin and vinculin on the structure, chain dynamics, elasticity and viscoelasticity of actin filaments with time." ], "offsets": [ [ 0, 261 ] ] } ]

[ { "id": "BioInfer.d48.s0.e0", "type": "Individual_protein", "text": [ "vinculin" ], "offsets": [ [ 158, 166 ] ], "normalized": [] }, { "id": "BioInfer.d48.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 235, 240 ] ], "normalized": [] }, { "id": "BioInfer.d48.s0.e2", "type": "Individual_protein", "text": [ "talin" ], "offsets": [ [ 148, 153 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d48.s1__text", "type": "Sentence", "text": [ "The viscoelasticity of entangled actin networks: the influence of defects and modulation by talin and vinculin." ], "offsets": [ [ 0, 111 ] ] } ]

[ { "id": "BioInfer.d48.s1.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 33, 38 ] ], "normalized": [] }, { "id": "BioInfer.d48.s1.e1", "type": "Individual_protein", "text": [ "talin" ], "offsets": [ [ 92, 97 ] ], "normalized": [] }, { "id": "BioInfer.d48.s1.e2", "type": "Individual_protein", "text": [ "vinculin" ], "offsets": [ [ 102, 110 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d48.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d48.s1.e0", "arg2_id": "BioInfer.d48.s1.e1", "normalized": [] }, { "id": "BioInfer.d48.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d48.s1.e0", "arg2_id": "BioInfer.d48.s1.e2", "normalized": [] } ]

[ { "id": "BioInfer.d49.s0__text", "type": "Sentence", "text": [ "A model is proposed for the function of profilin in actin-based motility." ], "offsets": [ [ 0, 73 ] ] } ]

[ { "id": "BioInfer.d49.s0.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 52, 57 ] ], "normalized": [] }, { "id": "BioInfer.d49.s0.e1", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 40, 48 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d49.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d49.s0.e0", "arg2_id": "BioInfer.d49.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d49.s1__text", "type": "Sentence", "text": [ "As a consequence, in the presence of thymosin beta 4 (T beta 4), low amounts of profilin promote extensive actin assembly off of the pool of actin-T beta 4 complex." ], "offsets": [ [ 0, 164 ] ] } ]

[ { "id": "BioInfer.d49.s1.e0", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 80, 88 ] ], "normalized": [] }, { "id": "BioInfer.d49.s1.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 107, 112 ] ], "normalized": [] }, { "id": "BioInfer.d49.s1.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 141, 146 ] ], "normalized": [] }, { "id": "BioInfer.d49.s1.e3", "type": "Individual_protein", "text": [ "thymosin beta 4" ], "offsets": [ [ 37, 52 ] ], "normalized": [] }, { "id": "BioInfer.d49.s1.e4", "type": "Individual_protein", "text": [ "T beta 4" ], "offsets": [ [ 147, 155 ] ], "normalized": [] }, { "id": "BioInfer.d49.s1.e5", "type": "Individual_protein", "text": [ "T beta 4" ], "offsets": [ [ 54, 62 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d49.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d49.s1.e0", "arg2_id": "BioInfer.d49.s1.e1", "normalized": [] }, { "id": "BioInfer.d49.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d49.s1.e1", "arg2_id": "BioInfer.d49.s1.e2", "normalized": [] }, { "id": "BioInfer.d49.s1.i2", "type": "PPI", "arg1_id": "BioInfer.d49.s1.e1", "arg2_id": "BioInfer.d49.s1.e4", "normalized": [] }, { "id": "BioInfer.d49.s1.i3", "type": "PPI", "arg1_id": "BioInfer.d49.s1.e2", "arg2_id": "BioInfer.d49.s1.e4", "normalized": [] } ]

[ { "id": "BioInfer.d49.s2__text", "type": "Sentence", "text": [ "How profilin promotes actin filament assembly in the presence of thymosin beta 4." ], "offsets": [ [ 0, 81 ] ] } ]

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[ { "id": "BioInfer.d49.s2.i0", "type": "PPI", "arg1_id": "BioInfer.d49.s2.e0", "arg2_id": "BioInfer.d49.s2.e2", "normalized": [] } ]

[ { "id": "BioInfer.d49.s3__text", "type": "Sentence", "text": [ "The role of profilin in the regulation of actin assembly has been reexamined." ], "offsets": [ [ 0, 77 ] ] } ]

[ { "id": "BioInfer.d49.s3.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 42, 47 ] ], "normalized": [] }, { "id": "BioInfer.d49.s3.e1", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 12, 20 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d49.s3.i0", "type": "PPI", "arg1_id": "BioInfer.d49.s3.e0", "arg2_id": "BioInfer.d49.s3.e1", "normalized": [] } ]

[ { "id": "BioInfer.d49.s4__text", "type": "Sentence", "text": [ "When barbed ends are capped, profilin simply sequesters globular actin." ], "offsets": [ [ 0, 71 ] ] } ]

[ { "id": "BioInfer.d49.s4.e0", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 29, 37 ] ], "normalized": [] }, { "id": "BioInfer.d49.s4.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 65, 70 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d49.s4.i0", "type": "PPI", "arg1_id": "BioInfer.d49.s4.e0", "arg2_id": "BioInfer.d49.s4.e1", "normalized": [] } ]

[ { "id": "BioInfer.d50.s0__text", "type": "Sentence", "text": [ "mDia binds profilin likely to promote actin polymerization." ], "offsets": [ [ 0, 59 ] ] } ]

[ { "id": "BioInfer.d50.s0.e0", "type": "Individual_protein", "text": [ "mDia" ], "offsets": [ [ 0, 4 ] ], "normalized": [] }, { "id": "BioInfer.d50.s0.e1", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 11, 19 ] ], "normalized": [] }, { "id": "BioInfer.d50.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 38, 43 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d50.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d50.s0.e0", "arg2_id": "BioInfer.d50.s0.e1", "normalized": [] }, { "id": "BioInfer.d50.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d50.s0.e0", "arg2_id": "BioInfer.d50.s0.e2", "normalized": [] }, { "id": "BioInfer.d50.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d50.s0.e1", "arg2_id": "BioInfer.d50.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d51.s0__text", "type": "Sentence", "text": [ "MSH2 plays a fundamental role in mispair recognition whereas MSH3 and MSH6 appear to modify the specificity of this recognition." ], "offsets": [ [ 0, 128 ] ] } ]

[ { "id": "BioInfer.d51.s0.e0", "type": "Gene/protein/RNA", "text": [ "MSH2" ], "offsets": [ [ 0, 4 ] ], "normalized": [] }, { "id": "BioInfer.d51.s0.e1", "type": "Gene/protein/RNA", "text": [ "MSH6" ], "offsets": [ [ 70, 74 ] ], "normalized": [] }, { "id": "BioInfer.d51.s0.e2", "type": "Gene/protein/RNA", "text": [ "MSH3" ], "offsets": [ [ 61, 65 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d52.s0__text", "type": "Sentence", "text": [ "Munc18-2 is a Sec1 homologue enriched in epithelial cells and forms a complex with syntaxin 3, a t-SNARE localized to the apical plasma membrane." ], "offsets": [ [ 0, 145 ] ] } ]

[ { "id": "BioInfer.d52.s0.e0", "type": "Protein_family_or_group", "text": [ "t-SNARE" ], "offsets": [ [ 97, 104 ] ], "normalized": [] }, { "id": "BioInfer.d52.s0.e1", "type": "Individual_protein", "text": [ "Munc18-2" ], "offsets": [ [ 0, 8 ] ], "normalized": [] }, { "id": "BioInfer.d52.s0.e2", "type": "Individual_protein", "text": [ "Sec1" ], "offsets": [ [ 14, 18 ] ], "normalized": [] }, { "id": "BioInfer.d52.s0.e3", "type": "Individual_protein", "text": [ "syntaxin 3" ], "offsets": [ [ 83, 93 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d52.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d52.s0.e0", "arg2_id": "BioInfer.d52.s0.e3", "normalized": [] }, { "id": "BioInfer.d52.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d52.s0.e1", "arg2_id": "BioInfer.d52.s0.e2", "normalized": [] }, { "id": "BioInfer.d52.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d52.s0.e1", "arg2_id": "BioInfer.d52.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d52.s1__text", "type": "Sentence", "text": [ "Even the Munc18-2 mutants that do not detectably bind syntaxin 3 were membrane associated in Caco-2 cells, suggesting that the syntaxin interaction is not the sole determinant of Sec1 protein membrane attachment." ], "offsets": [ [ 0, 212 ] ] } ]

[ { "id": "BioInfer.d52.s1.e0", "type": "Individual_protein", "text": [ "syntaxin" ], "offsets": [ [ 127, 135 ] ], "normalized": [] }, { "id": "BioInfer.d52.s1.e1", "type": "Individual_protein", "text": [ "Sec1" ], "offsets": [ [ 179, 183 ] ], "normalized": [] }, { "id": "BioInfer.d52.s1.e2", "type": "Individual_protein", "text": [ "syntaxin 3" ], "offsets": [ [ 54, 64 ] ], "normalized": [] }, { "id": "BioInfer.d52.s1.e3", "type": "Individual_protein", "text": [ "Munc18-2" ], "offsets": [ [ 9, 17 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d52.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d52.s1.e0", "arg2_id": "BioInfer.d52.s1.e1", "normalized": [] }, { "id": "BioInfer.d52.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d52.s1.e2", "arg2_id": "BioInfer.d52.s1.e3", "normalized": [] } ]

[ { "id": "BioInfer.d52.s2__text", "type": "Sentence", "text": [ "The in vitro and in vivo binding patterns were highly similar, and the association of the Munc18-2 variants with syntaxin 3 correlated well with their ability to displace SNAP-23 from syntaxin 3 complexes when overexpressed in Caco-2 cells." ], "offsets": [ [ 0, 240 ] ] } ]

[ { "id": "BioInfer.d52.s2.e0", "type": "Individual_protein", "text": [ "Munc18-2" ], "offsets": [ [ 90, 98 ] ], "normalized": [] }, { "id": "BioInfer.d52.s2.e1", "type": "Individual_protein", "text": [ "syntaxin 3" ], "offsets": [ [ 184, 194 ] ], "normalized": [] }, { "id": "BioInfer.d52.s2.e2", "type": "Individual_protein", "text": [ "SNAP-23" ], "offsets": [ [ 171, 178 ] ], "normalized": [] }, { "id": "BioInfer.d52.s2.e3", "type": "Individual_protein", "text": [ "syntaxin 3" ], "offsets": [ [ 113, 123 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d52.s3__text", "type": "Sentence", "text": [ "This implies that Munc18-2 function in apical membrane trafficking involves aspects independent of the syntaxin 3 interaction." ], "offsets": [ [ 0, 126 ] ] } ]

[ { "id": "BioInfer.d52.s3.e0", "type": "Gene/protein/RNA", "text": [ "syntaxin 3" ], "offsets": [ [ 103, 113 ] ], "normalized": [] }, { "id": "BioInfer.d52.s3.e1", "type": "Gene/protein/RNA", "text": [ "Munc18-2" ], "offsets": [ [ 18, 26 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d53.s0__text", "type": "Sentence", "text": [ "Analyses of beta-catenin or E-cadherin immunoprecipitates from BMMC lysate revealed that alpha-catenin, beta-catenin, and E-cadherin were co-precipitated, suggesting that E-cadherin and catenins form a complex in mast cells." ], "offsets": [ [ 0, 224 ] ] } ]

[ { "id": "BioInfer.d53.s0.e0", "type": "Gene/protein/RNA", "text": [ "E-cadherin" ], "offsets": [ [ 28, 38 ] ], "normalized": [] }, { "id": "BioInfer.d53.s0.e1", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 104, 116 ] ], "normalized": [] }, { "id": "BioInfer.d53.s0.e2", "type": "Individual_protein", "text": [ "catenins" ], "offsets": [ [ 186, 194 ] ], "normalized": [] }, { "id": "BioInfer.d53.s0.e3", "type": "Individual_protein", "text": [ "E-cadherin" ], "offsets": [ [ 171, 181 ] ], "normalized": [] }, { "id": "BioInfer.d53.s0.e4", "type": "Gene/protein/RNA", "text": [ "beta-catenin" ], "offsets": [ [ 12, 24 ] ], "normalized": [] }, { "id": "BioInfer.d53.s0.e5", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 89, 102 ] ], "normalized": [] }, { "id": "BioInfer.d53.s0.e6", "type": "Individual_protein", "text": [ "E-cadherin" ], "offsets": [ [ 122, 132 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d53.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d53.s0.e1", "arg2_id": "BioInfer.d53.s0.e5", "normalized": [] }, { "id": "BioInfer.d53.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d53.s0.e1", "arg2_id": "BioInfer.d53.s0.e6", "normalized": [] }, { "id": "BioInfer.d53.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d53.s0.e2", "arg2_id": "BioInfer.d53.s0.e3", "normalized": [] }, { "id": "BioInfer.d53.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d53.s0.e5", "arg2_id": "BioInfer.d53.s0.e6", "normalized": [] } ]

[ { "id": "BioInfer.d55.s0__text", "type": "Sentence", "text": [ "Analysis of profilin: actin crystals reveals an extensive intermolecular network, rather than a discrete \"monomeric complex\", comprising stacked actin ribbons held in place by columns of profilin molecules, wedged in between neighboring actin subunits and running perpendicular to the ribbons." ], "offsets": [ [ 0, 293 ] ] } ]

[ { "id": "BioInfer.d55.s0.e0", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 12, 20 ] ], "normalized": [] }, { "id": "BioInfer.d55.s0.e1", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 187, 195 ] ], "normalized": [] }, { "id": "BioInfer.d55.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 145, 150 ] ], "normalized": [] }, { "id": "BioInfer.d55.s0.e3", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 22, 27 ] ], "normalized": [] }, { "id": "BioInfer.d55.s0.e4", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 237, 242 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d55.s1__text", "type": "Sentence", "text": [ "Molecular packing in profilin: actin crystals and its implications." ], "offsets": [ [ 0, 67 ] ] } ]

[ { "id": "BioInfer.d55.s1.e0", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 21, 29 ] ], "normalized": [] }, { "id": "BioInfer.d55.s1.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 31, 36 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d56.s0__text", "type": "Sentence", "text": [ "Analysis of changes in state suggests that SIR1 protein has a role in the establishment but not the maintenance of repression of silent mating type genes, whereas SIR2, SIR3, and SIR4 are required for maintenance." ], "offsets": [ [ 0, 213 ] ] } ]

[ { "id": "BioInfer.d56.s0.e0", "type": "Gene/protein/RNA", "text": [ "SIR2" ], "offsets": [ [ 163, 167 ] ], "normalized": [] }, { "id": "BioInfer.d56.s0.e1", "type": "Gene/protein/RNA", "text": [ "SIR4" ], "offsets": [ [ 179, 183 ] ], "normalized": [] }, { "id": "BioInfer.d56.s0.e2", "type": "Gene/protein/RNA", "text": [ "SIR1" ], "offsets": [ [ 43, 47 ] ], "normalized": [] }, { "id": "BioInfer.d56.s0.e3", "type": "Gene/protein/RNA", "text": [ "SIR3" ], "offsets": [ [ 169, 173 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d57.s0__text", "type": "Sentence", "text": [ "Analysis of the formation of the calf spleen complex in the presence of varying concentrations of divalent cations gave evidence for the presence of a high-affinity divalent-cation-binding site on the spleen actin (beta, gamma) which appears to regulate the interaction with profilin." ], "offsets": [ [ 0, 284 ] ] } ]

[ { "id": "BioInfer.d57.s0.e0", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 275, 283 ] ], "normalized": [] }, { "id": "BioInfer.d57.s0.e1", "type": "Individual_protein", "text": [ "spleen actin", "gamma" ], "offsets": [ [ 201, 213 ], [ 221, 226 ] ], "normalized": [] }, { "id": "BioInfer.d57.s0.e2", "type": "Individual_protein", "text": [ "spleen actin", "beta" ], "offsets": [ [ 201, 213 ], [ 215, 219 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d57.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d57.s0.e0", "arg2_id": "BioInfer.d57.s0.e1", "normalized": [] }, { "id": "BioInfer.d57.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d57.s0.e0", "arg2_id": "BioInfer.d57.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d57.s1__text", "type": "Sentence", "text": [ "The interaction between calf spleen profilin and actin depends critically on the status of the C-terminus of the actin, and in the case of profilin, the C-terminus is of great importance for the physiochemical behaviour of the protein." ], "offsets": [ [ 0, 235 ] ] } ]

[ { "id": "BioInfer.d57.s1.e0", "type": "Gene/protein/RNA", "text": [ "profilin" ], "offsets": [ [ 139, 147 ] ], "normalized": [] }, { "id": "BioInfer.d57.s1.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 113, 118 ] ], "normalized": [] }, { "id": "BioInfer.d57.s1.e2", "type": "Individual_protein", "text": [ "spleen", "actin" ], "offsets": [ [ 29, 35 ], [ 49, 54 ] ], "normalized": [] }, { "id": "BioInfer.d57.s1.e3", "type": "Individual_protein", "text": [ "spleen profilin" ], "offsets": [ [ 29, 44 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d57.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d57.s1.e1", "arg2_id": "BioInfer.d57.s1.e2", "normalized": [] }, { "id": "BioInfer.d57.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d57.s1.e1", "arg2_id": "BioInfer.d57.s1.e3", "normalized": [] }, { "id": "BioInfer.d57.s1.i2", "type": "PPI", "arg1_id": "BioInfer.d57.s1.e2", "arg2_id": "BioInfer.d57.s1.e3", "normalized": [] } ]

[ { "id": "BioInfer.d58.s0__text", "type": "Sentence", "text": [ "Analysis of the u.v. absorbance and far-u.v. circular dichroism spectra of profilin and actin did not reveal any major changes in the conformation of the proteins accompanying the modifications at the C-terminal ends." ], "offsets": [ [ 0, 217 ] ] } ]

[ { "id": "BioInfer.d58.s0.e0", "type": "Gene/protein/RNA", "text": [ "profilin" ], "offsets": [ [ 75, 83 ] ], "normalized": [] }, { "id": "BioInfer.d58.s0.e1", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 88, 93 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d59.s0__text", "type": "Sentence", "text": [ "Analysis of this product by peptide mapping (Sutoh (1982) Biochemistry 21, 3654-3661) showed that cofilin was cross-linked with the N-terminal segment of actin containing residues 1-12." ], "offsets": [ [ 0, 185 ] ] } ]

[ { "id": "BioInfer.d59.s0.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 154, 159 ] ], "normalized": [] }, { "id": "BioInfer.d59.s0.e1", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 98, 105 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d59.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d59.s0.e0", "arg2_id": "BioInfer.d59.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d59.s1__text", "type": "Sentence", "text": [ "Purification of cofilin, a 21,000 molecular weight actin-binding protein, from porcine kidney and identification of the cofilin-binding site in the actin sequence." ], "offsets": [ [ 0, 163 ] ] } ]

[ { "id": "BioInfer.d59.s1.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 148, 153 ] ], "normalized": [] }, { "id": "BioInfer.d59.s1.e1", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 120, 127 ] ], "normalized": [] }, { "id": "BioInfer.d59.s1.e2", "type": "Protein_family_or_group", "text": [ "actin-binding protein" ], "offsets": [ [ 51, 72 ] ], "normalized": [] }, { "id": "BioInfer.d59.s1.e3", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 16, 23 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d59.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d59.s1.e0", "arg2_id": "BioInfer.d59.s1.e1", "normalized": [] }, { "id": "BioInfer.d59.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d59.s1.e2", "arg2_id": "BioInfer.d59.s1.e3", "normalized": [] } ]

[ { "id": "BioInfer.d60.s0__text", "type": "Sentence", "text": [ "Analysis of V3, a hamster equivalent of SCID, indicates that the protein level increases of RAD51 and RAD52 from G0 to G1/S/G2 do not require DNA-PK." ], "offsets": [ [ 0, 149 ] ] } ]

[ { "id": "BioInfer.d60.s0.e0", "type": "Individual_protein", "text": [ "DNA-PK" ], "offsets": [ [ 142, 148 ] ], "normalized": [] }, { "id": "BioInfer.d60.s0.e1", "type": "Gene", "text": [ "RAD51" ], "offsets": [ [ 92, 97 ] ], "normalized": [] }, { "id": "BioInfer.d60.s0.e2", "type": "Gene", "text": [ "RAD52" ], "offsets": [ [ 102, 107 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d60.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d60.s0.e0", "arg2_id": "BioInfer.d60.s0.e1", "normalized": [] }, { "id": "BioInfer.d60.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d60.s0.e0", "arg2_id": "BioInfer.d60.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d60.s1__text", "type": "Sentence", "text": [ "In this study, cell cycle-dependent expression of human and rodent RAD51 and RAD52 proteins was monitored using two approaches." ], "offsets": [ [ 0, 127 ] ] } ]

[ { "id": "BioInfer.d60.s1.e0", "type": "Gene/protein/RNA", "text": [ "RAD52" ], "offsets": [ [ 77, 82 ] ], "normalized": [] }, { "id": "BioInfer.d60.s1.e1", "type": "Gene/protein/RNA", "text": [ "RAD51" ], "offsets": [ [ 67, 72 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d61.s0__text", "type": "Sentence", "text": [ "Analysis of various truncated alpha-catenin molecules revealed that amino-terminal residues 48-163 are able to bind to beta-catenin and plakoglobin." ], "offsets": [ [ 0, 148 ] ] } ]

[ { "id": "BioInfer.d61.s0.e0", "type": "Individual_protein", "text": [ "plakoglobin" ], "offsets": [ [ 136, 147 ] ], "normalized": [] }, { "id": "BioInfer.d61.s0.e1", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 119, 131 ] ], "normalized": [] }, { "id": "BioInfer.d61.s0.e2", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 30, 43 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d61.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d61.s0.e0", "arg2_id": "BioInfer.d61.s0.e2", "normalized": [] }, { "id": "BioInfer.d61.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d61.s0.e1", "arg2_id": "BioInfer.d61.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d61.s1__text", "type": "Sentence", "text": [ "Consistent with the observation that beta-catenin and plakoglobin bind to the same region of alpha-catenin, beta-catenin competed with the binding of plakoglobin to alpha-catenin and vice versa." ], "offsets": [ [ 0, 194 ] ] } ]

[ { "id": "BioInfer.d61.s1.e0", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 93, 106 ] ], "normalized": [] }, { "id": "BioInfer.d61.s1.e1", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 165, 178 ] ], "normalized": [] }, { "id": "BioInfer.d61.s1.e2", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 108, 120 ] ], "normalized": [] }, { "id": "BioInfer.d61.s1.e3", "type": "Individual_protein", "text": [ "plakoglobin" ], "offsets": [ [ 150, 161 ] ], "normalized": [] }, { "id": "BioInfer.d61.s1.e4", "type": "Individual_protein", "text": [ "plakoglobin" ], "offsets": [ [ 54, 65 ] ], "normalized": [] }, { "id": "BioInfer.d61.s1.e5", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 37, 49 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d61.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d61.s1.e0", "arg2_id": "BioInfer.d61.s1.e4", "normalized": [] }, { "id": "BioInfer.d61.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d61.s1.e0", "arg2_id": "BioInfer.d61.s1.e5", "normalized": [] }, { "id": "BioInfer.d61.s1.i2", "type": "PPI", "arg1_id": "BioInfer.d61.s1.e1", "arg2_id": "BioInfer.d61.s1.e2", "normalized": [] }, { "id": "BioInfer.d61.s1.i3", "type": "PPI", "arg1_id": "BioInfer.d61.s1.e1", "arg2_id": "BioInfer.d61.s1.e3", "normalized": [] } ]

[ { "id": "BioInfer.d61.s2__text", "type": "Sentence", "text": [ "Using an in vitro assay system involving bacterially expressed proteins, we localized a region in alpha-catenin required for molecular interaction with beta-catenin and plakoglobin." ], "offsets": [ [ 0, 181 ] ] } ]

[ { "id": "BioInfer.d61.s2.e0", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 152, 164 ] ], "normalized": [] }, { "id": "BioInfer.d61.s2.e1", "type": "Individual_protein", "text": [ "plakoglobin" ], "offsets": [ [ 169, 180 ] ], "normalized": [] }, { "id": "BioInfer.d61.s2.e2", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 98, 111 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d61.s2.i0", "type": "PPI", "arg1_id": "BioInfer.d61.s2.e0", "arg2_id": "BioInfer.d61.s2.e2", "normalized": [] }, { "id": "BioInfer.d61.s2.i1", "type": "PPI", "arg1_id": "BioInfer.d61.s2.e1", "arg2_id": "BioInfer.d61.s2.e2", "normalized": [] } ]

[ { "id": "BioInfer.d61.s3__text", "type": "Sentence", "text": [ "When transfected into L cells expressing E-cadherin, the amino-terminal region of alpha-catenin (from residue 1 to 226) formed complexes with beta-catenin supporting the in vitro binding experiment results." ], "offsets": [ [ 0, 206 ] ] } ]

[ { "id": "BioInfer.d61.s3.e0", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 82, 95 ] ], "normalized": [] }, { "id": "BioInfer.d61.s3.e1", "type": "Gene/protein/RNA", "text": [ "E-cadherin" ], "offsets": [ [ 41, 51 ] ], "normalized": [] }, { "id": "BioInfer.d61.s3.e2", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 142, 154 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d61.s3.i0", "type": "PPI", "arg1_id": "BioInfer.d61.s3.e0", "arg2_id": "BioInfer.d61.s3.e2", "normalized": [] } ]

[ { "id": "BioInfer.d62.s0__text", "type": "Sentence", "text": [ "An assembly of the UL5 and UL52 subunits retains both enzymic activities, and the UL8 protein has been implicated in modulating these functions, facilitating efficient nuclear uptake of the complex and interacting with other viral DNA replication proteins." ], "offsets": [ [ 0, 256 ] ] } ]

[ { "id": "BioInfer.d62.s0.e0", "type": "Individual_protein", "text": [ "UL52" ], "offsets": [ [ 27, 31 ] ], "normalized": [] }, { "id": "BioInfer.d62.s0.e1", "type": "Individual_protein", "text": [ "UL5" ], "offsets": [ [ 19, 22 ] ], "normalized": [] }, { "id": "BioInfer.d62.s0.e2", "type": "Individual_protein", "text": [ "UL8" ], "offsets": [ [ 82, 85 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d62.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d62.s0.e0", "arg2_id": "BioInfer.d62.s0.e1", "normalized": [] }, { "id": "BioInfer.d62.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d62.s0.e0", "arg2_id": "BioInfer.d62.s0.e2", "normalized": [] }, { "id": "BioInfer.d62.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d62.s0.e1", "arg2_id": "BioInfer.d62.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d62.s1__text", "type": "Sentence", "text": [ "Deletion mutants of the herpes simplex virus type 1 UL8 protein: effect on DNA synthesis and ability to interact with and influence the intracellular localization of the UL5 and UL52 proteins." ], "offsets": [ [ 0, 192 ] ] } ]

[ { "id": "BioInfer.d62.s1.e0", "type": "Individual_protein", "text": [ "UL52" ], "offsets": [ [ 178, 182 ] ], "normalized": [] }, { "id": "BioInfer.d62.s1.e1", "type": "Individual_protein", "text": [ "UL5" ], "offsets": [ [ 170, 173 ] ], "normalized": [] }, { "id": "BioInfer.d62.s1.e2", "type": "Individual_protein", "text": [ "UL8" ], "offsets": [ [ 52, 55 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d62.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d62.s1.e0", "arg2_id": "BioInfer.d62.s1.e2", "normalized": [] }, { "id": "BioInfer.d62.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d62.s1.e1", "arg2_id": "BioInfer.d62.s1.e2", "normalized": [] } ]

[ { "id": "BioInfer.d62.s2__text", "type": "Sentence", "text": [ "The herpes simplex virus type 1 (HSV-1) helicase-primase, an essential component of the viral DNA replication machinery, is a trimeric complex of the virus-coded UL5, UL8, and UL52 proteins." ], "offsets": [ [ 0, 190 ] ] } ]

[ { "id": "BioInfer.d62.s2.e0", "type": "Protein_complex", "text": [ "helicase-primase" ], "offsets": [ [ 40, 56 ] ], "normalized": [] }, { "id": "BioInfer.d62.s2.e1", "type": "Individual_protein", "text": [ "UL5" ], "offsets": [ [ 162, 165 ] ], "normalized": [] }, { "id": "BioInfer.d62.s2.e2", "type": "Individual_protein", "text": [ "UL8" ], "offsets": [ [ 167, 170 ] ], "normalized": [] }, { "id": "BioInfer.d62.s2.e3", "type": "Individual_protein", "text": [ "UL52" ], "offsets": [ [ 176, 180 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d62.s2.i0", "type": "PPI", "arg1_id": "BioInfer.d62.s2.e0", "arg2_id": "BioInfer.d62.s2.e1", "normalized": [] }, { "id": "BioInfer.d62.s2.i1", "type": "PPI", "arg1_id": "BioInfer.d62.s2.e0", "arg2_id": "BioInfer.d62.s2.e2", "normalized": [] }, { "id": "BioInfer.d62.s2.i2", "type": "PPI", "arg1_id": "BioInfer.d62.s2.e0", "arg2_id": "BioInfer.d62.s2.e3", "normalized": [] }, { "id": "BioInfer.d62.s2.i3", "type": "PPI", "arg1_id": "BioInfer.d62.s2.e1", "arg2_id": "BioInfer.d62.s2.e2", "normalized": [] }, { "id": "BioInfer.d62.s2.i4", "type": "PPI", "arg1_id": "BioInfer.d62.s2.e1", "arg2_id": "BioInfer.d62.s2.e3", "normalized": [] }, { "id": "BioInfer.d62.s2.i5", "type": "PPI", "arg1_id": "BioInfer.d62.s2.e2", "arg2_id": "BioInfer.d62.s2.e3", "normalized": [] } ]

[ { "id": "BioInfer.d63.s0__text", "type": "Sentence", "text": [ "An association was seen between E-cadherin and alpha-catenin expression, in both effusions and solid tumours, and for beta-catenin in solid tumours (range p<0. 001 to p=0.014)." ], "offsets": [ [ 0, 176 ] ] } ]

[ { "id": "BioInfer.d63.s0.e0", "type": "Gene/protein/RNA", "text": [ "beta-catenin" ], "offsets": [ [ 118, 130 ] ], "normalized": [] }, { "id": "BioInfer.d63.s0.e1", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 47, 60 ] ], "normalized": [] }, { "id": "BioInfer.d63.s0.e2", "type": "Individual_protein", "text": [ "E-cadherin" ], "offsets": [ [ 32, 42 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d63.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d63.s0.e1", "arg2_id": "BioInfer.d63.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d65.s0__text", "type": "Sentence", "text": [ "An oligomeric form of simian virus 40 large T-antigen is immunologically related to the cellular tumor antigen p53." ], "offsets": [ [ 0, 115 ] ] } ]

[ { "id": "BioInfer.d65.s0.e0", "type": "Individual_protein", "text": [ "large T-antigen" ], "offsets": [ [ 38, 53 ] ], "normalized": [] }, { "id": "BioInfer.d65.s0.e1", "type": "Individual_protein", "text": [ "p53" ], "offsets": [ [ 111, 114 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d65.s1__text", "type": "Sentence", "text": [ "The cellular tumor antigen p53 is bound to the simian virus 40 (SV40) large T-antigen in SV40-infected and -transformed cells." ], "offsets": [ [ 0, 126 ] ] } ]

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[ { "id": "BioInfer.d66.s0__text", "type": "Sentence", "text": [ "Another cyclin-dependent kinase inhibitor, p27KIP1, and cyclin D increased slightly, whereas proliferating cell nuclear antigen and p130 remained unchanged." ], "offsets": [ [ 0, 156 ] ] } ]

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[ { "id": "BioInfer.d66.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d66.s0.e1", "arg2_id": "BioInfer.d66.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d67.s0__text", "type": "Sentence", "text": [ "A null mutation of the actin gene (ACT1) is lethal, but null mutations in the tropomyosin (TPM1), fimbrin (SAC6), Abp1p (ABP1), and capping protein (CAP1 and CAP2) genes have relatively mild or no effects." ], "offsets": [ [ 0, 205 ] ] } ]

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[ { "id": "BioInfer.d68.s0__text", "type": "Sentence", "text": [ "ORC1, ORC4 and Cdc6 were stable (T1/2 >2 h) and associated with a chromatin-containing fraction throughout the cell cycle." ], "offsets": [ [ 0, 122 ] ] } ]

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[ { "id": "BioInfer.d68.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d68.s0.e0", "arg2_id": "BioInfer.d68.s0.e1", "normalized": [] }, { "id": "BioInfer.d68.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d68.s0.e0", "arg2_id": "BioInfer.d68.s0.e2", "normalized": [] }, { "id": "BioInfer.d68.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d68.s0.e1", "arg2_id": "BioInfer.d68.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d68.s1__text", "type": "Sentence", "text": [ "Green fluorescent protein-tagged ORC1 associated with chromatin throughout mitosis in living cells and co-localized with ORC4 in metaphase spreads." ], "offsets": [ [ 0, 147 ] ] } ]

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[ { "id": "BioInfer.d68.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d68.s1.e0", "arg2_id": "BioInfer.d68.s1.e2", "normalized": [] }, { "id": "BioInfer.d68.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d68.s1.e1", "arg2_id": "BioInfer.d68.s1.e2", "normalized": [] } ]

[ { "id": "BioInfer.d69.s0__text", "type": "Sentence", "text": [ "A pre-treatment of cells with SGE from partially fed ticks in amounts corresponding to 1 or 3 salivary glands increased the level of both viral nucleocapsid (N) protein and phosphoprotein (P) in a dose-dependent manner." ], "offsets": [ [ 0, 219 ] ] } ]

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[ { "id": "BioInfer.d70.s0__text", "type": "Sentence", "text": [ "Aprotinin inhibited platelet aggregation induced by thrombin (0.25 U.ml-1) with IC50 200 kIU.ml-1, and inhibited the rise of cytosolic free calcium concentration in platelets stimulated by thrombin (0.1 U.ml-1) in the absence and in the presence of Ca2+ 0.5 mmol.L-1 (IC50 117 and 50 kIU.ml-1, respectively), but had no effect on the amounts of actin and myosin heavy chain associated with cytoskeletons." ], "offsets": [ [ 0, 404 ] ] } ]

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[ { "id": "BioInfer.d70.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d70.s0.e0", "arg2_id": "BioInfer.d70.s0.e2", "normalized": [] }, { "id": "BioInfer.d70.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d70.s0.e1", "arg2_id": "BioInfer.d70.s0.e2", "normalized": [] }, { "id": "BioInfer.d70.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d70.s0.e2", "arg2_id": "BioInfer.d70.s0.e4", "normalized": [] } ]

[ { "id": "BioInfer.d71.s0__text", "type": "Sentence", "text": [ "RAD51, RAD52, and RAD54 encode proteins that are critical to the repair of double-strand DNA breaks by homologous recombination." ], "offsets": [ [ 0, 128 ] ] } ]

[ { "id": "BioInfer.d71.s0.e0", "type": "Gene/protein/RNA", "text": [ "RAD52" ], "offsets": [ [ 7, 12 ] ], "normalized": [] }, { "id": "BioInfer.d71.s0.e1", "type": "Gene/protein/RNA", "text": [ "RAD51" ], "offsets": [ [ 0, 5 ] ], "normalized": [] }, { "id": "BioInfer.d71.s0.e2", "type": "Gene/protein/RNA", "text": [ "RAD54" ], "offsets": [ [ 18, 23 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d72.s0__text", "type": "Sentence", "text": [ "RAD51, RAD52, RAD57, and RAD59 were required for efficient gap repair using either chromosomal or plasmid donors." ], "offsets": [ [ 0, 113 ] ] } ]

[ { "id": "BioInfer.d72.s0.e0", "type": "Gene/protein/RNA", "text": [ "RAD59" ], "offsets": [ [ 25, 30 ] ], "normalized": [] }, { "id": "BioInfer.d72.s0.e1", "type": "Gene/protein/RNA", "text": [ "RAD52" ], "offsets": [ [ 7, 12 ] ], "normalized": [] }, { "id": "BioInfer.d72.s0.e2", "type": "Gene/protein/RNA", "text": [ "RAD57" ], "offsets": [ [ 14, 19 ] ], "normalized": [] }, { "id": "BioInfer.d72.s0.e3", "type": "Gene/protein/RNA", "text": [ "RAD51" ], "offsets": [ [ 0, 5 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d73.s0__text", "type": "Sentence", "text": [ "RAD51, RAD54, RAD55 and RAD57 are all required to facilitate strand invasion into otherwise inaccessible donor sequences." ], "offsets": [ [ 0, 121 ] ] } ]

[ { "id": "BioInfer.d73.s0.e0", "type": "Gene/protein/RNA", "text": [ "RAD51" ], "offsets": [ [ 0, 5 ] ], "normalized": [] }, { "id": "BioInfer.d73.s0.e1", "type": "Gene/protein/RNA", "text": [ "RAD55" ], "offsets": [ [ 14, 19 ] ], "normalized": [] }, { "id": "BioInfer.d73.s0.e2", "type": "Gene/protein/RNA", "text": [ "RAD54" ], "offsets": [ [ 7, 12 ] ], "normalized": [] }, { "id": "BioInfer.d73.s0.e3", "type": "Gene/protein/RNA", "text": [ "RAD57" ], "offsets": [ [ 24, 29 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d73.s1__text", "type": "Sentence", "text": [ "RAD51, RAD54, RAD55 and RAD57 are still required when the same transcribed donor is on the chromosome." ], "offsets": [ [ 0, 102 ] ] } ]

[ { "id": "BioInfer.d73.s1.e0", "type": "Gene/protein/RNA", "text": [ "RAD55" ], "offsets": [ [ 14, 19 ] ], "normalized": [] }, { "id": "BioInfer.d73.s1.e1", "type": "Gene/protein/RNA", "text": [ "RAD51" ], "offsets": [ [ 0, 5 ] ], "normalized": [] }, { "id": "BioInfer.d73.s1.e2", "type": "Gene/protein/RNA", "text": [ "RAD57" ], "offsets": [ [ 24, 29 ] ], "normalized": [] }, { "id": "BioInfer.d73.s1.e3", "type": "Gene/protein/RNA", "text": [ "RAD54" ], "offsets": [ [ 7, 12 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d73.s2__text", "type": "Sentence", "text": [ "Here we use physical monitoring of DNA to show that MAT switching is completely blocked at an early step in recombination in strains deleted for the DNA repair genes RAD51, RAD52, RAD54, RAD55 or RAD57." ], "offsets": [ [ 0, 202 ] ] } ]

[ { "id": "BioInfer.d73.s2.e0", "type": "Gene/protein/RNA", "text": [ "RAD55" ], "offsets": [ [ 187, 192 ] ], "normalized": [] }, { "id": "BioInfer.d73.s2.e1", "type": "Gene/protein/RNA", "text": [ "RAD52" ], "offsets": [ [ 173, 178 ] ], "normalized": [] }, { "id": "BioInfer.d73.s2.e2", "type": "Gene/protein/RNA", "text": [ "RAD57" ], "offsets": [ [ 196, 201 ] ], "normalized": [] }, { "id": "BioInfer.d73.s2.e3", "type": "Gene/protein/RNA", "text": [ "RAD51" ], "offsets": [ [ 166, 171 ] ], "normalized": [] }, { "id": "BioInfer.d73.s2.e4", "type": "Gene/protein/RNA", "text": [ "RAD54" ], "offsets": [ [ 180, 185 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d75.s0__text", "type": "Sentence", "text": [ "A reconstitution is described that requires not only the growth factor, its receptor with tyrosine kinase activity, and the soluble phospholipase C-gamma 1, but also the small soluble actin-binding protein profilin." ], "offsets": [ [ 0, 215 ] ] } ]

[ { "id": "BioInfer.d75.s0.e0", "type": "Gene/protein/RNA", "text": [ "phospholipase C-gamma 1" ], "offsets": [ [ 132, 155 ] ], "normalized": [] }, { "id": "BioInfer.d75.s0.e1", "type": "Protein_family_or_group", "text": [ "actin-binding protein" ], "offsets": [ [ 184, 205 ] ], "normalized": [] }, { "id": "BioInfer.d75.s0.e2", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 206, 214 ] ], "normalized": [] }, { "id": "BioInfer.d75.s0.e3", "type": "Gene/protein/RNA", "text": [ "tyrosine kinase" ], "offsets": [ [ 90, 105 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d75.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d75.s0.e1", "arg2_id": "BioInfer.d75.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d76.s0__text", "type": "Sentence", "text": [ "Armadillo (Arm) repeat 10 to the COOH terminus of beta-catenin is involved in binding to CBP, whereas beta-catenin interacts directly with the CREB-binding domain of CBP." ], "offsets": [ [ 0, 170 ] ] } ]

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[ { "id": "BioInfer.d77.s0__text", "type": "Sentence", "text": [ "Arp2/3 complex from Acanthamoeba binds profilin and cross-links actin filaments." ], "offsets": [ [ 0, 80 ] ] } ]

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[ { "id": "BioInfer.d77.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d77.s0.e0", "arg2_id": "BioInfer.d77.s0.e1", "normalized": [] }, { "id": "BioInfer.d77.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d77.s0.e0", "arg2_id": "BioInfer.d77.s0.e2", "normalized": [] }, { "id": "BioInfer.d77.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d77.s0.e1", "arg2_id": "BioInfer.d77.s0.e2", "normalized": [] }, { "id": "BioInfer.d77.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d77.s0.e1", "arg2_id": "BioInfer.d77.s0.e3", "normalized": [] }, { "id": "BioInfer.d77.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d77.s0.e2", "arg2_id": "BioInfer.d77.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d77.s1__text", "type": "Sentence", "text": [ "By analytical ultracentrifugation, rhodamine-labeled profilin binds Arp2/3 complex with a Kd of 7 microM, an affinity intermediate between the low affinity of profilin for barbed ends of actin filaments and its high affinity for actin monomers." ], "offsets": [ [ 0, 244 ] ] } ]

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[ { "id": "BioInfer.d77.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d77.s1.e0", "arg2_id": "BioInfer.d77.s1.e1", "normalized": [] }, { "id": "BioInfer.d77.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d77.s1.e1", "arg2_id": "BioInfer.d77.s1.e4", "normalized": [] }, { "id": "BioInfer.d77.s1.i2", "type": "PPI", "arg1_id": "BioInfer.d77.s1.e2", "arg2_id": "BioInfer.d77.s1.e3", "normalized": [] }, { "id": "BioInfer.d77.s1.i3", "type": "PPI", "arg1_id": "BioInfer.d77.s1.e2", "arg2_id": "BioInfer.d77.s1.e5", "normalized": [] }, { "id": "BioInfer.d77.s1.i4", "type": "PPI", "arg1_id": "BioInfer.d77.s1.e3", "arg2_id": "BioInfer.d77.s1.e5", "normalized": [] } ]

[ { "id": "BioInfer.d77.s2__text", "type": "Sentence", "text": [ "Here we show that the Arp2 subunit of the complex can be chemically cross-linked to the actin-binding site of profilin." ], "offsets": [ [ 0, 119 ] ] } ]

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[ { "id": "BioInfer.d77.s2.i0", "type": "PPI", "arg1_id": "BioInfer.d77.s2.e0", "arg2_id": "BioInfer.d77.s2.e2", "normalized": [] }, { "id": "BioInfer.d77.s2.i1", "type": "PPI", "arg1_id": "BioInfer.d77.s2.e1", "arg2_id": "BioInfer.d77.s2.e2", "normalized": [] } ]

[ { "id": "BioInfer.d78.s0__text", "type": "Sentence", "text": [ "As a nuclear transport signal sequence exists in cofilin and ADF but not in actin, ADF and/or cofilin may be responsible for the nuclear import of actin in myogenic cells under certain conditions." ], "offsets": [ [ 0, 196 ] ] } ]

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[ { "id": "BioInfer.d78.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d78.s0.e0", "arg2_id": "BioInfer.d78.s0.e3", "normalized": [] }, { "id": "BioInfer.d78.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d78.s0.e3", "arg2_id": "BioInfer.d78.s0.e4", "normalized": [] } ]

[ { "id": "BioInfer.d78.s1__text", "type": "Sentence", "text": [ "Immunofluorescence microscopy revealed that two actin-binding proteins of low molecular weight with different functional activity, ADF and cofilin, are transported into nuclei of cultured myogenic cells to form rod structures there together with actin, when the cells were incubated in medium containing dimethylsulfoxide." ], "offsets": [ [ 0, 322 ] ] } ]

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[ { "id": "BioInfer.d78.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d78.s1.e0", "arg2_id": "BioInfer.d78.s1.e2", "normalized": [] }, { "id": "BioInfer.d78.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d78.s1.e0", "arg2_id": "BioInfer.d78.s1.e3", "normalized": [] }, { "id": "BioInfer.d78.s1.i2", "type": "PPI", "arg1_id": "BioInfer.d78.s1.e1", "arg2_id": "BioInfer.d78.s1.e2", "normalized": [] }, { "id": "BioInfer.d78.s1.i3", "type": "PPI", "arg1_id": "BioInfer.d78.s1.e1", "arg2_id": "BioInfer.d78.s1.e3", "normalized": [] } ]

[ { "id": "BioInfer.d78.s2__text", "type": "Sentence", "text": [ "In most cases, ADF and cofilin colocalized in the same nuclear actin rods, but ADF appeared to predominate in mononucleated cells, while cofilin was present in multinucleated myotubes." ], "offsets": [ [ 0, 184 ] ] } ]

[ { "id": "BioInfer.d78.s2.e0", "type": "Gene/protein/RNA", "text": [ "cofilin" ], "offsets": [ [ 137, 144 ] ], "normalized": [] }, { "id": "BioInfer.d78.s2.e1", "type": "Individual_protein", "text": [ "ADF" ], "offsets": [ [ 15, 18 ] ], "normalized": [] }, { "id": "BioInfer.d78.s2.e2", "type": "Gene/protein/RNA", "text": [ "ADF" ], "offsets": [ [ 79, 82 ] ], "normalized": [] }, { "id": "BioInfer.d78.s2.e3", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 63, 68 ] ], "normalized": [] }, { "id": "BioInfer.d78.s2.e4", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 23, 30 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d78.s2.i0", "type": "PPI", "arg1_id": "BioInfer.d78.s2.e1", "arg2_id": "BioInfer.d78.s2.e3", "normalized": [] }, { "id": "BioInfer.d78.s2.i1", "type": "PPI", "arg1_id": "BioInfer.d78.s2.e1", "arg2_id": "BioInfer.d78.s2.e4", "normalized": [] }, { "id": "BioInfer.d78.s2.i2", "type": "PPI", "arg1_id": "BioInfer.d78.s2.e3", "arg2_id": "BioInfer.d78.s2.e4", "normalized": [] } ]

[ { "id": "BioInfer.d79.s0__text", "type": "Sentence", "text": [ "A series of truncations was carried out at the C terminus of profilin, a region that has been implicated in actin binding." ], "offsets": [ [ 0, 122 ] ] } ]

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[ { "id": "BioInfer.d79.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d79.s0.e0", "arg2_id": "BioInfer.d79.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d79.s1__text", "type": "Sentence", "text": [ "Since our earlier studies of Acanthamoeba profilins suggested the importance of PIP2 binding for suppression, we conclude that both activities are implicated and that an interplay between PIP2 binding and actin binding may be important for profilin function." ], "offsets": [ [ 0, 258 ] ] } ]

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[ { "id": "BioInfer.d79.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d79.s1.e0", "arg2_id": "BioInfer.d79.s1.e1", "normalized": [] } ]

[ { "id": "BioInfer.d81.s0__text", "type": "Sentence", "text": [ "As expected from immunofluorescence experiments, Abp1p, cofilin, and actin colocalized in immuno-EM to the dense patchlike structures but not to the cables." ], "offsets": [ [ 0, 156 ] ] } ]

[ { "id": "BioInfer.d81.s0.e0", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 56, 63 ] ], "normalized": [] }, { "id": "BioInfer.d81.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 69, 74 ] ], "normalized": [] }, { "id": "BioInfer.d81.s0.e2", "type": "Individual_protein", "text": [ "Abp1p" ], "offsets": [ [ 49, 54 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d81.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d81.s0.e0", "arg2_id": "BioInfer.d81.s0.e1", "normalized": [] }, { "id": "BioInfer.d81.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d81.s0.e0", "arg2_id": "BioInfer.d81.s0.e2", "normalized": [] }, { "id": "BioInfer.d81.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d81.s0.e1", "arg2_id": "BioInfer.d81.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d81.s1__text", "type": "Sentence", "text": [ "Immuno-EM double-labeling experiments were conducted with antibodies to actin together with antibodies to the actin binding proteins Abp1p and cofilin." ], "offsets": [ [ 0, 151 ] ] } ]

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[ { "id": "BioInfer.d81.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d81.s1.e0", "arg2_id": "BioInfer.d81.s1.e1", "normalized": [] }, { "id": "BioInfer.d81.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d81.s1.e1", "arg2_id": "BioInfer.d81.s1.e2", "normalized": [] } ]

[ { "id": "BioInfer.d82.s0__text", "type": "Sentence", "text": [ "A similar phenotype was seen in testes treated with cytochalasin B and has been noted previously in mutants at the twinstar locus, a gene that encodes a Drosophila member of the cofilin/ADF family of actin-severing proteins." ], "offsets": [ [ 0, 224 ] ] } ]

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[ { "id": "BioInfer.d82.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d82.s0.e0", "arg2_id": "BioInfer.d82.s0.e1", "normalized": [] }, { "id": "BioInfer.d82.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d82.s0.e1", "arg2_id": "BioInfer.d82.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d83.s0__text", "type": "Sentence", "text": [ "As previous studies indicated that the RVS161 and RVS167 gene products of Saccharomyces cerevisiae seem to be involved in the same cellular function, we considered the possibility of a complex between the proteins encoded by these two genes." ], "offsets": [ [ 0, 241 ] ] } ]

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[ { "id": "BioInfer.d83.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d83.s0.e0", "arg2_id": "BioInfer.d83.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d84.s0__text", "type": "Sentence", "text": [ "As shown by in situ hybridization with cloned probes and analysis of in vitro translation products, M. occulta embryos do not accumulate high levels of alpha actin or myosin heavy chain mRNA." ], "offsets": [ [ 0, 191 ] ] } ]

[ { "id": "BioInfer.d84.s0.e0", "type": "Gene/protein/RNA", "text": [ "myosin heavy chain" ], "offsets": [ [ 167, 185 ] ], "normalized": [] }, { "id": "BioInfer.d84.s0.e1", "type": "Gene/protein/RNA", "text": [ "alpha actin" ], "offsets": [ [ 152, 163 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d84.s1__text", "type": "Sentence", "text": [ "In contrast, alpha actin and myosin heavy chain mRNA accumulation was not enhanced in hybrid embryos." ], "offsets": [ [ 0, 101 ] ] } ]

[ { "id": "BioInfer.d84.s1.e0", "type": "Gene/protein/RNA", "text": [ "myosin heavy chain" ], "offsets": [ [ 29, 47 ] ], "normalized": [] }, { "id": "BioInfer.d84.s1.e1", "type": "Gene/protein/RNA", "text": [ "alpha actin" ], "offsets": [ [ 13, 24 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d85.s0__text", "type": "Sentence", "text": [ "Associations of UBE2I with RAD52, UBL1, p53, and RAD51 proteins in a yeast two-hybrid system." ], "offsets": [ [ 0, 93 ] ] } ]

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[ { "id": "BioInfer.d85.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d85.s0.e0", "arg2_id": "BioInfer.d85.s0.e3", "normalized": [] }, { "id": "BioInfer.d85.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d85.s0.e1", "arg2_id": "BioInfer.d85.s0.e3", "normalized": [] }, { "id": "BioInfer.d85.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d85.s0.e2", "arg2_id": "BioInfer.d85.s0.e3", "normalized": [] }, { "id": "BioInfer.d85.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d85.s0.e3", "arg2_id": "BioInfer.d85.s0.e4", "normalized": [] } ]

[ { "id": "BioInfer.d87.s0__text", "type": "Sentence", "text": [ "A truncated beta-catenin disrupts the interaction between E-cadherin and alpha-catenin: a cause of loss of intercellular adhesiveness in human cancer cell lines." ], "offsets": [ [ 0, 161 ] ] } ]

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[ { "id": "BioInfer.d87.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d87.s0.e0", "arg2_id": "BioInfer.d87.s0.e1", "normalized": [] }, { "id": "BioInfer.d87.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d87.s0.e0", "arg2_id": "BioInfer.d87.s0.e2", "normalized": [] }, { "id": "BioInfer.d87.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d87.s0.e1", "arg2_id": "BioInfer.d87.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d87.s1__text", "type": "Sentence", "text": [ "However, the recombinant fusion protein containing wild-type beta-catenin precipitated alpha-catenin from these cells." ], "offsets": [ [ 0, 118 ] ] } ]

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[ { "id": "BioInfer.d87.s2__text", "type": "Sentence", "text": [ "These results suggest that the dysfunction of E-cadherin in these cell lines is due primarily to its failure to interact with alpha-catenin, and that this defect results from the mutation in beta-catenin." ], "offsets": [ [ 0, 204 ] ] } ]

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[ { "id": "BioInfer.d87.s2.i0", "type": "PPI", "arg1_id": "BioInfer.d87.s2.e0", "arg2_id": "BioInfer.d87.s2.e1", "normalized": [] }, { "id": "BioInfer.d87.s2.i1", "type": "PPI", "arg1_id": "BioInfer.d87.s2.e0", "arg2_id": "BioInfer.d87.s2.e2", "normalized": [] }, { "id": "BioInfer.d87.s2.i2", "type": "PPI", "arg1_id": "BioInfer.d87.s2.e1", "arg2_id": "BioInfer.d87.s2.e2", "normalized": [] } ]

[ { "id": "BioInfer.d87.s3__text", "type": "Sentence", "text": [ "Thus, it is most likely that the association between E-cadherin and alpha-catenin is mediated by beta-catenin, and that this process is blocked by NH2-terminal deletion in beta-catenin." ], "offsets": [ [ 0, 185 ] ] } ]

[ { "id": "BioInfer.d87.s3.e0", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 68, 81 ] ], "normalized": [] }, { "id": "BioInfer.d87.s3.e1", "type": "Individual_protein", "text": [ "E-cadherin" ], "offsets": [ [ 53, 63 ] ], "normalized": [] }, { "id": "BioInfer.d87.s3.e2", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 97, 109 ] ], "normalized": [] }, { "id": "BioInfer.d87.s3.e3", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 172, 184 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d87.s3.i0", "type": "PPI", "arg1_id": "BioInfer.d87.s3.e0", "arg2_id": "BioInfer.d87.s3.e1", "normalized": [] }, { "id": "BioInfer.d87.s3.i1", "type": "PPI", "arg1_id": "BioInfer.d87.s3.e0", "arg2_id": "BioInfer.d87.s3.e2", "normalized": [] }, { "id": "BioInfer.d87.s3.i2", "type": "PPI", "arg1_id": "BioInfer.d87.s3.e0", "arg2_id": "BioInfer.d87.s3.e3", "normalized": [] }, { "id": "BioInfer.d87.s3.i3", "type": "PPI", "arg1_id": "BioInfer.d87.s3.e1", "arg2_id": "BioInfer.d87.s3.e2", "normalized": [] }, { "id": "BioInfer.d87.s3.i4", "type": "PPI", "arg1_id": "BioInfer.d87.s3.e1", "arg2_id": "BioInfer.d87.s3.e3", "normalized": [] }, { "id": "BioInfer.d87.s3.i5", "type": "PPI", "arg1_id": "BioInfer.d87.s3.e2", "arg2_id": "BioInfer.d87.s3.e3", "normalized": [] } ]

[ { "id": "BioInfer.d87.s4__text", "type": "Sentence", "text": [ "While alpha-catenin has been demonstrated to be crucial for cadherin function, the role of beta-catenin is not yet fully understood." ], "offsets": [ [ 0, 132 ] ] } ]

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[ { "id": "BioInfer.d87.s4.i0", "type": "PPI", "arg1_id": "BioInfer.d87.s4.e0", "arg2_id": "BioInfer.d87.s4.e1", "normalized": [] } ]

[ { "id": "BioInfer.d88.s0__text", "type": "Sentence", "text": [ "At the light microscope level, brush cells can be identified by antibodies against the actin filament crosslinking proteins villin and fimbrin that not only stain the apical tuft of microvilli and their rootlets, but also label projections emanating from the basolateral surface of these cells." ], "offsets": [ [ 0, 294 ] ] } ]

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[ { "id": "BioInfer.d88.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d88.s0.e0", "arg2_id": "BioInfer.d88.s0.e2", "normalized": [] }, { "id": "BioInfer.d88.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d88.s0.e1", "arg2_id": "BioInfer.d88.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d89.s0__text", "type": "Sentence", "text": [ "BACKGROUND: Although profilin is believed to be an essential regulator of the actin cytoskeleton in most cells, its precise role in mammalian cells remains unknown." ], "offsets": [ [ 0, 164 ] ] } ]

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[ { "id": "BioInfer.d89.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d89.s0.e0", "arg2_id": "BioInfer.d89.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d91.s0__text", "type": "Sentence", "text": [ "BACKGROUND: p27(Kip1), a cyclin-dependent kinase inhibitor, negatively regulates the G1 phase progression of the cell cycle by binding to the cyclin E/cyclin-dependent kinase 2 complex." ], "offsets": [ [ 0, 185 ] ] } ]

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[]

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[ { "id": "BioInfer.d91.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d91.s0.e0", "arg2_id": "BioInfer.d91.s0.e1", "normalized": [] }, { "id": "BioInfer.d91.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d91.s0.e0", "arg2_id": "BioInfer.d91.s0.e3", "normalized": [] }, { "id": "BioInfer.d91.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d91.s0.e0", "arg2_id": "BioInfer.d91.s0.e4", "normalized": [] }, { "id": "BioInfer.d91.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d91.s0.e1", "arg2_id": "BioInfer.d91.s0.e2", "normalized": [] }, { "id": "BioInfer.d91.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d91.s0.e1", "arg2_id": "BioInfer.d91.s0.e3", "normalized": [] }, { "id": "BioInfer.d91.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d91.s0.e2", "arg2_id": "BioInfer.d91.s0.e3", "normalized": [] }, { "id": "BioInfer.d91.s0.i6", "type": "PPI", "arg1_id": "BioInfer.d91.s0.e2", "arg2_id": "BioInfer.d91.s0.e4", "normalized": [] } ]

[ { "id": "BioInfer.d92.s0__text", "type": "Sentence", "text": [ "Because beta-catenin is known to interact with alpha-catenin, which binds to actin, we generated a fusion molecule consisting of the ectodomain of E-cadherin and the actin binding site of alpha-catenin." ], "offsets": [ [ 0, 202 ] ] } ]

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[]

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[ { "id": "BioInfer.d92.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d92.s0.e0", "arg2_id": "BioInfer.d92.s0.e5", "normalized": [] }, { "id": "BioInfer.d92.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d92.s0.e1", "arg2_id": "BioInfer.d92.s0.e2", "normalized": [] }, { "id": "BioInfer.d92.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d92.s0.e2", "arg2_id": "BioInfer.d92.s0.e4", "normalized": [] }, { "id": "BioInfer.d92.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d92.s0.e3", "arg2_id": "BioInfer.d92.s0.e5", "normalized": [] } ]

[ { "id": "BioInfer.d94.s0__text", "type": "Sentence", "text": [ "Because both proteins exchange rapidly between actin molecules, low concentrations of profilin can overcome the inhibitory effects of high concentrations of thymosin beta 4 on the nucleotide exchange." ], "offsets": [ [ 0, 200 ] ] } ]

[ { "id": "BioInfer.d94.s0.e0", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 86, 94 ] ], "normalized": [] }, { "id": "BioInfer.d94.s0.e1", "type": "Individual_protein", "text": [ "thymosin beta 4" ], "offsets": [ [ 157, 172 ] ], "normalized": [] }, { "id": "BioInfer.d94.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 47, 52 ] ], "normalized": [] } ]

[]

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[ { "id": "BioInfer.d94.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d94.s0.e0", "arg2_id": "BioInfer.d94.s0.e1", "normalized": [] }, { "id": "BioInfer.d94.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d94.s0.e0", "arg2_id": "BioInfer.d94.s0.e2", "normalized": [] }, { "id": "BioInfer.d94.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d94.s0.e1", "arg2_id": "BioInfer.d94.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d95.s0__text", "type": "Sentence", "text": [ "Because other researchers have shown that the RAD51 and RAD52 proteins interact, RAD51 on a high copy number plasmid was tested and found to suppress the rad52-20 allele, but RAD 54, 55 and 57 did not suppress." ], "offsets": [ [ 0, 210 ] ] } ]

[ { "id": "BioInfer.d95.s0.e0", "type": "Gene", "text": [ "RAD51" ], "offsets": [ [ 81, 86 ] ], "normalized": [] }, { "id": "BioInfer.d95.s0.e1", "type": "Gene", "text": [ "RAD 54" ], "offsets": [ [ 175, 181 ] ], "normalized": [] }, { "id": "BioInfer.d95.s0.e2", "type": "Gene", "text": [ "RAD", "57" ], "offsets": [ [ 175, 178 ], [ 190, 192 ] ], "normalized": [] }, { "id": "BioInfer.d95.s0.e3", "type": "Gene", "text": [ "RAD", "55" ], "offsets": [ [ 175, 178 ], [ 183, 185 ] ], "normalized": [] }, { "id": "BioInfer.d95.s0.e4", "type": "Gene", "text": [ "RAD51" ], "offsets": [ [ 46, 51 ] ], "normalized": [] }, { "id": "BioInfer.d95.s0.e5", "type": "Gene", "text": [ "RAD52" ], "offsets": [ [ 56, 61 ] ], "normalized": [] }, { "id": "BioInfer.d95.s0.e6", "type": "Gene", "text": [ "rad52-20" ], "offsets": [ [ 154, 162 ] ], "normalized": [] } ]

[]

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[ { "id": "BioInfer.d95.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d95.s0.e0", "arg2_id": "BioInfer.d95.s0.e1", "normalized": [] }, { "id": "BioInfer.d95.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d95.s0.e0", "arg2_id": "BioInfer.d95.s0.e2", "normalized": [] }, { "id": "BioInfer.d95.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d95.s0.e0", "arg2_id": "BioInfer.d95.s0.e3", "normalized": [] }, { "id": "BioInfer.d95.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d95.s0.e0", "arg2_id": "BioInfer.d95.s0.e6", "normalized": [] }, { "id": "BioInfer.d95.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d95.s0.e4", "arg2_id": "BioInfer.d95.s0.e5", "normalized": [] } ]

[ { "id": "BioInfer.d96.s0__text", "type": "Sentence", "text": [ "Between day 1 and day 3 in culture, the specific synthetic activities of total proteins and of electrophoretically purified myosin heavy chain and actin ([14C] phenylalanine incorporation into protein, in disintegrations per minute per microgram protein) decreased (-19%,-32%, and -73%, respectively)." ], "offsets": [ [ 0, 301 ] ] } ]

[ { "id": "BioInfer.d96.s0.e0", "type": "Gene/protein/RNA", "text": [ "myosin heavy chain" ], "offsets": [ [ 124, 142 ] ], "normalized": [] }, { "id": "BioInfer.d96.s0.e1", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 147, 152 ] ], "normalized": [] } ]

[]

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[ { "id": "BioInfer.d97.s0__text", "type": "Sentence", "text": [ "Binding of talin to actin occurs at a maximal molar ratio of 1:3 as determined by fluorescencetitration under G-buffer conditions." ], "offsets": [ [ 0, 130 ] ] } ]

[ { "id": "BioInfer.d97.s0.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 20, 25 ] ], "normalized": [] }, { "id": "BioInfer.d97.s0.e1", "type": "Individual_protein", "text": [ "talin" ], "offsets": [ [ 11, 16 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d97.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d97.s0.e0", "arg2_id": "BioInfer.d97.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d97.s1__text", "type": "Sentence", "text": [ "Platelet talin binds to actin in vitro and hence is an actin binding protein." ], "offsets": [ [ 0, 77 ] ] } ]

[ { "id": "BioInfer.d97.s1.e0", "type": "Individual_protein", "text": [ "Platelet talin" ], "offsets": [ [ 0, 14 ] ], "normalized": [] }, { "id": "BioInfer.d97.s1.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 24, 29 ] ], "normalized": [] }, { "id": "BioInfer.d97.s1.e2", "type": "Protein_family_or_group", "text": [ "actin binding protein" ], "offsets": [ [ 55, 76 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d97.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d97.s1.e0", "arg2_id": "BioInfer.d97.s1.e1", "normalized": [] }, { "id": "BioInfer.d97.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d97.s1.e0", "arg2_id": "BioInfer.d97.s1.e2", "normalized": [] } ]

[ { "id": "BioInfer.d99.s0__text", "type": "Sentence", "text": [ "Biochemical analyses revealed a strong induction of VEGF-receptor-2 (flk-1/KDR) tyrosine-autophosphorylation by VEGF which was maximal after 5 minutes and was followed by receptor downregulation." ], "offsets": [ [ 0, 195 ] ] } ]

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[ { "id": "BioInfer.d99.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d99.s0.e0", "arg2_id": "BioInfer.d99.s0.e1", "normalized": [] }, { "id": "BioInfer.d99.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d99.s0.e1", "arg2_id": "BioInfer.d99.s0.e2", "normalized": [] }, { "id": "BioInfer.d99.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d99.s0.e1", "arg2_id": "BioInfer.d99.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d100.s0__text", "type": "Sentence", "text": [ "Biochemical complementation experiments also indicate that the PRP9 and PRP11 proteins interact." ], "offsets": [ [ 0, 96 ] ] } ]

[ { "id": "BioInfer.d100.s0.e0", "type": "Individual_protein", "text": [ "PRP11" ], "offsets": [ [ 72, 77 ] ], "normalized": [] }, { "id": "BioInfer.d100.s0.e1", "type": "Individual_protein", "text": [ "PRP9" ], "offsets": [ [ 63, 67 ] ], "normalized": [] } ]

[]

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[ { "id": "BioInfer.d100.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d100.s0.e0", "arg2_id": "BioInfer.d100.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d100.s1__text", "type": "Sentence", "text": [ "Four yeast spliceosomal proteins (PRP5, PRP9, PRP11, and PRP21) interact to promote U2 snRNP binding to pre-mRNA." ], "offsets": [ [ 0, 113 ] ] } ]

[ { "id": "BioInfer.d100.s1.e0", "type": "Individual_protein", "text": [ "PRP5" ], "offsets": [ [ 34, 38 ] ], "normalized": [] }, { "id": "BioInfer.d100.s1.e1", "type": "Individual_protein", "text": [ "U2 snRNP" ], "offsets": [ [ 84, 92 ] ], "normalized": [] }, { "id": "BioInfer.d100.s1.e2", "type": "Individual_protein", "text": [ "PRP21" ], "offsets": [ [ 57, 62 ] ], "normalized": [] }, { "id": "BioInfer.d100.s1.e3", "type": "Individual_protein", "text": [ "PRP9" ], "offsets": [ [ 40, 44 ] ], "normalized": [] }, { "id": "BioInfer.d100.s1.e4", "type": "Individual_protein", "text": [ "PRP11" ], "offsets": [ [ 46, 51 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d100.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d100.s1.e0", "arg2_id": "BioInfer.d100.s1.e1", "normalized": [] }, { "id": "BioInfer.d100.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d100.s1.e0", "arg2_id": "BioInfer.d100.s1.e2", "normalized": [] }, { "id": "BioInfer.d100.s1.i2", "type": "PPI", "arg1_id": "BioInfer.d100.s1.e0", "arg2_id": "BioInfer.d100.s1.e3", "normalized": [] }, { "id": "BioInfer.d100.s1.i3", "type": "PPI", "arg1_id": "BioInfer.d100.s1.e0", "arg2_id": "BioInfer.d100.s1.e4", "normalized": [] }, { "id": "BioInfer.d100.s1.i4", "type": "PPI", "arg1_id": "BioInfer.d100.s1.e1", "arg2_id": "BioInfer.d100.s1.e2", "normalized": [] }, { "id": "BioInfer.d100.s1.i5", "type": "PPI", "arg1_id": "BioInfer.d100.s1.e1", "arg2_id": "BioInfer.d100.s1.e3", "normalized": [] }, { "id": "BioInfer.d100.s1.i6", "type": "PPI", "arg1_id": "BioInfer.d100.s1.e1", "arg2_id": "BioInfer.d100.s1.e4", "normalized": [] }, { "id": "BioInfer.d100.s1.i7", "type": "PPI", "arg1_id": "BioInfer.d100.s1.e2", "arg2_id": "BioInfer.d100.s1.e3", "normalized": [] }, { "id": "BioInfer.d100.s1.i8", "type": "PPI", "arg1_id": "BioInfer.d100.s1.e2", "arg2_id": "BioInfer.d100.s1.e4", "normalized": [] }, { "id": "BioInfer.d100.s1.i9", "type": "PPI", "arg1_id": "BioInfer.d100.s1.e3", "arg2_id": "BioInfer.d100.s1.e4", "normalized": [] } ]

[ { "id": "BioInfer.d100.s2__text", "type": "Sentence", "text": [ "Here, we show that PRP5 (a DEAD box helicase-like protein), PRP9, and PRP11 are each required for the U2 snRNP to bind to the pre-spliceosome during spliceosome assembly in vitro." ], "offsets": [ [ 0, 179 ] ] } ]

[ { "id": "BioInfer.d100.s2.e0", "type": "Individual_protein", "text": [ "PRP9" ], "offsets": [ [ 60, 64 ] ], "normalized": [] }, { "id": "BioInfer.d100.s2.e1", "type": "Individual_protein", "text": [ "PRP5" ], "offsets": [ [ 19, 23 ] ], "normalized": [] }, { "id": "BioInfer.d100.s2.e2", "type": "Individual_protein", "text": [ "PRP11" ], "offsets": [ [ 70, 75 ] ], "normalized": [] }, { "id": "BioInfer.d100.s2.e3", "type": "Individual_protein", "text": [ "U2 snRNP" ], "offsets": [ [ 102, 110 ] ], "normalized": [] }, { "id": "BioInfer.d100.s2.e4", "type": "Individual_protein", "text": [ "DEAD box helicase" ], "offsets": [ [ 27, 44 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d100.s2.i0", "type": "PPI", "arg1_id": "BioInfer.d100.s2.e0", "arg2_id": "BioInfer.d100.s2.e3", "normalized": [] }, { "id": "BioInfer.d100.s2.i1", "type": "PPI", "arg1_id": "BioInfer.d100.s2.e1", "arg2_id": "BioInfer.d100.s2.e3", "normalized": [] }, { "id": "BioInfer.d100.s2.i2", "type": "PPI", "arg1_id": "BioInfer.d100.s2.e1", "arg2_id": "BioInfer.d100.s2.e4", "normalized": [] }, { "id": "BioInfer.d100.s2.i3", "type": "PPI", "arg1_id": "BioInfer.d100.s2.e2", "arg2_id": "BioInfer.d100.s2.e3", "normalized": [] } ]

[ { "id": "BioInfer.d102.s0__text", "type": "Sentence", "text": [ "Birch pollen profilin and actin can be copurified as a complex, and purified recombinant birch profilin can be used as an affinity matrix to obtain birch pollen actin." ], "offsets": [ [ 0, 167 ] ] } ]

[ { "id": "BioInfer.d102.s0.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 26, 31 ] ], "normalized": [] }, { "id": "BioInfer.d102.s0.e1", "type": "Individual_protein", "text": [ "pollen actin" ], "offsets": [ [ 154, 166 ] ], "normalized": [] }, { "id": "BioInfer.d102.s0.e2", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 95, 103 ] ], "normalized": [] }, { "id": "BioInfer.d102.s0.e3", "type": "Individual_protein", "text": [ "pollen profilin" ], "offsets": [ [ 6, 21 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d102.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d102.s0.e0", "arg2_id": "BioInfer.d102.s0.e3", "normalized": [] }, { "id": "BioInfer.d102.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d102.s0.e1", "arg2_id": "BioInfer.d102.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d102.s1__text", "type": "Sentence", "text": [ "In this study, profilin is identified as an actin-binding protein in higher plants which is present in monocot and dicot angiosperms." ], "offsets": [ [ 0, 133 ] ] } ]

[ { "id": "BioInfer.d102.s1.e0", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 15, 23 ] ], "normalized": [] }, { "id": "BioInfer.d102.s1.e1", "type": "Protein_family_or_group", "text": [ "actin-binding protein" ], "offsets": [ [ 44, 65 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d102.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d102.s1.e0", "arg2_id": "BioInfer.d102.s1.e1", "normalized": [] } ]

[ { "id": "BioInfer.d102.s2__text", "type": "Sentence", "text": [ "The binding of 125I-labeled recombinant birch pollen profilin to plant and animal actins can be blocked by profilin-specific antibodies that react with different epitopes of birch profilin." ], "offsets": [ [ 0, 189 ] ] } ]

[ { "id": "BioInfer.d102.s2.e0", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 107, 115 ] ], "normalized": [] }, { "id": "BioInfer.d102.s2.e1", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 180, 188 ] ], "normalized": [] }, { "id": "BioInfer.d102.s2.e2", "type": "Individual_protein", "text": [ "actins" ], "offsets": [ [ 82, 88 ] ], "normalized": [] }, { "id": "BioInfer.d102.s2.e3", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 53, 61 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d102.s2.i0", "type": "PPI", "arg1_id": "BioInfer.d102.s2.e0", "arg2_id": "BioInfer.d102.s2.e1", "normalized": [] }, { "id": "BioInfer.d102.s2.i1", "type": "PPI", "arg1_id": "BioInfer.d102.s2.e0", "arg2_id": "BioInfer.d102.s2.e2", "normalized": [] }, { "id": "BioInfer.d102.s2.i2", "type": "PPI", "arg1_id": "BioInfer.d102.s2.e0", "arg2_id": "BioInfer.d102.s2.e3", "normalized": [] }, { "id": "BioInfer.d102.s2.i3", "type": "PPI", "arg1_id": "BioInfer.d102.s2.e2", "arg2_id": "BioInfer.d102.s2.e3", "normalized": [] } ]

[ { "id": "BioInfer.d103.s0__text", "type": "Sentence", "text": [ "Bistratene A causes phosphorylation of talin and redistribution of actin microfilaments in fibroblasts: possible role for PKC-delta." ], "offsets": [ [ 0, 132 ] ] } ]

[ { "id": "BioInfer.d103.s0.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 67, 72 ] ], "normalized": [] }, { "id": "BioInfer.d103.s0.e1", "type": "Individual_protein", "text": [ "talin" ], "offsets": [ [ 39, 44 ] ], "normalized": [] }, { "id": "BioInfer.d103.s0.e2", "type": "Individual_protein", "text": [ "PKC-delta" ], "offsets": [ [ 122, 131 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d104.s0__text", "type": "Sentence", "text": [ "MSH3 appears to be more closely related to the mouse Rep-3 gene and other similar eukaryotic mutS homologues than to the yeast gene MSH2 and other mutS homologues that are involved in replication repair." ], "offsets": [ [ 0, 203 ] ] } ]

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[ { "id": "BioInfer.d105.s0__text", "type": "Sentence", "text": [ "Neuropilin-1 is also expressed in endothelial cells and shown to bind vascular endothelial growth factor (VEGF), a potent regulator for vasculogenesis and angiogenesis." ], "offsets": [ [ 0, 168 ] ] } ]

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[ { "id": "BioInfer.d106.s0__text", "type": "Sentence", "text": [ "Neuropilin-1 is expressed by endothelial and tumor cells as an isoform-specific receptor for vascular endothelial growth factor." ], "offsets": [ [ 0, 128 ] ] } ]

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[ { "id": "BioInfer.d107.s0__text", "type": "Sentence", "text": [ "Neuropilin-1 mediates collapsin-1/semaphorin III inhibition of endothelial cell motility: functional competition of collapsin-1 and vascular endothelial growth factor-165." ], "offsets": [ [ 0, 171 ] ] } ]

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[ { "id": "BioInfer.d108.s0__text", "type": "Sentence", "text": [ "Neuropilin 1 (NP-1) is a receptor for vascular endothelial growth factor (VEGF) 165 (VEGF165) and acts as a coreceptor that enhances VEGF165 function through tyrosine kinase VEGF receptor 2 (VEGFR-2)." ], "offsets": [ [ 0, 200 ] ] } ]

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[ { "id": "BioInfer.d111.s0__text", "type": "Sentence", "text": [ "Both pathway cells and superior tarsal smooth muscle cells expressed alpha-smooth muscle actin and smooth muscle myosin heavy chain throughout development." ], "offsets": [ [ 0, 155 ] ] } ]

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[ { "id": "BioInfer.d112.s0__text", "type": "Sentence", "text": [ "Both types of beads induced the recruitment of N-cadherin, beta-catenin, alpha-catenin and p120, by lateral mobilization of preexisting cell membrane complexes." ], "offsets": [ [ 0, 160 ] ] } ]

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[ { "id": "BioInfer.d113.s0__text", "type": "Sentence", "text": [ "Both tyrosine phosphorylation and association of beta-catenin with EGFR were inhibited by tyrphostin, a specific inhibitor of the EGFR tyrosine kinase, whereas dissociation of alpha-catenin from E-cadherin was not." ], "offsets": [ [ 0, 214 ] ] } ]

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[ { "id": "BioInfer.d113.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d113.s0.e0", "arg2_id": "BioInfer.d113.s0.e5", "normalized": [] }, { "id": "BioInfer.d113.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d113.s0.e1", "arg2_id": "BioInfer.d113.s0.e4", "normalized": [] }, { "id": "BioInfer.d113.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d113.s0.e2", "arg2_id": "BioInfer.d113.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d113.s1__text", "type": "Sentence", "text": [ "The results suggest that tyrosine phosphorylation of beta-catenin is achieved by EGFR upon tryptic digestion of cells and concurrent with but independent of dissociation of alpha-catenin from E-cadherin." ], "offsets": [ [ 0, 203 ] ] } ]

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[ { "id": "BioInfer.d113.s2__text", "type": "Sentence", "text": [ "Tyrosine phosphorylation of beta-catenin was concomitantly induced with association of beta-catenin with EGF receptor (EGFR) when quiescent cells at confluence were dissociated into single cells by tryptic digestion, being accompanied by dissociation of alpha-catenin from E-cadherin." ], "offsets": [ [ 0, 284 ] ] } ]

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[ { "id": "BioInfer.d114.s0__text", "type": "Sentence", "text": [ "RAD52 or RAD51 recombination-deficient yeast strains stabilize otherwise unstable YACs containing ribosomal DNA or the human color vision locus (Kohno et al., 1994)." ], "offsets": [ [ 0, 165 ] ] } ]

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[ { "id": "BioInfer.d115.s0__text", "type": "Sentence", "text": [ "SNF11, a new component of the yeast SNF-SWI complex that interacts with a conserved region of SNF2." ], "offsets": [ [ 0, 99 ] ] } ]

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[ { "id": "BioInfer.d115.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d115.s0.e0", "arg2_id": "BioInfer.d115.s0.e1", "normalized": [] }, { "id": "BioInfer.d115.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d115.s0.e0", "arg2_id": "BioInfer.d115.s0.e2", "normalized": [] }, { "id": "BioInfer.d115.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d115.s0.e0", "arg2_id": "BioInfer.d115.s0.e3", "normalized": [] }, { "id": "BioInfer.d115.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d115.s0.e1", "arg2_id": "BioInfer.d115.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d115.s1__text", "type": "Sentence", "text": [ "SNF11 interacts with SNF2 in vitro and copurifies with the SNF-SWI complex from yeast cells." ], "offsets": [ [ 0, 92 ] ] } ]

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[ { "id": "BioInfer.d116.s0__text", "type": "Sentence", "text": [ "Bud-site selection directs both cell polarity and the cytoskeletal orientation during budding and is determined by at least five genes: BUD1/RSR1, BUD2, BUD3, BUD4 and BUD5." ], "offsets": [ [ 0, 173 ] ] } ]

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