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BigScience Biomedical Datasets 123

[ { "id": "BioInfer.d721.s0__text", "type": "Sentence", "text": [ "The sizes and characteristics of each of the proteins determined from various radiolabelling experiments allowed preliminary identification of the proteins as the large (L; 190 kDa), haemagglutinin neuraminidase (HN; 74 kDa), nucleocapsid (N; 66 kDa), fusion (F0; 63 kDa), phosphoprotein (P; 49 kDa), matrix (M; 43 kDa) and non-structural (V; 35 kDa) proteins." ], "offsets": [ [ 0, 360 ] ] } ]

[ { "id": "BioInfer.d721.s0.e0", "type": "Individual_protein", "text": [ "L" ], "offsets": [ [ 170, 171 ] ], "normalized": [] }, { "id": "BioInfer.d721.s0.e1", "type": "Individual_protein", "text": [ "F0" ], "offsets": [ [ 260, 262 ] ], "normalized": [] }, { "id": "BioInfer.d721.s0.e2", "type": "Individual_protein", "text": [ "fusion", "proteins" ], "offsets": [ [ 252, 258 ], [ 351, 359 ] ], "normalized": [] }, { "id": "BioInfer.d721.s0.e3", "type": "Individual_protein", "text": [ "non-structural", "proteins" ], "offsets": [ [ 324, 338 ], [ 351, 359 ] ], "normalized": [] }, { "id": "BioInfer.d721.s0.e4", "type": "Individual_protein", "text": [ "matrix", "proteins" ], "offsets": [ [ 301, 307 ], [ 351, 359 ] ], "normalized": [] }, { "id": "BioInfer.d721.s0.e5", "type": "Individual_protein", "text": [ "HN" ], "offsets": [ [ 213, 215 ] ], "normalized": [] }, { "id": "BioInfer.d721.s0.e6", "type": "Individual_protein", "text": [ "large", "proteins" ], "offsets": [ [ 163, 168 ], [ 351, 359 ] ], "normalized": [] }, { "id": "BioInfer.d721.s0.e7", "type": "Individual_protein", "text": [ "nucleocapsid", "proteins" ], "offsets": [ [ 226, 238 ], [ 351, 359 ] ], "normalized": [] }, { "id": "BioInfer.d721.s0.e8", "type": "Individual_protein", "text": [ "haemagglutinin neuraminidase", "proteins" ], "offsets": [ [ 183, 211 ], [ 351, 359 ] ], "normalized": [] }, { "id": "BioInfer.d721.s0.e9", "type": "Individual_protein", "text": [ "phosphoprotein", "proteins" ], "offsets": [ [ 273, 287 ], [ 351, 359 ] ], "normalized": [] }, { "id": "BioInfer.d721.s0.e10", "type": "Individual_protein", "text": [ "P" ], "offsets": [ [ 289, 290 ] ], "normalized": [] }, { "id": "BioInfer.d721.s0.e11", "type": "Individual_protein", "text": [ "V" ], "offsets": [ [ 340, 341 ] ], "normalized": [] }, { "id": "BioInfer.d721.s0.e12", "type": "Individual_protein", "text": [ "N" ], "offsets": [ [ 240, 241 ] ], "normalized": [] }, { "id": "BioInfer.d721.s0.e13", "type": "Individual_protein", "text": [ "M" ], "offsets": [ [ 309, 310 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d722.s0__text", "type": "Sentence", "text": [ "The Src homology domain 3 (SH3) of a yeast type I myosin, Myo5p, binds to verprolin and is required for targeting to sites of actin polarization." ], "offsets": [ [ 0, 145 ] ] } ]

[ { "id": "BioInfer.d722.s0.e0", "type": "Individual_protein", "text": [ "verprolin" ], "offsets": [ [ 74, 83 ] ], "normalized": [] }, { "id": "BioInfer.d722.s0.e1", "type": "Individual_protein", "text": [ "Myo5p" ], "offsets": [ [ 58, 63 ] ], "normalized": [] }, { "id": "BioInfer.d722.s0.e2", "type": "Individual_protein", "text": [ "type I myosin" ], "offsets": [ [ 43, 56 ] ], "normalized": [] }, { "id": "BioInfer.d722.s0.e3", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 126, 131 ] ], "normalized": [] }, { "id": "BioInfer.d722.s0.e4", "type": "Individual_protein", "text": [ "Src" ], "offsets": [ [ 4, 7 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d722.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d722.s0.e0", "arg2_id": "BioInfer.d722.s0.e1", "normalized": [] }, { "id": "BioInfer.d722.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d722.s0.e1", "arg2_id": "BioInfer.d722.s0.e2", "normalized": [] }, { "id": "BioInfer.d722.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d722.s0.e1", "arg2_id": "BioInfer.d722.s0.e4", "normalized": [] } ]

[ { "id": "BioInfer.d723.s0__text", "type": "Sentence", "text": [ "The structural homology between cofilin and gelsolin segment-1 binding to actin was confirmed experimentally by two types of competitive binding assays." ], "offsets": [ [ 0, 152 ] ] } ]

[ { "id": "BioInfer.d723.s0.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 74, 79 ] ], "normalized": [] }, { "id": "BioInfer.d723.s0.e1", "type": "Individual_protein", "text": [ "gelsolin" ], "offsets": [ [ 44, 52 ] ], "normalized": [] }, { "id": "BioInfer.d723.s0.e2", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 32, 39 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d723.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d723.s0.e0", "arg2_id": "BioInfer.d723.s0.e1", "normalized": [] }, { "id": "BioInfer.d723.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d723.s0.e0", "arg2_id": "BioInfer.d723.s0.e2", "normalized": [] }, { "id": "BioInfer.d723.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d723.s0.e1", "arg2_id": "BioInfer.d723.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d724.s0__text", "type": "Sentence", "text": [ "The structure of an actin-crosslinking domain from human fimbrin." ], "offsets": [ [ 0, 65 ] ] } ]

[ { "id": "BioInfer.d724.s0.e0", "type": "Individual_protein", "text": [ "fimbrin" ], "offsets": [ [ 57, 64 ] ], "normalized": [] }, { "id": "BioInfer.d724.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 20, 25 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d724.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d724.s0.e0", "arg2_id": "BioInfer.d724.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d725.s0__text", "type": "Sentence", "text": [ "The structure of Ykt6pN differed entirely from that of syntaxin and resembled the overall fold of the actin regulatory protein, profilin." ], "offsets": [ [ 0, 137 ] ] } ]

[ { "id": "BioInfer.d725.s0.e0", "type": "Individual_protein", "text": [ "syntaxin" ], "offsets": [ [ 55, 63 ] ], "normalized": [] }, { "id": "BioInfer.d725.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 102, 107 ] ], "normalized": [] }, { "id": "BioInfer.d725.s0.e2", "type": "Individual_protein", "text": [ "Ykt6pN" ], "offsets": [ [ 17, 23 ] ], "normalized": [] }, { "id": "BioInfer.d725.s0.e3", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 128, 136 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d725.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d725.s0.e0", "arg2_id": "BioInfer.d725.s0.e2", "normalized": [] }, { "id": "BioInfer.d725.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d725.s0.e1", "arg2_id": "BioInfer.d725.s0.e3", "normalized": [] }, { "id": "BioInfer.d725.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d725.s0.e2", "arg2_id": "BioInfer.d725.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d726.s0__text", "type": "Sentence", "text": [ "The Tetrahymena fimbrin has two actin-binding domains, but lacks the EF-hand Ca(2+)-binding motif, suggesting that Tetrahymena fimbrin probably cross-links actin filaments in a Ca(2+)- insensitive manner during cytokinesis." ], "offsets": [ [ 0, 223 ] ] } ]

[ { "id": "BioInfer.d726.s0.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 156, 161 ] ], "normalized": [] }, { "id": "BioInfer.d726.s0.e1", "type": "Individual_protein", "text": [ "fimbrin" ], "offsets": [ [ 16, 23 ] ], "normalized": [] }, { "id": "BioInfer.d726.s0.e2", "type": "Individual_protein", "text": [ "fimbrin" ], "offsets": [ [ 127, 134 ] ], "normalized": [] }, { "id": "BioInfer.d726.s0.e3", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 32, 37 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d726.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d726.s0.e0", "arg2_id": "BioInfer.d726.s0.e2", "normalized": [] }, { "id": "BioInfer.d726.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d726.s0.e1", "arg2_id": "BioInfer.d726.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d727.s0__text", "type": "Sentence", "text": [ "The tumor necrosis factor receptor 1 (TNFR1) and the Fas receptor recruit complexes formed by the interactions between RIP kinase, TRADD, FADD and RAIDD - adaptor proteins that contain death domains - which in turn recruit other proteins to initiate signaling [1][2][3][4][5]." ], "offsets": [ [ 0, 276 ] ] } ]

[ { "id": "BioInfer.d727.s0.e0", "type": "Individual_protein", "text": [ "TRADD" ], "offsets": [ [ 131, 136 ] ], "normalized": [] }, { "id": "BioInfer.d727.s0.e1", "type": "Individual_protein", "text": [ "RAIDD" ], "offsets": [ [ 147, 152 ] ], "normalized": [] }, { "id": "BioInfer.d727.s0.e2", "type": "Individual_protein", "text": [ "TNFR1" ], "offsets": [ [ 38, 43 ] ], "normalized": [] }, { "id": "BioInfer.d727.s0.e3", "type": "Individual_protein", "text": [ "Fas" ], "offsets": [ [ 53, 56 ] ], "normalized": [] }, { "id": "BioInfer.d727.s0.e4", "type": "Individual_protein", "text": [ "tumor necrosis factor receptor 1" ], "offsets": [ [ 4, 36 ] ], "normalized": [] }, { "id": "BioInfer.d727.s0.e5", "type": "Individual_protein", "text": [ "RIP kinase" ], "offsets": [ [ 119, 129 ] ], "normalized": [] }, { "id": "BioInfer.d727.s0.e6", "type": "Individual_protein", "text": [ "FADD" ], "offsets": [ [ 138, 142 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d727.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d727.s0.e0", "arg2_id": "BioInfer.d727.s0.e1", "normalized": [] }, { "id": "BioInfer.d727.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d727.s0.e0", "arg2_id": "BioInfer.d727.s0.e2", "normalized": [] }, { "id": "BioInfer.d727.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d727.s0.e0", "arg2_id": "BioInfer.d727.s0.e3", "normalized": [] }, { "id": "BioInfer.d727.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d727.s0.e0", "arg2_id": "BioInfer.d727.s0.e4", "normalized": [] }, { "id": "BioInfer.d727.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d727.s0.e0", "arg2_id": "BioInfer.d727.s0.e5", "normalized": [] }, { "id": "BioInfer.d727.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d727.s0.e0", "arg2_id": "BioInfer.d727.s0.e6", "normalized": [] }, { "id": "BioInfer.d727.s0.i6", "type": "PPI", "arg1_id": "BioInfer.d727.s0.e1", "arg2_id": "BioInfer.d727.s0.e2", "normalized": [] }, { "id": "BioInfer.d727.s0.i7", "type": "PPI", "arg1_id": "BioInfer.d727.s0.e1", "arg2_id": "BioInfer.d727.s0.e3", "normalized": [] }, { "id": "BioInfer.d727.s0.i8", "type": "PPI", "arg1_id": "BioInfer.d727.s0.e1", "arg2_id": "BioInfer.d727.s0.e4", "normalized": [] }, { "id": "BioInfer.d727.s0.i9", "type": "PPI", "arg1_id": "BioInfer.d727.s0.e1", "arg2_id": "BioInfer.d727.s0.e5", "normalized": [] }, { "id": "BioInfer.d727.s0.i10", "type": "PPI", "arg1_id": "BioInfer.d727.s0.e1", "arg2_id": "BioInfer.d727.s0.e6", "normalized": [] }, { "id": "BioInfer.d727.s0.i11", "type": "PPI", "arg1_id": "BioInfer.d727.s0.e2", "arg2_id": "BioInfer.d727.s0.e5", "normalized": [] }, { "id": "BioInfer.d727.s0.i12", "type": "PPI", "arg1_id": "BioInfer.d727.s0.e2", "arg2_id": "BioInfer.d727.s0.e6", "normalized": [] }, { "id": "BioInfer.d727.s0.i13", "type": "PPI", "arg1_id": "BioInfer.d727.s0.e3", "arg2_id": "BioInfer.d727.s0.e5", "normalized": [] }, { "id": "BioInfer.d727.s0.i14", "type": "PPI", "arg1_id": "BioInfer.d727.s0.e3", "arg2_id": "BioInfer.d727.s0.e6", "normalized": [] }, { "id": "BioInfer.d727.s0.i15", "type": "PPI", "arg1_id": "BioInfer.d727.s0.e4", "arg2_id": "BioInfer.d727.s0.e5", "normalized": [] }, { "id": "BioInfer.d727.s0.i16", "type": "PPI", "arg1_id": "BioInfer.d727.s0.e4", "arg2_id": "BioInfer.d727.s0.e6", "normalized": [] }, { "id": "BioInfer.d727.s0.i17", "type": "PPI", "arg1_id": "BioInfer.d727.s0.e5", "arg2_id": "BioInfer.d727.s0.e6", "normalized": [] } ]

[ { "id": "BioInfer.d728.s0__text", "type": "Sentence", "text": [ "The two cardiac myosin heavy chain isoforms, alpha and beta, differ functionally, alpha Myosin exhibits higher actin-activated ATPase than does beta myosin, and hearts expressing alpha myosin exhibit increased contractility relative to hearts expressing beta myosin." ], "offsets": [ [ 0, 266 ] ] } ]

[ { "id": "BioInfer.d728.s0.e0", "type": "Individual_protein", "text": [ "ATPase" ], "offsets": [ [ 127, 133 ] ], "normalized": [] }, { "id": "BioInfer.d728.s0.e1", "type": "Individual_protein", "text": [ "beta myosin" ], "offsets": [ [ 144, 155 ] ], "normalized": [] }, { "id": "BioInfer.d728.s0.e2", "type": "Individual_protein", "text": [ "alpha Myosin" ], "offsets": [ [ 82, 94 ] ], "normalized": [] }, { "id": "BioInfer.d728.s0.e3", "type": "Gene/protein/RNA", "text": [ "alpha myosin" ], "offsets": [ [ 179, 191 ] ], "normalized": [] }, { "id": "BioInfer.d728.s0.e4", "type": "Gene/protein/RNA", "text": [ "beta myosin" ], "offsets": [ [ 254, 265 ] ], "normalized": [] }, { "id": "BioInfer.d728.s0.e5", "type": "Individual_protein", "text": [ "cardiac myosin heavy chain", "alpha" ], "offsets": [ [ 8, 34 ], [ 45, 50 ] ], "normalized": [] }, { "id": "BioInfer.d728.s0.e6", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 111, 116 ] ], "normalized": [] }, { "id": "BioInfer.d728.s0.e7", "type": "Individual_protein", "text": [ "cardiac myosin heavy chain", "beta" ], "offsets": [ [ 8, 34 ], [ 55, 59 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d728.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d728.s0.e0", "arg2_id": "BioInfer.d728.s0.e1", "normalized": [] }, { "id": "BioInfer.d728.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d728.s0.e0", "arg2_id": "BioInfer.d728.s0.e2", "normalized": [] }, { "id": "BioInfer.d728.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d728.s0.e0", "arg2_id": "BioInfer.d728.s0.e6", "normalized": [] }, { "id": "BioInfer.d728.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d728.s0.e5", "arg2_id": "BioInfer.d728.s0.e7", "normalized": [] } ]

[ { "id": "BioInfer.d729.s0__text", "type": "Sentence", "text": [ "The two proteins were found to differ in their interaction with actin, like destrin and cofilin isolated from porcine brain." ], "offsets": [ [ 0, 124 ] ] } ]

[ { "id": "BioInfer.d729.s0.e0", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 88, 95 ] ], "normalized": [] }, { "id": "BioInfer.d729.s0.e1", "type": "Individual_protein", "text": [ "destrin" ], "offsets": [ [ 76, 83 ] ], "normalized": [] }, { "id": "BioInfer.d729.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 64, 69 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d729.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d729.s0.e0", "arg2_id": "BioInfer.d729.s0.e1", "normalized": [] }, { "id": "BioInfer.d729.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d729.s0.e0", "arg2_id": "BioInfer.d729.s0.e2", "normalized": [] }, { "id": "BioInfer.d729.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d729.s0.e1", "arg2_id": "BioInfer.d729.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d730.s0__text", "type": "Sentence", "text": [ "The undifferentiated cells (a) were unable to spread on gelatin or laminin and grew as rounded colonies, although they were able to spread on fibronectin (b) showed reduced adhesion to laminin, but not fibronectin (c) expressed much reduced levels of beta1 integrin, although levels of alpha5 and alphaV were wild-type (d) were less polarized with increased membrane protrusions compared with a vinculin (-/-) ES cell mutant (e) were unable to assemble vinculin or paxillin-containing focal adhesions or actin stress fibers on fibronectin, whereas vinculin (-/-) ES cells were able to assemble talin-containing focal adhesions." ], "offsets": [ [ 0, 627 ] ] } ]

[ { "id": "BioInfer.d730.s0.e0", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 504, 509 ] ], "normalized": [] }, { "id": "BioInfer.d730.s0.e1", "type": "Gene/protein/RNA", "text": [ "talin" ], "offsets": [ [ 594, 599 ] ], "normalized": [] }, { "id": "BioInfer.d730.s0.e2", "type": "Gene/protein/RNA", "text": [ "vinculin" ], "offsets": [ [ 548, 556 ] ], "normalized": [] }, { "id": "BioInfer.d730.s0.e3", "type": "Gene/protein/RNA", "text": [ "vinculin" ], "offsets": [ [ 453, 461 ] ], "normalized": [] }, { "id": "BioInfer.d730.s0.e4", "type": "Gene/protein/RNA", "text": [ "fibronectin" ], "offsets": [ [ 527, 538 ] ], "normalized": [] }, { "id": "BioInfer.d730.s0.e5", "type": "Gene/protein/RNA", "text": [ "laminin" ], "offsets": [ [ 67, 74 ] ], "normalized": [] }, { "id": "BioInfer.d730.s0.e6", "type": "Gene/protein/RNA", "text": [ "fibronectin" ], "offsets": [ [ 202, 213 ] ], "normalized": [] }, { "id": "BioInfer.d730.s0.e7", "type": "Gene/protein/RNA", "text": [ "gelatin" ], "offsets": [ [ 56, 63 ] ], "normalized": [] }, { "id": "BioInfer.d730.s0.e8", "type": "Gene/protein/RNA", "text": [ "fibronectin" ], "offsets": [ [ 142, 153 ] ], "normalized": [] }, { "id": "BioInfer.d730.s0.e9", "type": "Gene/protein/RNA", "text": [ "beta1 integrin" ], "offsets": [ [ 251, 265 ] ], "normalized": [] }, { "id": "BioInfer.d730.s0.e10", "type": "Gene/protein/RNA", "text": [ "paxillin" ], "offsets": [ [ 465, 473 ] ], "normalized": [] }, { "id": "BioInfer.d730.s0.e11", "type": "Gene/protein/RNA", "text": [ "laminin" ], "offsets": [ [ 185, 192 ] ], "normalized": [] }, { "id": "BioInfer.d730.s0.e12", "type": "Gene/protein/RNA", "text": [ "vinculin" ], "offsets": [ [ 395, 403 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d731.s0__text", "type": "Sentence", "text": [ "The vaccinia virus E3L gene product, pE3, is a dsRNA binding protein that prevents activation of the interferon-induced, dsRNA-activated protein kinase, PKR." ], "offsets": [ [ 0, 157 ] ] } ]

[ { "id": "BioInfer.d731.s0.e0", "type": "Gene", "text": [ "E3L" ], "offsets": [ [ 19, 22 ] ], "normalized": [] }, { "id": "BioInfer.d731.s0.e1", "type": "Protein_family_or_group", "text": [ "protein kinase" ], "offsets": [ [ 137, 151 ] ], "normalized": [] }, { "id": "BioInfer.d731.s0.e2", "type": "Individual_protein", "text": [ "pE3" ], "offsets": [ [ 37, 40 ] ], "normalized": [] }, { "id": "BioInfer.d731.s0.e3", "type": "Individual_protein", "text": [ "interferon" ], "offsets": [ [ 101, 111 ] ], "normalized": [] }, { "id": "BioInfer.d731.s0.e4", "type": "Individual_protein", "text": [ "PKR" ], "offsets": [ [ 153, 156 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d732.s0__text", "type": "Sentence", "text": [ "The yeast two-hybrid system was used to identify domains involved in specific in vivo interactions between the Rinderpest virus (RPV) phosphoprotein (P) and nucleocapsid protein (N)." ], "offsets": [ [ 0, 182 ] ] } ]

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[ { "id": "BioInfer.d733.s0__text", "type": "Sentence", "text": [ "They exhibited strong synergistic increases in CAN1 duplication mutations, intrachromosomal and interchromosomal recombination, and required the wild-type double-strand break repair genes RAD50, RAD51, and RAD52 for viability." ], "offsets": [ [ 0, 226 ] ] } ]

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[ { "id": "BioInfer.d734.s0__text", "type": "Sentence", "text": [ "They had altered adhesive properties as measured by their ability to bind to a fibronectin-coated glass surface, suggesting that the expression of a rac-1 GAP alters the assembly of integrin receptors, actin and cytoskeletal proteins such as vinculin and talin." ], "offsets": [ [ 0, 261 ] ] } ]

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[ { "id": "BioInfer.d735.s0__text", "type": "Sentence", "text": [ "This activity is independent of FADD-DN's ability to bind to three known interacting proteins, Fas, TRADD or RIP suggesting that it is distinct from FADD's functions at activated death receptors." ], "offsets": [ [ 0, 195 ] ] } ]

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[ { "id": "BioInfer.d736.s0__text", "type": "Sentence", "text": [ "This approach is based on the assumption that an actin mutation that specifically impairs the interaction with an actin-binding protein will cause a phenotype similar to a null mutation in the gene that encodes the actin-binding protein." ], "offsets": [ [ 0, 237 ] ] } ]

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[ { "id": "BioInfer.d736.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d736.s0.e1", "arg2_id": "BioInfer.d736.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d736.s1__text", "type": "Sentence", "text": [ "21 actin mutations were analyzed in budding yeast, and specific regions of actin subdomain 1 were implicated in the interaction with fimbrin, an actin filament-bundling protein." ], "offsets": [ [ 0, 177 ] ] } ]

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[ { "id": "BioInfer.d736.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d736.s1.e0", "arg2_id": "BioInfer.d736.s1.e3", "normalized": [] }, { "id": "BioInfer.d736.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d736.s1.e2", "arg2_id": "BioInfer.d736.s1.e3", "normalized": [] } ]

[ { "id": "BioInfer.d737.s0__text", "type": "Sentence", "text": [ "This arrest can be suppressed by mutations in RAD51, RAD52, and RAD57, suggesting that the cell cycle defect in sgs1 srs2 mutants results from inappropriate homologous recombination." ], "offsets": [ [ 0, 182 ] ] } ]

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[ { "id": "BioInfer.d739.s0__text", "type": "Sentence", "text": [ "This filament growth is driven by a large storage pool of actin bound to the sequestering protein, profilin." ], "offsets": [ [ 0, 108 ] ] } ]

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[ { "id": "BioInfer.d739.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d739.s0.e0", "arg2_id": "BioInfer.d739.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d740.s0__text", "type": "Sentence", "text": [ "This is consistent with cofilin activation being required for actin reorganization during exocytosis." ], "offsets": [ [ 0, 101 ] ] } ]

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[ { "id": "BioInfer.d740.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d740.s0.e0", "arg2_id": "BioInfer.d740.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d741.s0__text", "type": "Sentence", "text": [ "This is the first report describing the coexistence of profilin with actin filaments in the division furrow, implying the possible involvement of profilin in assembly and disassembly of contractile ring microfilaments in the process of cytokinesis." ], "offsets": [ [ 0, 248 ] ] } ]

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[ { "id": "BioInfer.d741.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d741.s0.e0", "arg2_id": "BioInfer.d741.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d742.s0__text", "type": "Sentence", "text": [ "This novel mutation was predicted to disrupt the binding of beta-catenin to alpha-catenin and may be related to the diffuse type morphology." ], "offsets": [ [ 0, 140 ] ] } ]

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[ { "id": "BioInfer.d742.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d742.s0.e0", "arg2_id": "BioInfer.d742.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d746.s0__text", "type": "Sentence", "text": [ "This shows that structural changes in the poly(L-proline)-binding region of profilin can affect the distantly located actin-binding site." ], "offsets": [ [ 0, 137 ] ] } ]

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[ { "id": "BioInfer.d746.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d746.s0.e0", "arg2_id": "BioInfer.d746.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d747.s0__text", "type": "Sentence", "text": [ "This technique was employed to quantify changes caused by the lack of talin, a protein that couples the actin network to the plasma membrane, or by the lack of cortexillin I or II, two isoforms of the actin-bundling protein cortexillin." ], "offsets": [ [ 0, 236 ] ] } ]

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[ { "id": "BioInfer.d749.s0__text", "type": "Sentence", "text": [ "Three actin-associated proteins, actin-binding protein, gelsolin, and profilin, influence gelation, solation, and polymerization, respectively, of actin in vitro." ], "offsets": [ [ 0, 162 ] ] } ]

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[ { "id": "BioInfer.d749.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d749.s0.e0", "arg2_id": "BioInfer.d749.s0.e2", "normalized": [] }, { "id": "BioInfer.d749.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d749.s0.e1", "arg2_id": "BioInfer.d749.s0.e2", "normalized": [] }, { "id": "BioInfer.d749.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d749.s0.e2", "arg2_id": "BioInfer.d749.s0.e4", "normalized": [] }, { "id": "BioInfer.d749.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d749.s0.e3", "arg2_id": "BioInfer.d749.s0.e4", "normalized": [] } ]

[ { "id": "BioInfer.d750.s0__text", "type": "Sentence", "text": [ "Three components of Drosophila adherens junctions, analogous to those in vertebrates, have been identified: Armadillo (homolog of beta-catenin), Drosophila E-cadherin (DE-cadherin), and alpha-catenin." ], "offsets": [ [ 0, 200 ] ] } ]

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[ { "id": "BioInfer.d750.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d750.s0.e1", "arg2_id": "BioInfer.d750.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d751.s0__text", "type": "Sentence", "text": [ "Thus, actin was found in association with fimbrin in the mechanoreceptive region of hair cells, whereas supporting cells, although rich in actin, did not reveal fimbrin." ], "offsets": [ [ 0, 169 ] ] } ]

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[ { "id": "BioInfer.d751.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d751.s0.e0", "arg2_id": "BioInfer.d751.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d752.s0__text", "type": "Sentence", "text": [ "Thus, beta-catenin, E-cadherin, and alpha-catenin have similar prognostic values." ], "offsets": [ [ 0, 81 ] ] } ]

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[ { "id": "BioInfer.d755.s0__text", "type": "Sentence", "text": [ "Thus, mHip1R contains an NH(2)-terminal domain homologous to that implicated in Sla2p's endocytic function, three predicted coiled-coils, a leucine zipper, and a talin-like actin-binding domain at the COOH terminus." ], "offsets": [ [ 0, 215 ] ] } ]

[ { "id": "BioInfer.d755.s0.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 173, 178 ] ], "normalized": [] }, { "id": "BioInfer.d755.s0.e1", "type": "Individual_protein", "text": [ "Sla2p" ], "offsets": [ [ 80, 85 ] ], "normalized": [] }, { "id": "BioInfer.d755.s0.e2", "type": "Individual_protein", "text": [ "talin" ], "offsets": [ [ 162, 167 ] ], "normalized": [] }, { "id": "BioInfer.d755.s0.e3", "type": "Individual_protein", "text": [ "mHip1R" ], "offsets": [ [ 6, 12 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d755.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d755.s0.e0", "arg2_id": "BioInfer.d755.s0.e3", "normalized": [] }, { "id": "BioInfer.d755.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d755.s0.e1", "arg2_id": "BioInfer.d755.s0.e3", "normalized": [] }, { "id": "BioInfer.d755.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d755.s0.e2", "arg2_id": "BioInfer.d755.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d756.s0__text", "type": "Sentence", "text": [ "Thus, poly-L-proline binding, actin binding, and actin nucleotide exchange are each independent requirements for profilin function in fission yeast." ], "offsets": [ [ 0, 148 ] ] } ]

[ { "id": "BioInfer.d756.s0.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 30, 35 ] ], "normalized": [] }, { "id": "BioInfer.d756.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 49, 54 ] ], "normalized": [] }, { "id": "BioInfer.d756.s0.e2", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 113, 121 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d756.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d756.s0.e0", "arg2_id": "BioInfer.d756.s0.e2", "normalized": [] }, { "id": "BioInfer.d756.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d756.s0.e1", "arg2_id": "BioInfer.d756.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d757.s0__text", "type": "Sentence", "text": [ "Thus, the actin-binding dodecapeptide sequence of cofilin may constitute a multifunctional domain in cofilin." ], "offsets": [ [ 0, 109 ] ] } ]

[ { "id": "BioInfer.d757.s0.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 10, 15 ] ], "normalized": [] }, { "id": "BioInfer.d757.s0.e1", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 50, 57 ] ], "normalized": [] }, { "id": "BioInfer.d757.s0.e2", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 101, 108 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d757.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d757.s0.e0", "arg2_id": "BioInfer.d757.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d757.s1__text", "type": "Sentence", "text": [ "We have previously shown that the synthetic dodecapeptide corresponding to Trp104-Met115 of cofilin is a potent inhibitor of actin polymerization (Yonezawa, N., Nishida, E., Iida, K., Kumagai, H., Yahara, I., and Sakai, H. (1991) J. Biol. Chem. 266, 10485-10489)." ], "offsets": [ [ 0, 263 ] ] } ]

[ { "id": "BioInfer.d757.s1.e0", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 92, 99 ] ], "normalized": [] }, { "id": "BioInfer.d757.s1.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 125, 130 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d757.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d757.s1.e0", "arg2_id": "BioInfer.d757.s1.e1", "normalized": [] } ]

[ { "id": "BioInfer.d758.s0__text", "type": "Sentence", "text": [ "TNF also inhibited muscle differentiation as measured by several parameters, including cell fusion and the expression of other muscle-specific genes, such as alpha-skeletal actin and myosin heavy chain." ], "offsets": [ [ 0, 202 ] ] } ]

[ { "id": "BioInfer.d758.s0.e0", "type": "Gene/protein/RNA", "text": [ "TNF" ], "offsets": [ [ 0, 3 ] ], "normalized": [] }, { "id": "BioInfer.d758.s0.e1", "type": "Gene/protein/RNA", "text": [ "myosin heavy chain" ], "offsets": [ [ 183, 201 ] ], "normalized": [] }, { "id": "BioInfer.d758.s0.e2", "type": "Gene/protein/RNA", "text": [ "alpha-skeletal actin" ], "offsets": [ [ 158, 178 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d760.s0__text", "type": "Sentence", "text": [ "To characterize the AAV functions mediating this effect, cloned AAV type 2 wild-type or mutant genomes were transfected into simian virus 40 (SV40)-transformed hamster cells together with the six HSV replication genes (encoding UL5, UL8, major DNA-binding protein, DNA polymerase, UL42, and UL52) which together are necessary and sufficient for the induction of SV40 DNA amplification (R. Heilbronn and H. zur Hausen, J. Virol. 63:3683-3692, 1989)." ], "offsets": [ [ 0, 448 ] ] } ]

[ { "id": "BioInfer.d760.s0.e0", "type": "Gene/protein/RNA", "text": [ "DNA polymerase" ], "offsets": [ [ 265, 279 ] ], "normalized": [] }, { "id": "BioInfer.d760.s0.e1", "type": "Gene/protein/RNA", "text": [ "major DNA-binding protein" ], "offsets": [ [ 238, 263 ] ], "normalized": [] }, { "id": "BioInfer.d760.s0.e2", "type": "Gene/protein/RNA", "text": [ "UL8" ], "offsets": [ [ 233, 236 ] ], "normalized": [] }, { "id": "BioInfer.d760.s0.e3", "type": "Gene/protein/RNA", "text": [ "UL5" ], "offsets": [ [ 228, 231 ] ], "normalized": [] }, { "id": "BioInfer.d760.s0.e4", "type": "Gene/protein/RNA", "text": [ "UL52" ], "offsets": [ [ 291, 295 ] ], "normalized": [] }, { "id": "BioInfer.d760.s0.e5", "type": "Gene/protein/RNA", "text": [ "UL42" ], "offsets": [ [ 281, 285 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d761.s0__text", "type": "Sentence", "text": [ "To characterize the phenotypic alteration in mesangial cells in human glomerulonephritis, we investigated the expression of nonmuscle-type myosin heavy chain, SMemb, and alpha-smooth muscle actin (alpha-SM actin) in IgA nephropathy." ], "offsets": [ [ 0, 232 ] ] } ]

[ { "id": "BioInfer.d761.s0.e0", "type": "Gene/protein/RNA", "text": [ "IgA" ], "offsets": [ [ 216, 219 ] ], "normalized": [] }, { "id": "BioInfer.d761.s0.e1", "type": "Individual_protein", "text": [ "alpha-smooth muscle actin" ], "offsets": [ [ 170, 195 ] ], "normalized": [] }, { "id": "BioInfer.d761.s0.e2", "type": "Gene/protein/RNA", "text": [ "nonmuscle-type myosin heavy chain" ], "offsets": [ [ 124, 157 ] ], "normalized": [] }, { "id": "BioInfer.d761.s0.e3", "type": "Individual_protein", "text": [ "alpha-SM actin" ], "offsets": [ [ 197, 211 ] ], "normalized": [] }, { "id": "BioInfer.d761.s0.e4", "type": "Gene/protein/RNA", "text": [ "SMemb" ], "offsets": [ [ 159, 164 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d762.s0__text", "type": "Sentence", "text": [ "To check its applicability, well characterized, commercially available antibodies (against E-cadherin, alpha-catenin, and beta-catenin) were used on sections of human small intestine." ], "offsets": [ [ 0, 183 ] ] } ]

[ { "id": "BioInfer.d762.s0.e0", "type": "Gene/protein/RNA", "text": [ "alpha-catenin" ], "offsets": [ [ 103, 116 ] ], "normalized": [] }, { "id": "BioInfer.d762.s0.e1", "type": "Gene/protein/RNA", "text": [ "beta-catenin" ], "offsets": [ [ 122, 134 ] ], "normalized": [] }, { "id": "BioInfer.d762.s0.e2", "type": "Gene/protein/RNA", "text": [ "E-cadherin" ], "offsets": [ [ 91, 101 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d763.s0__text", "type": "Sentence", "text": [ "To clarify the relation between alteration of expression of cell adhesion molecules and progression of extrahepatic bile duct carcinomas 55 cases were immunohistochemically examined for E-cadherin, alpha-catenin, beta-catenin, and CD44, with additional reverse transcription-polymerase chain reaction and Southern blotting hybridization (RT-PCR/SBH) assays." ], "offsets": [ [ 0, 357 ] ] } ]

[ { "id": "BioInfer.d763.s0.e0", "type": "Gene/protein/RNA", "text": [ "CD44" ], "offsets": [ [ 231, 235 ] ], "normalized": [] }, { "id": "BioInfer.d763.s0.e1", "type": "Gene/protein/RNA", "text": [ "polymerase" ], "offsets": [ [ 275, 285 ] ], "normalized": [] }, { "id": "BioInfer.d763.s0.e2", "type": "Gene/protein/RNA", "text": [ "alpha-catenin" ], "offsets": [ [ 198, 211 ] ], "normalized": [] }, { "id": "BioInfer.d763.s0.e3", "type": "Gene/protein/RNA", "text": [ "cell adhesion molecules" ], "offsets": [ [ 60, 83 ] ], "normalized": [] }, { "id": "BioInfer.d763.s0.e4", "type": "Gene/protein/RNA", "text": [ "E-cadherin" ], "offsets": [ [ 186, 196 ] ], "normalized": [] }, { "id": "BioInfer.d763.s0.e5", "type": "Gene/protein/RNA", "text": [ "beta-catenin" ], "offsets": [ [ 213, 225 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d764.s0__text", "type": "Sentence", "text": [ "To determine the phenotypes of smooth muscle cells (SMCs) in such lesions, the authors conducted an immunohistochemical analysis of lung tissues from two patients with PPH, using two antimuscle actin antibodies, HHF35 and CGA7, and two anti-SMC myosin heavy chain markers, anti-SM1 and anti-SM2 antibodies and related antibodies." ], "offsets": [ [ 0, 329 ] ] } ]

[ { "id": "BioInfer.d764.s0.e0", "type": "Individual_protein", "text": [ "HHF35" ], "offsets": [ [ 212, 217 ] ], "normalized": [] }, { "id": "BioInfer.d764.s0.e1", "type": "Gene/protein/RNA", "text": [ "SM1" ], "offsets": [ [ 278, 281 ] ], "normalized": [] }, { "id": "BioInfer.d764.s0.e2", "type": "Gene/protein/RNA", "text": [ "SMC myosin heavy chain" ], "offsets": [ [ 241, 263 ] ], "normalized": [] }, { "id": "BioInfer.d764.s0.e3", "type": "Gene/protein/RNA", "text": [ "SM2" ], "offsets": [ [ 291, 294 ] ], "normalized": [] }, { "id": "BioInfer.d764.s0.e4", "type": "Individual_protein", "text": [ "CGA7" ], "offsets": [ [ 222, 226 ] ], "normalized": [] }, { "id": "BioInfer.d764.s0.e5", "type": "Individual_protein", "text": [ "muscle actin" ], "offsets": [ [ 187, 199 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d764.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d764.s0.e0", "arg2_id": "BioInfer.d764.s0.e5", "normalized": [] }, { "id": "BioInfer.d764.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d764.s0.e4", "arg2_id": "BioInfer.d764.s0.e5", "normalized": [] } ]

[ { "id": "BioInfer.d765.s0__text", "type": "Sentence", "text": [ "To determine the relationship between cell cycle regulation and differentiation, the spatiotemporal expression of cyclin A, cyclin B1, cyclin D1, the cyclin-dependent kinase inhibitors (CKIs) p27 and p57, and markers of differentiating podocytes in developing human kidneys was investigated by immunohistochemistry." ], "offsets": [ [ 0, 315 ] ] } ]

[ { "id": "BioInfer.d765.s0.e0", "type": "Individual_protein", "text": [ "p27" ], "offsets": [ [ 192, 195 ] ], "normalized": [] }, { "id": "BioInfer.d765.s0.e1", "type": "Protein_family_or_group", "text": [ "CKIs" ], "offsets": [ [ 186, 190 ] ], "normalized": [] }, { "id": "BioInfer.d765.s0.e2", "type": "Protein_family_or_group", "text": [ "cyclin-dependent kinase inhibitors" ], "offsets": [ [ 150, 184 ] ], "normalized": [] }, { "id": "BioInfer.d765.s0.e3", "type": "Gene/protein/RNA", "text": [ "cyclin D1" ], "offsets": [ [ 135, 144 ] ], "normalized": [] }, { "id": "BioInfer.d765.s0.e4", "type": "Gene/protein/RNA", "text": [ "cyclin A" ], "offsets": [ [ 114, 122 ] ], "normalized": [] }, { "id": "BioInfer.d765.s0.e5", "type": "Gene/protein/RNA", "text": [ "cyclin B1" ], "offsets": [ [ 124, 133 ] ], "normalized": [] }, { "id": "BioInfer.d765.s0.e6", "type": "Individual_protein", "text": [ "p57" ], "offsets": [ [ 200, 203 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d765.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d765.s0.e0", "arg2_id": "BioInfer.d765.s0.e1", "normalized": [] }, { "id": "BioInfer.d765.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d765.s0.e0", "arg2_id": "BioInfer.d765.s0.e2", "normalized": [] }, { "id": "BioInfer.d765.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d765.s0.e1", "arg2_id": "BioInfer.d765.s0.e6", "normalized": [] }, { "id": "BioInfer.d765.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d765.s0.e2", "arg2_id": "BioInfer.d765.s0.e6", "normalized": [] } ]

[ { "id": "BioInfer.d766.s0__text", "type": "Sentence", "text": [ "To determine the relative importance of protein degradation in the development of starvation-induced cardiac atrophy, in vivo fractional synthetic rates of total cardiac protein, myosin heavy chain, actin, light chain 1, and light chain 2 were measured in fed and fasted rabbits by continuous infusion of [3H] leucine." ], "offsets": [ [ 0, 318 ] ] } ]

[ { "id": "BioInfer.d766.s0.e0", "type": "Gene/protein/RNA", "text": [ "myosin", "light chain 2" ], "offsets": [ [ 179, 185 ], [ 225, 238 ] ], "normalized": [] }, { "id": "BioInfer.d766.s0.e1", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 199, 204 ] ], "normalized": [] }, { "id": "BioInfer.d766.s0.e2", "type": "Gene/protein/RNA", "text": [ "myosin", "light chain 1" ], "offsets": [ [ 179, 185 ], [ 206, 219 ] ], "normalized": [] }, { "id": "BioInfer.d766.s0.e3", "type": "Gene/protein/RNA", "text": [ "myosin heavy chain" ], "offsets": [ [ 179, 197 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d767.s0__text", "type": "Sentence", "text": [ "To determine whether alpha 1-adrenergic stimulation produced similar effects on the turnover of myofibrillar proteins, rates of synthesis and degradation were estimated for a myofibrillar-enriched protein fraction and for myosin heavy chain and actin." ], "offsets": [ [ 0, 251 ] ] } ]

[ { "id": "BioInfer.d767.s0.e0", "type": "Gene/protein/RNA", "text": [ "myosin heavy chain" ], "offsets": [ [ 222, 240 ] ], "normalized": [] }, { "id": "BioInfer.d767.s0.e1", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 245, 250 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d768.s0__text", "type": "Sentence", "text": [ "Together these results indicate that TGFbeta regulates clusterin gene expression through an AP-1 site and its cognate transcription factor AP-1, and requires the involvement of protein kinase C." ], "offsets": [ [ 0, 194 ] ] } ]

[ { "id": "BioInfer.d768.s0.e0", "type": "Individual_protein", "text": [ "TGFbeta" ], "offsets": [ [ 37, 44 ] ], "normalized": [] }, { "id": "BioInfer.d768.s0.e1", "type": "Individual_protein", "text": [ "clusterin" ], "offsets": [ [ 55, 64 ] ], "normalized": [] }, { "id": "BioInfer.d768.s0.e2", "type": "Individual_protein", "text": [ "AP-1" ], "offsets": [ [ 139, 143 ] ], "normalized": [] }, { "id": "BioInfer.d768.s0.e3", "type": "Individual_protein", "text": [ "AP-1" ], "offsets": [ [ 92, 96 ] ], "normalized": [] }, { "id": "BioInfer.d768.s0.e4", "type": "Individual_protein", "text": [ "protein kinase C" ], "offsets": [ [ 177, 193 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d768.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d768.s0.e0", "arg2_id": "BioInfer.d768.s0.e1", "normalized": [] }, { "id": "BioInfer.d768.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d768.s0.e0", "arg2_id": "BioInfer.d768.s0.e2", "normalized": [] }, { "id": "BioInfer.d768.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d768.s0.e0", "arg2_id": "BioInfer.d768.s0.e3", "normalized": [] }, { "id": "BioInfer.d768.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d768.s0.e0", "arg2_id": "BioInfer.d768.s0.e4", "normalized": [] }, { "id": "BioInfer.d768.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d768.s0.e1", "arg2_id": "BioInfer.d768.s0.e2", "normalized": [] }, { "id": "BioInfer.d768.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d768.s0.e1", "arg2_id": "BioInfer.d768.s0.e3", "normalized": [] }, { "id": "BioInfer.d768.s0.i6", "type": "PPI", "arg1_id": "BioInfer.d768.s0.e2", "arg2_id": "BioInfer.d768.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d769.s0__text", "type": "Sentence", "text": [ "To improve our ability to study these proteins, we have expressed UL5, UL8, UL9, and UL52 in insect cells by using the baculovirus expression system." ], "offsets": [ [ 0, 149 ] ] } ]

[ { "id": "BioInfer.d769.s0.e0", "type": "Gene/protein/RNA", "text": [ "UL5" ], "offsets": [ [ 66, 69 ] ], "normalized": [] }, { "id": "BioInfer.d769.s0.e1", "type": "Gene/protein/RNA", "text": [ "UL9" ], "offsets": [ [ 76, 79 ] ], "normalized": [] }, { "id": "BioInfer.d769.s0.e2", "type": "Gene/protein/RNA", "text": [ "UL8" ], "offsets": [ [ 71, 74 ] ], "normalized": [] }, { "id": "BioInfer.d769.s0.e3", "type": "Gene/protein/RNA", "text": [ "UL52" ], "offsets": [ [ 85, 89 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d769.s1__text", "type": "Sentence", "text": [ "Various immunological assays suggest that four of these proteins (UL5, UL8, UL9, and UL52) are made in infected cells in very low abundance relative to the other three." ], "offsets": [ [ 0, 168 ] ] } ]

[ { "id": "BioInfer.d769.s1.e0", "type": "Gene/protein/RNA", "text": [ "UL52" ], "offsets": [ [ 85, 89 ] ], "normalized": [] }, { "id": "BioInfer.d769.s1.e1", "type": "Gene/protein/RNA", "text": [ "UL8" ], "offsets": [ [ 71, 74 ] ], "normalized": [] }, { "id": "BioInfer.d769.s1.e2", "type": "Gene/protein/RNA", "text": [ "UL9" ], "offsets": [ [ 76, 79 ] ], "normalized": [] }, { "id": "BioInfer.d769.s1.e3", "type": "Gene/protein/RNA", "text": [ "UL5" ], "offsets": [ [ 66, 69 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d772.s0__text", "type": "Sentence", "text": [ "Transcriptional expression of TNFR1(p55), as well as that of FLICE, Fas, FADD, DR3, FAF, TRADD, and RIP was similar in these cell lines, indicating that the susceptibility to TNFalpha-induced apoptosis may not be determined by the constitutive expression level of these factors." ], "offsets": [ [ 0, 278 ] ] } ]

[ { "id": "BioInfer.d772.s0.e0", "type": "Individual_protein", "text": [ "FLICE" ], "offsets": [ [ 61, 66 ] ], "normalized": [] }, { "id": "BioInfer.d772.s0.e1", "type": "Individual_protein", "text": [ "TRADD" ], "offsets": [ [ 89, 94 ] ], "normalized": [] }, { "id": "BioInfer.d772.s0.e2", "type": "Individual_protein", "text": [ "FADD" ], "offsets": [ [ 73, 77 ] ], "normalized": [] }, { "id": "BioInfer.d772.s0.e3", "type": "Individual_protein", "text": [ "TNFalpha" ], "offsets": [ [ 175, 183 ] ], "normalized": [] }, { "id": "BioInfer.d772.s0.e4", "type": "Individual_protein", "text": [ "FAF" ], "offsets": [ [ 84, 87 ] ], "normalized": [] }, { "id": "BioInfer.d772.s0.e5", "type": "Individual_protein", "text": [ "TNFR1" ], "offsets": [ [ 30, 35 ] ], "normalized": [] }, { "id": "BioInfer.d772.s0.e6", "type": "Individual_protein", "text": [ "DR3" ], "offsets": [ [ 79, 82 ] ], "normalized": [] }, { "id": "BioInfer.d772.s0.e7", "type": "Individual_protein", "text": [ "Fas" ], "offsets": [ [ 68, 71 ] ], "normalized": [] }, { "id": "BioInfer.d772.s0.e8", "type": "Individual_protein", "text": [ "p55" ], "offsets": [ [ 36, 39 ] ], "normalized": [] }, { "id": "BioInfer.d772.s0.e9", "type": "Individual_protein", "text": [ "RIP" ], "offsets": [ [ 100, 103 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d772.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d772.s0.e0", "arg2_id": "BioInfer.d772.s0.e3", "normalized": [] }, { "id": "BioInfer.d772.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d772.s0.e1", "arg2_id": "BioInfer.d772.s0.e3", "normalized": [] }, { "id": "BioInfer.d772.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d772.s0.e2", "arg2_id": "BioInfer.d772.s0.e3", "normalized": [] }, { "id": "BioInfer.d772.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d772.s0.e3", "arg2_id": "BioInfer.d772.s0.e4", "normalized": [] }, { "id": "BioInfer.d772.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d772.s0.e3", "arg2_id": "BioInfer.d772.s0.e5", "normalized": [] }, { "id": "BioInfer.d772.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d772.s0.e3", "arg2_id": "BioInfer.d772.s0.e6", "normalized": [] }, { "id": "BioInfer.d772.s0.i6", "type": "PPI", "arg1_id": "BioInfer.d772.s0.e3", "arg2_id": "BioInfer.d772.s0.e7", "normalized": [] }, { "id": "BioInfer.d772.s0.i7", "type": "PPI", "arg1_id": "BioInfer.d772.s0.e3", "arg2_id": "BioInfer.d772.s0.e8", "normalized": [] }, { "id": "BioInfer.d772.s0.i8", "type": "PPI", "arg1_id": "BioInfer.d772.s0.e3", "arg2_id": "BioInfer.d772.s0.e9", "normalized": [] } ]

[ { "id": "BioInfer.d773.s0__text", "type": "Sentence", "text": [ "Transcriptional regulation in the galactose regulon of yeast is determined by an interplay between a positive regulatory protein, GAL4, and a negative regulatory protein, GAL80." ], "offsets": [ [ 0, 177 ] ] } ]

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[ { "id": "BioInfer.d774.s0__text", "type": "Sentence", "text": [ "Transfection of alpha-catenin-deficient colon carcinoma cells recruited E-cadherin and beta-catenin to cell-cell contacts and functional cadherin-mediated cell-cell adhesion was restored in this way." ], "offsets": [ [ 0, 199 ] ] } ]

[ { "id": "BioInfer.d774.s0.e0", "type": "Gene/protein/RNA", "text": [ "beta-catenin" ], "offsets": [ [ 87, 99 ] ], "normalized": [] }, { "id": "BioInfer.d774.s0.e1", "type": "Gene/protein/RNA", "text": [ "alpha-catenin" ], "offsets": [ [ 16, 29 ] ], "normalized": [] }, { "id": "BioInfer.d774.s0.e2", "type": "Gene/protein/RNA", "text": [ "cadherin" ], "offsets": [ [ 137, 145 ] ], "normalized": [] }, { "id": "BioInfer.d774.s0.e3", "type": "Gene/protein/RNA", "text": [ "E-cadherin" ], "offsets": [ [ 72, 82 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d776.s0__text", "type": "Sentence", "text": [ "Treatment of cells with gamma linolenic acid (GLA) increased alpha catenin expression in most cell lines, while beta catenin levels were reduced, and gamma catenin expression was unchanged." ], "offsets": [ [ 0, 189 ] ] } ]

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[ { "id": "BioInfer.d777.s0__text", "type": "Sentence", "text": [ "Treatment with HNE resulted in activation of extracellular signal-regulated protein kinases ERK1 and ERK2, induction of c-fos and c-jun protein expression, and an increase in transcription factor AP-1 DNA binding activity." ], "offsets": [ [ 0, 222 ] ] } ]

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[ { "id": "BioInfer.d779.s0__text", "type": "Sentence", "text": [ "Two cDNAs, isolated from a Xenopus laevis embryonic library, encode proteins of 168 amino acids, both of which are 77% identical to chick cofilin and 66% identical to chick actin-depolymerizing factor (ADF), two structurally and functionally related proteins." ], "offsets": [ [ 0, 259 ] ] } ]

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[ { "id": "BioInfer.d781.s0__text", "type": "Sentence", "text": [ "Under all conditions, platelets retained 40-50% of their total actin and greater than 70% of their actin-binding protein (ABP) but lost greater than 80% of talin and myosin to the supernatant." ], "offsets": [ [ 0, 192 ] ] } ]

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[ { "id": "BioInfer.d782.s0__text", "type": "Sentence", "text": [ "Unexpectedly, treatment with the actin-depolymerizing drug latrunculin-A disrupted the medial region targeting pattern, and cells deficient in the actin-binding proteins tropomyosin and profilin also did not exhibit medial GFP-Cdc42p staining." ], "offsets": [ [ 0, 243 ] ] } ]

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[ { "id": "BioInfer.d783.s0__text", "type": "Sentence", "text": [ "Unlike fimbrin, L-plastin's actin-bundling action was strictly calcium-dependent: the bundles were formed at pCa 7, but not at pCa 6." ], "offsets": [ [ 0, 133 ] ] } ]

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[ { "id": "BioInfer.d784.s0__text", "type": "Sentence", "text": [ "Unmasking of this site serves as a molecular switch that initiates assembly of an actin-based motility complex containing VASP and profilin." ], "offsets": [ [ 0, 140 ] ] } ]

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[ { "id": "BioInfer.d784.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d784.s0.e0", "arg2_id": "BioInfer.d784.s0.e1", "normalized": [] }, { "id": "BioInfer.d784.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d784.s0.e0", "arg2_id": "BioInfer.d784.s0.e2", "normalized": [] }, { "id": "BioInfer.d784.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d784.s0.e1", "arg2_id": "BioInfer.d784.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d786.s0__text", "type": "Sentence", "text": [ "Using a complementary sequence or antipeptide to selectively neutralize the stretch of residues 633-642 of skeletal myosin heavy chain, we recently demonstrated that this segment is an actin binding site operating in the absence as in the presence of nucleotide and that this stretch 633-642 is not part of the nucleotide binding site [Chaussepied & Morales (1988) Proc. Natl. Acad. Sci. U.S.A. 85, 7471-7475]." ], "offsets": [ [ 0, 410 ] ] } ]

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[ { "id": "BioInfer.d786.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d786.s0.e0", "arg2_id": "BioInfer.d786.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d787.s0__text", "type": "Sentence", "text": [ "Using ITP (a substrate for myosin II ATPase) and/or ATP gamma S (a substrate for myosin II heavy-chain kinase [MHCK]), we demonstrated that phosphorylation of myosin heavy chains occurred at the foci within the actin network, a result that suggests that MHCK was localized at the foci." ], "offsets": [ [ 0, 285 ] ] } ]

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[ { "id": "BioInfer.d787.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d787.s0.e1", "arg2_id": "BioInfer.d787.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d788.s0__text", "type": "Sentence", "text": [ "Using the known three-dimensional structure of the homologous actin-binding domain of fimbrin, these results have enabled us to determine the likely orientation of the utrophin actin-binding domain with respect to the actin filament." ], "offsets": [ [ 0, 233 ] ] } ]

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[ { "id": "BioInfer.d789.s0__text", "type": "Sentence", "text": [ "Using the 'nuclear displacement assay' as a measure of the integrity of the actin cytoskeleton in living stamen hair cells, we demonstrated that AtFim1 protects actin filaments in these cells from Z. mays profilin (ZmPRO5)-induced depolymerization, in a dose-dependent manner." ], "offsets": [ [ 0, 276 ] ] } ]

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[ { "id": "BioInfer.d790.s0__text", "type": "Sentence", "text": [ "Using these methods, we confirm previous reports that intact talin induces cross-linking as well as filament shortening on actin networks." ], "offsets": [ [ 0, 138 ] ] } ]

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[ { "id": "BioInfer.d790.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d790.s0.e0", "arg2_id": "BioInfer.d790.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d791.s0__text", "type": "Sentence", "text": [ "Vascular endothelial cadherin (VE-cadherin) clusters were co-localized with beta-catenin, an important signal transduction ligand, and with alpha-catenin, which is thought to link the complex to the peri-junctional actin." ], "offsets": [ [ 0, 221 ] ] } ]

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[ { "id": "BioInfer.d791.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d791.s0.e0", "arg2_id": "BioInfer.d791.s0.e3", "normalized": [] }, { "id": "BioInfer.d791.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d791.s0.e0", "arg2_id": "BioInfer.d791.s0.e4", "normalized": [] }, { "id": "BioInfer.d791.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d791.s0.e1", "arg2_id": "BioInfer.d791.s0.e3", "normalized": [] }, { "id": "BioInfer.d791.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d791.s0.e2", "arg2_id": "BioInfer.d791.s0.e3", "normalized": [] }, { "id": "BioInfer.d791.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d791.s0.e2", "arg2_id": "BioInfer.d791.s0.e4", "normalized": [] } ]

[ { "id": "BioInfer.d792.s0__text", "type": "Sentence", "text": [ "VASP, in turn, provides the ABM-2 sequences [XPPPPP, X = G, P, L, S, A] for binding profilin, an actin-regulatory protein that stimulates actin filament assembly." ], "offsets": [ [ 0, 162 ] ] } ]

[ { "id": "BioInfer.d792.s0.e0", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 84, 92 ] ], "normalized": [] }, { "id": "BioInfer.d792.s0.e1", "type": "Individual_protein", "text": [ "VASP" ], "offsets": [ [ 0, 4 ] ], "normalized": [] }, { "id": "BioInfer.d792.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 97, 102 ] ], "normalized": [] }, { "id": "BioInfer.d792.s0.e3", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 138, 143 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d793.s0__text", "type": "Sentence", "text": [ "Villin and fimbrin are two actin-binding proteins that bundle actin filaments in the intestine and kidney brush border epithelium." ], "offsets": [ [ 0, 130 ] ] } ]

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[ { "id": "BioInfer.d795.s0__text", "type": "Sentence", "text": [ "WASp contains a binding motif for the Rho GTPase CDC42Hs as well as verprolin/cofilin-like actin-regulatory domains, but no specific actin structure regulated by CDC42Hs-WASp has been identified." ], "offsets": [ [ 0, 195 ] ] } ]

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[ { "id": "BioInfer.d796.s0__text", "type": "Sentence", "text": [ "We also analysed NHEJ in other DNA damage response mutants and showed that the checkpoint mutant rad3-d and two recombination mutants defective in rhp51 and rhp54 (homologues of S.cerevisiae RAD51 and RAD54, respectively) are not affected." ], "offsets": [ [ 0, 239 ] ] } ]

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[ { "id": "BioInfer.d797.s0__text", "type": "Sentence", "text": [ "We believe that this complex may mediate the cortical functions of profilin at actin patches in S. pombe." ], "offsets": [ [ 0, 105 ] ] } ]

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[ { "id": "BioInfer.d799.s0__text", "type": "Sentence", "text": [ "We constructed recombinant viruses based on the herpes simplex virus type 1 mutant tsK which individually were able to express the products of four viral DNA replication genes (UL5, UL8, UL9 and UL52) in the absence of any of the other proteins required for viral DNA synthesis." ], "offsets": [ [ 0, 278 ] ] } ]

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[ { "id": "BioInfer.d800.s0__text", "type": "Sentence", "text": [ "We describe the localization of cadherin-11 and N-cadherin along the cell margins of mouse osteoblast-like cells, the colocalization of \"pancadherin\" with alpha-catenin, beta-catenin, p120, and vinculin, and the association of these complexes with the actin microfilaments." ], "offsets": [ [ 0, 273 ] ] } ]

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[ { "id": "BioInfer.d801.s0__text", "type": "Sentence", "text": [ "We determined whether short-term weight-lifting exercise increases the synthesis rate of the major contractile proteins, myosin heavy chain (MHC), actin, and mixed muscle proteins in nonfrail elders and younger women and men." ], "offsets": [ [ 0, 225 ] ] } ]

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[ { "id": "BioInfer.d802.s0__text", "type": "Sentence", "text": [ "We examined whether levels of alpha-smooth-muscle actin or proliferating cell nuclear antigen correlated with myosin heavy-chain levels in the glomeruli of rats with puromycin aminonucleoside nephrosis." ], "offsets": [ [ 0, 202 ] ] } ]

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[ { "id": "BioInfer.d803.s0__text", "type": "Sentence", "text": [ "We find that profilin and cofilin regulate actin-filament formation throughout the cell cortex." ], "offsets": [ [ 0, 95 ] ] } ]

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[ { "id": "BioInfer.d804.s0__text", "type": "Sentence", "text": [ "We find that profilin contributes in several ways to Cdc42-induced nucleation of actin filaments in high speed supernatant of lysed neutrophils." ], "offsets": [ [ 0, 144 ] ] } ]

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[ { "id": "BioInfer.d805.s0__text", "type": "Sentence", "text": [ "We found normal levels of alpha-catenin and beta-catenin in BT549 and HS578t cells; however, low levels of plakoglobin were expressed in these cells compared to those found in weakly invasive MCF-7 cells." ], "offsets": [ [ 0, 204 ] ] } ]

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[ { "id": "BioInfer.d807.s0__text", "type": "Sentence", "text": [ "We have analyzed the expression levels of the genes encoding alpha-catenin, beta-catenin and plakoglobin in correlation to the E-cadherin expression levels in cell lines derived from human cervical carcinomas." ], "offsets": [ [ 0, 209 ] ] } ]

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[ { "id": "BioInfer.d809.s0__text", "type": "Sentence", "text": [ "We have characterized this actin with respect to its ability to interact with yeast profilin and tropomyosin, the only yeast actin-binding proteins so far purified and characterized." ], "offsets": [ [ 0, 182 ] ] } ]

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[ { "id": "BioInfer.d809.s1__text", "type": "Sentence", "text": [ "Yeast profilin can sequester yeast actin monomers and thereby reduce the ability of yeast actin to polymerize, whereas it has little effect on the degree of polymerization of rabbit skeletal muscle actin." ], "offsets": [ [ 0, 204 ] ] } ]

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[ { "id": "BioInfer.d810.s0__text", "type": "Sentence", "text": [ "We have cloned a Saccharomyces cerevisiae gene (COF1) encoding a low-M(r) actin-binding protein of 143 amino acid (aa) residues (yeast cofilin; Cof); its aa sequence is 35% identical to porcine Cof." ], "offsets": [ [ 0, 198 ] ] } ]

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[ { "id": "BioInfer.d812.s0__text", "type": "Sentence", "text": [ "We have examined the level of cyclin E, a G1 cyclin, and p27kip, a cyclin-dependent kinase inhibitor, in BALB/c 3T3 cells." ], "offsets": [ [ 0, 122 ] ] } ]

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[ { "id": "BioInfer.d813.s0__text", "type": "Sentence", "text": [ "We have found that cofilin, a 21-kDa actin-binding protein, is a component of these rods." ], "offsets": [ [ 0, 89 ] ] } ]

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[ { "id": "BioInfer.d814.s0__text", "type": "Sentence", "text": [ "We have shown that the FH proteins Bni1p and Bnr1p are potential targets of the Rho family small GTP-binding proteins and bind to an actin-binding protein, profilin, at their proline-rich FH1 domains to regulate reorganization of the actin cytoskeleton in the yeast Saccharomyces cerevisiae." ], "offsets": [ [ 0, 291 ] ] } ]

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[ { "id": "BioInfer.d815.s0__text", "type": "Sentence", "text": [ "We have shown that these proteins are indeed nuclear basic proteins: the 14 kd is the histone H4, the 19 kd is the histone H3, and the 25 kd is the sperm-specific protein SP2." ], "offsets": [ [ 0, 175 ] ] } ]

[ { "id": "BioInfer.d815.s0.e0", "type": "Protein_family_or_group", "text": [ "nuclear basic proteins" ], "offsets": [ [ 45, 67 ] ], "normalized": [] }, { "id": "BioInfer.d815.s0.e1", "type": "Protein_family_or_group", "text": [ "histone" ], "offsets": [ [ 115, 122 ] ], "normalized": [] }, { "id": "BioInfer.d815.s0.e2", "type": "Protein_family_or_group", "text": [ "histone" ], "offsets": [ [ 86, 93 ] ], "normalized": [] }, { "id": "BioInfer.d815.s0.e3", "type": "Individual_protein", "text": [ "H4" ], "offsets": [ [ 94, 96 ] ], "normalized": [] }, { "id": "BioInfer.d815.s0.e4", "type": "Individual_protein", "text": [ "SP2" ], "offsets": [ [ 171, 174 ] ], "normalized": [] }, { "id": "BioInfer.d815.s0.e5", "type": "Individual_protein", "text": [ "H3" ], "offsets": [ [ 123, 125 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d815.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d815.s0.e0", "arg2_id": "BioInfer.d815.s0.e3", "normalized": [] }, { "id": "BioInfer.d815.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d815.s0.e0", "arg2_id": "BioInfer.d815.s0.e4", "normalized": [] }, { "id": "BioInfer.d815.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d815.s0.e0", "arg2_id": "BioInfer.d815.s0.e5", "normalized": [] }, { "id": "BioInfer.d815.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d815.s0.e1", "arg2_id": "BioInfer.d815.s0.e5", "normalized": [] }, { "id": "BioInfer.d815.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d815.s0.e2", "arg2_id": "BioInfer.d815.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d817.s0__text", "type": "Sentence", "text": [ "We previously showed that actin is transported in an unassembled form with its associated proteins actin depolymerizing factor, cofilin, and profilin." ], "offsets": [ [ 0, 150 ] ] } ]

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[ { "id": "BioInfer.d817.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d817.s0.e0", "arg2_id": "BioInfer.d817.s0.e1", "normalized": [] }, { "id": "BioInfer.d817.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d817.s0.e0", "arg2_id": "BioInfer.d817.s0.e2", "normalized": [] }, { "id": "BioInfer.d817.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d817.s0.e0", "arg2_id": "BioInfer.d817.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d819.s0__text", "type": "Sentence", "text": [ "We report here that tropomyosin, which is found in the rootlet but not in the microvillus core, can bind to and saturate the actin of isolated cores, and can cause the dissociation of up to 30% of the villin and fimbrin from the cores but does not affect actin binding by 110-kD calmodulin." ], "offsets": [ [ 0, 290 ] ] } ]

[ { "id": "BioInfer.d819.s0.e0", "type": "Individual_protein", "text": [ "villin" ], "offsets": [ [ 201, 207 ] ], "normalized": [] }, { "id": "BioInfer.d819.s0.e1", "type": "Individual_protein", "text": [ "calmodulin" ], "offsets": [ [ 279, 289 ] ], "normalized": [] }, { "id": "BioInfer.d819.s0.e2", "type": "Individual_protein", "text": [ "fimbrin" ], "offsets": [ [ 212, 219 ] ], "normalized": [] }, { "id": "BioInfer.d819.s0.e3", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 255, 260 ] ], "normalized": [] }, { "id": "BioInfer.d819.s0.e4", "type": "Individual_protein", "text": [ "tropomyosin" ], "offsets": [ [ 20, 31 ] ], "normalized": [] }, { "id": "BioInfer.d819.s0.e5", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 125, 130 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d819.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d819.s0.e0", "arg2_id": "BioInfer.d819.s0.e4", "normalized": [] }, { "id": "BioInfer.d819.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d819.s0.e1", "arg2_id": "BioInfer.d819.s0.e3", "normalized": [] }, { "id": "BioInfer.d819.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d819.s0.e1", "arg2_id": "BioInfer.d819.s0.e4", "normalized": [] }, { "id": "BioInfer.d819.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d819.s0.e2", "arg2_id": "BioInfer.d819.s0.e4", "normalized": [] }, { "id": "BioInfer.d819.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d819.s0.e3", "arg2_id": "BioInfer.d819.s0.e4", "normalized": [] }, { "id": "BioInfer.d819.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d819.s0.e4", "arg2_id": "BioInfer.d819.s0.e5", "normalized": [] } ]

[ { "id": "BioInfer.d821.s0__text", "type": "Sentence", "text": [ "We show that the HSV-1 UL5, UL8, UL29, UL30, UL42, and UL52 gene products along with the AAV Rep68 protein are sufficient to initiate replication on duplex DNA containing the AAV origins of replication, resulting in products several hundred nucleotides in length." ], "offsets": [ [ 0, 263 ] ] } ]

[ { "id": "BioInfer.d821.s0.e0", "type": "Gene/protein/RNA", "text": [ "UL30" ], "offsets": [ [ 39, 43 ] ], "normalized": [] }, { "id": "BioInfer.d821.s0.e1", "type": "Gene/protein/RNA", "text": [ "UL29" ], "offsets": [ [ 33, 37 ] ], "normalized": [] }, { "id": "BioInfer.d821.s0.e2", "type": "Gene/protein/RNA", "text": [ "UL8" ], "offsets": [ [ 28, 31 ] ], "normalized": [] }, { "id": "BioInfer.d821.s0.e3", "type": "Gene/protein/RNA", "text": [ "UL5" ], "offsets": [ [ 23, 26 ] ], "normalized": [] }, { "id": "BioInfer.d821.s0.e4", "type": "Gene/protein/RNA", "text": [ "Rep68" ], "offsets": [ [ 93, 98 ] ], "normalized": [] }, { "id": "BioInfer.d821.s0.e5", "type": "Gene/protein/RNA", "text": [ "UL52" ], "offsets": [ [ 55, 59 ] ], "normalized": [] }, { "id": "BioInfer.d821.s0.e6", "type": "Gene/protein/RNA", "text": [ "UL42" ], "offsets": [ [ 45, 49 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d822.s0__text", "type": "Sentence", "text": [ "We speculate that fimbrin may help maintain the parallel growth of actin filaments within the stereocilia." ], "offsets": [ [ 0, 106 ] ] } ]

[ { "id": "BioInfer.d822.s0.e0", "type": "Individual_protein", "text": [ "fimbrin" ], "offsets": [ [ 18, 25 ] ], "normalized": [] }, { "id": "BioInfer.d822.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 67, 72 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d822.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d822.s0.e0", "arg2_id": "BioInfer.d822.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d823.s0__text", "type": "Sentence", "text": [ "Western analysis of gel-purified USF-nucleosome and GAL4-AH-nucleosome complexes demonstrated the predominant presence of acetylated histone H4 relative to acetylated histone H3." ], "offsets": [ [ 0, 178 ] ] } ]

[ { "id": "BioInfer.d823.s0.e0", "type": "Individual_protein", "text": [ "H3" ], "offsets": [ [ 175, 177 ] ], "normalized": [] }, { "id": "BioInfer.d823.s0.e1", "type": "Individual_protein", "text": [ "nucleosome" ], "offsets": [ [ 60, 70 ] ], "normalized": [] }, { "id": "BioInfer.d823.s0.e2", "type": "Protein_family_or_group", "text": [ "histone" ], "offsets": [ [ 167, 174 ] ], "normalized": [] }, { "id": "BioInfer.d823.s0.e3", "type": "Individual_protein", "text": [ "nucleosome" ], "offsets": [ [ 37, 47 ] ], "normalized": [] }, { "id": "BioInfer.d823.s0.e4", "type": "Individual_protein", "text": [ "AH" ], "offsets": [ [ 57, 59 ] ], "normalized": [] }, { "id": "BioInfer.d823.s0.e5", "type": "Protein_family_or_group", "text": [ "histone" ], "offsets": [ [ 133, 140 ] ], "normalized": [] }, { "id": "BioInfer.d823.s0.e6", "type": "Individual_protein", "text": [ "USF" ], "offsets": [ [ 33, 36 ] ], "normalized": [] }, { "id": "BioInfer.d823.s0.e7", "type": "Individual_protein", "text": [ "GAL4" ], "offsets": [ [ 52, 56 ] ], "normalized": [] }, { "id": "BioInfer.d823.s0.e8", "type": "Individual_protein", "text": [ "H4" ], "offsets": [ [ 141, 143 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d823.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d823.s0.e0", "arg2_id": "BioInfer.d823.s0.e1", "normalized": [] }, { "id": "BioInfer.d823.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d823.s0.e0", "arg2_id": "BioInfer.d823.s0.e2", "normalized": [] }, { "id": "BioInfer.d823.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d823.s0.e0", "arg2_id": "BioInfer.d823.s0.e3", "normalized": [] }, { "id": "BioInfer.d823.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d823.s0.e0", "arg2_id": "BioInfer.d823.s0.e4", "normalized": [] }, { "id": "BioInfer.d823.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d823.s0.e0", "arg2_id": "BioInfer.d823.s0.e6", "normalized": [] }, { "id": "BioInfer.d823.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d823.s0.e0", "arg2_id": "BioInfer.d823.s0.e7", "normalized": [] }, { "id": "BioInfer.d823.s0.i6", "type": "PPI", "arg1_id": "BioInfer.d823.s0.e0", "arg2_id": "BioInfer.d823.s0.e8", "normalized": [] }, { "id": "BioInfer.d823.s0.i7", "type": "PPI", "arg1_id": "BioInfer.d823.s0.e1", "arg2_id": "BioInfer.d823.s0.e4", "normalized": [] }, { "id": "BioInfer.d823.s0.i8", "type": "PPI", "arg1_id": "BioInfer.d823.s0.e1", "arg2_id": "BioInfer.d823.s0.e7", "normalized": [] }, { "id": "BioInfer.d823.s0.i9", "type": "PPI", "arg1_id": "BioInfer.d823.s0.e1", "arg2_id": "BioInfer.d823.s0.e8", "normalized": [] }, { "id": "BioInfer.d823.s0.i10", "type": "PPI", "arg1_id": "BioInfer.d823.s0.e3", "arg2_id": "BioInfer.d823.s0.e6", "normalized": [] }, { "id": "BioInfer.d823.s0.i11", "type": "PPI", "arg1_id": "BioInfer.d823.s0.e3", "arg2_id": "BioInfer.d823.s0.e8", "normalized": [] }, { "id": "BioInfer.d823.s0.i12", "type": "PPI", "arg1_id": "BioInfer.d823.s0.e4", "arg2_id": "BioInfer.d823.s0.e7", "normalized": [] }, { "id": "BioInfer.d823.s0.i13", "type": "PPI", "arg1_id": "BioInfer.d823.s0.e4", "arg2_id": "BioInfer.d823.s0.e8", "normalized": [] }, { "id": "BioInfer.d823.s0.i14", "type": "PPI", "arg1_id": "BioInfer.d823.s0.e5", "arg2_id": "BioInfer.d823.s0.e8", "normalized": [] }, { "id": "BioInfer.d823.s0.i15", "type": "PPI", "arg1_id": "BioInfer.d823.s0.e6", "arg2_id": "BioInfer.d823.s0.e8", "normalized": [] }, { "id": "BioInfer.d823.s0.i16", "type": "PPI", "arg1_id": "BioInfer.d823.s0.e7", "arg2_id": "BioInfer.d823.s0.e8", "normalized": [] } ]

[ { "id": "BioInfer.d827.s0__text", "type": "Sentence", "text": [ "We then compared colorectal cancers with 'mild' RER (n = 15), and those with 'severe' RER without (n = 11) or with (n = 22) detectable mutations in MSH2 or MLH1 to assess the involvement of mononucleotide repeats contained in the coding regions of MSH3, MSH6, BAX, and TGFbeta RII." ], "offsets": [ [ 0, 281 ] ] } ]

[ { "id": "BioInfer.d827.s0.e0", "type": "Gene/protein/RNA", "text": [ "MSH2" ], "offsets": [ [ 148, 152 ] ], "normalized": [] }, { "id": "BioInfer.d827.s0.e1", "type": "Gene/protein/RNA", "text": [ "MSH3" ], "offsets": [ [ 248, 252 ] ], "normalized": [] }, { "id": "BioInfer.d827.s0.e2", "type": "Gene/protein/RNA", "text": [ "MLH1" ], "offsets": [ [ 156, 160 ] ], "normalized": [] }, { "id": "BioInfer.d827.s0.e3", "type": "Gene/protein/RNA", "text": [ "BAX" ], "offsets": [ [ 260, 263 ] ], "normalized": [] }, { "id": "BioInfer.d827.s0.e4", "type": "Gene/protein/RNA", "text": [ "MSH6" ], "offsets": [ [ 254, 258 ] ], "normalized": [] }, { "id": "BioInfer.d827.s0.e5", "type": "Gene/protein/RNA", "text": [ "TGFbeta RII" ], "offsets": [ [ 269, 280 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d828.s0__text", "type": "Sentence", "text": [ "We used yeast as a model to test this hypothesis and found that chromosome deletion of any known nuclear mitotic mismatch repair genes, including MLH1, MSH2, MSH3, MSH6, and PMS1, did not rescue mgt1delta O6 MeG DNA repair methyltransferase-deficient cells from killing by MNNG." ], "offsets": [ [ 0, 278 ] ] } ]

[ { "id": "BioInfer.d828.s0.e0", "type": "Gene/protein/RNA", "text": [ "methyltransferase" ], "offsets": [ [ 223, 240 ] ], "normalized": [] }, { "id": "BioInfer.d828.s0.e1", "type": "Gene/protein/RNA", "text": [ "mgt1" ], "offsets": [ [ 195, 199 ] ], "normalized": [] }, { "id": "BioInfer.d828.s0.e2", "type": "Gene/protein/RNA", "text": [ "MSH6" ], "offsets": [ [ 164, 168 ] ], "normalized": [] }, { "id": "BioInfer.d828.s0.e3", "type": "Gene/protein/RNA", "text": [ "PMS1" ], "offsets": [ [ 174, 178 ] ], "normalized": [] }, { "id": "BioInfer.d828.s0.e4", "type": "Gene/protein/RNA", "text": [ "MSH2" ], "offsets": [ [ 152, 156 ] ], "normalized": [] }, { "id": "BioInfer.d828.s0.e5", "type": "Gene/protein/RNA", "text": [ "MSH3" ], "offsets": [ [ 158, 162 ] ], "normalized": [] }, { "id": "BioInfer.d828.s0.e6", "type": "Gene/protein/RNA", "text": [ "MLH1" ], "offsets": [ [ 146, 150 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d829.s0__text", "type": "Sentence", "text": [ "When a lyophilized Mf and AO mixture was incubated at 40 degrees C and 65% relative humidity, the conjugation of AO was confirmed at myosin heavy chain, actin, and tropomyosin." ], "offsets": [ [ 0, 176 ] ] } ]

[ { "id": "BioInfer.d829.s0.e0", "type": "Gene/protein/RNA", "text": [ "tropomyosin" ], "offsets": [ [ 164, 175 ] ], "normalized": [] }, { "id": "BioInfer.d829.s0.e1", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 153, 158 ] ], "normalized": [] }, { "id": "BioInfer.d829.s0.e2", "type": "Gene/protein/RNA", "text": [ "myosin heavy chain" ], "offsets": [ [ 133, 151 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d830.s0__text", "type": "Sentence", "text": [ "When the actin monomer pool in untransfected myoblasts is increased 70% by treatment with latrunculin A, synthesis of ADF and actin are down-regulated compared with cofilin and 19 other proteins selected at random." ], "offsets": [ [ 0, 214 ] ] } ]

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[ { "id": "BioInfer.d831.s0__text", "type": "Sentence", "text": [ "While levels of most of these proteins decrease, accumulation of cyclin D1 and the cyclin-dependent kinase inhibitor p21 Cip1/WAF1 is observed." ], "offsets": [ [ 0, 143 ] ] } ]

[ { "id": "BioInfer.d831.s0.e0", "type": "Individual_protein", "text": [ "WAF1" ], "offsets": [ [ 126, 130 ] ], "normalized": [] }, { "id": "BioInfer.d831.s0.e1", "type": "Individual_protein", "text": [ "p21" ], "offsets": [ [ 117, 120 ] ], "normalized": [] }, { "id": "BioInfer.d831.s0.e2", "type": "Gene/protein/RNA", "text": [ "cyclin D1" ], "offsets": [ [ 65, 74 ] ], "normalized": [] }, { "id": "BioInfer.d831.s0.e3", "type": "Protein_family_or_group", "text": [ "cyclin-dependent kinase inhibitor" ], "offsets": [ [ 83, 116 ] ], "normalized": [] }, { "id": "BioInfer.d831.s0.e4", "type": "Individual_protein", "text": [ "Cip1" ], "offsets": [ [ 121, 125 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d831.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d831.s0.e0", "arg2_id": "BioInfer.d831.s0.e3", "normalized": [] }, { "id": "BioInfer.d831.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d831.s0.e1", "arg2_id": "BioInfer.d831.s0.e3", "normalized": [] }, { "id": "BioInfer.d831.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d831.s0.e3", "arg2_id": "BioInfer.d831.s0.e4", "normalized": [] } ]

[ { "id": "BioInfer.d832.s0__text", "type": "Sentence", "text": [ "While poly(ADP-ribose) effectively competed with DNA for binding of histone H4, it equally competed with DNA for binding of histone H3 and only inefficiently competed with DNA for binding of histone H1." ], "offsets": [ [ 0, 202 ] ] } ]

[ { "id": "BioInfer.d832.s0.e0", "type": "Protein_family_or_group", "text": [ "histone" ], "offsets": [ [ 124, 131 ] ], "normalized": [] }, { "id": "BioInfer.d832.s0.e1", "type": "Individual_protein", "text": [ "H3" ], "offsets": [ [ 132, 134 ] ], "normalized": [] }, { "id": "BioInfer.d832.s0.e2", "type": "Protein_family_or_group", "text": [ "histone" ], "offsets": [ [ 191, 198 ] ], "normalized": [] }, { "id": "BioInfer.d832.s0.e3", "type": "Protein_family_or_group", "text": [ "histone" ], "offsets": [ [ 68, 75 ] ], "normalized": [] }, { "id": "BioInfer.d832.s0.e4", "type": "Individual_protein", "text": [ "H4" ], "offsets": [ [ 76, 78 ] ], "normalized": [] }, { "id": "BioInfer.d832.s0.e5", "type": "Individual_protein", "text": [ "H1" ], "offsets": [ [ 199, 201 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d832.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d832.s0.e0", "arg2_id": "BioInfer.d832.s0.e1", "normalized": [] }, { "id": "BioInfer.d832.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d832.s0.e2", "arg2_id": "BioInfer.d832.s0.e5", "normalized": [] }, { "id": "BioInfer.d832.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d832.s0.e3", "arg2_id": "BioInfer.d832.s0.e4", "normalized": [] } ]

[ { "id": "BioInfer.d833.s0__text", "type": "Sentence", "text": [ "Within 1 hour of raising the concentration of calcium ions, integrins, cadherins, alpha-catenin, beta-catenin, plakoglobin, vinculin and alpha-actinin appeared to accumulate at cell-cell borders, whereas the focal contact proteins, paxillin and talin, did not." ], "offsets": [ [ 0, 260 ] ] } ]

[ { "id": "BioInfer.d833.s0.e0", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 97, 109 ] ], "normalized": [] }, { "id": "BioInfer.d833.s0.e1", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 82, 95 ] ], "normalized": [] }, { "id": "BioInfer.d833.s0.e2", "type": "Individual_protein", "text": [ "paxillin" ], "offsets": [ [ 232, 240 ] ], "normalized": [] }, { "id": "BioInfer.d833.s0.e3", "type": "Individual_protein", "text": [ "talin" ], "offsets": [ [ 245, 250 ] ], "normalized": [] }, { "id": "BioInfer.d833.s0.e4", "type": "Individual_protein", "text": [ "plakoglobin" ], "offsets": [ [ 111, 122 ] ], "normalized": [] }, { "id": "BioInfer.d833.s0.e5", "type": "Individual_protein", "text": [ "alpha-actinin" ], "offsets": [ [ 137, 150 ] ], "normalized": [] }, { "id": "BioInfer.d833.s0.e6", "type": "Individual_protein", "text": [ "vinculin" ], "offsets": [ [ 124, 132 ] ], "normalized": [] }, { "id": "BioInfer.d833.s0.e7", "type": "Individual_protein", "text": [ "cadherins" ], "offsets": [ [ 71, 80 ] ], "normalized": [] }, { "id": "BioInfer.d833.s0.e8", "type": "Individual_protein", "text": [ "integrins" ], "offsets": [ [ 60, 69 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d834.s0__text", "type": "Sentence", "text": [ "Within the sieve-tube exudate, profilin was present in 15-fold molar excess to actin." ], "offsets": [ [ 0, 85 ] ] } ]

[ { "id": "BioInfer.d834.s0.e0", "type": "Gene/protein/RNA", "text": [ "profilin" ], "offsets": [ [ 31, 39 ] ], "normalized": [] }, { "id": "BioInfer.d834.s0.e1", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 79, 84 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d835.s0__text", "type": "Sentence", "text": [ "YACs containing color vision red pigment gene DNA or 1.5 rDNA tandem repeat units were transformed into hosts bearing lesions at the RAD1, RAD6, RAD51, or RAD52 loci." ], "offsets": [ [ 0, 166 ] ] } ]

[ { "id": "BioInfer.d835.s0.e0", "type": "Gene/protein/RNA", "text": [ "RAD52" ], "offsets": [ [ 155, 160 ] ], "normalized": [] }, { "id": "BioInfer.d835.s0.e1", "type": "Gene/protein/RNA", "text": [ "color vision red pigment" ], "offsets": [ [ 16, 40 ] ], "normalized": [] }, { "id": "BioInfer.d835.s0.e2", "type": "Gene/protein/RNA", "text": [ "RAD6" ], "offsets": [ [ 139, 143 ] ], "normalized": [] }, { "id": "BioInfer.d835.s0.e3", "type": "Gene/protein/RNA", "text": [ "RAD51" ], "offsets": [ [ 145, 150 ] ], "normalized": [] }, { "id": "BioInfer.d835.s0.e4", "type": "Gene/protein/RNA", "text": [ "RAD1" ], "offsets": [ [ 133, 137 ] ], "normalized": [] } ]

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