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[ { "id": "BioInfer.d373.s0__text", "type": "Sentence", "text": [ "In this actin clustering, profilin, a monomeric actin-binding protein that has been suggested to be involved in actin polymerization, was shown to be essential." ], "offsets": [ [ 0, 160 ] ] } ]

[ { "id": "BioInfer.d373.s0.e0", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 26, 34 ] ], "normalized": [] }, { "id": "BioInfer.d373.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 112, 117 ] ], "normalized": [] }, { "id": "BioInfer.d373.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 8, 13 ] ], "normalized": [] }, { "id": "BioInfer.d373.s0.e3", "type": "Protein_family_or_group", "text": [ "actin-binding protein" ], "offsets": [ [ 48, 69 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d373.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d373.s0.e0", "arg2_id": "BioInfer.d373.s0.e1", "normalized": [] }, { "id": "BioInfer.d373.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d373.s0.e0", "arg2_id": "BioInfer.d373.s0.e2", "normalized": [] }, { "id": "BioInfer.d373.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d373.s0.e0", "arg2_id": "BioInfer.d373.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d374.s0__text", "type": "Sentence", "text": [ "In this case, efficient repair does not require RAD1 and MSH2, consistent with our previous observations." ], "offsets": [ [ 0, 105 ] ] } ]

[ { "id": "BioInfer.d374.s0.e0", "type": "Gene/protein/RNA", "text": [ "MSH2" ], "offsets": [ [ 57, 61 ] ], "normalized": [] }, { "id": "BioInfer.d374.s0.e1", "type": "Gene/protein/RNA", "text": [ "RAD1" ], "offsets": [ [ 48, 52 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d375.s0__text", "type": "Sentence", "text": [ "In this model, profilin can bind both to actin monomers with a Kd of about 5 microM and to the barbed end of actin filaments with a Kd of about 50-100 microM." ], "offsets": [ [ 0, 158 ] ] } ]

[ { "id": "BioInfer.d375.s0.e0", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 15, 23 ] ], "normalized": [] }, { "id": "BioInfer.d375.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 41, 46 ] ], "normalized": [] }, { "id": "BioInfer.d375.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 109, 114 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d375.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d375.s0.e0", "arg2_id": "BioInfer.d375.s0.e1", "normalized": [] }, { "id": "BioInfer.d375.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d375.s0.e0", "arg2_id": "BioInfer.d375.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d375.s1__text", "type": "Sentence", "text": [ "Quantitative analysis of the effect of Acanthamoeba profilin on actin filament nucleation and elongation." ], "offsets": [ [ 0, 105 ] ] } ]

[ { "id": "BioInfer.d375.s1.e0", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 52, 60 ] ], "normalized": [] }, { "id": "BioInfer.d375.s1.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 64, 69 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d375.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d375.s1.e0", "arg2_id": "BioInfer.d375.s1.e1", "normalized": [] } ]

[ { "id": "BioInfer.d375.s2__text", "type": "Sentence", "text": [ "The current view of the mechanism of action of Acanthamoeba profilin is that it binds to actin monomers, forming a complex that cannot polymerize [Tobacman, L. S., & Korn, E. D. (1982) J. Biol. Chem. 257, 4166-4170; Tseng, P., & Pollard, T. D. (1982) J. Cell Biol. 94, 213-218; Tobacman, L. S., Brenner, S. L., & Korn, E. D. (1983) J. Biol. Chem. 258, 8806-8812]." ], "offsets": [ [ 0, 363 ] ] } ]

[ { "id": "BioInfer.d375.s2.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 89, 94 ] ], "normalized": [] }, { "id": "BioInfer.d375.s2.e1", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 60, 68 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d375.s2.i0", "type": "PPI", "arg1_id": "BioInfer.d375.s2.e0", "arg2_id": "BioInfer.d375.s2.e1", "normalized": [] } ]

[ { "id": "BioInfer.d375.s3__text", "type": "Sentence", "text": [ "This model includes two different Kd's--one for profilin bound to actin monomers and one for profilin bound to an actin molecule at the barbed end of a filament." ], "offsets": [ [ 0, 161 ] ] } ]

[ { "id": "BioInfer.d375.s3.e0", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 48, 56 ] ], "normalized": [] }, { "id": "BioInfer.d375.s3.e1", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 93, 101 ] ], "normalized": [] }, { "id": "BioInfer.d375.s3.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 66, 71 ] ], "normalized": [] }, { "id": "BioInfer.d375.s3.e3", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 114, 119 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d375.s3.i0", "type": "PPI", "arg1_id": "BioInfer.d375.s3.e0", "arg2_id": "BioInfer.d375.s3.e2", "normalized": [] }, { "id": "BioInfer.d375.s3.i1", "type": "PPI", "arg1_id": "BioInfer.d375.s3.e1", "arg2_id": "BioInfer.d375.s3.e3", "normalized": [] } ]

[ { "id": "BioInfer.d376.s0__text", "type": "Sentence", "text": [ "In this recombinant expression system, the dystrophin relatives, human dystrophin related protein (DRP or utrophin) and the 87K postsynaptic protein from Torpedo electric organ, also bind to translated beta 1-syntrophin." ], "offsets": [ [ 0, 220 ] ] } ]

[ { "id": "BioInfer.d376.s0.e0", "type": "Individual_protein", "text": [ "DRP" ], "offsets": [ [ 99, 102 ] ], "normalized": [] }, { "id": "BioInfer.d376.s0.e1", "type": "Individual_protein", "text": [ "dystrophin related protein" ], "offsets": [ [ 71, 97 ] ], "normalized": [] }, { "id": "BioInfer.d376.s0.e2", "type": "Individual_protein", "text": [ "87K postsynaptic protein" ], "offsets": [ [ 124, 148 ] ], "normalized": [] }, { "id": "BioInfer.d376.s0.e3", "type": "Individual_protein", "text": [ "utrophin" ], "offsets": [ [ 106, 114 ] ], "normalized": [] }, { "id": "BioInfer.d376.s0.e4", "type": "Individual_protein", "text": [ "beta 1-syntrophin" ], "offsets": [ [ 202, 219 ] ], "normalized": [] }, { "id": "BioInfer.d376.s0.e5", "type": "Individual_protein", "text": [ "dystrophin" ], "offsets": [ [ 43, 53 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d376.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d376.s0.e0", "arg2_id": "BioInfer.d376.s0.e4", "normalized": [] }, { "id": "BioInfer.d376.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d376.s0.e0", "arg2_id": "BioInfer.d376.s0.e5", "normalized": [] }, { "id": "BioInfer.d376.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d376.s0.e1", "arg2_id": "BioInfer.d376.s0.e4", "normalized": [] }, { "id": "BioInfer.d376.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d376.s0.e1", "arg2_id": "BioInfer.d376.s0.e5", "normalized": [] }, { "id": "BioInfer.d376.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d376.s0.e2", "arg2_id": "BioInfer.d376.s0.e4", "normalized": [] }, { "id": "BioInfer.d376.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d376.s0.e2", "arg2_id": "BioInfer.d376.s0.e5", "normalized": [] }, { "id": "BioInfer.d376.s0.i6", "type": "PPI", "arg1_id": "BioInfer.d376.s0.e3", "arg2_id": "BioInfer.d376.s0.e4", "normalized": [] }, { "id": "BioInfer.d376.s0.i7", "type": "PPI", "arg1_id": "BioInfer.d376.s0.e3", "arg2_id": "BioInfer.d376.s0.e5", "normalized": [] } ]

[ { "id": "BioInfer.d377.s0__text", "type": "Sentence", "text": [ "In this study, by immunoprecipitation and affinity chromatography it is shown that adenosine deaminase and A1 adenosine receptors interact in pig brain cortical membranes." ], "offsets": [ [ 0, 171 ] ] } ]

[ { "id": "BioInfer.d377.s0.e0", "type": "Individual_protein", "text": [ "A1 adenosine receptors" ], "offsets": [ [ 107, 129 ] ], "normalized": [] }, { "id": "BioInfer.d377.s0.e1", "type": "Individual_protein", "text": [ "adenosine deaminase" ], "offsets": [ [ 83, 102 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d377.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d377.s0.e0", "arg2_id": "BioInfer.d377.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d378.s0__text", "type": "Sentence", "text": [ "In this study, the expressions of smooth muscle-specific proteins (desmin, alpha-smooth muscle actin, basic calponin and the smooth muscle myosin heavy-chain isoforms of SM1 and SM2) in three parent and four cloned neuroblastoma cell lines, composed of S-type cells, were examined by indirect immunofluorescence, Western blot and/or by reverse transcription-polymerase chain reaction (RT-PCR)." ], "offsets": [ [ 0, 393 ] ] } ]

[ { "id": "BioInfer.d378.s0.e0", "type": "Gene/protein/RNA", "text": [ "basic calponin" ], "offsets": [ [ 102, 116 ] ], "normalized": [] }, { "id": "BioInfer.d378.s0.e1", "type": "Individual_protein", "text": [ "SM2" ], "offsets": [ [ 178, 181 ] ], "normalized": [] }, { "id": "BioInfer.d378.s0.e2", "type": "Gene/protein/RNA", "text": [ "desmin" ], "offsets": [ [ 67, 73 ] ], "normalized": [] }, { "id": "BioInfer.d378.s0.e3", "type": "Gene/protein/RNA", "text": [ "polymerase" ], "offsets": [ [ 358, 368 ] ], "normalized": [] }, { "id": "BioInfer.d378.s0.e4", "type": "Individual_protein", "text": [ "smooth muscle myosin heavy-chain" ], "offsets": [ [ 125, 157 ] ], "normalized": [] }, { "id": "BioInfer.d378.s0.e5", "type": "Gene/protein/RNA", "text": [ "alpha-smooth muscle actin" ], "offsets": [ [ 75, 100 ] ], "normalized": [] }, { "id": "BioInfer.d378.s0.e6", "type": "Individual_protein", "text": [ "SM1" ], "offsets": [ [ 170, 173 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d378.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d378.s0.e1", "arg2_id": "BioInfer.d378.s0.e4", "normalized": [] }, { "id": "BioInfer.d378.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d378.s0.e4", "arg2_id": "BioInfer.d378.s0.e6", "normalized": [] } ]

[ { "id": "BioInfer.d379.s0__text", "type": "Sentence", "text": [ "In this study the role of MSH2, MSH3, and MSH6 in mismatch repair has been examined by measuring the rate of accumulating mutations and mutation spectrum in strains containing different combinations of msh2, msh3, and msh6 mutations and by studying the physical interaction between the MSH2 protein and the MSH3 and MSH6 proteins." ], "offsets": [ [ 0, 330 ] ] } ]

[ { "id": "BioInfer.d379.s0.e0", "type": "Individual_protein", "text": [ "MSH2" ], "offsets": [ [ 286, 290 ] ], "normalized": [] }, { "id": "BioInfer.d379.s0.e1", "type": "Individual_protein", "text": [ "MSH6" ], "offsets": [ [ 316, 320 ] ], "normalized": [] }, { "id": "BioInfer.d379.s0.e2", "type": "Individual_protein", "text": [ "MSH3" ], "offsets": [ [ 307, 311 ] ], "normalized": [] }, { "id": "BioInfer.d379.s0.e3", "type": "Gene/protein/RNA", "text": [ "msh3" ], "offsets": [ [ 208, 212 ] ], "normalized": [] }, { "id": "BioInfer.d379.s0.e4", "type": "Gene/protein/RNA", "text": [ "msh2" ], "offsets": [ [ 202, 206 ] ], "normalized": [] }, { "id": "BioInfer.d379.s0.e5", "type": "Gene/protein/RNA", "text": [ "msh6" ], "offsets": [ [ 218, 222 ] ], "normalized": [] }, { "id": "BioInfer.d379.s0.e6", "type": "Gene/protein/RNA", "text": [ "MSH2" ], "offsets": [ [ 26, 30 ] ], "normalized": [] }, { "id": "BioInfer.d379.s0.e7", "type": "Gene/protein/RNA", "text": [ "MSH6" ], "offsets": [ [ 42, 46 ] ], "normalized": [] }, { "id": "BioInfer.d379.s0.e8", "type": "Gene/protein/RNA", "text": [ "MSH3" ], "offsets": [ [ 32, 36 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d379.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d379.s0.e0", "arg2_id": "BioInfer.d379.s0.e1", "normalized": [] }, { "id": "BioInfer.d379.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d379.s0.e0", "arg2_id": "BioInfer.d379.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d379.s1__text", "type": "Sentence", "text": [ "Redundancy of Saccharomyces cerevisiae MSH3 and MSH6 in MSH2-dependent mismatch repair." ], "offsets": [ [ 0, 87 ] ] } ]

[ { "id": "BioInfer.d379.s1.e0", "type": "Gene/protein/RNA", "text": [ "MSH2" ], "offsets": [ [ 56, 60 ] ], "normalized": [] }, { "id": "BioInfer.d379.s1.e1", "type": "Gene/protein/RNA", "text": [ "MSH3" ], "offsets": [ [ 39, 43 ] ], "normalized": [] }, { "id": "BioInfer.d379.s1.e2", "type": "Gene/protein/RNA", "text": [ "MSH6" ], "offsets": [ [ 48, 52 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d379.s2__text", "type": "Sentence", "text": [ "The results indicate that S. cerevisiae has two pathways of MSH2-dependent mismatch repair: one that recognized single-base mispairs and requires MSH2 and MSH6, and a second that recognizes insertion/deletion mispairs and requires a combination of either MSH2 and MSH6 or MSH2 and MSH3." ], "offsets": [ [ 0, 286 ] ] } ]

[ { "id": "BioInfer.d379.s2.e0", "type": "Gene", "text": [ "MSH2" ], "offsets": [ [ 272, 276 ] ], "normalized": [] }, { "id": "BioInfer.d379.s2.e1", "type": "Gene", "text": [ "MSH2" ], "offsets": [ [ 255, 259 ] ], "normalized": [] }, { "id": "BioInfer.d379.s2.e2", "type": "Gene", "text": [ "MSH6" ], "offsets": [ [ 264, 268 ] ], "normalized": [] }, { "id": "BioInfer.d379.s2.e3", "type": "Gene", "text": [ "MSH3" ], "offsets": [ [ 281, 285 ] ], "normalized": [] }, { "id": "BioInfer.d379.s2.e4", "type": "Gene", "text": [ "MSH2" ], "offsets": [ [ 146, 150 ] ], "normalized": [] }, { "id": "BioInfer.d379.s2.e5", "type": "Gene", "text": [ "MSH6" ], "offsets": [ [ 155, 159 ] ], "normalized": [] }, { "id": "BioInfer.d379.s2.e6", "type": "Gene", "text": [ "MSH2" ], "offsets": [ [ 60, 64 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d379.s2.i0", "type": "PPI", "arg1_id": "BioInfer.d379.s2.e0", "arg2_id": "BioInfer.d379.s2.e6", "normalized": [] }, { "id": "BioInfer.d379.s2.i1", "type": "PPI", "arg1_id": "BioInfer.d379.s2.e1", "arg2_id": "BioInfer.d379.s2.e6", "normalized": [] }, { "id": "BioInfer.d379.s2.i2", "type": "PPI", "arg1_id": "BioInfer.d379.s2.e2", "arg2_id": "BioInfer.d379.s2.e6", "normalized": [] }, { "id": "BioInfer.d379.s2.i3", "type": "PPI", "arg1_id": "BioInfer.d379.s2.e3", "arg2_id": "BioInfer.d379.s2.e6", "normalized": [] }, { "id": "BioInfer.d379.s2.i4", "type": "PPI", "arg1_id": "BioInfer.d379.s2.e4", "arg2_id": "BioInfer.d379.s2.e6", "normalized": [] }, { "id": "BioInfer.d379.s2.i5", "type": "PPI", "arg1_id": "BioInfer.d379.s2.e5", "arg2_id": "BioInfer.d379.s2.e6", "normalized": [] } ]

[ { "id": "BioInfer.d381.s0__text", "type": "Sentence", "text": [ "In this study we demonstrate that histone H3 and histone H4 synthesized in young (5 hr) conjugating Tetrahymena are deposited into micronuclei in acetylated forms." ], "offsets": [ [ 0, 163 ] ] } ]

[ { "id": "BioInfer.d381.s0.e0", "type": "Protein_family_or_group", "text": [ "histone" ], "offsets": [ [ 34, 41 ] ], "normalized": [] }, { "id": "BioInfer.d381.s0.e1", "type": "Individual_protein", "text": [ "H4" ], "offsets": [ [ 57, 59 ] ], "normalized": [] }, { "id": "BioInfer.d381.s0.e2", "type": "Individual_protein", "text": [ "H3" ], "offsets": [ [ 42, 44 ] ], "normalized": [] }, { "id": "BioInfer.d381.s0.e3", "type": "Protein_family_or_group", "text": [ "histone" ], "offsets": [ [ 49, 56 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d381.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d381.s0.e0", "arg2_id": "BioInfer.d381.s0.e2", "normalized": [] }, { "id": "BioInfer.d381.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d381.s0.e1", "arg2_id": "BioInfer.d381.s0.e2", "normalized": [] }, { "id": "BioInfer.d381.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d381.s0.e1", "arg2_id": "BioInfer.d381.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d384.s0__text", "type": "Sentence", "text": [ "In three of the cell lines with CTNNB1 mutations, complexes of beta-catenin with alpha-catenin and APC were detectable." ], "offsets": [ [ 0, 119 ] ] } ]

[ { "id": "BioInfer.d384.s0.e0", "type": "Individual_protein", "text": [ "APC" ], "offsets": [ [ 99, 102 ] ], "normalized": [] }, { "id": "BioInfer.d384.s0.e1", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 81, 94 ] ], "normalized": [] }, { "id": "BioInfer.d384.s0.e2", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 63, 75 ] ], "normalized": [] }, { "id": "BioInfer.d384.s0.e3", "type": "Gene/protein/RNA", "text": [ "CTNNB1" ], "offsets": [ [ 32, 38 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d384.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d384.s0.e0", "arg2_id": "BioInfer.d384.s0.e2", "normalized": [] }, { "id": "BioInfer.d384.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d384.s0.e1", "arg2_id": "BioInfer.d384.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d385.s0__text", "type": "Sentence", "text": [ "Introduction of high concentrations of profilin (estimated injected intracellular concentration 11-22 microM) into infected PtK2 cells causes a marked slowing of actin tail elongation and bacterial migration." ], "offsets": [ [ 0, 208 ] ] } ]

[ { "id": "BioInfer.d385.s0.e0", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 39, 47 ] ], "normalized": [] }, { "id": "BioInfer.d385.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 162, 167 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d385.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d385.s0.e0", "arg2_id": "BioInfer.d385.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d387.s0__text", "type": "Sentence", "text": [ "In vitro studies indicated that suramin completely blocked PDGF receptor activation or phosphorylation stimulated by PDGF-AB, inhibited activation of mitogen-activated protein kinase (ERK) kinases (MEK1/2) and ERK1/2, and abrogated transcription factor AP-1 DNA-binding activity." ], "offsets": [ [ 0, 279 ] ] } ]

[ { "id": "BioInfer.d387.s0.e0", "type": "Individual_protein", "text": [ "PDGF receptor" ], "offsets": [ [ 59, 72 ] ], "normalized": [] }, { "id": "BioInfer.d387.s0.e1", "type": "Individual_protein", "text": [ "MEK", "2" ], "offsets": [ [ 198, 201 ], [ 203, 204 ] ], "normalized": [] }, { "id": "BioInfer.d387.s0.e2", "type": "Gene/protein/RNA", "text": [ "AP-1" ], "offsets": [ [ 253, 257 ] ], "normalized": [] }, { "id": "BioInfer.d387.s0.e3", "type": "Gene/protein/RNA", "text": [ "ERK" ], "offsets": [ [ 184, 187 ] ], "normalized": [] }, { "id": "BioInfer.d387.s0.e4", "type": "Gene/protein/RNA", "text": [ "ERK", "2" ], "offsets": [ [ 210, 213 ], [ 215, 216 ] ], "normalized": [] }, { "id": "BioInfer.d387.s0.e5", "type": "Individual_protein", "text": [ "MEK1" ], "offsets": [ [ 198, 202 ] ], "normalized": [] }, { "id": "BioInfer.d387.s0.e6", "type": "Individual_protein", "text": [ "PDGF-AB" ], "offsets": [ [ 117, 124 ] ], "normalized": [] }, { "id": "BioInfer.d387.s0.e7", "type": "Gene/protein/RNA", "text": [ "ERK1" ], "offsets": [ [ 210, 214 ] ], "normalized": [] }, { "id": "BioInfer.d387.s0.e8", "type": "Protein_family_or_group", "text": [ "mitogen-activated protein kinase", "kinases" ], "offsets": [ [ 150, 182 ], [ 189, 196 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d388.s0__text", "type": "Sentence", "text": [ "In vivo importance of actin nucleotide exchange catalyzed by profilin." ], "offsets": [ [ 0, 70 ] ] } ]

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[ { "id": "BioInfer.d388.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d388.s0.e0", "arg2_id": "BioInfer.d388.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d388.s1__text", "type": "Sentence", "text": [ "act1-157, an actin mutant with an increased intrinsic rate of nucleotide exchange, suppressed defects in actin organization, cell growth, and fluid-phase endocytosis of pfy1-4, a profilin mutant defective in actin binding." ], "offsets": [ [ 0, 222 ] ] } ]

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[ { "id": "BioInfer.d388.s2__text", "type": "Sentence", "text": [ "The actin monomer-binding protein, profilin, influences the dynamics of actin filaments in vitro by suppressing nucleation, enhancing nucleotide exchange on actin, and promoting barbed-end assembly." ], "offsets": [ [ 0, 198 ] ] } ]

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[ { "id": "BioInfer.d388.s2.i0", "type": "PPI", "arg1_id": "BioInfer.d388.s2.e0", "arg2_id": "BioInfer.d388.s2.e3", "normalized": [] }, { "id": "BioInfer.d388.s2.i1", "type": "PPI", "arg1_id": "BioInfer.d388.s2.e1", "arg2_id": "BioInfer.d388.s2.e2", "normalized": [] }, { "id": "BioInfer.d388.s2.i2", "type": "PPI", "arg1_id": "BioInfer.d388.s2.e1", "arg2_id": "BioInfer.d388.s2.e3", "normalized": [] }, { "id": "BioInfer.d388.s2.i3", "type": "PPI", "arg1_id": "BioInfer.d388.s2.e2", "arg2_id": "BioInfer.d388.s2.e3", "normalized": [] } ]

[ { "id": "BioInfer.d388.s3__text", "type": "Sentence", "text": [ "To study profilin function, we extensively mutagenized the Saccharomyces cerevisiae profilin gene (PFY1) and examined the consequences of specific point mutations on growth and actin organization." ], "offsets": [ [ 0, 196 ] ] } ]

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[ { "id": "BioInfer.d389.s0__text", "type": "Sentence", "text": [ "Involvement of profilin in the actin-based motility of L. monocytogenes in cells and in cell-free extracts." ], "offsets": [ [ 0, 107 ] ] } ]

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[ { "id": "BioInfer.d389.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d389.s0.e0", "arg2_id": "BioInfer.d389.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d390.s0__text", "type": "Sentence", "text": [ "Isolation and characterization of death domain (TNF-RI, Fas, TRADD, FADD/MORT-1, RIP) and TRAF domain-containing proteins (TRAF-1, TRAF-2, TRAF-3) have partially bridged a large molecular gap within one of several signaling pathways which originate at the plasma membrane and terminate in the nucleus." ], "offsets": [ [ 0, 301 ] ] } ]

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[ { "id": "BioInfer.d391.s0__text", "type": "Sentence", "text": [ "Isolation of profilin from embryonic chicken skeletal muscle and evaluation of its interaction with different actin isoforms." ], "offsets": [ [ 0, 125 ] ] } ]

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[ { "id": "BioInfer.d391.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d391.s0.e0", "arg2_id": "BioInfer.d391.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d391.s1__text", "type": "Sentence", "text": [ "These results indicate that the assembly of cytoskeletal and sarcomeric actins is regulated differently by profilin in the developing skeletal muscle, and that the former may not be involved in myofibril assembly." ], "offsets": [ [ 0, 213 ] ] } ]

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[ { "id": "BioInfer.d391.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d391.s1.e0", "arg2_id": "BioInfer.d391.s1.e1", "normalized": [] }, { "id": "BioInfer.d391.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d391.s1.e0", "arg2_id": "BioInfer.d391.s1.e2", "normalized": [] } ]

[ { "id": "BioInfer.d392.s0__text", "type": "Sentence", "text": [ "Isolation of human delta-catenin and its binding specificity with presenilin 1." ], "offsets": [ [ 0, 79 ] ] } ]

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[ { "id": "BioInfer.d392.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d392.s0.e0", "arg2_id": "BioInfer.d392.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d393.s0__text", "type": "Sentence", "text": [ "Isolation of human skeletal muscle myosin heavy chain and actin for measurement of fractional synthesis rates." ], "offsets": [ [ 0, 110 ] ] } ]

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[ { "id": "BioInfer.d393.s1__text", "type": "Sentence", "text": [ "Using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), we have developed a simple method to isolate myosin heavy chain (MHC) and actin from small (60-80 mg) human skeletal muscle samples for the determination of their fractional synthesis rates." ], "offsets": [ [ 0, 266 ] ] } ]

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[ { "id": "BioInfer.d394.s0__text", "type": "Sentence", "text": [ "It is also possible that PtdIns-4,5-P2 has other roles, such as promoting the release of G actin from profilin or promoting the cross-linking of actin or its anchorage to the plasma membrane." ], "offsets": [ [ 0, 191 ] ] } ]

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[ { "id": "BioInfer.d394.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d394.s0.e0", "arg2_id": "BioInfer.d394.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d395.s0__text", "type": "Sentence", "text": [ "It is estimated that at optimal levels of transcription, every molecule of viral genomic RNA associates with approximately the following number of protein molecules: 30 molecules of L, 120 molecules of phosphoprotein P, and 60 molecules each of actin and profilin." ], "offsets": [ [ 0, 264 ] ] } ]

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[ { "id": "BioInfer.d395.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d395.s0.e2", "arg2_id": "BioInfer.d395.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d395.s1__text", "type": "Sentence", "text": [ "Native profilin, purified from extracts of lung epithelial cells by affinity binding to a poly-L-proline matrix, stimulated the actin-saturated RSV transcription by 2.5- to 3-fold." ], "offsets": [ [ 0, 180 ] ] } ]

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[ { "id": "BioInfer.d395.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d395.s1.e0", "arg2_id": "BioInfer.d395.s1.e1", "normalized": [] } ]

[ { "id": "BioInfer.d396.s0__text", "type": "Sentence", "text": [ "It reduced the rate of actin polymerization as reported in the cases of profilins from other organisms." ], "offsets": [ [ 0, 103 ] ] } ]

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[ { "id": "BioInfer.d397.s0__text", "type": "Sentence", "text": [ "It therefore appears that myosin heavy chain and actin multigene families are both expressed in a species specific fashion but are independently regulated within a species." ], "offsets": [ [ 0, 172 ] ] } ]

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[ { "id": "BioInfer.d397.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d397.s0.e0", "arg2_id": "BioInfer.d397.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d397.s1__text", "type": "Sentence", "text": [ "Regulation of myosin heavy chain and actin isogenes expression during cardiac growth." ], "offsets": [ [ 0, 85 ] ] } ]

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[ { "id": "BioInfer.d397.s2__text", "type": "Sentence", "text": [ "The cardiac ventricular myosin heavy chain phenotype is developmentally and hormonally regulated, but less is known concerning the actin phenotype." ], "offsets": [ [ 0, 147 ] ] } ]

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[ { "id": "BioInfer.d398.s0__text", "type": "Sentence", "text": [ "Kinetic measurements indicate that profilin binding to actin weakens the affinity of actin for nucleotides primarily due to an increased nucleotide dissociation rate constant, but the nucleotide association rate constant is also increased about 2-fold." ], "offsets": [ [ 0, 252 ] ] } ]

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[ { "id": "BioInfer.d398.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d398.s0.e0", "arg2_id": "BioInfer.d398.s0.e1", "normalized": [] }, { "id": "BioInfer.d398.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d398.s0.e0", "arg2_id": "BioInfer.d398.s0.e2", "normalized": [] }, { "id": "BioInfer.d398.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d398.s0.e1", "arg2_id": "BioInfer.d398.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d398.s1__text", "type": "Sentence", "text": [ "The data suggest that profilin binding to actin weakens nucleotide binding to actin by disrupting Mg(2+) coordination in the actin central cleft." ], "offsets": [ [ 0, 145 ] ] } ]

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[ { "id": "BioInfer.d398.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d398.s1.e0", "arg2_id": "BioInfer.d398.s1.e1", "normalized": [] }, { "id": "BioInfer.d398.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d398.s1.e0", "arg2_id": "BioInfer.d398.s1.e2", "normalized": [] }, { "id": "BioInfer.d398.s1.i2", "type": "PPI", "arg1_id": "BioInfer.d398.s1.e0", "arg2_id": "BioInfer.d398.s1.e3", "normalized": [] }, { "id": "BioInfer.d398.s1.i3", "type": "PPI", "arg1_id": "BioInfer.d398.s1.e1", "arg2_id": "BioInfer.d398.s1.e2", "normalized": [] }, { "id": "BioInfer.d398.s1.i4", "type": "PPI", "arg1_id": "BioInfer.d398.s1.e1", "arg2_id": "BioInfer.d398.s1.e3", "normalized": [] }, { "id": "BioInfer.d398.s1.i5", "type": "PPI", "arg1_id": "BioInfer.d398.s1.e2", "arg2_id": "BioInfer.d398.s1.e3", "normalized": [] } ]

[ { "id": "BioInfer.d399.s0__text", "type": "Sentence", "text": [ "Kinetic studies on the effect of yeast cofilin on yeast actin polymerization." ], "offsets": [ [ 0, 77 ] ] } ]

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[ { "id": "BioInfer.d399.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d399.s1.e0", "arg2_id": "BioInfer.d399.s1.e1", "normalized": [] } ]

[ { "id": "BioInfer.d400.s0__text", "type": "Sentence", "text": [ "Lack of detection in these preparations of a constituent that binds RBC alpha-spectrin antibody plus the presence of significant quantities of actin, further suggests that the principal membrane skeletal element is actin with perhaps smaller quantities of a 240-kd component, identified by others as the protein talin." ], "offsets": [ [ 0, 318 ] ] } ]

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[ { "id": "BioInfer.d401.s0__text", "type": "Sentence", "text": [ "Lethality of the srs2Delta rad54Delta and srs2Delta rdh54Delta double mutants can also be rescued by mutations in the DNA damage checkpoint functions RAD9, RAD17, RAD24, and MEC3, indicating that the srs2 rad54 and srs2 rdh54 mutant combinations lead to an intermediate that is sensed by these checkpoint functions." ], "offsets": [ [ 0, 315 ] ] } ]

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[ { "id": "BioInfer.d404.s0__text", "type": "Sentence", "text": [ "Like the spectrin alpha-chain, the major central part of the spectrin beta-chain is made up of repeat units of 106 amino-acids." ], "offsets": [ [ 0, 127 ] ] } ]

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[ { "id": "BioInfer.d405.s0__text", "type": "Sentence", "text": [ "LIM-kinase 1 (LIMK1) phosphorylates cofilin, an actin-depolymerizing factor, and regulates actin cytoskeletal reorganization." ], "offsets": [ [ 0, 125 ] ] } ]

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[ { "id": "BioInfer.d405.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d405.s0.e0", "arg2_id": "BioInfer.d405.s0.e3", "normalized": [] }, { "id": "BioInfer.d405.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d405.s0.e0", "arg2_id": "BioInfer.d405.s0.e4", "normalized": [] }, { "id": "BioInfer.d405.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d405.s0.e1", "arg2_id": "BioInfer.d405.s0.e2", "normalized": [] }, { "id": "BioInfer.d405.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d405.s0.e2", "arg2_id": "BioInfer.d405.s0.e3", "normalized": [] }, { "id": "BioInfer.d405.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d405.s0.e2", "arg2_id": "BioInfer.d405.s0.e4", "normalized": [] } ]

[ { "id": "BioInfer.d406.s0__text", "type": "Sentence", "text": [ "Linkage between cancer susceptibility and the candidate DNA mismatch repair genes MLH1, MSH2, MSH3, and MSH6 (GTBP) was investigated." ], "offsets": [ [ 0, 133 ] ] } ]

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[ { "id": "BioInfer.d407.s0__text", "type": "Sentence", "text": [ "Live dynamics of Dictyostelium cofilin suggests a role in remodeling actin latticework into bundles." ], "offsets": [ [ 0, 100 ] ] } ]

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[ { "id": "BioInfer.d407.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d407.s0.e0", "arg2_id": "BioInfer.d407.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d407.s1__text", "type": "Sentence", "text": [ "These results demonstrate that cofilin plays a crucial role in vivo in rapid remodeling of the cortical actin meshwork into bundles." ], "offsets": [ [ 0, 132 ] ] } ]

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[ { "id": "BioInfer.d407.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d407.s1.e0", "arg2_id": "BioInfer.d407.s1.e1", "normalized": [] } ]

[ { "id": "BioInfer.d408.s0__text", "type": "Sentence", "text": [ "Localization of VASP to the leading edge of a migrating cell can lead to local accumulation of profilin, which in turn can supply actin monomers to growing filament ends." ], "offsets": [ [ 0, 170 ] ] } ]

[ { "id": "BioInfer.d408.s0.e0", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 95, 103 ] ], "normalized": [] }, { "id": "BioInfer.d408.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 130, 135 ] ], "normalized": [] }, { "id": "BioInfer.d408.s0.e2", "type": "Individual_protein", "text": [ "VASP" ], "offsets": [ [ 16, 20 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d408.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d408.s0.e0", "arg2_id": "BioInfer.d408.s0.e1", "normalized": [] }, { "id": "BioInfer.d408.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d408.s0.e0", "arg2_id": "BioInfer.d408.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d409.s0__text", "type": "Sentence", "text": [ "Location of profilin at presynaptic sites in the cerebellar cortex; implication for the regulation of the actin-polymerization state during axonal elongation and synaptogenesis." ], "offsets": [ [ 0, 177 ] ] } ]

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[ { "id": "BioInfer.d410.s0__text", "type": "Sentence", "text": [ "Loss of memberanous expression of E-cadherin, alpha-catenin and beta-catenin was demonstrated in 52%, 85% and 40% of tumours respectively." ], "offsets": [ [ 0, 138 ] ] } ]

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[ { "id": "BioInfer.d410.s1__text", "type": "Sentence", "text": [ "There was a trend towards an association between advanced tumour stage and loss of membranous expression of alpha-catenin or beta-catenin, although these associations were not statistically significant." ], "offsets": [ [ 0, 202 ] ] } ]

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[ { "id": "BioInfer.d411.s0__text", "type": "Sentence", "text": [ "Mammalian homologues of two important yeast genes involved in DNA double-strand break repair and recombination, RAD51 and RAD54, have been isolated." ], "offsets": [ [ 0, 148 ] ] } ]

[ { "id": "BioInfer.d411.s0.e0", "type": "Gene/protein/RNA", "text": [ "RAD54" ], "offsets": [ [ 122, 127 ] ], "normalized": [] }, { "id": "BioInfer.d411.s0.e1", "type": "Gene/protein/RNA", "text": [ "RAD51" ], "offsets": [ [ 112, 117 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d412.s0__text", "type": "Sentence", "text": [ "Mammalian LIM-kinases (LIMKs) phosphorylate cofilin and induce actin cytoskeletal reorganization." ], "offsets": [ [ 0, 97 ] ] } ]

[ { "id": "BioInfer.d412.s0.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 63, 68 ] ], "normalized": [] }, { "id": "BioInfer.d412.s0.e1", "type": "Individual_protein", "text": [ "LIMKs" ], "offsets": [ [ 23, 28 ] ], "normalized": [] }, { "id": "BioInfer.d412.s0.e2", "type": "Individual_protein", "text": [ "LIM-kinases" ], "offsets": [ [ 10, 21 ] ], "normalized": [] }, { "id": "BioInfer.d412.s0.e3", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 44, 51 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d412.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d412.s0.e0", "arg2_id": "BioInfer.d412.s0.e1", "normalized": [] }, { "id": "BioInfer.d412.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d412.s0.e0", "arg2_id": "BioInfer.d412.s0.e2", "normalized": [] }, { "id": "BioInfer.d412.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d412.s0.e1", "arg2_id": "BioInfer.d412.s0.e3", "normalized": [] }, { "id": "BioInfer.d412.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d412.s0.e2", "arg2_id": "BioInfer.d412.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d413.s0__text", "type": "Sentence", "text": [ "MATERIALS AND METHODS: A mutation in the myosin heavy chain (Myh) predicted to interfere strongly with myosin's binding to actin was designed and used to create an animal model for HCM." ], "offsets": [ [ 0, 185 ] ] } ]

[ { "id": "BioInfer.d413.s0.e0", "type": "Individual_protein", "text": [ "myosin" ], "offsets": [ [ 103, 109 ] ], "normalized": [] }, { "id": "BioInfer.d413.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 123, 128 ] ], "normalized": [] }, { "id": "BioInfer.d413.s0.e2", "type": "Individual_protein", "text": [ "myosin heavy chain" ], "offsets": [ [ 41, 59 ] ], "normalized": [] }, { "id": "BioInfer.d413.s0.e3", "type": "Individual_protein", "text": [ "Myh" ], "offsets": [ [ 61, 64 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d413.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d413.s0.e0", "arg2_id": "BioInfer.d413.s0.e1", "normalized": [] }, { "id": "BioInfer.d413.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d413.s0.e0", "arg2_id": "BioInfer.d413.s0.e2", "normalized": [] }, { "id": "BioInfer.d413.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d413.s0.e0", "arg2_id": "BioInfer.d413.s0.e3", "normalized": [] }, { "id": "BioInfer.d413.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d413.s0.e1", "arg2_id": "BioInfer.d413.s0.e2", "normalized": [] }, { "id": "BioInfer.d413.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d413.s0.e1", "arg2_id": "BioInfer.d413.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d416.s0__text", "type": "Sentence", "text": [ "Mechanism of inhibition of proliferating cell nuclear antigen-dependent DNA synthesis by the cyclin-dependent kinase inhibitor p21." ], "offsets": [ [ 0, 131 ] ] } ]

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[ { "id": "BioInfer.d416.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d416.s0.e1", "arg2_id": "BioInfer.d416.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d417.s0__text", "type": "Sentence", "text": [ "Mechanism of regulation of actin polymerization by Physarum profilin." ], "offsets": [ [ 0, 69 ] ] } ]

[ { "id": "BioInfer.d417.s0.e0", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 60, 68 ] ], "normalized": [] }, { "id": "BioInfer.d417.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 27, 32 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d417.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d417.s0.e0", "arg2_id": "BioInfer.d417.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d417.s1__text", "type": "Sentence", "text": [ "The apparent critical concentration for polymerization of actin is increased by the addition of profilin." ], "offsets": [ [ 0, 105 ] ] } ]

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[ { "id": "BioInfer.d417.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d417.s1.e0", "arg2_id": "BioInfer.d417.s1.e1", "normalized": [] } ]

[ { "id": "BioInfer.d418.s0__text", "type": "Sentence", "text": [ "Membranous staining and concomitant cytoplasmic localization of E-cadherin, alpha-catenin and gamma-catenin were seen in one case with abnormal beta-catenin immunoreactivity." ], "offsets": [ [ 0, 174 ] ] } ]

[ { "id": "BioInfer.d418.s0.e0", "type": "Individual_protein", "text": [ "gamma-catenin" ], "offsets": [ [ 94, 107 ] ], "normalized": [] }, { "id": "BioInfer.d418.s0.e1", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 76, 89 ] ], "normalized": [] }, { "id": "BioInfer.d418.s0.e2", "type": "Individual_protein", "text": [ "E-cadherin" ], "offsets": [ [ 64, 74 ] ], "normalized": [] }, { "id": "BioInfer.d418.s0.e3", "type": "Gene/protein/RNA", "text": [ "beta-catenin" ], "offsets": [ [ 144, 156 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d418.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d418.s0.e0", "arg2_id": "BioInfer.d418.s0.e1", "normalized": [] }, { "id": "BioInfer.d418.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d418.s0.e0", "arg2_id": "BioInfer.d418.s0.e2", "normalized": [] }, { "id": "BioInfer.d418.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d418.s0.e1", "arg2_id": "BioInfer.d418.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d420.s0__text", "type": "Sentence", "text": [ "METHODS: Ileal and colonic biopsy specimens from 19 SpA patients with subclinical inflammatory gut lesions and from seven controls were stained with monoclonal antibodies against E-cadherin, beta-catenin and plakoglobin and a polyclonal antibody against alpha-catenin." ], "offsets": [ [ 0, 268 ] ] } ]

[ { "id": "BioInfer.d420.s0.e0", "type": "Gene/protein/RNA", "text": [ "beta-catenin" ], "offsets": [ [ 191, 203 ] ], "normalized": [] }, { "id": "BioInfer.d420.s0.e1", "type": "Gene/protein/RNA", "text": [ "alpha-catenin" ], "offsets": [ [ 254, 267 ] ], "normalized": [] }, { "id": "BioInfer.d420.s0.e2", "type": "Gene/protein/RNA", "text": [ "E-cadherin" ], "offsets": [ [ 179, 189 ] ], "normalized": [] }, { "id": "BioInfer.d420.s0.e3", "type": "Gene/protein/RNA", "text": [ "plakoglobin" ], "offsets": [ [ 208, 219 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d421.s0__text", "type": "Sentence", "text": [ "METHODS: Paraffin-embedded sections of five AVMs, CCMs, and control brain tissues were stained immunohistochemically with antibodies to alpha-smooth muscle actin (alpha-SMA), myosin heavy chain, and smoothelin, a novel marker for contractile VSMC phenotype." ], "offsets": [ [ 0, 257 ] ] } ]

[ { "id": "BioInfer.d421.s0.e0", "type": "Individual_protein", "text": [ "alpha-SMA" ], "offsets": [ [ 163, 172 ] ], "normalized": [] }, { "id": "BioInfer.d421.s0.e1", "type": "Gene/protein/RNA", "text": [ "myosin heavy chain" ], "offsets": [ [ 175, 193 ] ], "normalized": [] }, { "id": "BioInfer.d421.s0.e2", "type": "Gene/protein/RNA", "text": [ "smoothelin" ], "offsets": [ [ 199, 209 ] ], "normalized": [] }, { "id": "BioInfer.d421.s0.e3", "type": "Individual_protein", "text": [ "alpha-smooth muscle actin" ], "offsets": [ [ 136, 161 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d423.s0__text", "type": "Sentence", "text": [ "METHODS: We have performed a detailed study of the pattern of expression of myosin heavy chain (MHC), myosin light chain (MLC), troponin I (TnI) isoforms, connexin 43 (Cx43), desmin and alpha-smooth muscle actin (alpha-SMA), in the ventricular conduction system of normal and congenitally malformed mouse hearts (iv background) from embryonic day 14.5 to 19.5." ], "offsets": [ [ 0, 360 ] ] } ]

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[ { "id": "BioInfer.d425.s0__text", "type": "Sentence", "text": [ "Microinjection or stable expression of V12Ras into keratinocytes promotes the loss of E-cadherin and alpha-catenin and relocalization of beta-catenin to the cytoplasm and nucleus." ], "offsets": [ [ 0, 179 ] ] } ]

[ { "id": "BioInfer.d425.s0.e0", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 137, 149 ] ], "normalized": [] }, { "id": "BioInfer.d425.s0.e1", "type": "Individual_protein", "text": [ "E-cadherin" ], "offsets": [ [ 86, 96 ] ], "normalized": [] }, { "id": "BioInfer.d425.s0.e2", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 101, 114 ] ], "normalized": [] }, { "id": "BioInfer.d425.s0.e3", "type": "Individual_protein", "text": [ "V12Ras" ], "offsets": [ [ 39, 45 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d425.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d425.s0.e0", "arg2_id": "BioInfer.d425.s0.e3", "normalized": [] }, { "id": "BioInfer.d425.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d425.s0.e1", "arg2_id": "BioInfer.d425.s0.e3", "normalized": [] }, { "id": "BioInfer.d425.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d425.s0.e2", "arg2_id": "BioInfer.d425.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d427.s0__text", "type": "Sentence", "text": [ "MLL is fused in-frame to a different exon of CBP in two patients producing chimeric proteins containing the AT-hooks, methyltransferase homology domain, and transcriptional repression domain of MLL fused to the CREB binding domain or to the bromodomain of CBP." ], "offsets": [ [ 0, 260 ] ] } ]

[ { "id": "BioInfer.d427.s0.e0", "type": "Gene", "text": [ "MLL" ], "offsets": [ [ 0, 3 ] ], "normalized": [] }, { "id": "BioInfer.d427.s0.e1", "type": "Gene", "text": [ "CBP" ], "offsets": [ [ 45, 48 ] ], "normalized": [] }, { "id": "BioInfer.d427.s0.e2", "type": "Individual_protein", "text": [ "CBP" ], "offsets": [ [ 256, 259 ] ], "normalized": [] }, { "id": "BioInfer.d427.s0.e3", "type": "Individual_protein", "text": [ "CREB" ], "offsets": [ [ 211, 215 ] ], "normalized": [] }, { "id": "BioInfer.d427.s0.e4", "type": "Individual_protein", "text": [ "MLL" ], "offsets": [ [ 194, 197 ] ], "normalized": [] }, { "id": "BioInfer.d427.s0.e5", "type": "Individual_protein", "text": [ "methyltransferase" ], "offsets": [ [ 118, 135 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d427.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d427.s0.e2", "arg2_id": "BioInfer.d427.s0.e3", "normalized": [] }, { "id": "BioInfer.d427.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d427.s0.e4", "arg2_id": "BioInfer.d427.s0.e5", "normalized": [] } ]

[ { "id": "BioInfer.d428.s0__text", "type": "Sentence", "text": [ "Modifying preselected sites on proteins: the stretch of residues 633-642 of the myosin heavy chain is part of the actin-binding site." ], "offsets": [ [ 0, 133 ] ] } ]

[ { "id": "BioInfer.d428.s0.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 114, 119 ] ], "normalized": [] }, { "id": "BioInfer.d428.s0.e1", "type": "Individual_protein", "text": [ "myosin heavy chain" ], "offsets": [ [ 80, 98 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d428.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d428.s0.e0", "arg2_id": "BioInfer.d428.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d429.s0__text", "type": "Sentence", "text": [ "Molecular analysis of the cadherin-catenin complex elucidated the central role of beta-catenin in this adhesion complex, as it binds to the cytoplasmic domain of E-cadherin and to alpha-catenin." ], "offsets": [ [ 0, 194 ] ] } ]

[ { "id": "BioInfer.d429.s0.e0", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 82, 94 ] ], "normalized": [] }, { "id": "BioInfer.d429.s0.e1", "type": "Individual_protein", "text": [ "cadherin" ], "offsets": [ [ 26, 34 ] ], "normalized": [] }, { "id": "BioInfer.d429.s0.e2", "type": "Individual_protein", "text": [ "catenin" ], "offsets": [ [ 35, 42 ] ], "normalized": [] }, { "id": "BioInfer.d429.s0.e3", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 180, 193 ] ], "normalized": [] }, { "id": "BioInfer.d429.s0.e4", "type": "Individual_protein", "text": [ "E-cadherin" ], "offsets": [ [ 162, 172 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d429.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d429.s0.e0", "arg2_id": "BioInfer.d429.s0.e1", "normalized": [] }, { "id": "BioInfer.d429.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d429.s0.e0", "arg2_id": "BioInfer.d429.s0.e2", "normalized": [] }, { "id": "BioInfer.d429.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d429.s0.e0", "arg2_id": "BioInfer.d429.s0.e3", "normalized": [] }, { "id": "BioInfer.d429.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d429.s0.e0", "arg2_id": "BioInfer.d429.s0.e4", "normalized": [] }, { "id": "BioInfer.d429.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d429.s0.e1", "arg2_id": "BioInfer.d429.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d429.s1__text", "type": "Sentence", "text": [ "beta-Catenin may also function in signalling pathways, given its homology to the gene product of the Drosophila segment polarity gene armadillo, which is known to be involved in the wingless signalling cascade." ], "offsets": [ [ 0, 210 ] ] } ]

[ { "id": "BioInfer.d429.s1.e0", "type": "Gene", "text": [ "armadillo" ], "offsets": [ [ 134, 143 ] ], "normalized": [] }, { "id": "BioInfer.d429.s1.e1", "type": "Individual_protein", "text": [ "beta-Catenin" ], "offsets": [ [ 0, 12 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d429.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d429.s1.e0", "arg2_id": "BioInfer.d429.s1.e1", "normalized": [] } ]

[ { "id": "BioInfer.d430.s0__text", "type": "Sentence", "text": [ "Molecular cloning and primary structure analysis demonstrated that alpha-catenin is homologous to vinculin and the beta-catenin is homologous to human plakoglobin and the Drosophila gene product armadillo." ], "offsets": [ [ 0, 205 ] ] } ]

[ { "id": "BioInfer.d430.s0.e0", "type": "Individual_protein", "text": [ "plakoglobin" ], "offsets": [ [ 151, 162 ] ], "normalized": [] }, { "id": "BioInfer.d430.s0.e1", "type": "Individual_protein", "text": [ "armadillo" ], "offsets": [ [ 195, 204 ] ], "normalized": [] }, { "id": "BioInfer.d430.s0.e2", "type": "Individual_protein", "text": [ "vinculin" ], "offsets": [ [ 98, 106 ] ], "normalized": [] }, { "id": "BioInfer.d430.s0.e3", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 115, 127 ] ], "normalized": [] }, { "id": "BioInfer.d430.s0.e4", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 67, 80 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d430.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d430.s0.e0", "arg2_id": "BioInfer.d430.s0.e3", "normalized": [] }, { "id": "BioInfer.d430.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d430.s0.e1", "arg2_id": "BioInfer.d430.s0.e3", "normalized": [] }, { "id": "BioInfer.d430.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d430.s0.e2", "arg2_id": "BioInfer.d430.s0.e4", "normalized": [] } ]

[ { "id": "BioInfer.d430.s1__text", "type": "Sentence", "text": [ "One complex is composed of E-cadherin, alpha- and beta-catenin, the other of E-cadherin, alpha-catenin and plakoglobin." ], "offsets": [ [ 0, 119 ] ] } ]

[ { "id": "BioInfer.d430.s1.e0", "type": "Individual_protein", "text": [ "E-cadherin" ], "offsets": [ [ 77, 87 ] ], "normalized": [] }, { "id": "BioInfer.d430.s1.e1", "type": "Individual_protein", "text": [ "plakoglobin" ], "offsets": [ [ 107, 118 ] ], "normalized": [] }, { "id": "BioInfer.d430.s1.e2", "type": "Individual_protein", "text": [ "alpha-", "catenin" ], "offsets": [ [ 39, 45 ], [ 55, 62 ] ], "normalized": [] }, { "id": "BioInfer.d430.s1.e3", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 89, 102 ] ], "normalized": [] }, { "id": "BioInfer.d430.s1.e4", "type": "Individual_protein", "text": [ "E-cadherin" ], "offsets": [ [ 27, 37 ] ], "normalized": [] }, { "id": "BioInfer.d430.s1.e5", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 50, 62 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d430.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d430.s1.e0", "arg2_id": "BioInfer.d430.s1.e1", "normalized": [] }, { "id": "BioInfer.d430.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d430.s1.e0", "arg2_id": "BioInfer.d430.s1.e3", "normalized": [] }, { "id": "BioInfer.d430.s1.i2", "type": "PPI", "arg1_id": "BioInfer.d430.s1.e1", "arg2_id": "BioInfer.d430.s1.e3", "normalized": [] }, { "id": "BioInfer.d430.s1.i3", "type": "PPI", "arg1_id": "BioInfer.d430.s1.e2", "arg2_id": "BioInfer.d430.s1.e4", "normalized": [] }, { "id": "BioInfer.d430.s1.i4", "type": "PPI", "arg1_id": "BioInfer.d430.s1.e2", "arg2_id": "BioInfer.d430.s1.e5", "normalized": [] }, { "id": "BioInfer.d430.s1.i5", "type": "PPI", "arg1_id": "BioInfer.d430.s1.e4", "arg2_id": "BioInfer.d430.s1.e5", "normalized": [] } ]

[ { "id": "BioInfer.d431.s0__text", "type": "Sentence", "text": [ "[Molecular functions of cofilin which regulates reorganization of actin cytoskeleton]." ], "offsets": [ [ 0, 86 ] ] } ]

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[ { "id": "BioInfer.d431.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d431.s0.e0", "arg2_id": "BioInfer.d431.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d432.s0__text", "type": "Sentence", "text": [ "Molecules known to link actin filaments to membrane were also examined, including alpha-catenin, beta-catenin, plakoglobin, and zyxin, but none was identified at the host-parasite junction." ], "offsets": [ [ 0, 189 ] ] } ]

[ { "id": "BioInfer.d432.s0.e0", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 97, 109 ] ], "normalized": [] }, { "id": "BioInfer.d432.s0.e1", "type": "Individual_protein", "text": [ "plakoglobin" ], "offsets": [ [ 111, 122 ] ], "normalized": [] }, { "id": "BioInfer.d432.s0.e2", "type": "Individual_protein", "text": [ "zyxin" ], "offsets": [ [ 128, 133 ] ], "normalized": [] }, { "id": "BioInfer.d432.s0.e3", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 24, 29 ] ], "normalized": [] }, { "id": "BioInfer.d432.s0.e4", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 82, 95 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d432.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d432.s0.e0", "arg2_id": "BioInfer.d432.s0.e3", "normalized": [] }, { "id": "BioInfer.d432.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d432.s0.e1", "arg2_id": "BioInfer.d432.s0.e3", "normalized": [] }, { "id": "BioInfer.d432.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d432.s0.e2", "arg2_id": "BioInfer.d432.s0.e3", "normalized": [] }, { "id": "BioInfer.d432.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d432.s0.e3", "arg2_id": "BioInfer.d432.s0.e4", "normalized": [] } ]

[ { "id": "BioInfer.d432.s1__text", "type": "Sentence", "text": [ "Other actin-associated proteins, including vinculin, talin, and ezrin, are not present." ], "offsets": [ [ 0, 87 ] ] } ]

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[ { "id": "BioInfer.d432.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d432.s1.e0", "arg2_id": "BioInfer.d432.s1.e1", "normalized": [] }, { "id": "BioInfer.d432.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d432.s1.e1", "arg2_id": "BioInfer.d432.s1.e2", "normalized": [] }, { "id": "BioInfer.d432.s1.i2", "type": "PPI", "arg1_id": "BioInfer.d432.s1.e1", "arg2_id": "BioInfer.d432.s1.e3", "normalized": [] } ]

[ { "id": "BioInfer.d433.s0__text", "type": "Sentence", "text": [ "Monoclonal antibodies recognizing the N- and C-terminal regions of talin disrupt actin stress fibers when microinjected into human fibroblasts." ], "offsets": [ [ 0, 143 ] ] } ]

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[ { "id": "BioInfer.d433.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d433.s0.e0", "arg2_id": "BioInfer.d433.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d433.s1__text", "type": "Sentence", "text": [ "These results show that the C-terminal actin-binding site is distinct from the region recognized by the anti-functional antibody TD77, raising the possibility that it binds to a novel functionally important ligand-binding site in the talin molecule." ], "offsets": [ [ 0, 249 ] ] } ]

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[ { "id": "BioInfer.d433.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d433.s1.e0", "arg2_id": "BioInfer.d433.s1.e1", "normalized": [] }, { "id": "BioInfer.d433.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d433.s1.e0", "arg2_id": "BioInfer.d433.s1.e2", "normalized": [] } ]

[ { "id": "BioInfer.d433.s2__text", "type": "Sentence", "text": [ "To investigate the possibility that TD77 disrupts actin stress fibers by binding directly to the C-terminal actin binding site, additional talin fusion proteins were generated and analyzed for TD77 and actin binding." ], "offsets": [ [ 0, 216 ] ] } ]

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[ { "id": "BioInfer.d433.s2.i0", "type": "PPI", "arg1_id": "BioInfer.d433.s2.e0", "arg2_id": "BioInfer.d433.s2.e1", "normalized": [] }, { "id": "BioInfer.d433.s2.i1", "type": "PPI", "arg1_id": "BioInfer.d433.s2.e0", "arg2_id": "BioInfer.d433.s2.e2", "normalized": [] }, { "id": "BioInfer.d433.s2.i2", "type": "PPI", "arg1_id": "BioInfer.d433.s2.e0", "arg2_id": "BioInfer.d433.s2.e3", "normalized": [] }, { "id": "BioInfer.d433.s2.i3", "type": "PPI", "arg1_id": "BioInfer.d433.s2.e0", "arg2_id": "BioInfer.d433.s2.e4", "normalized": [] }, { "id": "BioInfer.d433.s2.i4", "type": "PPI", "arg1_id": "BioInfer.d433.s2.e0", "arg2_id": "BioInfer.d433.s2.e5", "normalized": [] }, { "id": "BioInfer.d433.s2.i5", "type": "PPI", "arg1_id": "BioInfer.d433.s2.e1", "arg2_id": "BioInfer.d433.s2.e5", "normalized": [] } ]

[ { "id": "BioInfer.d434.s0__text", "type": "Sentence", "text": [ "Monocytes and in vitro differentiated U937 cells induce focal loss in the staining of VE-cadherin, alpha-catenin, beta-catenin, and plakoglobin during transendothelial migration under physiological flow conditions." ], "offsets": [ [ 0, 214 ] ] } ]

[ { "id": "BioInfer.d434.s0.e0", "type": "Gene/protein/RNA", "text": [ "plakoglobin" ], "offsets": [ [ 132, 143 ] ], "normalized": [] }, { "id": "BioInfer.d434.s0.e1", "type": "Gene/protein/RNA", "text": [ "alpha-catenin" ], "offsets": [ [ 99, 112 ] ], "normalized": [] }, { "id": "BioInfer.d434.s0.e2", "type": "Gene/protein/RNA", "text": [ "beta-catenin" ], "offsets": [ [ 114, 126 ] ], "normalized": [] }, { "id": "BioInfer.d434.s0.e3", "type": "Gene/protein/RNA", "text": [ "VE-cadherin" ], "offsets": [ [ 86, 97 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d435.s0__text", "type": "Sentence", "text": [ "Moreover, talin, but not vinculin or tubulin, appears to co-localize with actin microfilaments in the membrane ruffles of NK cells that undergo cytoskeleton rearrangement following CD31 cross-linking." ], "offsets": [ [ 0, 200 ] ] } ]

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[ { "id": "BioInfer.d437.s0__text", "type": "Sentence", "text": [ "Moreover, in the presence of cofilin, rapid interconversion of monomeric and polymeric forms of actin can be induced by simply changing the pH of the medium." ], "offsets": [ [ 0, 157 ] ] } ]

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[ { "id": "BioInfer.d437.s1__text", "type": "Sentence", "text": [ "pH control of actin polymerization by cofilin." ], "offsets": [ [ 0, 46 ] ] } ]

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[ { "id": "BioInfer.d437.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d437.s1.e0", "arg2_id": "BioInfer.d437.s1.e1", "normalized": [] } ]

[ { "id": "BioInfer.d438.s0__text", "type": "Sentence", "text": [ "Moreover, the virus-encoded profilin homolog was not required for actin-associated events, including intracellular virus movement to the periphery of the cell, formation of specialized microvilli, or release of mature virions, as shown by electron microscopy and yields of infectious intra- and extracellular virus." ], "offsets": [ [ 0, 315 ] ] } ]

[ { "id": "BioInfer.d438.s0.e0", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 28, 36 ] ], "normalized": [] }, { "id": "BioInfer.d438.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 66, 71 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d440.s0__text", "type": "Sentence", "text": [ "Most previous studies have focused on profilin itself rather than its complex with actin." ], "offsets": [ [ 0, 89 ] ] } ]

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[ { "id": "BioInfer.d441.s0__text", "type": "Sentence", "text": [ "Motile areas of leech neurites are rich in microfilaments and two actin-binding proteins: gelsolin and profilin." ], "offsets": [ [ 0, 112 ] ] } ]

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[ { "id": "BioInfer.d441.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d441.s0.e0", "arg2_id": "BioInfer.d441.s0.e2", "normalized": [] }, { "id": "BioInfer.d441.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d441.s0.e1", "arg2_id": "BioInfer.d441.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d441.s1__text", "type": "Sentence", "text": [ "The colocalization of gelsolin and profilin in motile, microfilament-rich areas supports the hypothesis that they synergistically regulate the actin dynamics that underlie neurite growth." ], "offsets": [ [ 0, 187 ] ] } ]

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[ { "id": "BioInfer.d441.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d441.s1.e0", "arg2_id": "BioInfer.d441.s1.e1", "normalized": [] }, { "id": "BioInfer.d441.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d441.s1.e0", "arg2_id": "BioInfer.d441.s1.e2", "normalized": [] }, { "id": "BioInfer.d441.s1.i2", "type": "PPI", "arg1_id": "BioInfer.d441.s1.e1", "arg2_id": "BioInfer.d441.s1.e2", "normalized": [] } ]

[ { "id": "BioInfer.d442.s0__text", "type": "Sentence", "text": [ "Mutants of cdc3 and cdc8, which encode profilin and tropomyosin respectively, display disorganized actin patches in all cells." ], "offsets": [ [ 0, 126 ] ] } ]

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[ { "id": "BioInfer.d442.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d442.s0.e0", "arg2_id": "BioInfer.d442.s0.e3", "normalized": [] }, { "id": "BioInfer.d442.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d442.s0.e1", "arg2_id": "BioInfer.d442.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d443.s0__text", "type": "Sentence", "text": [ "Mutations in BUD3, BUD4, and AXL1 cause a and alpha cells to exhibit the bipolar pattern, indicating that these genes are necessary to specify the axial budding pattern (Chant, J., and I. Herskowitz. 1991. Cell. 65:1203-1212; Fujita, A., C. Oka, Y. Arikawa, T. Katagi, A. Tonouchi, S. Kuhara, and Y. Misumi. 1994. Nature (Lond.). 372:567-570)." ], "offsets": [ [ 0, 343 ] ] } ]

[ { "id": "BioInfer.d443.s0.e0", "type": "Gene/protein/RNA", "text": [ "BUD4" ], "offsets": [ [ 19, 23 ] ], "normalized": [] }, { "id": "BioInfer.d443.s0.e1", "type": "Gene/protein/RNA", "text": [ "AXL1" ], "offsets": [ [ 29, 33 ] ], "normalized": [] }, { "id": "BioInfer.d443.s0.e2", "type": "Gene/protein/RNA", "text": [ "BUD3" ], "offsets": [ [ 13, 17 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d444.s0__text", "type": "Sentence", "text": [ "Mutations in RVS161 and RVS167, the two yeast amphiphysin homologs, cause very similar growth phenotypes, a depolarized actin cytoskeleton, and a defect in the internalization step of endocytosis." ], "offsets": [ [ 0, 196 ] ] } ]

[ { "id": "BioInfer.d444.s0.e0", "type": "Individual_protein", "text": [ "RVS167" ], "offsets": [ [ 24, 30 ] ], "normalized": [] }, { "id": "BioInfer.d444.s0.e1", "type": "Individual_protein", "text": [ "amphiphysin" ], "offsets": [ [ 46, 57 ] ], "normalized": [] }, { "id": "BioInfer.d444.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 120, 125 ] ], "normalized": [] }, { "id": "BioInfer.d444.s0.e3", "type": "Individual_protein", "text": [ "RVS161" ], "offsets": [ [ 13, 19 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d444.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d444.s0.e0", "arg2_id": "BioInfer.d444.s0.e1", "normalized": [] }, { "id": "BioInfer.d444.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d444.s0.e0", "arg2_id": "BioInfer.d444.s0.e2", "normalized": [] }, { "id": "BioInfer.d444.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d444.s0.e1", "arg2_id": "BioInfer.d444.s0.e3", "normalized": [] }, { "id": "BioInfer.d444.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d444.s0.e2", "arg2_id": "BioInfer.d444.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d446.s0__text", "type": "Sentence", "text": [ "Mutations in Saccharomyces cerevisiae RFC5, DPB11, MEC1, DDC2 MEC3, RAD53, CHK1, PDS1, and DUN1 increased the rate of genome rearrangements up to 200-fold whereas mutations in RAD9, RAD17, RAD24, BUB3, and MAD3 had little effect." ], "offsets": [ [ 0, 229 ] ] } ]

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[ { "id": "BioInfer.d447.s0__text", "type": "Sentence", "text": [ "Mutations that alter putative RNA-binding residues of either HSH49 RRM are lethal in vivo, but do not prevent binding to CUS1 in vitro, suggesting that the predicted RNA-binding surfaces of HSH49 are not required for interaction with CUS1." ], "offsets": [ [ 0, 239 ] ] } ]

[ { "id": "BioInfer.d447.s0.e0", "type": "Individual_protein", "text": [ "CUS1" ], "offsets": [ [ 234, 238 ] ], "normalized": [] }, { "id": "BioInfer.d447.s0.e1", "type": "Individual_protein", "text": [ "HSH49" ], "offsets": [ [ 190, 195 ] ], "normalized": [] }, { "id": "BioInfer.d447.s0.e2", "type": "Individual_protein", "text": [ "CUS1" ], "offsets": [ [ 121, 125 ] ], "normalized": [] }, { "id": "BioInfer.d447.s0.e3", "type": "Individual_protein", "text": [ "HSH49" ], "offsets": [ [ 61, 66 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d447.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d447.s0.e0", "arg2_id": "BioInfer.d447.s0.e1", "normalized": [] }, { "id": "BioInfer.d447.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d447.s0.e2", "arg2_id": "BioInfer.d447.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d447.s1__text", "type": "Sentence", "text": [ "Recombinant HSH49 protein has a general RNA-binding activity that does not require CUS1." ], "offsets": [ [ 0, 88 ] ] } ]

[ { "id": "BioInfer.d447.s1.e0", "type": "Individual_protein", "text": [ "CUS1" ], "offsets": [ [ 83, 87 ] ], "normalized": [] }, { "id": "BioInfer.d447.s1.e1", "type": "Individual_protein", "text": [ "HSH49" ], "offsets": [ [ 12, 17 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d447.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d447.s1.e0", "arg2_id": "BioInfer.d447.s1.e1", "normalized": [] } ]

[ { "id": "BioInfer.d448.s0__text", "type": "Sentence", "text": [ "Myo2p shows homology to the head domains and the coiledcoil tail of the conventional type II myosin heavy chain and carries putative binding sites for ATP and actin." ], "offsets": [ [ 0, 165 ] ] } ]

[ { "id": "BioInfer.d448.s0.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 159, 164 ] ], "normalized": [] }, { "id": "BioInfer.d448.s0.e1", "type": "Individual_protein", "text": [ "Myo2p" ], "offsets": [ [ 0, 5 ] ], "normalized": [] }, { "id": "BioInfer.d448.s0.e2", "type": "Individual_protein", "text": [ "type II myosin heavy chain" ], "offsets": [ [ 85, 111 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d448.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d448.s0.e0", "arg2_id": "BioInfer.d448.s0.e1", "normalized": [] }, { "id": "BioInfer.d448.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d448.s0.e1", "arg2_id": "BioInfer.d448.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d449.s0__text", "type": "Sentence", "text": [ "Myogenin mRNAs were transiently expressed in forming myotubes." ], "offsets": [ [ 0, 62 ] ] } ]

[ { "id": "BioInfer.d449.s0.e0", "type": "Gene/protein/RNA", "text": [ "Myogenin" ], "offsets": [ [ 0, 8 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d449.s1__text", "type": "Sentence", "text": [ "alpha-Skeletal actin and fast myosin heavy chain mRNAs were detected precociously, before the young myotube stage." ], "offsets": [ [ 0, 114 ] ] } ]

[ { "id": "BioInfer.d449.s1.e0", "type": "Gene/protein/RNA", "text": [ "alpha-Skeletal actin" ], "offsets": [ [ 0, 20 ] ], "normalized": [] }, { "id": "BioInfer.d449.s1.e1", "type": "Gene/protein/RNA", "text": [ "fast myosin heavy chain" ], "offsets": [ [ 25, 48 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d450.s0__text", "type": "Sentence", "text": [ "Neither can profilin I, in the presence of the peptide, promote actin polymerization during its early phase consistent with a lower affinity." ], "offsets": [ [ 0, 141 ] ] } ]

[ { "id": "BioInfer.d450.s0.e0", "type": "Individual_protein", "text": [ "profilin I" ], "offsets": [ [ 12, 22 ] ], "normalized": [] }, { "id": "BioInfer.d450.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 64, 69 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d450.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d450.s0.e0", "arg2_id": "BioInfer.d450.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d450.s1__text", "type": "Sentence", "text": [ "The resulting profilin II-peptide complex overcomes the combined capacity of thymosin beta4 and profilin II to inhibit actin nucleation and restores the extent of filament formation." ], "offsets": [ [ 0, 182 ] ] } ]

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[ { "id": "BioInfer.d450.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d450.s1.e0", "arg2_id": "BioInfer.d450.s1.e1", "normalized": [] }, { "id": "BioInfer.d450.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d450.s1.e0", "arg2_id": "BioInfer.d450.s1.e2", "normalized": [] }, { "id": "BioInfer.d450.s1.i2", "type": "PPI", "arg1_id": "BioInfer.d450.s1.e0", "arg2_id": "BioInfer.d450.s1.e3", "normalized": [] } ]

[ { "id": "BioInfer.d451.s0__text", "type": "Sentence", "text": [ "Newly disclosed interactions between gephyrin, exchange factors for G proteins of the Rho and Rac families, the translational regulator RAFT1, and actin-binding proteins like profilin might integrate activity-dependent and trophic-factor-mediated signals at developing postsynaptic sites." ], "offsets": [ [ 0, 288 ] ] } ]

[ { "id": "BioInfer.d451.s0.e0", "type": "Individual_protein", "text": [ "Rho" ], "offsets": [ [ 86, 89 ] ], "normalized": [] }, { "id": "BioInfer.d451.s0.e1", "type": "Individual_protein", "text": [ "G proteins" ], "offsets": [ [ 68, 78 ] ], "normalized": [] }, { "id": "BioInfer.d451.s0.e2", "type": "Individual_protein", "text": [ "G proteins" ], "offsets": [ [ 68, 78 ] ], "normalized": [] }, { "id": "BioInfer.d451.s0.e3", "type": "Individual_protein", "text": [ "RAFT1" ], "offsets": [ [ 136, 141 ] ], "normalized": [] }, { "id": "BioInfer.d451.s0.e4", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 175, 183 ] ], "normalized": [] }, { "id": "BioInfer.d451.s0.e5", "type": "Protein_family_or_group", "text": [ "actin-binding proteins" ], "offsets": [ [ 147, 169 ] ], "normalized": [] }, { "id": "BioInfer.d451.s0.e6", "type": "Individual_protein", "text": [ "gephyrin" ], "offsets": [ [ 37, 45 ] ], "normalized": [] }, { "id": "BioInfer.d451.s0.e7", "type": "Individual_protein", "text": [ "Rac" ], "offsets": [ [ 94, 97 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d452.s0__text", "type": "Sentence", "text": [ "N-formyl peptide chemoattractants in neutrophils stimulate the formation of phosphatidylinositol-4,5-bisphosphate (PIP2), a reservoir for second messenger molecules and regulator of actin assembly through its association with the actin-binding proteins, profilin, and gelsolin." ], "offsets": [ [ 0, 277 ] ] } ]

[ { "id": "BioInfer.d452.s0.e0", "type": "Protein_family_or_group", "text": [ "actin-binding proteins" ], "offsets": [ [ 230, 252 ] ], "normalized": [] }, { "id": "BioInfer.d452.s0.e1", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 254, 262 ] ], "normalized": [] }, { "id": "BioInfer.d452.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 182, 187 ] ], "normalized": [] }, { "id": "BioInfer.d452.s0.e3", "type": "Individual_protein", "text": [ "gelsolin" ], "offsets": [ [ 268, 276 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d452.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d452.s0.e0", "arg2_id": "BioInfer.d452.s0.e1", "normalized": [] }, { "id": "BioInfer.d452.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d452.s0.e0", "arg2_id": "BioInfer.d452.s0.e3", "normalized": [] }, { "id": "BioInfer.d452.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d452.s0.e1", "arg2_id": "BioInfer.d452.s0.e2", "normalized": [] }, { "id": "BioInfer.d452.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d452.s0.e2", "arg2_id": "BioInfer.d452.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d453.s0__text", "type": "Sentence", "text": [ "No evidence for the surface expression of the phosphoprotein (P), matrix (M) or nucleocapsid (N) proteins was found." ], "offsets": [ [ 0, 116 ] ] } ]

[ { "id": "BioInfer.d453.s0.e0", "type": "Individual_protein", "text": [ "P" ], "offsets": [ [ 62, 63 ] ], "normalized": [] }, { "id": "BioInfer.d453.s0.e1", "type": "Individual_protein", "text": [ "N" ], "offsets": [ [ 94, 95 ] ], "normalized": [] }, { "id": "BioInfer.d453.s0.e2", "type": "Individual_protein", "text": [ "nucleocapsid", "proteins" ], "offsets": [ [ 80, 92 ], [ 97, 105 ] ], "normalized": [] }, { "id": "BioInfer.d453.s0.e3", "type": "Individual_protein", "text": [ "phosphoprotein", "proteins" ], "offsets": [ [ 46, 60 ], [ 97, 105 ] ], "normalized": [] }, { "id": "BioInfer.d453.s0.e4", "type": "Individual_protein", "text": [ "M" ], "offsets": [ [ 74, 75 ] ], "normalized": [] }, { "id": "BioInfer.d453.s0.e5", "type": "Individual_protein", "text": [ "matrix", "proteins" ], "offsets": [ [ 66, 72 ], [ 97, 105 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d454.s0__text", "type": "Sentence", "text": [ "No significant changes in glomerular vinculin, talin, beta 1-integrin, or total actin expression occurred at any time point during disease development." ], "offsets": [ [ 0, 151 ] ] } ]

[ { "id": "BioInfer.d454.s0.e0", "type": "Gene/protein/RNA", "text": [ "beta 1-integrin" ], "offsets": [ [ 54, 69 ] ], "normalized": [] }, { "id": "BioInfer.d454.s0.e1", "type": "Gene/protein/RNA", "text": [ "vinculin" ], "offsets": [ [ 37, 45 ] ], "normalized": [] }, { "id": "BioInfer.d454.s0.e2", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 80, 85 ] ], "normalized": [] }, { "id": "BioInfer.d454.s0.e3", "type": "Gene/protein/RNA", "text": [ "talin" ], "offsets": [ [ 47, 52 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d455.s0__text", "type": "Sentence", "text": [ "Notably, the two pro-apoptotic adapter proteins TRADD and FADD are also involved in the activation of A-SMase." ], "offsets": [ [ 0, 110 ] ] } ]

[ { "id": "BioInfer.d455.s0.e0", "type": "Individual_protein", "text": [ "FADD" ], "offsets": [ [ 58, 62 ] ], "normalized": [] }, { "id": "BioInfer.d455.s0.e1", "type": "Individual_protein", "text": [ "TRADD" ], "offsets": [ [ 48, 53 ] ], "normalized": [] }, { "id": "BioInfer.d455.s0.e2", "type": "Individual_protein", "text": [ "A-SMase" ], "offsets": [ [ 102, 109 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d455.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d455.s0.e0", "arg2_id": "BioInfer.d455.s0.e2", "normalized": [] }, { "id": "BioInfer.d455.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d455.s0.e1", "arg2_id": "BioInfer.d455.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d456.s0__text", "type": "Sentence", "text": [ "OBJECTIVE: To determine whether other glycoprotein 130 (gp130) binding cytokines can mimic the effects of oncostatin M (OSM) in acting synergistically with interleukin-1alpha (IL-1alpha) to induce cartilage collagen breakdown and collagenase expression, and to determine which receptors mediate these effects." ], "offsets": [ [ 0, 309 ] ] } ]

[ { "id": "BioInfer.d456.s0.e0", "type": "Individual_protein", "text": [ "oncostatin M" ], "offsets": [ [ 106, 118 ] ], "normalized": [] }, { "id": "BioInfer.d456.s0.e1", "type": "Individual_protein", "text": [ "collagenase" ], "offsets": [ [ 230, 241 ] ], "normalized": [] }, { "id": "BioInfer.d456.s0.e2", "type": "Protein_family_or_group", "text": [ "cytokines" ], "offsets": [ [ 71, 80 ] ], "normalized": [] }, { "id": "BioInfer.d456.s0.e3", "type": "Individual_protein", "text": [ "interleukin-1alpha" ], "offsets": [ [ 156, 174 ] ], "normalized": [] }, { "id": "BioInfer.d456.s0.e4", "type": "Individual_protein", "text": [ "IL-1alpha" ], "offsets": [ [ 176, 185 ] ], "normalized": [] }, { "id": "BioInfer.d456.s0.e5", "type": "Individual_protein", "text": [ "collagen" ], "offsets": [ [ 207, 215 ] ], "normalized": [] }, { "id": "BioInfer.d456.s0.e6", "type": "Individual_protein", "text": [ "glycoprotein 130" ], "offsets": [ [ 38, 54 ] ], "normalized": [] }, { "id": "BioInfer.d456.s0.e7", "type": "Individual_protein", "text": [ "OSM" ], "offsets": [ [ 120, 123 ] ], "normalized": [] }, { "id": "BioInfer.d456.s0.e8", "type": "Individual_protein", "text": [ "gp130" ], "offsets": [ [ 56, 61 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d456.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d456.s0.e0", "arg2_id": "BioInfer.d456.s0.e1", "normalized": [] }, { "id": "BioInfer.d456.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d456.s0.e0", "arg2_id": "BioInfer.d456.s0.e3", "normalized": [] }, { "id": "BioInfer.d456.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d456.s0.e0", "arg2_id": "BioInfer.d456.s0.e4", "normalized": [] }, { "id": "BioInfer.d456.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d456.s0.e0", "arg2_id": "BioInfer.d456.s0.e5", "normalized": [] }, { "id": "BioInfer.d456.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d456.s0.e1", "arg2_id": "BioInfer.d456.s0.e2", "normalized": [] }, { "id": "BioInfer.d456.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d456.s0.e1", "arg2_id": "BioInfer.d456.s0.e3", "normalized": [] }, { "id": "BioInfer.d456.s0.i6", "type": "PPI", "arg1_id": "BioInfer.d456.s0.e1", "arg2_id": "BioInfer.d456.s0.e4", "normalized": [] }, { "id": "BioInfer.d456.s0.i7", "type": "PPI", "arg1_id": "BioInfer.d456.s0.e1", "arg2_id": "BioInfer.d456.s0.e7", "normalized": [] }, { "id": "BioInfer.d456.s0.i8", "type": "PPI", "arg1_id": "BioInfer.d456.s0.e2", "arg2_id": "BioInfer.d456.s0.e3", "normalized": [] }, { "id": "BioInfer.d456.s0.i9", "type": "PPI", "arg1_id": "BioInfer.d456.s0.e2", "arg2_id": "BioInfer.d456.s0.e4", "normalized": [] }, { "id": "BioInfer.d456.s0.i10", "type": "PPI", "arg1_id": "BioInfer.d456.s0.e2", "arg2_id": "BioInfer.d456.s0.e5", "normalized": [] }, { "id": "BioInfer.d456.s0.i11", "type": "PPI", "arg1_id": "BioInfer.d456.s0.e2", "arg2_id": "BioInfer.d456.s0.e6", "normalized": [] }, { "id": "BioInfer.d456.s0.i12", "type": "PPI", "arg1_id": "BioInfer.d456.s0.e2", "arg2_id": "BioInfer.d456.s0.e8", "normalized": [] }, { "id": "BioInfer.d456.s0.i13", "type": "PPI", "arg1_id": "BioInfer.d456.s0.e3", "arg2_id": "BioInfer.d456.s0.e5", "normalized": [] }, { "id": "BioInfer.d456.s0.i14", "type": "PPI", "arg1_id": "BioInfer.d456.s0.e3", "arg2_id": "BioInfer.d456.s0.e7", "normalized": [] }, { "id": "BioInfer.d456.s0.i15", "type": "PPI", "arg1_id": "BioInfer.d456.s0.e4", "arg2_id": "BioInfer.d456.s0.e5", "normalized": [] }, { "id": "BioInfer.d456.s0.i16", "type": "PPI", "arg1_id": "BioInfer.d456.s0.e4", "arg2_id": "BioInfer.d456.s0.e7", "normalized": [] }, { "id": "BioInfer.d456.s0.i17", "type": "PPI", "arg1_id": "BioInfer.d456.s0.e5", "arg2_id": "BioInfer.d456.s0.e7", "normalized": [] } ]

[ { "id": "BioInfer.d457.s0__text", "type": "Sentence", "text": [ "Of the five major structural proteins of MV, only nucleocapsid (N) protein and phosphoprotein (P protein) were consistently detected in diseased brain areas." ], "offsets": [ [ 0, 157 ] ] } ]

[ { "id": "BioInfer.d457.s0.e0", "type": "Individual_protein", "text": [ "nucleocapsid", "protein" ], "offsets": [ [ 50, 62 ], [ 67, 74 ] ], "normalized": [] }, { "id": "BioInfer.d457.s0.e1", "type": "Individual_protein", "text": [ "N" ], "offsets": [ [ 64, 65 ] ], "normalized": [] }, { "id": "BioInfer.d457.s0.e2", "type": "Individual_protein", "text": [ "phosphoprotein" ], "offsets": [ [ 79, 93 ] ], "normalized": [] }, { "id": "BioInfer.d457.s0.e3", "type": "Individual_protein", "text": [ "P protein" ], "offsets": [ [ 95, 104 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d459.s0__text", "type": "Sentence", "text": [ "Once the actin monomer is bound to the filament, the profilin is released, and is available to bind to additional actin monomers." ], "offsets": [ [ 0, 129 ] ] } ]

[ { "id": "BioInfer.d459.s0.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 114, 119 ] ], "normalized": [] }, { "id": "BioInfer.d459.s0.e1", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 53, 61 ] ], "normalized": [] }, { "id": "BioInfer.d459.s0.e2", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 9, 14 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d459.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d459.s0.e0", "arg2_id": "BioInfer.d459.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d460.s0__text", "type": "Sentence", "text": [ "One involves talin, which has recently been shown to bind actin directly." ], "offsets": [ [ 0, 73 ] ] } ]

[ { "id": "BioInfer.d460.s0.e0", "type": "Individual_protein", "text": [ "talin" ], "offsets": [ [ 13, 18 ] ], "normalized": [] }, { "id": "BioInfer.d460.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 58, 63 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d460.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d460.s0.e0", "arg2_id": "BioInfer.d460.s0.e1", "normalized": [] } ]