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BigScience Biomedical Datasets 131

[ { "id": "BioInfer.d305.s0__text", "type": "Sentence", "text": [ "In 50 mM KCl, high concentrations of Acanthamoeba profilin inhibit the elongation rate of muscle actin filaments measured directly by electron microscopy, but the effect is minimal in KCl with 2 MgCl2." ], "offsets": [ [ 0, 201 ] ] } ]

[ { "id": "BioInfer.d305.s0.e0", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 50, 58 ] ], "normalized": [] }, { "id": "BioInfer.d305.s0.e1", "type": "Individual_protein", "text": [ "muscle actin" ], "offsets": [ [ 90, 102 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d305.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d305.s0.e0", "arg2_id": "BioInfer.d305.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d306.s0__text", "type": "Sentence", "text": [ "In a blot overlay experiment, purified 125I-labeled recombinant profilin bound not only to plant actin, but also to mammalian actin, demonstrating that cytoskeletal components from distantly related organisms with divergent primary structures can be compatible." ], "offsets": [ [ 0, 261 ] ] } ]

[ { "id": "BioInfer.d306.s0.e0", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 64, 72 ] ], "normalized": [] }, { "id": "BioInfer.d306.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 97, 102 ] ], "normalized": [] }, { "id": "BioInfer.d306.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 126, 131 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d306.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d306.s0.e0", "arg2_id": "BioInfer.d306.s0.e1", "normalized": [] }, { "id": "BioInfer.d306.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d306.s0.e0", "arg2_id": "BioInfer.d306.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d306.s1__text", "type": "Sentence", "text": [ "cDNA cloning, heterologous expression, and actin-binding properties." ], "offsets": [ [ 0, 68 ] ] } ]

[ { "id": "BioInfer.d306.s1.e0", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 43, 48 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d307.s0__text", "type": "Sentence", "text": [ "In Acanthamoeba actin polymerization is regulated, at least in part, by profilin, which binds to actin monomers, and by capping protein, which both nucleates polymerization and blocks monomer addition at the 'barbed' end of the filament." ], "offsets": [ [ 0, 237 ] ] } ]

[ { "id": "BioInfer.d307.s0.e0", "type": "Individual_protein", "text": [ "capping protein" ], "offsets": [ [ 120, 135 ] ], "normalized": [] }, { "id": "BioInfer.d307.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 97, 102 ] ], "normalized": [] }, { "id": "BioInfer.d307.s0.e2", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 72, 80 ] ], "normalized": [] }, { "id": "BioInfer.d307.s0.e3", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 16, 21 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d307.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d307.s0.e0", "arg2_id": "BioInfer.d307.s0.e3", "normalized": [] }, { "id": "BioInfer.d307.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d307.s0.e1", "arg2_id": "BioInfer.d307.s0.e2", "normalized": [] }, { "id": "BioInfer.d307.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d307.s0.e2", "arg2_id": "BioInfer.d307.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d308.s0__text", "type": "Sentence", "text": [ "In Acanthamoeba, the two isoforms of profilin may have specialized functions on the basis of their identical (approximately 10 microM) affinities for actin monomers and different affinities for PIP2." ], "offsets": [ [ 0, 199 ] ] } ]

[ { "id": "BioInfer.d308.s0.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 150, 155 ] ], "normalized": [] }, { "id": "BioInfer.d308.s0.e1", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 37, 45 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d308.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d308.s0.e0", "arg2_id": "BioInfer.d308.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d309.s0__text", "type": "Sentence", "text": [ "Inactivation of the Rb pathway in non-small cell lung carcinoma (NSCLC) occurs mostly through inactivation of the cyclin-dependent kinase inhibitor p16(INK4A) and/or up-regulation of cyclin D1." ], "offsets": [ [ 0, 193 ] ] } ]

[ { "id": "BioInfer.d309.s0.e0", "type": "Individual_protein", "text": [ "INK4A" ], "offsets": [ [ 152, 157 ] ], "normalized": [] }, { "id": "BioInfer.d309.s0.e1", "type": "Individual_protein", "text": [ "cyclin D1" ], "offsets": [ [ 183, 192 ] ], "normalized": [] }, { "id": "BioInfer.d309.s0.e2", "type": "Protein_family_or_group", "text": [ "cyclin-dependent kinase inhibitor" ], "offsets": [ [ 114, 147 ] ], "normalized": [] }, { "id": "BioInfer.d309.s0.e3", "type": "Individual_protein", "text": [ "p16" ], "offsets": [ [ 148, 151 ] ], "normalized": [] }, { "id": "BioInfer.d309.s0.e4", "type": "Individual_protein", "text": [ "Rb" ], "offsets": [ [ 20, 22 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d309.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d309.s0.e0", "arg2_id": "BioInfer.d309.s0.e2", "normalized": [] }, { "id": "BioInfer.d309.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d309.s0.e0", "arg2_id": "BioInfer.d309.s0.e4", "normalized": [] }, { "id": "BioInfer.d309.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d309.s0.e1", "arg2_id": "BioInfer.d309.s0.e4", "normalized": [] }, { "id": "BioInfer.d309.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d309.s0.e2", "arg2_id": "BioInfer.d309.s0.e3", "normalized": [] }, { "id": "BioInfer.d309.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d309.s0.e3", "arg2_id": "BioInfer.d309.s0.e4", "normalized": [] } ]

[ { "id": "BioInfer.d311.s0__text", "type": "Sentence", "text": [ "In addition to their role in mismatch repair (MMR), the MSH2 and MSH3 gene products are required to remove 3' nonhomologous DNA tails during genetic recombination." ], "offsets": [ [ 0, 163 ] ] } ]

[ { "id": "BioInfer.d311.s0.e0", "type": "Gene/protein/RNA", "text": [ "MSH2" ], "offsets": [ [ 56, 60 ] ], "normalized": [] }, { "id": "BioInfer.d311.s0.e1", "type": "Gene/protein/RNA", "text": [ "MSH3" ], "offsets": [ [ 65, 69 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d312.s0__text", "type": "Sentence", "text": [ "In addition to the TNF-alpha-induced increase in the general protein synthesis, stimulation with TNF-alpha led to a 2.4-fold increase in net actin protein synthesis and a 3.3-fold increase in net myosin heavy chain synthesis." ], "offsets": [ [ 0, 225 ] ] } ]

[ { "id": "BioInfer.d312.s0.e0", "type": "Individual_protein", "text": [ "myosin heavy chain" ], "offsets": [ [ 196, 214 ] ], "normalized": [] }, { "id": "BioInfer.d312.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 141, 146 ] ], "normalized": [] }, { "id": "BioInfer.d312.s0.e2", "type": "Individual_protein", "text": [ "TNF-alpha" ], "offsets": [ [ 19, 28 ] ], "normalized": [] }, { "id": "BioInfer.d312.s0.e3", "type": "Individual_protein", "text": [ "TNF-alpha" ], "offsets": [ [ 97, 106 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d312.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d312.s0.e0", "arg2_id": "BioInfer.d312.s0.e3", "normalized": [] }, { "id": "BioInfer.d312.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d312.s0.e1", "arg2_id": "BioInfer.d312.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d313.s0__text", "type": "Sentence", "text": [ "In addition, we also provide new evidence to suggest that HRG stimulation of the EF-1alpha promoter involves increased physical interactions with acetylated histone H3 and histone H4." ], "offsets": [ [ 0, 183 ] ] } ]

[ { "id": "BioInfer.d313.s0.e0", "type": "Protein_family_or_group", "text": [ "histone" ], "offsets": [ [ 172, 179 ] ], "normalized": [] }, { "id": "BioInfer.d313.s0.e1", "type": "Individual_protein", "text": [ "H3" ], "offsets": [ [ 165, 167 ] ], "normalized": [] }, { "id": "BioInfer.d313.s0.e2", "type": "Gene", "text": [ "EF-1alpha" ], "offsets": [ [ 81, 90 ] ], "normalized": [] }, { "id": "BioInfer.d313.s0.e3", "type": "Individual_protein", "text": [ "HRG" ], "offsets": [ [ 58, 61 ] ], "normalized": [] }, { "id": "BioInfer.d313.s0.e4", "type": "Protein_family_or_group", "text": [ "histone" ], "offsets": [ [ 157, 164 ] ], "normalized": [] }, { "id": "BioInfer.d313.s0.e5", "type": "Individual_protein", "text": [ "H4" ], "offsets": [ [ 180, 182 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d313.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d313.s0.e0", "arg2_id": "BioInfer.d313.s0.e5", "normalized": [] }, { "id": "BioInfer.d313.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d313.s0.e1", "arg2_id": "BioInfer.d313.s0.e2", "normalized": [] }, { "id": "BioInfer.d313.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d313.s0.e1", "arg2_id": "BioInfer.d313.s0.e3", "normalized": [] }, { "id": "BioInfer.d313.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d313.s0.e1", "arg2_id": "BioInfer.d313.s0.e4", "normalized": [] }, { "id": "BioInfer.d313.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d313.s0.e2", "arg2_id": "BioInfer.d313.s0.e3", "normalized": [] }, { "id": "BioInfer.d313.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d313.s0.e2", "arg2_id": "BioInfer.d313.s0.e5", "normalized": [] }, { "id": "BioInfer.d313.s0.i6", "type": "PPI", "arg1_id": "BioInfer.d313.s0.e3", "arg2_id": "BioInfer.d313.s0.e5", "normalized": [] } ]

[ { "id": "BioInfer.d314.s0__text", "type": "Sentence", "text": [ "In addition, we demonstrate that cofilin and its actin binding peptide compete with gelsolin segments 2-3 for binding to actin filaments." ], "offsets": [ [ 0, 137 ] ] } ]

[ { "id": "BioInfer.d314.s0.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 49, 54 ] ], "normalized": [] }, { "id": "BioInfer.d314.s0.e1", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 33, 40 ] ], "normalized": [] }, { "id": "BioInfer.d314.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 121, 126 ] ], "normalized": [] }, { "id": "BioInfer.d314.s0.e3", "type": "Individual_protein", "text": [ "gelsolin" ], "offsets": [ [ 84, 92 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d314.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d314.s0.e0", "arg2_id": "BioInfer.d314.s0.e1", "normalized": [] }, { "id": "BioInfer.d314.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d314.s0.e1", "arg2_id": "BioInfer.d314.s0.e2", "normalized": [] }, { "id": "BioInfer.d314.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d314.s0.e2", "arg2_id": "BioInfer.d314.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d315.s0__text", "type": "Sentence", "text": [ "In addition, we have demonstrated that increased gene dosage of either SIR1 or SIR4, two other factors required for silencing, suppresses the silencing defect of the rap1 mutants." ], "offsets": [ [ 0, 179 ] ] } ]

[ { "id": "BioInfer.d315.s0.e0", "type": "Individual_protein", "text": [ "SIR4" ], "offsets": [ [ 79, 83 ] ], "normalized": [] }, { "id": "BioInfer.d315.s0.e1", "type": "Gene", "text": [ "rap1" ], "offsets": [ [ 166, 170 ] ], "normalized": [] }, { "id": "BioInfer.d315.s0.e2", "type": "Individual_protein", "text": [ "SIR1" ], "offsets": [ [ 71, 75 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d315.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d315.s0.e0", "arg2_id": "BioInfer.d315.s0.e1", "normalized": [] }, { "id": "BioInfer.d315.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d315.s0.e1", "arg2_id": "BioInfer.d315.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d316.s0__text", "type": "Sentence", "text": [ "In addition, we performed immunohistochemistry on sectioned Myf-5 and MyoD mutant embryos with antibodies reactive with desmin, nestin, myosin heavy chain, sarcomeric actin, Myf-5, MyoD and myogenin." ], "offsets": [ [ 0, 199 ] ] } ]

[ { "id": "BioInfer.d316.s0.e0", "type": "Gene/protein/RNA", "text": [ "MyoD" ], "offsets": [ [ 181, 185 ] ], "normalized": [] }, { "id": "BioInfer.d316.s0.e1", "type": "Gene/protein/RNA", "text": [ "myogenin" ], "offsets": [ [ 190, 198 ] ], "normalized": [] }, { "id": "BioInfer.d316.s0.e2", "type": "Gene/protein/RNA", "text": [ "sarcomeric actin" ], "offsets": [ [ 156, 172 ] ], "normalized": [] }, { "id": "BioInfer.d316.s0.e3", "type": "Gene/protein/RNA", "text": [ "Myf-5" ], "offsets": [ [ 174, 179 ] ], "normalized": [] }, { "id": "BioInfer.d316.s0.e4", "type": "Gene/protein/RNA", "text": [ "nestin" ], "offsets": [ [ 128, 134 ] ], "normalized": [] }, { "id": "BioInfer.d316.s0.e5", "type": "Gene/protein/RNA", "text": [ "myosin heavy chain" ], "offsets": [ [ 136, 154 ] ], "normalized": [] }, { "id": "BioInfer.d316.s0.e6", "type": "Gene/protein/RNA", "text": [ "MyoD" ], "offsets": [ [ 70, 74 ] ], "normalized": [] }, { "id": "BioInfer.d316.s0.e7", "type": "Gene/protein/RNA", "text": [ "desmin" ], "offsets": [ [ 120, 126 ] ], "normalized": [] }, { "id": "BioInfer.d316.s0.e8", "type": "Gene/protein/RNA", "text": [ "Myf-5" ], "offsets": [ [ 60, 65 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d317.s0__text", "type": "Sentence", "text": [ "In addition, we report that radiation induced transient activation of c-Jun N-terminal kinase/stress-activated protein kinase (JNK/SAPK) activation and the transcription factor, AP-1." ], "offsets": [ [ 0, 183 ] ] } ]

[ { "id": "BioInfer.d317.s0.e0", "type": "Individual_protein", "text": [ "c-Jun N-terminal kinase" ], "offsets": [ [ 70, 93 ] ], "normalized": [] }, { "id": "BioInfer.d317.s0.e1", "type": "Individual_protein", "text": [ "stress-activated protein kinase" ], "offsets": [ [ 94, 125 ] ], "normalized": [] }, { "id": "BioInfer.d317.s0.e2", "type": "Gene/protein/RNA", "text": [ "AP-1" ], "offsets": [ [ 178, 182 ] ], "normalized": [] }, { "id": "BioInfer.d317.s0.e3", "type": "Individual_protein", "text": [ "JNK" ], "offsets": [ [ 127, 130 ] ], "normalized": [] }, { "id": "BioInfer.d317.s0.e4", "type": "Individual_protein", "text": [ "SAPK" ], "offsets": [ [ 131, 135 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d319.s0__text", "type": "Sentence", "text": [ "In a model system, the interacting proteins recruiting TFIIIC to DNA were PRP21 and PRP9 or PRP21 and PRP11." ], "offsets": [ [ 0, 108 ] ] } ]

[ { "id": "BioInfer.d319.s0.e0", "type": "Individual_protein", "text": [ "PRP9" ], "offsets": [ [ 84, 88 ] ], "normalized": [] }, { "id": "BioInfer.d319.s0.e1", "type": "Individual_protein", "text": [ "TFIIIC" ], "offsets": [ [ 55, 61 ] ], "normalized": [] }, { "id": "BioInfer.d319.s0.e2", "type": "Individual_protein", "text": [ "PRP21" ], "offsets": [ [ 92, 97 ] ], "normalized": [] }, { "id": "BioInfer.d319.s0.e3", "type": "Individual_protein", "text": [ "PRP11" ], "offsets": [ [ 102, 107 ] ], "normalized": [] }, { "id": "BioInfer.d319.s0.e4", "type": "Individual_protein", "text": [ "PRP21" ], "offsets": [ [ 74, 79 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d319.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d319.s0.e0", "arg2_id": "BioInfer.d319.s0.e1", "normalized": [] }, { "id": "BioInfer.d319.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d319.s0.e0", "arg2_id": "BioInfer.d319.s0.e4", "normalized": [] }, { "id": "BioInfer.d319.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d319.s0.e1", "arg2_id": "BioInfer.d319.s0.e2", "normalized": [] }, { "id": "BioInfer.d319.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d319.s0.e1", "arg2_id": "BioInfer.d319.s0.e3", "normalized": [] }, { "id": "BioInfer.d319.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d319.s0.e1", "arg2_id": "BioInfer.d319.s0.e4", "normalized": [] }, { "id": "BioInfer.d319.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d319.s0.e2", "arg2_id": "BioInfer.d319.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d320.s0__text", "type": "Sentence", "text": [ "In brush cells, villin and fimbrin are not only present in the actin filament core bundles of apical microvilli and their long rootlets but, in addition, both proteins are also associated with microvilli extending from the basolateral cell surface of the brush cells." ], "offsets": [ [ 0, 267 ] ] } ]

[ { "id": "BioInfer.d320.s0.e0", "type": "Individual_protein", "text": [ "fimbrin" ], "offsets": [ [ 27, 34 ] ], "normalized": [] }, { "id": "BioInfer.d320.s0.e1", "type": "Individual_protein", "text": [ "villin" ], "offsets": [ [ 16, 22 ] ], "normalized": [] }, { "id": "BioInfer.d320.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 63, 68 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d320.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d320.s0.e0", "arg2_id": "BioInfer.d320.s0.e2", "normalized": [] }, { "id": "BioInfer.d320.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d320.s0.e1", "arg2_id": "BioInfer.d320.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d320.s1__text", "type": "Sentence", "text": [ "In the present study we show that brush cells can be identified in tissue sections even at the light microscopic level by immunostaining with antibodies against villin and fimbrin, two proteins that crosslink actin filaments to form bundles." ], "offsets": [ [ 0, 241 ] ] } ]

[ { "id": "BioInfer.d320.s1.e0", "type": "Individual_protein", "text": [ "villin" ], "offsets": [ [ 161, 167 ] ], "normalized": [] }, { "id": "BioInfer.d320.s1.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 209, 214 ] ], "normalized": [] }, { "id": "BioInfer.d320.s1.e2", "type": "Individual_protein", "text": [ "fimbrin" ], "offsets": [ [ 172, 179 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d320.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d320.s1.e0", "arg2_id": "BioInfer.d320.s1.e1", "normalized": [] }, { "id": "BioInfer.d320.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d320.s1.e1", "arg2_id": "BioInfer.d320.s1.e2", "normalized": [] } ]

[ { "id": "BioInfer.d321.s0__text", "type": "Sentence", "text": [ "In cancerous tissues, the frequency of reduced expression of beta-catenin (28 of 86, 33%) was similar to that of E-cadherin (19 of 86, 22%), but less than that of alpha-catenin (47 of 86, 55%)." ], "offsets": [ [ 0, 193 ] ] } ]

[ { "id": "BioInfer.d321.s0.e0", "type": "Gene/protein/RNA", "text": [ "E-cadherin" ], "offsets": [ [ 113, 123 ] ], "normalized": [] }, { "id": "BioInfer.d321.s0.e1", "type": "Gene/protein/RNA", "text": [ "alpha-catenin" ], "offsets": [ [ 163, 176 ] ], "normalized": [] }, { "id": "BioInfer.d321.s0.e2", "type": "Gene/protein/RNA", "text": [ "beta-catenin" ], "offsets": [ [ 61, 73 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d321.s1__text", "type": "Sentence", "text": [ "In this study, we immunohistochemically investigated the expression of beta-catenin as well as E-cadherin and alpha-catenin in 86 human colorectal cancers, and we analysed their coexpression pattern and relationship to clinicopathological factors." ], "offsets": [ [ 0, 247 ] ] } ]

[ { "id": "BioInfer.d321.s1.e0", "type": "Gene/protein/RNA", "text": [ "beta-catenin" ], "offsets": [ [ 71, 83 ] ], "normalized": [] }, { "id": "BioInfer.d321.s1.e1", "type": "Gene/protein/RNA", "text": [ "alpha-catenin" ], "offsets": [ [ 110, 123 ] ], "normalized": [] }, { "id": "BioInfer.d321.s1.e2", "type": "Gene/protein/RNA", "text": [ "E-cadherin" ], "offsets": [ [ 95, 105 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d322.s0__text", "type": "Sentence", "text": [ "In cell extracts, we found that complementary strand synthesis was inhibited by the cyclin-dependent kinase inhibitor p21(WAF1/CIP1) and rescued by the addition of proliferating cell nuclear antigen, arguing for the involvement of DNA polymerase (Pol) delta in the conversion reaction." ], "offsets": [ [ 0, 285 ] ] } ]

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[ { "id": "BioInfer.d323.s0__text", "type": "Sentence", "text": [ "In cells lacking the myosin-II heavy chain, the bundles, which were induced by an over-expression of cofilin, shortened and became straight following hyperosmotic stress, forming a polygonal structure." ], "offsets": [ [ 0, 201 ] ] } ]

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[ { "id": "BioInfer.d324.s0__text", "type": "Sentence", "text": [ "In contrast, act1-159 partially suppresses the temperature sensitivity of a tropomyosin mutant, and the loss of cytoplasmic cables seen in fimbrin, Mdm20p, and tropomyosin null mutants, suggesting filament stabilizing functions for these actin-binding proteins." ], "offsets": [ [ 0, 261 ] ] } ]

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[ { "id": "BioInfer.d325.s0__text", "type": "Sentence", "text": [ "In contrast, talin, another putative actin-membrane linker protein, could not be detected in significant amounts in human neutrophils using a polyclonal antibody raised against chicken gizzard talin, which reacted with human platelet and lymphocyte talin." ], "offsets": [ [ 0, 255 ] ] } ]

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[ { "id": "BioInfer.d327.s0__text", "type": "Sentence", "text": [ "In contrast, the RAD51 and RAD52 genes are essential for homothallic mating-type switching." ], "offsets": [ [ 0, 91 ] ] } ]

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[ { "id": "BioInfer.d329.s0__text", "type": "Sentence", "text": [ "In contrast to the model of actin binding proposed for fimbrin, the utrophin actin-binding domain appears to associate with actin in an extended conformation." ], "offsets": [ [ 0, 158 ] ] } ]

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[ { "id": "BioInfer.d330.s0__text", "type": "Sentence", "text": [ "In COS-7 cells overexpressing a N-WASP mutant lacking the proline-rich domain (Deltap) unable to interact with profilin, the actin tail formation of intracellular Shigella was inhibited." ], "offsets": [ [ 0, 186 ] ] } ]

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[ { "id": "BioInfer.d331.s0__text", "type": "Sentence", "text": [ "Increased interaction of beta1D integrin with the actin cytoskeleton is consistent with and might be mediated by its enhanced binding to talin." ], "offsets": [ [ 0, 143 ] ] } ]

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[ { "id": "BioInfer.d332.s0__text", "type": "Sentence", "text": [ "Increasing the ionic strength within a relatively narrow range significantly decreased ability of talin to bind to actin, regardless of pH." ], "offsets": [ [ 0, 139 ] ] } ]

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[ { "id": "BioInfer.d333.s0__text", "type": "Sentence", "text": [ "In enriched cell lines and in a pure myocyte cell strain, EGF inhibited increases in immunoreactive sarcomeric actin and sarcomeric myosin heavy chain (SMHC) normally seen after serum withdrawal." ], "offsets": [ [ 0, 195 ] ] } ]

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[ { "id": "BioInfer.d334.s0__text", "type": "Sentence", "text": [ "In extracts from mouse brain, profilin I and profilin II can form complexes with regulators of endocytosis, synaptic vesicle recycling and actin assembly." ], "offsets": [ [ 0, 154 ] ] } ]

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[ { "id": "BioInfer.d334.s1__text", "type": "Sentence", "text": [ "In mouse brain profilin I and profilin II associate with regulators of the endocytic pathway and actin assembly." ], "offsets": [ [ 0, 112 ] ] } ]

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[ { "id": "BioInfer.d334.s2__text", "type": "Sentence", "text": [ "Our findings strongly suggest that in brain profilin I and profilin II complexes link the actin cytoskeleton and endocytic membrane flow, directing actin and clathrin assembly to distinct membrane domains." ], "offsets": [ [ 0, 205 ] ] } ]

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[ { "id": "BioInfer.d335.s0__text", "type": "Sentence", "text": [ "In flattened cells under starvation stress, cofilin localized at dramatically reorganizing actin-cytoskeletons in ruffling membranes of the leading edge, but not at rigid actin meshwork in focal adhesion plaques." ], "offsets": [ [ 0, 212 ] ] } ]

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[ { "id": "BioInfer.d336.s0__text", "type": "Sentence", "text": [ "In growth cones, myosin heavy chain B was most concentrated in the margin bordering the thickened, organelle-rich central region and the thin, actin-rich peripheral region." ], "offsets": [ [ 0, 172 ] ] } ]

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[ { "id": "BioInfer.d336.s1__text", "type": "Sentence", "text": [ "Myosin heavy chain A staining was dimmer and its colocalization with filamentous actin bundles in growth cones was less striking than that of myosin heavy chain B." ], "offsets": [ [ 0, 163 ] ] } ]

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[ { "id": "BioInfer.d337.s0__text", "type": "Sentence", "text": [ "Inhibition of 12P-CRE binding was also observed in the presence of an antibody to CREB-binding protein (265-kDa CBP), an integrator and coactivator of cAMP-responsive genes." ], "offsets": [ [ 0, 173 ] ] } ]

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[ { "id": "BioInfer.d338.s0__text", "type": "Sentence", "text": [ "Inhibition of actin polymerization by a synthetic dodecapeptide patterned on the sequence around the actin-binding site of cofilin." ], "offsets": [ [ 0, 131 ] ] } ]

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[ { "id": "BioInfer.d339.s0__text", "type": "Sentence", "text": [ "Inhibition of actin polymerization in KCl was stronger than that of the parental profilin, and the Kd value of its interaction with rabbit skeletal muscle actin, as determined by falling ball viscometry, was smaller (mean value 0.5 x 10(-6) M, as compared to 1.9 x 10(-6) M for bovine profilin)." ], "offsets": [ [ 0, 295 ] ] } ]

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[ { "id": "BioInfer.d339.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d339.s0.e0", "arg2_id": "BioInfer.d339.s0.e1", "normalized": [] }, { "id": "BioInfer.d339.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d339.s0.e2", "arg2_id": "BioInfer.d339.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d340.s0__text", "type": "Sentence", "text": [ "Inhibition of actomyosin subfragment 1 ATPase activity by analog peptides of the actin-binding site around the Cys(SH1) of myosin heavy chain." ], "offsets": [ [ 0, 142 ] ] } ]

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[ { "id": "BioInfer.d340.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d340.s0.e0", "arg2_id": "BioInfer.d340.s0.e2", "normalized": [] }, { "id": "BioInfer.d340.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d340.s0.e0", "arg2_id": "BioInfer.d340.s0.e3", "normalized": [] }, { "id": "BioInfer.d340.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d340.s0.e1", "arg2_id": "BioInfer.d340.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d342.s0__text", "type": "Sentence", "text": [ "Inhibition of the interactions of cofilin, destrin, and deoxyribonuclease I with actin by phosphoinositides." ], "offsets": [ [ 0, 108 ] ] } ]

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[ { "id": "BioInfer.d342.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d342.s0.e0", "arg2_id": "BioInfer.d342.s0.e2", "normalized": [] }, { "id": "BioInfer.d342.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d342.s0.e1", "arg2_id": "BioInfer.d342.s0.e2", "normalized": [] }, { "id": "BioInfer.d342.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d342.s0.e2", "arg2_id": "BioInfer.d342.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d343.s0__text", "type": "Sentence", "text": [ "In higher plants, a large number of isoforms for the actin monomer-binding protein profilin have been identified, whereas other organisms express only few profilins." ], "offsets": [ [ 0, 165 ] ] } ]

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[ { "id": "BioInfer.d343.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d343.s0.e0", "arg2_id": "BioInfer.d343.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d346.s0__text", "type": "Sentence", "text": [ "In isolated hearts, PD 81,723 alone produced only a small stimulus to His bundle (S-H) interval prolongation of 1.5 to 4 msec, which was completely reversed by the A1 adenosine receptor antagonist 8-cyclopentyltheophylline and adenosine deaminase." ], "offsets": [ [ 0, 247 ] ] } ]

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[ { "id": "BioInfer.d347.s0__text", "type": "Sentence", "text": [ "In localization studies with mammalian cells, all fusion proteins showed the localization expected for profilin in areas of high actin dynamics, such as leading lamellae and ruffles induced by epidermal growth factor." ], "offsets": [ [ 0, 217 ] ] } ]

[ { "id": "BioInfer.d347.s0.e0", "type": "Gene/protein/RNA", "text": [ "profilin" ], "offsets": [ [ 103, 111 ] ], "normalized": [] }, { "id": "BioInfer.d347.s0.e1", "type": "Gene/protein/RNA", "text": [ "epidermal growth factor" ], "offsets": [ [ 193, 216 ] ], "normalized": [] }, { "id": "BioInfer.d347.s0.e2", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 129, 134 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d348.s0__text", "type": "Sentence", "text": [ "In order to clarify cofilin-dependent regulation of actin assembly in muscle cells, cofilin tagged with fluorescence dyes was introduced into C2 myoblasts by a micro injection method." ], "offsets": [ [ 0, 183 ] ] } ]

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[ { "id": "BioInfer.d348.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d348.s0.e0", "arg2_id": "BioInfer.d348.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d348.s1__text", "type": "Sentence", "text": [ "The exogeneous cofilin, but not ADF, caused quick disassembly of actin filaments and accumulated in furrow region of dividing cells." ], "offsets": [ [ 0, 132 ] ] } ]

[ { "id": "BioInfer.d348.s1.e0", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 15, 22 ] ], "normalized": [] }, { "id": "BioInfer.d348.s1.e1", "type": "Individual_protein", "text": [ "ADF" ], "offsets": [ [ 32, 35 ] ], "normalized": [] }, { "id": "BioInfer.d348.s1.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 65, 70 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d348.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d348.s1.e0", "arg2_id": "BioInfer.d348.s1.e2", "normalized": [] }, { "id": "BioInfer.d348.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d348.s1.e1", "arg2_id": "BioInfer.d348.s1.e2", "normalized": [] } ]

[ { "id": "BioInfer.d348.s2__text", "type": "Sentence", "text": [ "These results suggest that the subcellular distribution of cofilin as well as its interaction with actin in vivo is regulated by its phosphorylation and dephosphorylation." ], "offsets": [ [ 0, 171 ] ] } ]

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[ { "id": "BioInfer.d348.s2.i0", "type": "PPI", "arg1_id": "BioInfer.d348.s2.e0", "arg2_id": "BioInfer.d348.s2.e1", "normalized": [] } ]

[ { "id": "BioInfer.d350.s0__text", "type": "Sentence", "text": [ "In order to help explain the apparent beneficial effects of cyclin D1 over-expression, a number of closely associated cell cycle proteins have also been evaluated, including the cyclin dependent kinase inhibitor p27, which blocks the activating effects of cyclin D1." ], "offsets": [ [ 0, 266 ] ] } ]

[ { "id": "BioInfer.d350.s0.e0", "type": "Protein_family_or_group", "text": [ "cyclin dependent kinase inhibitor" ], "offsets": [ [ 178, 211 ] ], "normalized": [] }, { "id": "BioInfer.d350.s0.e1", "type": "Individual_protein", "text": [ "cyclin D1" ], "offsets": [ [ 256, 265 ] ], "normalized": [] }, { "id": "BioInfer.d350.s0.e2", "type": "Gene/protein/RNA", "text": [ "cyclin D1" ], "offsets": [ [ 60, 69 ] ], "normalized": [] }, { "id": "BioInfer.d350.s0.e3", "type": "Individual_protein", "text": [ "p27" ], "offsets": [ [ 212, 215 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d350.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d350.s0.e0", "arg2_id": "BioInfer.d350.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d351.s0__text", "type": "Sentence", "text": [ "In reconstitution experiments, actin filaments incubated in EGTA with purified fimbrin and villin form smooth-sided bundles containing an apparently random number of filaments." ], "offsets": [ [ 0, 176 ] ] } ]

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[ { "id": "BioInfer.d351.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d351.s0.e0", "arg2_id": "BioInfer.d351.s0.e1", "normalized": [] }, { "id": "BioInfer.d351.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d351.s0.e1", "arg2_id": "BioInfer.d351.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d352.s0__text", "type": "Sentence", "text": [ "In resting leukocytes, beta2 integrins are constitutively linked to the actin cytoskeleton via the protein talin." ], "offsets": [ [ 0, 113 ] ] } ]

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[ { "id": "BioInfer.d352.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d352.s0.e0", "arg2_id": "BioInfer.d352.s0.e1", "normalized": [] }, { "id": "BioInfer.d352.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d352.s0.e0", "arg2_id": "BioInfer.d352.s0.e2", "normalized": [] }, { "id": "BioInfer.d352.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d352.s0.e1", "arg2_id": "BioInfer.d352.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d353.s0__text", "type": "Sentence", "text": [ "In search for genes which might participate in chicken immunoglobulin gene conversion, we have identified chicken counterparts of the yeast RAD51, RAD52, and RAD54 genes." ], "offsets": [ [ 0, 170 ] ] } ]

[ { "id": "BioInfer.d353.s0.e0", "type": "Gene/protein/RNA", "text": [ "RAD54" ], "offsets": [ [ 158, 163 ] ], "normalized": [] }, { "id": "BioInfer.d353.s0.e1", "type": "Gene/protein/RNA", "text": [ "RAD51" ], "offsets": [ [ 140, 145 ] ], "normalized": [] }, { "id": "BioInfer.d353.s0.e2", "type": "Gene/protein/RNA", "text": [ "RAD52" ], "offsets": [ [ 147, 152 ] ], "normalized": [] }, { "id": "BioInfer.d353.s0.e3", "type": "Gene/protein/RNA", "text": [ "immunoglobulin" ], "offsets": [ [ 55, 69 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d354.s0__text", "type": "Sentence", "text": [ "Insulin-like growth factor-I, actin, and myosin heavy chain messenger RNAs in skeletal muscle after an injection of growth hormone in subjects over 60 years old." ], "offsets": [ [ 0, 161 ] ] } ]

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[ { "id": "BioInfer.d355.s0__text", "type": "Sentence", "text": [ "Insulin-like growth factor I stimulates cardiac myosin heavy chain and actin synthesis in the awake rat." ], "offsets": [ [ 0, 104 ] ] } ]

[ { "id": "BioInfer.d355.s0.e0", "type": "Individual_protein", "text": [ "cardiac myosin heavy chain" ], "offsets": [ [ 40, 66 ] ], "normalized": [] }, { "id": "BioInfer.d355.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 71, 76 ] ], "normalized": [] }, { "id": "BioInfer.d355.s0.e2", "type": "Individual_protein", "text": [ "Insulin-like growth factor I" ], "offsets": [ [ 0, 28 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d355.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d355.s0.e0", "arg2_id": "BioInfer.d355.s0.e2", "normalized": [] }, { "id": "BioInfer.d355.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d355.s0.e1", "arg2_id": "BioInfer.d355.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d355.s1__text", "type": "Sentence", "text": [ "To determine the effect of insulin-like growth factor I (IGF-I) on cardiac contractile protein synthesis in vivo, we measured L-[ring-2, 6-3H]phenylalanine incorporation into myosin heavy chain and actin during intravenous infusions (4 h) of either saline or IGF-I (1 microgram. kg-1. min-1) in awake rats." ], "offsets": [ [ 0, 306 ] ] } ]

[ { "id": "BioInfer.d355.s1.e0", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 198, 203 ] ], "normalized": [] }, { "id": "BioInfer.d355.s1.e1", "type": "Gene/protein/RNA", "text": [ "myosin heavy chain" ], "offsets": [ [ 175, 193 ] ], "normalized": [] }, { "id": "BioInfer.d355.s1.e2", "type": "Individual_protein", "text": [ "insulin-like growth factor I" ], "offsets": [ [ 27, 55 ] ], "normalized": [] }, { "id": "BioInfer.d355.s1.e3", "type": "Gene/protein/RNA", "text": [ "IGF-I" ], "offsets": [ [ 259, 264 ] ], "normalized": [] }, { "id": "BioInfer.d355.s1.e4", "type": "Individual_protein", "text": [ "IGF-I" ], "offsets": [ [ 57, 62 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d356.s0__text", "type": "Sentence", "text": [ "Integrating the actin and vimentin cytoskeletons." ], "offsets": [ [ 0, 49 ] ] } ]

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[ { "id": "BioInfer.d356.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d356.s0.e0", "arg2_id": "BioInfer.d356.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d357.s0__text", "type": "Sentence", "text": [ "Integrin (beta) chains, for example, interact with actin-binding proteins (e.g. talin and filamin), which form mechanical links to the cytoskeleton." ], "offsets": [ [ 0, 148 ] ] } ]

[ { "id": "BioInfer.d357.s0.e0", "type": "Individual_protein", "text": [ "Integrin", "beta", "chains" ], "offsets": [ [ 0, 8 ], [ 10, 14 ], [ 16, 22 ] ], "normalized": [] }, { "id": "BioInfer.d357.s0.e1", "type": "Protein_family_or_group", "text": [ "actin-binding proteins" ], "offsets": [ [ 51, 73 ] ], "normalized": [] }, { "id": "BioInfer.d357.s0.e2", "type": "Individual_protein", "text": [ "talin" ], "offsets": [ [ 80, 85 ] ], "normalized": [] }, { "id": "BioInfer.d357.s0.e3", "type": "Individual_protein", "text": [ "filamin" ], "offsets": [ [ 90, 97 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d357.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d357.s0.e0", "arg2_id": "BioInfer.d357.s0.e1", "normalized": [] }, { "id": "BioInfer.d357.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d357.s0.e1", "arg2_id": "BioInfer.d357.s0.e2", "normalized": [] }, { "id": "BioInfer.d357.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d357.s0.e1", "arg2_id": "BioInfer.d357.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d358.s0__text", "type": "Sentence", "text": [ "Integrin binding may be promoted by disruption of links to the cytoskeleton, effected through depolymerisation of actin or cleavage of linking protein talin by calpain." ], "offsets": [ [ 0, 168 ] ] } ]

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[ { "id": "BioInfer.d358.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d358.s0.e0", "arg2_id": "BioInfer.d358.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d359.s0__text", "type": "Sentence", "text": [ "Interaction between nucleocapsid protein (NP) and phosphoprotein (P) of human parainfluenza virus type 2: one of the two NP binding sites on P is essential for granule formation." ], "offsets": [ [ 0, 178 ] ] } ]

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[ { "id": "BioInfer.d359.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d359.s0.e0", "arg2_id": "BioInfer.d359.s0.e2", "normalized": [] }, { "id": "BioInfer.d359.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d359.s0.e0", "arg2_id": "BioInfer.d359.s0.e3", "normalized": [] }, { "id": "BioInfer.d359.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d359.s0.e1", "arg2_id": "BioInfer.d359.s0.e5", "normalized": [] }, { "id": "BioInfer.d359.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d359.s0.e2", "arg2_id": "BioInfer.d359.s0.e4", "normalized": [] }, { "id": "BioInfer.d359.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d359.s0.e3", "arg2_id": "BioInfer.d359.s0.e4", "normalized": [] } ]

[ { "id": "BioInfer.d360.s0__text", "type": "Sentence", "text": [ "Interaction of Munc-18-2 with syntaxin 3 controls the association of apical SNAREs in epithelial cells." ], "offsets": [ [ 0, 103 ] ] } ]

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[ { "id": "BioInfer.d360.s1__text", "type": "Sentence", "text": [ "The quantity of the complex is reduced by treatment of Caco-2 cells with the alkylating agent N-ethylmaleimide which also has an inhibitory effect on the ability of Munc-18-2 to associate with syntaxin 3 in vitro." ], "offsets": [ [ 0, 213 ] ] } ]

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[ { "id": "BioInfer.d361.s0__text", "type": "Sentence", "text": [ "Interactions of ADF/cofilin, Arp2/3 complex, capping protein and profilin in remodeling of branched actin filament networks." ], "offsets": [ [ 0, 124 ] ] } ]

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[ { "id": "BioInfer.d364.s0__text", "type": "Sentence", "text": [ "In the ADE2 assay system, silencing depends completely upon the function of the SIR genes, known trans-acting regulators of the silent loci, and is sensitive to the gene dosage of two SIR genes, SIR1 and SIR4." ], "offsets": [ [ 0, 209 ] ] } ]

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[ { "id": "BioInfer.d365.s0__text", "type": "Sentence", "text": [ "In the basal layer, patches of brightly labeled cells were detected with antibodies to E-cadherin, beta-catenin, and gamma-catenin, but not with antibodies to P-cadherin, alpha-catenin, or with pan-desmocollin and pan-desmoglein antibodies." ], "offsets": [ [ 0, 240 ] ] } ]

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[ { "id": "BioInfer.d366.s0__text", "type": "Sentence", "text": [ "In the budding yeast Saccharomyces cerevisiae, the DNA damage-induced G2 arrest requires the checkpoint control genes RAD9, RAD17, RAD24, MEC1, MEC2 and MEC3." ], "offsets": [ [ 0, 158 ] ] } ]

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[ { "id": "BioInfer.d367.s0__text", "type": "Sentence", "text": [ "In the cytoplasm, HBx was shown to stimulate the Ras-Raf-mitogen-activated protein kinase (MAP kinase) cascade, which is essential for activation of transcription factor AP-1." ], "offsets": [ [ 0, 175 ] ] } ]

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[ { "id": "BioInfer.d370.s0__text", "type": "Sentence", "text": [ "In the present paper, using indirect immunofluorescence, we found that PMN adhesion to tumor necrosis factor-activated endothelial cells (EC) induced the disappearance from endothelial cell-to-cell contacts of adherens junction (AJ) components: vascular endothelial (VE)-cadherin, alpha-catenin, beta-catenin, and plakoglobin." ], "offsets": [ [ 0, 326 ] ] } ]

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[ { "id": "BioInfer.d372.s0__text", "type": "Sentence", "text": [ "In these investigations, we determine that recruitment of a coactivator protein, CBP (the CREBbinding protein), to the CYBB or NCF2 promoter is the molecular mechanism of transcriptional activation by PU.1, IRF1, and ICSBP." ], "offsets": [ [ 0, 223 ] ] } ]

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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 ] ] } ]

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[ { "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 ] ] } ]

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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 ] ] } ]

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[ { "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 ] ] } ]

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[ { "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 ] ] } ]

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[ { "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 ] ] } ]

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[ { "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 ] ] } ]

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[ { "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 ] ] } ]

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[ { "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 ] ] } ]

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[ { "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 ] ] } ]

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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 ] ] } ]

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[ { "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 ] ] } ]

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[ { "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 ] ] } ]

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[ { "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 ] ] } ]

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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 ] ] } ]

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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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