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Knowledgator Engineering 49

[ { "id": "BioInfer.d571.s0__text", "type": "Sentence", "text": [ "The aim of our study on human seminiferous tubules of adolescent testes was to study the localization of two actin-associated proteins of the adherens junctions, such as vinculin and talin, and to verify if there were modifications in their pattern in varicocele, a frequent disease of the testis in adolescent age." ], "offsets": [ [ 0, 315 ] ] } ]

[ { "id": "BioInfer.d571.s0.e0", "type": "Individual_protein", "text": [ "vinculin" ], "offsets": [ [ 170, 178 ] ], "normalized": [] }, { "id": "BioInfer.d571.s0.e1", "type": "Individual_protein", "text": [ "talin" ], "offsets": [ [ 183, 188 ] ], "normalized": [] }, { "id": "BioInfer.d571.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 109, 114 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d571.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d571.s0.e0", "arg2_id": "BioInfer.d571.s0.e2", "normalized": [] }, { "id": "BioInfer.d571.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d571.s0.e1", "arg2_id": "BioInfer.d571.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d573.s0__text", "type": "Sentence", "text": [ "The amount of unassembled actin (12 microM) is accounted for by the sequestering functions of T beta 4Xen (20 microM) and profilin (5 microM), the barbed ends being capped." ], "offsets": [ [ 0, 172 ] ] } ]

[ { "id": "BioInfer.d573.s0.e0", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 122, 130 ] ], "normalized": [] }, { "id": "BioInfer.d573.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 26, 31 ] ], "normalized": [] }, { "id": "BioInfer.d573.s0.e2", "type": "Individual_protein", "text": [ "T beta 4Xen" ], "offsets": [ [ 94, 105 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d573.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d573.s0.e0", "arg2_id": "BioInfer.d573.s0.e1", "normalized": [] }, { "id": "BioInfer.d573.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d573.s0.e1", "arg2_id": "BioInfer.d573.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d574.s0__text", "type": "Sentence", "text": [ "The analysis of the viral proteins by electrophoresis indicates molecular weight differences between CDV and PDV in the fusion (F), phosphoprotein (P), H, nucleocapsid (N) and matrix (M) proteins." ], "offsets": [ [ 0, 196 ] ] } ]

[ { "id": "BioInfer.d574.s0.e0", "type": "Individual_protein", "text": [ "M" ], "offsets": [ [ 184, 185 ] ], "normalized": [] }, { "id": "BioInfer.d574.s0.e1", "type": "Individual_protein", "text": [ "F" ], "offsets": [ [ 128, 129 ] ], "normalized": [] }, { "id": "BioInfer.d574.s0.e2", "type": "Individual_protein", "text": [ "nucleocapsid", "proteins" ], "offsets": [ [ 155, 167 ], [ 187, 195 ] ], "normalized": [] }, { "id": "BioInfer.d574.s0.e3", "type": "Individual_protein", "text": [ "P" ], "offsets": [ [ 148, 149 ] ], "normalized": [] }, { "id": "BioInfer.d574.s0.e4", "type": "Individual_protein", "text": [ "N" ], "offsets": [ [ 169, 170 ] ], "normalized": [] }, { "id": "BioInfer.d574.s0.e5", "type": "Gene/protein/RNA", "text": [ "H", "proteins" ], "offsets": [ [ 152, 153 ], [ 187, 195 ] ], "normalized": [] }, { "id": "BioInfer.d574.s0.e6", "type": "Individual_protein", "text": [ "fusion", "proteins" ], "offsets": [ [ 120, 126 ], [ 187, 195 ] ], "normalized": [] }, { "id": "BioInfer.d574.s0.e7", "type": "Individual_protein", "text": [ "matrix", "proteins" ], "offsets": [ [ 176, 182 ], [ 187, 195 ] ], "normalized": [] }, { "id": "BioInfer.d574.s0.e8", "type": "Individual_protein", "text": [ "phosphoprotein", "proteins" ], "offsets": [ [ 132, 146 ], [ 187, 195 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d575.s0__text", "type": "Sentence", "text": [ "The APC binding site on beta-catenin may be discontinuous since neither the carboxyl- nor amino-terminal halves of beta-catenin will independently associate with APC, although the amino-terminal half independently binds alpha-catenin." ], "offsets": [ [ 0, 234 ] ] } ]

[ { "id": "BioInfer.d575.s0.e0", "type": "Individual_protein", "text": [ "APC" ], "offsets": [ [ 4, 7 ] ], "normalized": [] }, { "id": "BioInfer.d575.s0.e1", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 220, 233 ] ], "normalized": [] }, { "id": "BioInfer.d575.s0.e2", "type": "Individual_protein", "text": [ "APC" ], "offsets": [ [ 162, 165 ] ], "normalized": [] }, { "id": "BioInfer.d575.s0.e3", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 24, 36 ] ], "normalized": [] }, { "id": "BioInfer.d575.s0.e4", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 115, 127 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d575.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d575.s0.e0", "arg2_id": "BioInfer.d575.s0.e3", "normalized": [] }, { "id": "BioInfer.d575.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d575.s0.e1", "arg2_id": "BioInfer.d575.s0.e4", "normalized": [] }, { "id": "BioInfer.d575.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d575.s0.e2", "arg2_id": "BioInfer.d575.s0.e4", "normalized": [] } ]

[ { "id": "BioInfer.d575.s1__text", "type": "Sentence", "text": [ "The APC protein and E-cadherin form similar but independent complexes with alpha-catenin, beta-catenin, and plakoglobin." ], "offsets": [ [ 0, 120 ] ] } ]

[ { "id": "BioInfer.d575.s1.e0", "type": "Individual_protein", "text": [ "E-cadherin" ], "offsets": [ [ 20, 30 ] ], "normalized": [] }, { "id": "BioInfer.d575.s1.e1", "type": "Individual_protein", "text": [ "APC" ], "offsets": [ [ 4, 7 ] ], "normalized": [] }, { "id": "BioInfer.d575.s1.e2", "type": "Individual_protein", "text": [ "plakoglobin" ], "offsets": [ [ 108, 119 ] ], "normalized": [] }, { "id": "BioInfer.d575.s1.e3", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 75, 88 ] ], "normalized": [] }, { "id": "BioInfer.d575.s1.e4", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 90, 102 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d575.s2__text", "type": "Sentence", "text": [ "Thus, APC forms distinct heteromeric complexes containing combinations of alpha-catenin, beta-catenin, and plakoglobin which are independent from the cadherin-catenin complexes." ], "offsets": [ [ 0, 177 ] ] } ]

[ { "id": "BioInfer.d575.s2.e0", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 89, 101 ] ], "normalized": [] }, { "id": "BioInfer.d575.s2.e1", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 74, 87 ] ], "normalized": [] }, { "id": "BioInfer.d575.s2.e2", "type": "Individual_protein", "text": [ "plakoglobin" ], "offsets": [ [ 107, 118 ] ], "normalized": [] }, { "id": "BioInfer.d575.s2.e3", "type": "Individual_protein", "text": [ "cadherin" ], "offsets": [ [ 150, 158 ] ], "normalized": [] }, { "id": "BioInfer.d575.s2.e4", "type": "Individual_protein", "text": [ "APC" ], "offsets": [ [ 6, 9 ] ], "normalized": [] }, { "id": "BioInfer.d575.s2.e5", "type": "Individual_protein", "text": [ "catenin" ], "offsets": [ [ 159, 166 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d576.s0__text", "type": "Sentence", "text": [ "The Arp2/3 complex, first isolated from Acanthamoeba castellani by affinity chromatography on profilin, consists of seven polypeptides; two actin-related proteins, Arp2 and Arp3; and five apparently novel proteins, p40, p35, p19, p18, and p14 (Machesky et al., 1994)." ], "offsets": [ [ 0, 267 ] ] } ]

[ { "id": "BioInfer.d576.s0.e0", "type": "Individual_protein", "text": [ "p18" ], "offsets": [ [ 230, 233 ] ], "normalized": [] }, { "id": "BioInfer.d576.s0.e1", "type": "Individual_protein", "text": [ "p14" ], "offsets": [ [ 239, 242 ] ], "normalized": [] }, { "id": "BioInfer.d576.s0.e2", "type": "Individual_protein", "text": [ "Arp2" ], "offsets": [ [ 4, 8 ] ], "normalized": [] }, { "id": "BioInfer.d576.s0.e3", "type": "Individual_protein", "text": [ "Arp", "3" ], "offsets": [ [ 4, 7 ], [ 9, 10 ] ], "normalized": [] }, { "id": "BioInfer.d576.s0.e4", "type": "Individual_protein", "text": [ "p35" ], "offsets": [ [ 220, 223 ] ], "normalized": [] }, { "id": "BioInfer.d576.s0.e5", "type": "Individual_protein", "text": [ "Arp3" ], "offsets": [ [ 173, 177 ] ], "normalized": [] }, { "id": "BioInfer.d576.s0.e6", "type": "Individual_protein", "text": [ "p40" ], "offsets": [ [ 215, 218 ] ], "normalized": [] }, { "id": "BioInfer.d576.s0.e7", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 140, 145 ] ], "normalized": [] }, { "id": "BioInfer.d576.s0.e8", "type": "Gene/protein/RNA", "text": [ "profilin" ], "offsets": [ [ 94, 102 ] ], "normalized": [] }, { "id": "BioInfer.d576.s0.e9", "type": "Individual_protein", "text": [ "p19" ], "offsets": [ [ 225, 228 ] ], "normalized": [] }, { "id": "BioInfer.d576.s0.e10", "type": "Individual_protein", "text": [ "Arp2" ], "offsets": [ [ 164, 168 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d577.s0__text", "type": "Sentence", "text": [ "The Arp2/3 complex with full-length Scar, Scar containing P, W, and A domains, or Scar containing W and A domains overcomes inhibition of nucleation by the actin monomer-binding protein profilin, giving active nucleation over a low background of spontaneous nucleation." ], "offsets": [ [ 0, 269 ] ] } ]

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[ { "id": "BioInfer.d579.s0__text", "type": "Sentence", "text": [ "The assembly of complete HSV replication compartments and incorporation of BrdU were both abolished by treatment with phosphonoacetic acid (PAA) and by omission of any one of the seven viral replication proteins, UL5, UL8, UL9, UL42, UL52, SSB, and Pol, that are essential for viral DNA replication." ], "offsets": [ [ 0, 299 ] ] } ]

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[ { "id": "BioInfer.d580.s0__text", "type": "Sentence", "text": [ "The UL8 component of the herpes simplex virus helicase-primase complex stimulates primer synthesis by a subassembly of the UL5 and UL52 components." ], "offsets": [ [ 0, 147 ] ] } ]

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[ { "id": "BioInfer.d580.s1__text", "type": "Sentence", "text": [ "The herpes simplex virus type 1 (HSV) UL5, UL8, and UL52 proteins form a helicase-primase complex in infected cells." ], "offsets": [ [ 0, 116 ] ] } ]

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[ { "id": "BioInfer.d581.s0__text", "type": "Sentence", "text": [ "The adenosine deaminase-binding region is distinct from major anti-CD26 mAb epitopes on the human dipeptidyl peptidase IV(CD26) molecule." ], "offsets": [ [ 0, 137 ] ] } ]

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[ { "id": "BioInfer.d581.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d581.s0.e1", "arg2_id": "BioInfer.d581.s0.e2", "normalized": [] }, { "id": "BioInfer.d581.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d581.s0.e2", "arg2_id": "BioInfer.d581.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d583.s0__text", "type": "Sentence", "text": [ "The binding surfaces for segment 1 and profilin are different, although they peripherally overlap on actin." ], "offsets": [ [ 0, 107 ] ] } ]

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[ { "id": "BioInfer.d583.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d583.s0.e0", "arg2_id": "BioInfer.d583.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d583.s1__text", "type": "Sentence", "text": [ "This review describes three structures of actin complexed with different monomer-binding proteins, namely with DNase I, gelsolin segment 1, and profilin." ], "offsets": [ [ 0, 153 ] ] } ]

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[ { "id": "BioInfer.d583.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d583.s1.e0", "arg2_id": "BioInfer.d583.s1.e1", "normalized": [] }, { "id": "BioInfer.d583.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d583.s1.e0", "arg2_id": "BioInfer.d583.s1.e2", "normalized": [] }, { "id": "BioInfer.d583.s1.i2", "type": "PPI", "arg1_id": "BioInfer.d583.s1.e0", "arg2_id": "BioInfer.d583.s1.e3", "normalized": [] } ]

[ { "id": "BioInfer.d584.s0__text", "type": "Sentence", "text": [ "The myosin heavy chain (MHC) contains the actin- and ATP-binding sites and represents the molecular motor of muscle contraction." ], "offsets": [ [ 0, 128 ] ] } ]

[ { "id": "BioInfer.d584.s0.e0", "type": "Individual_protein", "text": [ "myosin heavy chain" ], "offsets": [ [ 4, 22 ] ], "normalized": [] }, { "id": "BioInfer.d584.s0.e1", "type": "Individual_protein", "text": [ "MHC" ], "offsets": [ [ 24, 27 ] ], "normalized": [] }, { "id": "BioInfer.d584.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 42, 47 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d584.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d584.s0.e0", "arg2_id": "BioInfer.d584.s0.e2", "normalized": [] }, { "id": "BioInfer.d584.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d584.s0.e1", "arg2_id": "BioInfer.d584.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d586.s0__text", "type": "Sentence", "text": [ "The RAD54 and RAD51 genes are involved in genetic recombination and double-strand break repair in the yeast Saccharomyces cerevisiae." ], "offsets": [ [ 0, 133 ] ] } ]

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[ { "id": "BioInfer.d587.s0__text", "type": "Sentence", "text": [ "The verprolin-like central (vc) region of Wiskott-Aldrich syndrome protein induces Arp2/3 complex-dependent actin nucleation." ], "offsets": [ [ 0, 125 ] ] } ]

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[ { "id": "BioInfer.d587.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d587.s0.e0", "arg2_id": "BioInfer.d587.s0.e2", "normalized": [] }, { "id": "BioInfer.d587.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d587.s0.e0", "arg2_id": "BioInfer.d587.s0.e3", "normalized": [] }, { "id": "BioInfer.d587.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d587.s0.e0", "arg2_id": "BioInfer.d587.s0.e4", "normalized": [] }, { "id": "BioInfer.d587.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d587.s0.e1", "arg2_id": "BioInfer.d587.s0.e4", "normalized": [] }, { "id": "BioInfer.d587.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d587.s0.e2", "arg2_id": "BioInfer.d587.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d588.s0__text", "type": "Sentence", "text": [ "The C374S mutation had the most pronounced effect; it reduced the polymerizability of the actin, abolished its binding to profilin, and filaments containing this mutation moved at reduced rates in the in vitro 'motility assay'." ], "offsets": [ [ 0, 227 ] ] } ]

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[ { "id": "BioInfer.d588.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d588.s0.e0", "arg2_id": "BioInfer.d588.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d590.s0__text", "type": "Sentence", "text": [ "The cardiac myosin heavy chain Arg-403-->Gln mutation that causes hypertrophic cardiomyopathy does not affect the actin- or ATP-binding capacities of two size-limited recombinant myosin heavy chain fragments." ], "offsets": [ [ 0, 208 ] ] } ]

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[ { "id": "BioInfer.d590.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d590.s0.e0", "arg2_id": "BioInfer.d590.s0.e1", "normalized": [] }, { "id": "BioInfer.d590.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d590.s0.e0", "arg2_id": "BioInfer.d590.s0.e2", "normalized": [] }, { "id": "BioInfer.d590.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d590.s0.e1", "arg2_id": "BioInfer.d590.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d591.s0__text", "type": "Sentence", "text": [ "The cellular morphological changes were analyzed and correlated with the distribution of cell-substratum contacts viewed by confocal images obtained after immunostaining with antibodies raised against the fibronectin receptor, talin, vinculin and actin." ], "offsets": [ [ 0, 253 ] ] } ]

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[ { "id": "BioInfer.d592.s0__text", "type": "Sentence", "text": [ "The cellular transcription co-activators p300 and the CREB-binding protein CBP are cellular targets for transformation by the E1A proteins of non-oncogenic adenovirus 5 (Ad5)." ], "offsets": [ [ 0, 175 ] ] } ]

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[ { "id": "BioInfer.d595.s0__text", "type": "Sentence", "text": [ "The common denominator is impaired beta-catenin association with either E-cadherin (PaTuII) or alpha-catenin (BxPc3 and T3M4)." ], "offsets": [ [ 0, 126 ] ] } ]

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[ { "id": "BioInfer.d595.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d595.s0.e0", "arg2_id": "BioInfer.d595.s0.e1", "normalized": [] }, { "id": "BioInfer.d595.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d595.s0.e0", "arg2_id": "BioInfer.d595.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d596.s0__text", "type": "Sentence", "text": [ "The comparison of E-CD proteins synthesized by E62 and E24 cell lines revealed no structural or functional differences because both localized at cell-cell contacts and associated with alpha-catenin, beta-catenin, and plakoglobin." ], "offsets": [ [ 0, 229 ] ] } ]

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[ { "id": "BioInfer.d596.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d596.s0.e0", "arg2_id": "BioInfer.d596.s0.e1", "normalized": [] }, { "id": "BioInfer.d596.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d596.s0.e0", "arg2_id": "BioInfer.d596.s0.e2", "normalized": [] }, { "id": "BioInfer.d596.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d596.s0.e0", "arg2_id": "BioInfer.d596.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d597.s0__text", "type": "Sentence", "text": [ "The concentration of beta-catenin was constant during the follicular phase, whereas the content of alpha-catenin decreased in granulosa cells after treatment with diethylstilboestrol or hCG." ], "offsets": [ [ 0, 190 ] ] } ]

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[ { "id": "BioInfer.d597.s1__text", "type": "Sentence", "text": [ "alpha- and beta-catenin were present in most ovarian cells at all stages of folliculogenesis." ], "offsets": [ [ 0, 93 ] ] } ]

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[ { "id": "BioInfer.d599.s0__text", "type": "Sentence", "text": [ "The core histones from Physarum, histones H2A, H2B, H3, and H4, are rapidly acetylated; histone H4 shows five subfractions, analogous to the five subfractions of mammalian histone H4 (containing zero to four acetyllysine residues per molecule); histone H3 has a more complex pattern that we interpret as zero to four acetyllysine residues on each of two sequence variants of histone H3; histones H2A and H2B show less heterogeneity." ], "offsets": [ [ 0, 432 ] ] } ]

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[ { "id": "BioInfer.d602.s0__text", "type": "Sentence", "text": [ "The C-terminal region of ORC3 was, however, necessary to bring ORC4 and ORC5 into the core complex." ], "offsets": [ [ 0, 99 ] ] } ]

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[ { "id": "BioInfer.d603.s0__text", "type": "Sentence", "text": [ "The cytoplasmic domain of E-cadherin cannot directly associate with alpha-catenin but interacts with high affinity with beta-catenin, whereas the binding of gamma-catenin (plakoglobin) to E-cadherin is less efficient." ], "offsets": [ [ 0, 217 ] ] } ]

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[ { "id": "BioInfer.d603.s1__text", "type": "Sentence", "text": [ "alpha- and beta-catenin assemble into a 1:1 heterodimeric complex." ], "offsets": [ [ 0, 66 ] ] } ]

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[ { "id": "BioInfer.d604.s0__text", "type": "Sentence", "text": [ "The deduced peptide sequence contained a nuclear localization signal and a putative actin-binding sequence as reported in NM-type cofilin." ], "offsets": [ [ 0, 138 ] ] } ]

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[ { "id": "BioInfer.d605.s0__text", "type": "Sentence", "text": [ "The domain consists of a mixed alpha-helical/beta-sheet fold that resembles a circular permutation of the actin/poly-proline binding protein, profilin, and the GAF/PAS family of regulatory modules." ], "offsets": [ [ 0, 197 ] ] } ]

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[ { "id": "BioInfer.d606.s0__text", "type": "Sentence", "text": [ "The domains in CBP that are involved in CREB binding and transcriptional activation are highly related to the adenoviral E1A-associated cellular protein p300 (refs 2, 3), and to two hypothetical proteins from Caenorhabditis elegans, R10E11.1 and K03H1.10 (refs 4 and 5, respectively), whose functions are unknown." ], "offsets": [ [ 0, 313 ] ] } ]

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[ { "id": "BioInfer.d607.s0__text", "type": "Sentence", "text": [ "The drastic effects of the exogenous cofilin on actin assembly were suppressed by phosphatidylinositol 4,5-bisphosphate (PIP2)." ], "offsets": [ [ 0, 127 ] ] } ]

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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[ { "id": "BioInfer.d622.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d622.s0.e0", "arg2_id": "BioInfer.d622.s0.e3", "normalized": [] }, { "id": "BioInfer.d622.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d622.s0.e1", "arg2_id": "BioInfer.d622.s0.e3", "normalized": [] }, { "id": "BioInfer.d622.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d622.s0.e2", "arg2_id": "BioInfer.d622.s0.e3", "normalized": [] } ]

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

[ { "id": "BioInfer.d623.s0.e0", "type": "Gene/protein/RNA", "text": [ "profilin" ], "offsets": [ [ 247, 255 ] ], "normalized": [] }, { "id": "BioInfer.d623.s0.e1", "type": "Gene/protein/RNA", "text": [ "profilin" ], "offsets": [ [ 157, 165 ] ], "normalized": [] }, { "id": "BioInfer.d623.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 98, 103 ] ], "normalized": [] }, { "id": "BioInfer.d623.s0.e3", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 32, 40 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d623.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d623.s0.e2", "arg2_id": "BioInfer.d623.s0.e3", "normalized": [] } ]

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

[ { "id": "BioInfer.d623.s1.e0", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 135, 143 ] ], "normalized": [] }, { "id": "BioInfer.d623.s1.e1", "type": "Individual_protein", "text": [ "profilins" ], "offsets": [ [ 93, 102 ] ], "normalized": [] }, { "id": "BioInfer.d623.s1.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 185, 190 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d623.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d623.s1.e0", "arg2_id": "BioInfer.d623.s1.e2", "normalized": [] } ]

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

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

[ { "id": "BioInfer.d625.s0.e0", "type": "Protein_family_or_group", "text": [ "cyclin dependent kinase inhibitor" ], "offsets": [ [ 247, 280 ] ], "normalized": [] }, { "id": "BioInfer.d625.s0.e1", "type": "Individual_protein", "text": [ "p27kip1" ], "offsets": [ [ 281, 288 ] ], "normalized": [] }, { "id": "BioInfer.d625.s0.e2", "type": "Gene/protein/RNA", "text": [ "p53" ], "offsets": [ [ 211, 214 ] ], "normalized": [] }, { "id": "BioInfer.d625.s0.e3", "type": "Individual_protein", "text": [ "p16ink4a" ], "offsets": [ [ 195, 203 ] ], "normalized": [] }, { "id": "BioInfer.d625.s0.e4", "type": "Protein_family_or_group", "text": [ "cyclin dependent kinase inhibitor" ], "offsets": [ [ 161, 194 ] ], "normalized": [] }, { "id": "BioInfer.d625.s0.e5", "type": "Gene/protein/RNA", "text": [ "cyclin D1" ], "offsets": [ [ 146, 155 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d625.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d625.s0.e0", "arg2_id": "BioInfer.d625.s0.e1", "normalized": [] }, { "id": "BioInfer.d625.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d625.s0.e3", "arg2_id": "BioInfer.d625.s0.e4", "normalized": [] } ]

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

[ { "id": "BioInfer.d627.s0.e0", "type": "Protein_family_or_group", "text": [ "collagens" ], "offsets": [ [ 23, 32 ] ], "normalized": [] }, { "id": "BioInfer.d627.s0.e1", "type": "Individual_protein", "text": [ "vimentin" ], "offsets": [ [ 91, 99 ] ], "normalized": [] }, { "id": "BioInfer.d627.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 84, 89 ] ], "normalized": [] }, { "id": "BioInfer.d627.s0.e3", "type": "Individual_protein", "text": [ "vinculin" ], "offsets": [ [ 112, 120 ] ], "normalized": [] }, { "id": "BioInfer.d627.s0.e4", "type": "Individual_protein", "text": [ "talin" ], "offsets": [ [ 101, 106 ] ], "normalized": [] } ]

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

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

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

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

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

[ { "id": "BioInfer.d639.s0.e0", "type": "Protein_family_or_group", "text": [ "CDKI" ], "offsets": [ [ 72, 76 ] ], "normalized": [] }, { "id": "BioInfer.d639.s0.e1", "type": "Individual_protein", "text": [ "cyclin-dependent kinase 2" ], "offsets": [ [ 121, 146 ] ], "normalized": [] }, { "id": "BioInfer.d639.s0.e2", "type": "Individual_protein", "text": [ "p27" ], "offsets": [ [ 30, 33 ] ], "normalized": [] }, { "id": "BioInfer.d639.s0.e3", "type": "Individual_protein", "text": [ "Cdk2" ], "offsets": [ [ 148, 152 ] ], "normalized": [] }, { "id": "BioInfer.d639.s0.e4", "type": "Protein_family_or_group", "text": [ "cyclin-dependent kinase inhibitor" ], "offsets": [ [ 37, 70 ] ], "normalized": [] }, { "id": "BioInfer.d639.s0.e5", "type": "Individual_protein", "text": [ "cyclin E" ], "offsets": [ [ 112, 120 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d639.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d639.s0.e0", "arg2_id": "BioInfer.d639.s0.e2", "normalized": [] }, { "id": "BioInfer.d639.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d639.s0.e1", "arg2_id": "BioInfer.d639.s0.e2", "normalized": [] }, { "id": "BioInfer.d639.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d639.s0.e1", "arg2_id": "BioInfer.d639.s0.e3", "normalized": [] }, { "id": "BioInfer.d639.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d639.s0.e1", "arg2_id": "BioInfer.d639.s0.e5", "normalized": [] }, { "id": "BioInfer.d639.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d639.s0.e2", "arg2_id": "BioInfer.d639.s0.e3", "normalized": [] }, { "id": "BioInfer.d639.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d639.s0.e2", "arg2_id": "BioInfer.d639.s0.e4", "normalized": [] }, { "id": "BioInfer.d639.s0.i6", "type": "PPI", "arg1_id": "BioInfer.d639.s0.e2", "arg2_id": "BioInfer.d639.s0.e5", "normalized": [] }, { "id": "BioInfer.d639.s0.i7", "type": "PPI", "arg1_id": "BioInfer.d639.s0.e3", "arg2_id": "BioInfer.d639.s0.e5", "normalized": [] } ]

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

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

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[ { "id": "BioInfer.d641.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d641.s0.e0", "arg2_id": "BioInfer.d641.s0.e1", "normalized": [] } ]

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

[ { "id": "BioInfer.d644.s0.e0", "type": "Individual_protein", "text": [ "villin" ], "offsets": [ [ 177, 183 ] ], "normalized": [] }, { "id": "BioInfer.d644.s0.e1", "type": "Individual_protein", "text": [ "calmodulin" ], "offsets": [ [ 256, 266 ] ], "normalized": [] }, { "id": "BioInfer.d644.s0.e2", "type": "Individual_protein", "text": [ "fimbrin" ], "offsets": [ [ 202, 209 ] ], "normalized": [] }, { "id": "BioInfer.d644.s0.e3", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 228, 233 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d644.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d644.s0.e0", "arg2_id": "BioInfer.d644.s0.e1", "normalized": [] }, { "id": "BioInfer.d644.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d644.s0.e0", "arg2_id": "BioInfer.d644.s0.e2", "normalized": [] }, { "id": "BioInfer.d644.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d644.s0.e0", "arg2_id": "BioInfer.d644.s0.e3", "normalized": [] }, { "id": "BioInfer.d644.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d644.s0.e1", "arg2_id": "BioInfer.d644.s0.e2", "normalized": [] }, { "id": "BioInfer.d644.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d644.s0.e1", "arg2_id": "BioInfer.d644.s0.e3", "normalized": [] }, { "id": "BioInfer.d644.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d644.s0.e2", "arg2_id": "BioInfer.d644.s0.e3", "normalized": [] } ]

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

[ { "id": "BioInfer.d645.s0.e0", "type": "Protein_family_or_group", "text": [ "actin-binding protein" ], "offsets": [ [ 14, 35 ] ], "normalized": [] }, { "id": "BioInfer.d645.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 69, 74 ] ], "normalized": [] }, { "id": "BioInfer.d645.s0.e2", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 37, 45 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d645.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d645.s0.e0", "arg2_id": "BioInfer.d645.s0.e2", "normalized": [] }, { "id": "BioInfer.d645.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d645.s0.e1", "arg2_id": "BioInfer.d645.s0.e2", "normalized": [] } ]

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

[ { "id": "BioInfer.d646.s0.e0", "type": "Gene/protein/RNA", "text": [ "gamma-catenin" ], "offsets": [ [ 132, 145 ] ], "normalized": [] }, { "id": "BioInfer.d646.s0.e1", "type": "Gene/protein/RNA", "text": [ "alpha-catenin" ], "offsets": [ [ 66, 79 ] ], "normalized": [] }, { "id": "BioInfer.d646.s0.e2", "type": "Gene/protein/RNA", "text": [ "beta-catenin" ], "offsets": [ [ 85, 97 ] ], "normalized": [] }, { "id": "BioInfer.d646.s0.e3", "type": "Gene/protein/RNA", "text": [ "E-cadherin" ], "offsets": [ [ 54, 64 ] ], "normalized": [] } ]

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

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[ { "id": "BioInfer.d647.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d647.s0.e0", "arg2_id": "BioInfer.d647.s0.e2", "normalized": [] }, { "id": "BioInfer.d647.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d647.s0.e1", "arg2_id": "BioInfer.d647.s0.e8", "normalized": [] }, { "id": "BioInfer.d647.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d647.s0.e3", "arg2_id": "BioInfer.d647.s0.e5", "normalized": [] }, { "id": "BioInfer.d647.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d647.s0.e3", "arg2_id": "BioInfer.d647.s0.e6", "normalized": [] }, { "id": "BioInfer.d647.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d647.s0.e3", "arg2_id": "BioInfer.d647.s0.e9", "normalized": [] }, { "id": "BioInfer.d647.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d647.s0.e4", "arg2_id": "BioInfer.d647.s0.e7", "normalized": [] }, { "id": "BioInfer.d647.s0.i6", "type": "PPI", "arg1_id": "BioInfer.d647.s0.e5", "arg2_id": "BioInfer.d647.s0.e8", "normalized": [] }, { "id": "BioInfer.d647.s0.i7", "type": "PPI", "arg1_id": "BioInfer.d647.s0.e6", "arg2_id": "BioInfer.d647.s0.e8", "normalized": [] } ]

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

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[ { "id": "BioInfer.d648.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d648.s0.e0", "arg2_id": "BioInfer.d648.s0.e1", "normalized": [] } ]

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

[ { "id": "BioInfer.d649.s0.e0", "type": "Gene/protein/RNA", "text": [ "calcium vector protein" ], "offsets": [ [ 166, 188 ] ], "normalized": [] }, { "id": "BioInfer.d649.s0.e1", "type": "Gene/protein/RNA", "text": [ "myosin heavy chain" ], "offsets": [ [ 124, 142 ] ], "normalized": [] }, { "id": "BioInfer.d649.s0.e2", "type": "Gene/protein/RNA", "text": [ "calmodulin" ], "offsets": [ [ 144, 154 ] ], "normalized": [] }, { "id": "BioInfer.d649.s0.e3", "type": "Gene/protein/RNA", "text": [ "myosin regulatory light chain" ], "offsets": [ [ 66, 95 ] ], "normalized": [] }, { "id": "BioInfer.d649.s0.e4", "type": "Gene/protein/RNA", "text": [ "myosin light chain kinase" ], "offsets": [ [ 97, 122 ] ], "normalized": [] }, { "id": "BioInfer.d649.s0.e5", "type": "Gene/protein/RNA", "text": [ "tropomyosin" ], "offsets": [ [ 41, 52 ] ], "normalized": [] }, { "id": "BioInfer.d649.s0.e6", "type": "Gene/protein/RNA", "text": [ "troponin I" ], "offsets": [ [ 54, 64 ] ], "normalized": [] }, { "id": "BioInfer.d649.s0.e7", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 34, 39 ] ], "normalized": [] }, { "id": "BioInfer.d649.s0.e8", "type": "Gene/protein/RNA", "text": [ "muscle LIM" ], "offsets": [ [ 207, 217 ] ], "normalized": [] }, { "id": "BioInfer.d649.s0.e9", "type": "Gene/protein/RNA", "text": [ "calponin" ], "offsets": [ [ 156, 164 ] ], "normalized": [] }, { "id": "BioInfer.d649.s0.e10", "type": "Gene/protein/RNA", "text": [ "SH3-binding glutamate-rich protein" ], "offsets": [ [ 231, 265 ] ], "normalized": [] }, { "id": "BioInfer.d649.s0.e11", "type": "Gene/protein/RNA", "text": [ "creatine kinase" ], "offsets": [ [ 190, 205 ] ], "normalized": [] } ]

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

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[ { "id": "BioInfer.d650.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d650.s0.e0", "arg2_id": "BioInfer.d650.s0.e2", "normalized": [] } ]

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

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

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

[ { "id": "BioInfer.d650.s2.e0", "type": "Gene/protein/RNA", "text": [ "profilins" ], "offsets": [ [ 5, 14 ] ], "normalized": [] }, { "id": "BioInfer.d650.s2.e1", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 174, 179 ] ], "normalized": [] }, { "id": "BioInfer.d650.s2.e2", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 79, 84 ] ], "normalized": [] } ]

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

[ { "id": "BioInfer.d651.s0.e0", "type": "Gene/protein/RNA", "text": [ "smooth muscle myosin heavy chain" ], "offsets": [ [ 167, 199 ] ], "normalized": [] }, { "id": "BioInfer.d651.s0.e1", "type": "Gene/protein/RNA", "text": [ "S-100" ], "offsets": [ [ 231, 236 ] ], "normalized": [] }, { "id": "BioInfer.d651.s0.e2", "type": "Gene/protein/RNA", "text": [ "vimentin" ], "offsets": [ [ 39, 47 ] ], "normalized": [] }, { "id": "BioInfer.d651.s0.e3", "type": "Gene/protein/RNA", "text": [ "alpha-smooth muscle actin" ], "offsets": [ [ 63, 88 ] ], "normalized": [] }, { "id": "BioInfer.d651.s0.e4", "type": "Gene/protein/RNA", "text": [ "Factor-XIIIa" ], "offsets": [ [ 49, 61 ] ], "normalized": [] }, { "id": "BioInfer.d651.s0.e5", "type": "Gene/protein/RNA", "text": [ "desmin" ], "offsets": [ [ 116, 122 ] ], "normalized": [] }, { "id": "BioInfer.d651.s0.e6", "type": "Gene/protein/RNA", "text": [ "CD34" ], "offsets": [ [ 93, 97 ] ], "normalized": [] }, { "id": "BioInfer.d651.s0.e7", "type": "Gene/protein/RNA", "text": [ "high molecular weight caldesmon" ], "offsets": [ [ 134, 165 ] ], "normalized": [] }, { "id": "BioInfer.d651.s0.e8", "type": "Gene/protein/RNA", "text": [ "calponin" ], "offsets": [ [ 124, 132 ] ], "normalized": [] }, { "id": "BioInfer.d651.s0.e9", "type": "Gene/protein/RNA", "text": [ "collagen type IV" ], "offsets": [ [ 201, 217 ] ], "normalized": [] }, { "id": "BioInfer.d651.s0.e10", "type": "Gene/protein/RNA", "text": [ "laminin" ], "offsets": [ [ 219, 226 ] ], "normalized": [] } ]

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

[]

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

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

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

[]

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