Datasets:

---

knowledgator

/

bio-NER-relations

like 3

Follow

Knowledgator Engineering 126

[ { "id": "BioInfer.d193.s0__text", "type": "Sentence", "text": [ "Evaluation of the binding of Acanthamoeba profilin to pyrene-labeled actin by fluorescence enhancement." ], "offsets": [ [ 0, 103 ] ] } ]

[ { "id": "BioInfer.d193.s0.e0", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 42, 50 ] ], "normalized": [] }, { "id": "BioInfer.d193.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 69, 74 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d193.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d193.s0.e0", "arg2_id": "BioInfer.d193.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d195.s0__text", "type": "Sentence", "text": [ "Evidence for a conformational change in actin induced by fimbrin (N375) binding." ], "offsets": [ [ 0, 80 ] ] } ]

[ { "id": "BioInfer.d195.s0.e0", "type": "Individual_protein", "text": [ "fimbrin" ], "offsets": [ [ 57, 64 ] ], "normalized": [] }, { "id": "BioInfer.d195.s0.e1", "type": "Individual_protein", "text": [ "N375" ], "offsets": [ [ 66, 70 ] ], "normalized": [] }, { "id": "BioInfer.d195.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 40, 45 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d195.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d195.s0.e0", "arg2_id": "BioInfer.d195.s0.e1", "normalized": [] }, { "id": "BioInfer.d195.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d195.s0.e1", "arg2_id": "BioInfer.d195.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d197.s0__text", "type": "Sentence", "text": [ "Exclusion of cardiac myosin heavy chain and actin gene involvement in hypertrophic cardiomyopathy of several French families." ], "offsets": [ [ 0, 125 ] ] } ]

[ { "id": "BioInfer.d197.s0.e0", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 44, 49 ] ], "normalized": [] }, { "id": "BioInfer.d197.s0.e1", "type": "Gene/protein/RNA", "text": [ "cardiac myosin heavy chain" ], "offsets": [ [ 13, 39 ] ], "normalized": [] } ]

[]

[]

[]

[ { "id": "BioInfer.d199.s0__text", "type": "Sentence", "text": [ "Exposure of the cells to tumor promoter did, however, result in a loss of actin and talin-rich cell surface elaborations that resemble focal contact precursor structures." ], "offsets": [ [ 0, 170 ] ] } ]

[ { "id": "BioInfer.d199.s0.e0", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 74, 79 ] ], "normalized": [] }, { "id": "BioInfer.d199.s0.e1", "type": "Gene/protein/RNA", "text": [ "talin" ], "offsets": [ [ 84, 89 ] ], "normalized": [] } ]

[]

[]

[]

[ { "id": "BioInfer.d201.s0__text", "type": "Sentence", "text": [ "Expression of actin and myosin heavy chain genes in skeletal, cardiac and uterine muscles of young and old rats." ], "offsets": [ [ 0, 112 ] ] } ]

[ { "id": "BioInfer.d201.s0.e0", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 14, 19 ] ], "normalized": [] }, { "id": "BioInfer.d201.s0.e1", "type": "Gene/protein/RNA", "text": [ "myosin heavy chain" ], "offsets": [ [ 24, 42 ] ], "normalized": [] } ]

[]

[]

[]

[ { "id": "BioInfer.d202.s0__text", "type": "Sentence", "text": [ "Expression of alpha-catenin was generally weak and did not correlate with the expression of either beta-catenin or E-cadherin." ], "offsets": [ [ 0, 126 ] ] } ]

[ { "id": "BioInfer.d202.s0.e0", "type": "Individual_protein", "text": [ "E-cadherin" ], "offsets": [ [ 115, 125 ] ], "normalized": [] }, { "id": "BioInfer.d202.s0.e1", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 14, 27 ] ], "normalized": [] }, { "id": "BioInfer.d202.s0.e2", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 99, 111 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d202.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d202.s0.e0", "arg2_id": "BioInfer.d202.s0.e1", "normalized": [] }, { "id": "BioInfer.d202.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d202.s0.e1", "arg2_id": "BioInfer.d202.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d204.s0__text", "type": "Sentence", "text": [ "Expression of c-Myc or cyclin D1 was sufficient to activate cyclin E-Cdk2 by promoting the formation of high-molecular-weight complexes lacking the cyclin-dependent kinase inhibitor p21, as has been described, following estrogen treatment." ], "offsets": [ [ 0, 239 ] ] } ]

[ { "id": "BioInfer.d204.s0.e0", "type": "Individual_protein", "text": [ "cyclin D1" ], "offsets": [ [ 23, 32 ] ], "normalized": [] }, { "id": "BioInfer.d204.s0.e1", "type": "Individual_protein", "text": [ "Cdk2" ], "offsets": [ [ 69, 73 ] ], "normalized": [] }, { "id": "BioInfer.d204.s0.e2", "type": "Individual_protein", "text": [ "cyclin E" ], "offsets": [ [ 60, 68 ] ], "normalized": [] }, { "id": "BioInfer.d204.s0.e3", "type": "Protein_family_or_group", "text": [ "cyclin-dependent kinase inhibitor" ], "offsets": [ [ 148, 181 ] ], "normalized": [] }, { "id": "BioInfer.d204.s0.e4", "type": "Individual_protein", "text": [ "c-Myc" ], "offsets": [ [ 14, 19 ] ], "normalized": [] }, { "id": "BioInfer.d204.s0.e5", "type": "Individual_protein", "text": [ "p21" ], "offsets": [ [ 182, 185 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d204.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d204.s0.e0", "arg2_id": "BioInfer.d204.s0.e1", "normalized": [] }, { "id": "BioInfer.d204.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d204.s0.e0", "arg2_id": "BioInfer.d204.s0.e2", "normalized": [] }, { "id": "BioInfer.d204.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d204.s0.e1", "arg2_id": "BioInfer.d204.s0.e2", "normalized": [] }, { "id": "BioInfer.d204.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d204.s0.e1", "arg2_id": "BioInfer.d204.s0.e4", "normalized": [] }, { "id": "BioInfer.d204.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d204.s0.e2", "arg2_id": "BioInfer.d204.s0.e4", "normalized": [] }, { "id": "BioInfer.d204.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d204.s0.e3", "arg2_id": "BioInfer.d204.s0.e5", "normalized": [] } ]

[ { "id": "BioInfer.d205.s0__text", "type": "Sentence", "text": [ "Expression of E-cadherin, alpha-catenin and beta-catenin in normal ovarian surface epithelium and epithelial ovarian cancers." ], "offsets": [ [ 0, 125 ] ] } ]

[ { "id": "BioInfer.d205.s0.e0", "type": "Gene/protein/RNA", "text": [ "E-cadherin" ], "offsets": [ [ 14, 24 ] ], "normalized": [] }, { "id": "BioInfer.d205.s0.e1", "type": "Gene/protein/RNA", "text": [ "beta-catenin" ], "offsets": [ [ 44, 56 ] ], "normalized": [] }, { "id": "BioInfer.d205.s0.e2", "type": "Gene/protein/RNA", "text": [ "alpha-catenin" ], "offsets": [ [ 26, 39 ] ], "normalized": [] } ]

[]

[]

[]

[ { "id": "BioInfer.d207.s0__text", "type": "Sentence", "text": [ "Features studied were actin, microtubules, vinculin, and talin, using immunofluorescence, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and immunoblotting; permeability of the cell sheet; wound healing; and phagocytic capacity." ], "offsets": [ [ 0, 240 ] ] } ]

[ { "id": "BioInfer.d207.s0.e0", "type": "Gene/protein/RNA", "text": [ "talin" ], "offsets": [ [ 57, 62 ] ], "normalized": [] }, { "id": "BioInfer.d207.s0.e1", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 22, 27 ] ], "normalized": [] }, { "id": "BioInfer.d207.s0.e2", "type": "Gene/protein/RNA", "text": [ "vinculin" ], "offsets": [ [ 43, 51 ] ], "normalized": [] } ]

[]

[]

[]

[ { "id": "BioInfer.d208.s0__text", "type": "Sentence", "text": [ "Finally, both receptors can interact with FADD, TRADD, and RIP." ], "offsets": [ [ 0, 63 ] ] } ]

[ { "id": "BioInfer.d208.s0.e0", "type": "Gene/protein/RNA", "text": [ "TRADD" ], "offsets": [ [ 48, 53 ] ], "normalized": [] }, { "id": "BioInfer.d208.s0.e1", "type": "Gene/protein/RNA", "text": [ "RIP" ], "offsets": [ [ 59, 62 ] ], "normalized": [] }, { "id": "BioInfer.d208.s0.e2", "type": "Gene/protein/RNA", "text": [ "FADD" ], "offsets": [ [ 42, 46 ] ], "normalized": [] } ]

[]

[]

[]

[ { "id": "BioInfer.d208.s1__text", "type": "Sentence", "text": [ "Thus, both DR5 and DR4 use FADD, TRADD, and RIP in their signal transduction pathways, and FADD is the common mediator of apoptosis by all known death domain-containing receptors." ], "offsets": [ [ 0, 179 ] ] } ]

[ { "id": "BioInfer.d208.s1.e0", "type": "Individual_protein", "text": [ "DR4" ], "offsets": [ [ 19, 22 ] ], "normalized": [] }, { "id": "BioInfer.d208.s1.e1", "type": "Individual_protein", "text": [ "RIP" ], "offsets": [ [ 44, 47 ] ], "normalized": [] }, { "id": "BioInfer.d208.s1.e2", "type": "Individual_protein", "text": [ "TRADD" ], "offsets": [ [ 33, 38 ] ], "normalized": [] }, { "id": "BioInfer.d208.s1.e3", "type": "Individual_protein", "text": [ "DR5" ], "offsets": [ [ 11, 14 ] ], "normalized": [] }, { "id": "BioInfer.d208.s1.e4", "type": "Individual_protein", "text": [ "FADD" ], "offsets": [ [ 27, 31 ] ], "normalized": [] }, { "id": "BioInfer.d208.s1.e5", "type": "Gene/protein/RNA", "text": [ "FADD" ], "offsets": [ [ 91, 95 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d208.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d208.s1.e0", "arg2_id": "BioInfer.d208.s1.e1", "normalized": [] }, { "id": "BioInfer.d208.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d208.s1.e0", "arg2_id": "BioInfer.d208.s1.e2", "normalized": [] }, { "id": "BioInfer.d208.s1.i2", "type": "PPI", "arg1_id": "BioInfer.d208.s1.e0", "arg2_id": "BioInfer.d208.s1.e4", "normalized": [] }, { "id": "BioInfer.d208.s1.i3", "type": "PPI", "arg1_id": "BioInfer.d208.s1.e1", "arg2_id": "BioInfer.d208.s1.e3", "normalized": [] }, { "id": "BioInfer.d208.s1.i4", "type": "PPI", "arg1_id": "BioInfer.d208.s1.e2", "arg2_id": "BioInfer.d208.s1.e3", "normalized": [] }, { "id": "BioInfer.d208.s1.i5", "type": "PPI", "arg1_id": "BioInfer.d208.s1.e3", "arg2_id": "BioInfer.d208.s1.e4", "normalized": [] } ]

[ { "id": "BioInfer.d209.s0__text", "type": "Sentence", "text": [ "Finally it was shown that the two isoforms of actin can be separated from each other in the absence of profilin also by chromatography on hydroxyapatite." ], "offsets": [ [ 0, 153 ] ] } ]

[ { "id": "BioInfer.d209.s0.e0", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 46, 51 ] ], "normalized": [] }, { "id": "BioInfer.d209.s0.e1", "type": "Gene/protein/RNA", "text": [ "profilin" ], "offsets": [ [ 103, 111 ] ], "normalized": [] } ]

[]

[]

[]

[ { "id": "BioInfer.d210.s0__text", "type": "Sentence", "text": [ "Finally, we evaluated the acetylation of three putative PCAF substrates, histones H3 and H4 and the transcription factor p53, and have determined that histone H3 is significantly preferred over the histone H4 and p53 substrates." ], "offsets": [ [ 0, 228 ] ] } ]

[ { "id": "BioInfer.d210.s0.e0", "type": "Individual_protein", "text": [ "p53" ], "offsets": [ [ 121, 124 ] ], "normalized": [] }, { "id": "BioInfer.d210.s0.e1", "type": "Individual_protein", "text": [ "H3" ], "offsets": [ [ 159, 161 ] ], "normalized": [] }, { "id": "BioInfer.d210.s0.e2", "type": "Individual_protein", "text": [ "H4" ], "offsets": [ [ 206, 208 ] ], "normalized": [] }, { "id": "BioInfer.d210.s0.e3", "type": "Protein_family_or_group", "text": [ "histone" ], "offsets": [ [ 151, 158 ] ], "normalized": [] }, { "id": "BioInfer.d210.s0.e4", "type": "Individual_protein", "text": [ "H4" ], "offsets": [ [ 89, 91 ] ], "normalized": [] }, { "id": "BioInfer.d210.s0.e5", "type": "Individual_protein", "text": [ "PCAF" ], "offsets": [ [ 56, 60 ] ], "normalized": [] }, { "id": "BioInfer.d210.s0.e6", "type": "Individual_protein", "text": [ "H3" ], "offsets": [ [ 82, 84 ] ], "normalized": [] }, { "id": "BioInfer.d210.s0.e7", "type": "Individual_protein", "text": [ "histones" ], "offsets": [ [ 73, 81 ] ], "normalized": [] }, { "id": "BioInfer.d210.s0.e8", "type": "Protein_family_or_group", "text": [ "histone" ], "offsets": [ [ 198, 205 ] ], "normalized": [] }, { "id": "BioInfer.d210.s0.e9", "type": "Gene/protein/RNA", "text": [ "p53" ], "offsets": [ [ 213, 216 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d210.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d210.s0.e0", "arg2_id": "BioInfer.d210.s0.e5", "normalized": [] }, { "id": "BioInfer.d210.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d210.s0.e1", "arg2_id": "BioInfer.d210.s0.e3", "normalized": [] }, { "id": "BioInfer.d210.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d210.s0.e2", "arg2_id": "BioInfer.d210.s0.e8", "normalized": [] }, { "id": "BioInfer.d210.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d210.s0.e4", "arg2_id": "BioInfer.d210.s0.e5", "normalized": [] }, { "id": "BioInfer.d210.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d210.s0.e4", "arg2_id": "BioInfer.d210.s0.e7", "normalized": [] }, { "id": "BioInfer.d210.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d210.s0.e5", "arg2_id": "BioInfer.d210.s0.e6", "normalized": [] }, { "id": "BioInfer.d210.s0.i6", "type": "PPI", "arg1_id": "BioInfer.d210.s0.e6", "arg2_id": "BioInfer.d210.s0.e7", "normalized": [] } ]

[ { "id": "BioInfer.d212.s0__text", "type": "Sentence", "text": [ "First, the C-terminal verprolin-cofilin-acidic domain was shown to be essential for the regulation of actin cytoskeleton." ], "offsets": [ [ 0, 121 ] ] } ]

[ { "id": "BioInfer.d212.s0.e0", "type": "Gene/protein/RNA", "text": [ "cofilin" ], "offsets": [ [ 32, 39 ] ], "normalized": [] }, { "id": "BioInfer.d212.s0.e1", "type": "Gene/protein/RNA", "text": [ "verprolin" ], "offsets": [ [ 22, 31 ] ], "normalized": [] }, { "id": "BioInfer.d212.s0.e2", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 102, 107 ] ], "normalized": [] } ]

[]

[]

[]

[ { "id": "BioInfer.d213.s0__text", "type": "Sentence", "text": [ "Fluorescent actin analogs with a high affinity for profilin in vitro exhibit an enhanced gradient of assembly in living cells." ], "offsets": [ [ 0, 126 ] ] } ]

[ { "id": "BioInfer.d213.s0.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 12, 17 ] ], "normalized": [] }, { "id": "BioInfer.d213.s0.e1", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 51, 59 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d213.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d213.s0.e0", "arg2_id": "BioInfer.d213.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d213.s1__text", "type": "Sentence", "text": [ "Three-dimensional fluorescence microscopy of the fluorescent analog of actin with a high affinity for profilin revealed that it incorporated into cortical cytoplasmic fibers and was also distributed diffusely in the non-cortical cytoplasm consistent with a bias of actin assembly near the surface of the cell." ], "offsets": [ [ 0, 309 ] ] } ]

[ { "id": "BioInfer.d213.s1.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 71, 76 ] ], "normalized": [] }, { "id": "BioInfer.d213.s1.e1", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 102, 110 ] ], "normalized": [] }, { "id": "BioInfer.d213.s1.e2", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 265, 270 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d213.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d213.s1.e0", "arg2_id": "BioInfer.d213.s1.e1", "normalized": [] } ]

[ { "id": "BioInfer.d213.s2__text", "type": "Sentence", "text": [ "To test these models in living cells using imaging techniques, we prepared a new fluorescent analog of actin that bound profilin, a protein that interacts with phosphoinositides and actin-monomers in a mutually exclusive manner, with an order of magnitude greater affinity (Kd = 3.6 microM) than cys-374-labeled actin (Kd > 30 microM), yet retained the ability to inhibit DNase I." ], "offsets": [ [ 0, 380 ] ] } ]

[ { "id": "BioInfer.d213.s2.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 103, 108 ] ], "normalized": [] }, { "id": "BioInfer.d213.s2.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 182, 187 ] ], "normalized": [] }, { "id": "BioInfer.d213.s2.e2", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 120, 128 ] ], "normalized": [] }, { "id": "BioInfer.d213.s2.e3", "type": "Individual_protein", "text": [ "DNase I" ], "offsets": [ [ 372, 379 ] ], "normalized": [] }, { "id": "BioInfer.d213.s2.e4", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 312, 317 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d213.s2.i0", "type": "PPI", "arg1_id": "BioInfer.d213.s2.e0", "arg2_id": "BioInfer.d213.s2.e2", "normalized": [] }, { "id": "BioInfer.d213.s2.i1", "type": "PPI", "arg1_id": "BioInfer.d213.s2.e0", "arg2_id": "BioInfer.d213.s2.e3", "normalized": [] }, { "id": "BioInfer.d213.s2.i2", "type": "PPI", "arg1_id": "BioInfer.d213.s2.e1", "arg2_id": "BioInfer.d213.s2.e2", "normalized": [] }, { "id": "BioInfer.d213.s2.i3", "type": "PPI", "arg1_id": "BioInfer.d213.s2.e2", "arg2_id": "BioInfer.d213.s2.e4", "normalized": [] } ]

[ { "id": "BioInfer.d214.s0__text", "type": "Sentence", "text": [ "Fluorographic analysis showed that the specific activity of soluble actin was two to three times that of its particulate form and that soluble actin, cofilin, actin depolymerizing factor, and profilin were transported at similar rates in slow component b of axonal flow." ], "offsets": [ [ 0, 270 ] ] } ]

[ { "id": "BioInfer.d214.s0.e0", "type": "Gene/protein/RNA", "text": [ "actin depolymerizing factor" ], "offsets": [ [ 159, 186 ] ], "normalized": [] }, { "id": "BioInfer.d214.s0.e1", "type": "Gene/protein/RNA", "text": [ "profilin" ], "offsets": [ [ 192, 200 ] ], "normalized": [] }, { "id": "BioInfer.d214.s0.e2", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 143, 148 ] ], "normalized": [] }, { "id": "BioInfer.d214.s0.e3", "type": "Gene/protein/RNA", "text": [ "cofilin" ], "offsets": [ [ 150, 157 ] ], "normalized": [] }, { "id": "BioInfer.d214.s0.e4", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 68, 73 ] ], "normalized": [] } ]

[]

[]

[]

[ { "id": "BioInfer.d214.s1__text", "type": "Sentence", "text": [ "Our data strongly support the view that the mobile form of actin in slow transport is soluble and that a substantial amount of this actin may travel as a complex with actin depolymerizing factor, cofilin, and profilin." ], "offsets": [ [ 0, 218 ] ] } ]

[ { "id": "BioInfer.d214.s1.e0", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 59, 64 ] ], "normalized": [] }, { "id": "BioInfer.d214.s1.e1", "type": "Individual_protein", "text": [ "actin depolymerizing factor" ], "offsets": [ [ 167, 194 ] ], "normalized": [] }, { "id": "BioInfer.d214.s1.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 132, 137 ] ], "normalized": [] }, { "id": "BioInfer.d214.s1.e3", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 196, 203 ] ], "normalized": [] }, { "id": "BioInfer.d214.s1.e4", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 209, 217 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d214.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d214.s1.e1", "arg2_id": "BioInfer.d214.s1.e2", "normalized": [] }, { "id": "BioInfer.d214.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d214.s1.e1", "arg2_id": "BioInfer.d214.s1.e3", "normalized": [] }, { "id": "BioInfer.d214.s1.i2", "type": "PPI", "arg1_id": "BioInfer.d214.s1.e1", "arg2_id": "BioInfer.d214.s1.e4", "normalized": [] }, { "id": "BioInfer.d214.s1.i3", "type": "PPI", "arg1_id": "BioInfer.d214.s1.e2", "arg2_id": "BioInfer.d214.s1.e3", "normalized": [] }, { "id": "BioInfer.d214.s1.i4", "type": "PPI", "arg1_id": "BioInfer.d214.s1.e2", "arg2_id": "BioInfer.d214.s1.e4", "normalized": [] }, { "id": "BioInfer.d214.s1.i5", "type": "PPI", "arg1_id": "BioInfer.d214.s1.e3", "arg2_id": "BioInfer.d214.s1.e4", "normalized": [] } ]

[ { "id": "BioInfer.d214.s2__text", "type": "Sentence", "text": [ "We examined the axonal transport of actin and its monomer binding proteins, actin depolymerizing factor, cofilin, and profilin, in the chicken sciatic nerve following injection of [35S]methionine into the lumbar spinal cord." ], "offsets": [ [ 0, 224 ] ] } ]

[ { "id": "BioInfer.d214.s2.e0", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 118, 126 ] ], "normalized": [] }, { "id": "BioInfer.d214.s2.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 36, 41 ] ], "normalized": [] }, { "id": "BioInfer.d214.s2.e2", "type": "Individual_protein", "text": [ "actin depolymerizing factor" ], "offsets": [ [ 76, 103 ] ], "normalized": [] }, { "id": "BioInfer.d214.s2.e3", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 105, 112 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d214.s2.i0", "type": "PPI", "arg1_id": "BioInfer.d214.s2.e0", "arg2_id": "BioInfer.d214.s2.e1", "normalized": [] }, { "id": "BioInfer.d214.s2.i1", "type": "PPI", "arg1_id": "BioInfer.d214.s2.e1", "arg2_id": "BioInfer.d214.s2.e2", "normalized": [] }, { "id": "BioInfer.d214.s2.i2", "type": "PPI", "arg1_id": "BioInfer.d214.s2.e1", "arg2_id": "BioInfer.d214.s2.e3", "normalized": [] } ]

[ { "id": "BioInfer.d215.s0__text", "type": "Sentence", "text": [ "For example, it is associated with alpha-catenin and beta-catenin (Armadillo), and protected from trypsin digestion only in the presence of Ca2+, as is the case for many of classic cadherins." ], "offsets": [ [ 0, 191 ] ] } ]

[ { "id": "BioInfer.d215.s0.e0", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 53, 65 ] ], "normalized": [] }, { "id": "BioInfer.d215.s0.e1", "type": "Individual_protein", "text": [ "Armadillo" ], "offsets": [ [ 67, 76 ] ], "normalized": [] }, { "id": "BioInfer.d215.s0.e2", "type": "Individual_protein", "text": [ "cadherins" ], "offsets": [ [ 181, 190 ] ], "normalized": [] }, { "id": "BioInfer.d215.s0.e3", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 35, 48 ] ], "normalized": [] }, { "id": "BioInfer.d215.s0.e4", "type": "Individual_protein", "text": [ "trypsin" ], "offsets": [ [ 98, 105 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d215.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d215.s0.e0", "arg2_id": "BioInfer.d215.s0.e2", "normalized": [] }, { "id": "BioInfer.d215.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d215.s0.e1", "arg2_id": "BioInfer.d215.s0.e2", "normalized": [] }, { "id": "BioInfer.d215.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d215.s0.e2", "arg2_id": "BioInfer.d215.s0.e3", "normalized": [] }, { "id": "BioInfer.d215.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d215.s0.e2", "arg2_id": "BioInfer.d215.s0.e4", "normalized": [] } ]

[ { "id": "BioInfer.d216.s0__text", "type": "Sentence", "text": [ "From an analysis of profilin mutants, whose actin cytoskeleton is disrupted, we found that E-APC also requires actin filaments to associate with adhesive cell membranes in the ovary." ], "offsets": [ [ 0, 182 ] ] } ]

[ { "id": "BioInfer.d216.s0.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 111, 116 ] ], "normalized": [] }, { "id": "BioInfer.d216.s0.e1", "type": "Individual_protein", "text": [ "E-APC" ], "offsets": [ [ 91, 96 ] ], "normalized": [] }, { "id": "BioInfer.d216.s0.e2", "type": "Gene/protein/RNA", "text": [ "profilin" ], "offsets": [ [ 20, 28 ] ], "normalized": [] }, { "id": "BioInfer.d216.s0.e3", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 44, 49 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d216.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d216.s0.e0", "arg2_id": "BioInfer.d216.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d218.s0__text", "type": "Sentence", "text": [ "From these observations it is concluded that (i) RAD52 is required for high levels of both gene conversions and reciprocal crossovers, (ii) that RAD51 is not required for intrachromosomal crossovers, and (iii) that RAD51 and RAD52 have different functions, or that RAD52 has functions in addition to those of the Rad51/Rad52 protein complex." ], "offsets": [ [ 0, 341 ] ] } ]

[ { "id": "BioInfer.d218.s0.e0", "type": "Gene/protein/RNA", "text": [ "RAD52" ], "offsets": [ [ 49, 54 ] ], "normalized": [] }, { "id": "BioInfer.d218.s0.e1", "type": "Gene", "text": [ "RAD51" ], "offsets": [ [ 215, 220 ] ], "normalized": [] }, { "id": "BioInfer.d218.s0.e2", "type": "Gene/protein/RNA", "text": [ "RAD51" ], "offsets": [ [ 145, 150 ] ], "normalized": [] }, { "id": "BioInfer.d218.s0.e3", "type": "Gene", "text": [ "RAD52" ], "offsets": [ [ 225, 230 ] ], "normalized": [] }, { "id": "BioInfer.d218.s0.e4", "type": "Individual_protein", "text": [ "Rad52" ], "offsets": [ [ 319, 324 ] ], "normalized": [] }, { "id": "BioInfer.d218.s0.e5", "type": "Gene/protein/RNA", "text": [ "RAD52" ], "offsets": [ [ 265, 270 ] ], "normalized": [] }, { "id": "BioInfer.d218.s0.e6", "type": "Individual_protein", "text": [ "Rad51" ], "offsets": [ [ 313, 318 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d218.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d218.s0.e1", "arg2_id": "BioInfer.d218.s0.e3", "normalized": [] }, { "id": "BioInfer.d218.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d218.s0.e4", "arg2_id": "BioInfer.d218.s0.e6", "normalized": [] } ]

[ { "id": "BioInfer.d222.s0__text", "type": "Sentence", "text": [ "Furthermore, a simultaneous expression of profilin, actin and extracellular matrix proteins was observed during the regeneration of rat liver, that is, all mRNAs of these proteins showed biphasic peaks around 6 h and 48 h after partial hepatectomy." ], "offsets": [ [ 0, 248 ] ] } ]

[ { "id": "BioInfer.d222.s0.e0", "type": "Individual_protein", "text": [ "extracellular matrix proteins" ], "offsets": [ [ 62, 91 ] ], "normalized": [] }, { "id": "BioInfer.d222.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 52, 57 ] ], "normalized": [] }, { "id": "BioInfer.d222.s0.e2", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 42, 50 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d222.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d222.s0.e0", "arg2_id": "BioInfer.d222.s0.e1", "normalized": [] }, { "id": "BioInfer.d222.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d222.s0.e0", "arg2_id": "BioInfer.d222.s0.e2", "normalized": [] }, { "id": "BioInfer.d222.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d222.s0.e1", "arg2_id": "BioInfer.d222.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d223.s0__text", "type": "Sentence", "text": [ "Furthermore, the deletion of SJL1 suppresses the temperature-sensitive growth defect of sac6, a mutant in yeast fimbrin, supporting a role for synaptojanin family members in actin function." ], "offsets": [ [ 0, 189 ] ] } ]

[ { "id": "BioInfer.d223.s0.e0", "type": "Protein_family_or_group", "text": [ "synaptojanin" ], "offsets": [ [ 143, 155 ] ], "normalized": [] }, { "id": "BioInfer.d223.s0.e1", "type": "Gene", "text": [ "sac6" ], "offsets": [ [ 88, 92 ] ], "normalized": [] }, { "id": "BioInfer.d223.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 174, 179 ] ], "normalized": [] }, { "id": "BioInfer.d223.s0.e3", "type": "Gene/protein/RNA", "text": [ "fimbrin" ], "offsets": [ [ 112, 119 ] ], "normalized": [] }, { "id": "BioInfer.d223.s0.e4", "type": "Gene", "text": [ "SJL1" ], "offsets": [ [ 29, 33 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d223.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d223.s0.e0", "arg2_id": "BioInfer.d223.s0.e2", "normalized": [] }, { "id": "BioInfer.d223.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d223.s0.e1", "arg2_id": "BioInfer.d223.s0.e4", "normalized": [] } ]

[ { "id": "BioInfer.d224.s0__text", "type": "Sentence", "text": [ "Furthermore, this inactivating effect of calmodulin can be prevented by coexpressing a region of the cytoskeletal protein alpha-actinin2 known to interact with the CO region of NR1." ], "offsets": [ [ 0, 181 ] ] } ]

[ { "id": "BioInfer.d224.s0.e0", "type": "Individual_protein", "text": [ "calmodulin" ], "offsets": [ [ 41, 51 ] ], "normalized": [] }, { "id": "BioInfer.d224.s0.e1", "type": "Individual_protein", "text": [ "alpha-actinin2" ], "offsets": [ [ 122, 136 ] ], "normalized": [] }, { "id": "BioInfer.d224.s0.e2", "type": "Individual_protein", "text": [ "NR1" ], "offsets": [ [ 177, 180 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d224.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d224.s0.e0", "arg2_id": "BioInfer.d224.s0.e1", "normalized": [] }, { "id": "BioInfer.d224.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d224.s0.e1", "arg2_id": "BioInfer.d224.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d225.s0__text", "type": "Sentence", "text": [ "Further, PRP incubated with IL-6 showed a dose dependent increase in TXB2 and BTG secretion as measured by RIA and an increased incorporation of actin binding protein, talin, and myosin into the cytoskeletal core (triton insoluble residue) as shown by SDS-PAGE." ], "offsets": [ [ 0, 261 ] ] } ]

[ { "id": "BioInfer.d225.s0.e0", "type": "Individual_protein", "text": [ "BTG" ], "offsets": [ [ 78, 81 ] ], "normalized": [] }, { "id": "BioInfer.d225.s0.e1", "type": "Individual_protein", "text": [ "myosin" ], "offsets": [ [ 179, 185 ] ], "normalized": [] }, { "id": "BioInfer.d225.s0.e2", "type": "Individual_protein", "text": [ "TXB2" ], "offsets": [ [ 69, 73 ] ], "normalized": [] }, { "id": "BioInfer.d225.s0.e3", "type": "Individual_protein", "text": [ "talin" ], "offsets": [ [ 168, 173 ] ], "normalized": [] }, { "id": "BioInfer.d225.s0.e4", "type": "Protein_family_or_group", "text": [ "actin binding protein" ], "offsets": [ [ 145, 166 ] ], "normalized": [] }, { "id": "BioInfer.d225.s0.e5", "type": "Individual_protein", "text": [ "IL-6" ], "offsets": [ [ 28, 32 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d225.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d225.s0.e0", "arg2_id": "BioInfer.d225.s0.e5", "normalized": [] }, { "id": "BioInfer.d225.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d225.s0.e1", "arg2_id": "BioInfer.d225.s0.e3", "normalized": [] }, { "id": "BioInfer.d225.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d225.s0.e1", "arg2_id": "BioInfer.d225.s0.e4", "normalized": [] }, { "id": "BioInfer.d225.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d225.s0.e2", "arg2_id": "BioInfer.d225.s0.e5", "normalized": [] }, { "id": "BioInfer.d225.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d225.s0.e3", "arg2_id": "BioInfer.d225.s0.e4", "normalized": [] } ]

[ { "id": "BioInfer.d226.s0__text", "type": "Sentence", "text": [ "Further, we show that talin, a high molecular weight structural protein that links integrins to the actin cytoskeleton, is proteolytically cleaved in fetal, but not in neonatal melanocytes." ], "offsets": [ [ 0, 189 ] ] } ]

[ { "id": "BioInfer.d226.s0.e0", "type": "Individual_protein", "text": [ "integrins" ], "offsets": [ [ 83, 92 ] ], "normalized": [] }, { "id": "BioInfer.d226.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 100, 105 ] ], "normalized": [] }, { "id": "BioInfer.d226.s0.e2", "type": "Individual_protein", "text": [ "talin" ], "offsets": [ [ 22, 27 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d226.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d226.s0.e0", "arg2_id": "BioInfer.d226.s0.e1", "normalized": [] }, { "id": "BioInfer.d226.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d226.s0.e0", "arg2_id": "BioInfer.d226.s0.e2", "normalized": [] }, { "id": "BioInfer.d226.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d226.s0.e1", "arg2_id": "BioInfer.d226.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d226.s1__text", "type": "Sentence", "text": [ "Immunofluorescence microscopy of cells grown on fibronectin confirmed the presence of paxillin, talin, and vinculin at the ends of actin stress fibers at presumptive focal contacts in melanocytes." ], "offsets": [ [ 0, 196 ] ] } ]

[ { "id": "BioInfer.d226.s1.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 131, 136 ] ], "normalized": [] }, { "id": "BioInfer.d226.s1.e1", "type": "Individual_protein", "text": [ "vinculin" ], "offsets": [ [ 107, 115 ] ], "normalized": [] }, { "id": "BioInfer.d226.s1.e2", "type": "Gene/protein/RNA", "text": [ "fibronectin" ], "offsets": [ [ 48, 59 ] ], "normalized": [] }, { "id": "BioInfer.d226.s1.e3", "type": "Individual_protein", "text": [ "paxillin" ], "offsets": [ [ 86, 94 ] ], "normalized": [] }, { "id": "BioInfer.d226.s1.e4", "type": "Individual_protein", "text": [ "talin" ], "offsets": [ [ 96, 101 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d226.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d226.s1.e0", "arg2_id": "BioInfer.d226.s1.e1", "normalized": [] }, { "id": "BioInfer.d226.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d226.s1.e0", "arg2_id": "BioInfer.d226.s1.e3", "normalized": [] }, { "id": "BioInfer.d226.s1.i2", "type": "PPI", "arg1_id": "BioInfer.d226.s1.e0", "arg2_id": "BioInfer.d226.s1.e4", "normalized": [] } ]

[ { "id": "BioInfer.d227.s0__text", "type": "Sentence", "text": [ "Fusiform RPE, however, were not deficient in these proteins, expressing amounts of N-cadherin, alpha-catenin, beta-catenin, plakoglobin, p120, alpha-actinin and vinculin that were equivalent to epithelioid cells." ], "offsets": [ [ 0, 212 ] ] } ]

[ { "id": "BioInfer.d227.s0.e0", "type": "Gene/protein/RNA", "text": [ "alpha-actinin" ], "offsets": [ [ 143, 156 ] ], "normalized": [] }, { "id": "BioInfer.d227.s0.e1", "type": "Gene/protein/RNA", "text": [ "vinculin" ], "offsets": [ [ 161, 169 ] ], "normalized": [] }, { "id": "BioInfer.d227.s0.e2", "type": "Gene/protein/RNA", "text": [ "plakoglobin" ], "offsets": [ [ 124, 135 ] ], "normalized": [] }, { "id": "BioInfer.d227.s0.e3", "type": "Gene/protein/RNA", "text": [ "p120" ], "offsets": [ [ 137, 141 ] ], "normalized": [] }, { "id": "BioInfer.d227.s0.e4", "type": "Gene/protein/RNA", "text": [ "alpha-catenin" ], "offsets": [ [ 95, 108 ] ], "normalized": [] }, { "id": "BioInfer.d227.s0.e5", "type": "Gene/protein/RNA", "text": [ "beta-catenin" ], "offsets": [ [ 110, 122 ] ], "normalized": [] }, { "id": "BioInfer.d227.s0.e6", "type": "Gene/protein/RNA", "text": [ "N-cadherin" ], "offsets": [ [ 83, 93 ] ], "normalized": [] } ]

[]

[]

[]

[ { "id": "BioInfer.d229.s0__text", "type": "Sentence", "text": [ "Gel electrophoresis was used to measure changes in the relative amounts of actin or myosin and of myosin heavy chain (MHC) isoforms." ], "offsets": [ [ 0, 132 ] ] } ]

[ { "id": "BioInfer.d229.s0.e0", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 75, 80 ] ], "normalized": [] }, { "id": "BioInfer.d229.s0.e1", "type": "Individual_protein", "text": [ "myosin heavy chain" ], "offsets": [ [ 98, 116 ] ], "normalized": [] }, { "id": "BioInfer.d229.s0.e2", "type": "Gene/protein/RNA", "text": [ "myosin" ], "offsets": [ [ 84, 90 ] ], "normalized": [] }, { "id": "BioInfer.d229.s0.e3", "type": "Individual_protein", "text": [ "MHC" ], "offsets": [ [ 118, 121 ] ], "normalized": [] } ]

[]

[]

[]

[ { "id": "BioInfer.d230.s0__text", "type": "Sentence", "text": [ "Generation of these membrane microparticles was dependent on the presence of extracellular calcium and was accompanied by proteolytic degradation of the cytoskeletal proteins, actin binding protein (ABP), talin, and myosin heavy chain." ], "offsets": [ [ 0, 235 ] ] } ]

[ { "id": "BioInfer.d230.s0.e0", "type": "Protein_family_or_group", "text": [ "actin binding protein" ], "offsets": [ [ 176, 197 ] ], "normalized": [] }, { "id": "BioInfer.d230.s0.e1", "type": "Gene/protein/RNA", "text": [ "myosin heavy chain" ], "offsets": [ [ 216, 234 ] ], "normalized": [] }, { "id": "BioInfer.d230.s0.e2", "type": "Gene/protein/RNA", "text": [ "talin" ], "offsets": [ [ 205, 210 ] ], "normalized": [] }, { "id": "BioInfer.d230.s0.e3", "type": "Protein_family_or_group", "text": [ "ABP" ], "offsets": [ [ 199, 202 ] ], "normalized": [] } ]

[]

[]

[]

[ { "id": "BioInfer.d232.s0__text", "type": "Sentence", "text": [ "Genetic dissection of Drosophila myofibril formation: effects of actin and myosin heavy chain null alleles." ], "offsets": [ [ 0, 107 ] ] } ]

[ { "id": "BioInfer.d232.s0.e0", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 65, 70 ] ], "normalized": [] }, { "id": "BioInfer.d232.s0.e1", "type": "Gene/protein/RNA", "text": [ "myosin heavy chain" ], "offsets": [ [ 75, 93 ] ], "normalized": [] } ]

[]

[]

[]

[ { "id": "BioInfer.d232.s1__text", "type": "Sentence", "text": [ "We find that heterozygotes for actin (Act88F) or myosin heavy chain (Mhc36B) null alleles have complex myofibrillar defects, whereas Mhc36B-/+; Act88F-/+ double heterozygotes have nearly normal myofibrils." ], "offsets": [ [ 0, 205 ] ] } ]

[ { "id": "BioInfer.d232.s1.e0", "type": "Gene/protein/RNA", "text": [ "Act88F" ], "offsets": [ [ 144, 150 ] ], "normalized": [] }, { "id": "BioInfer.d232.s1.e1", "type": "Individual_protein", "text": [ "Mhc36B" ], "offsets": [ [ 69, 75 ] ], "normalized": [] }, { "id": "BioInfer.d232.s1.e2", "type": "Individual_protein", "text": [ "myosin heavy chain" ], "offsets": [ [ 49, 67 ] ], "normalized": [] }, { "id": "BioInfer.d232.s1.e3", "type": "Individual_protein", "text": [ "Act88F" ], "offsets": [ [ 38, 44 ] ], "normalized": [] }, { "id": "BioInfer.d232.s1.e4", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 31, 36 ] ], "normalized": [] }, { "id": "BioInfer.d232.s1.e5", "type": "Gene/protein/RNA", "text": [ "Mhc36B" ], "offsets": [ [ 133, 139 ] ], "normalized": [] } ]

[]

[]

[]

[ { "id": "BioInfer.d233.s0__text", "type": "Sentence", "text": [ "Germline mutations in several members of these families, MSH2, MSH6, MLH1, and PMS2, but not MSH3, are responsible for hereditary non-polyposis colorectal cancer." ], "offsets": [ [ 0, 162 ] ] } ]

[ { "id": "BioInfer.d233.s0.e0", "type": "Gene/protein/RNA", "text": [ "MSH3" ], "offsets": [ [ 93, 97 ] ], "normalized": [] }, { "id": "BioInfer.d233.s0.e1", "type": "Gene/protein/RNA", "text": [ "MSH6" ], "offsets": [ [ 63, 67 ] ], "normalized": [] }, { "id": "BioInfer.d233.s0.e2", "type": "Gene/protein/RNA", "text": [ "MLH1" ], "offsets": [ [ 69, 73 ] ], "normalized": [] }, { "id": "BioInfer.d233.s0.e3", "type": "Gene/protein/RNA", "text": [ "MSH2" ], "offsets": [ [ 57, 61 ] ], "normalized": [] }, { "id": "BioInfer.d233.s0.e4", "type": "Gene/protein/RNA", "text": [ "PMS2" ], "offsets": [ [ 79, 83 ] ], "normalized": [] } ]

[]

[]

[]

[ { "id": "BioInfer.d234.s0__text", "type": "Sentence", "text": [ "Glutathione S-transferase pull-down performed with Tax deletion mutants and peptide competition have localized the site in Tax critical for binding CBP/p300 to a highly protease-sensitive region around amino acid residues 81 to 95 (81QRTSKTLKVLTPPIT95) which lies between the domains previously proposed to be important for CREB binding and Tax subunit dimerization." ], "offsets": [ [ 0, 366 ] ] } ]

[ { "id": "BioInfer.d234.s0.e0", "type": "Individual_protein", "text": [ "p300" ], "offsets": [ [ 152, 156 ] ], "normalized": [] }, { "id": "BioInfer.d234.s0.e1", "type": "Individual_protein", "text": [ "Tax" ], "offsets": [ [ 123, 126 ] ], "normalized": [] }, { "id": "BioInfer.d234.s0.e2", "type": "Individual_protein", "text": [ "CBP" ], "offsets": [ [ 148, 151 ] ], "normalized": [] }, { "id": "BioInfer.d234.s0.e3", "type": "Individual_protein", "text": [ "CREB" ], "offsets": [ [ 324, 328 ] ], "normalized": [] }, { "id": "BioInfer.d234.s0.e4", "type": "Gene/protein/RNA", "text": [ "Glutathione S-transferase" ], "offsets": [ [ 0, 25 ] ], "normalized": [] }, { "id": "BioInfer.d234.s0.e5", "type": "Individual_protein", "text": [ "Tax" ], "offsets": [ [ 341, 344 ] ], "normalized": [] }, { "id": "BioInfer.d234.s0.e6", "type": "Gene/protein/RNA", "text": [ "Tax" ], "offsets": [ [ 51, 54 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d234.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d234.s0.e0", "arg2_id": "BioInfer.d234.s0.e1", "normalized": [] }, { "id": "BioInfer.d234.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d234.s0.e1", "arg2_id": "BioInfer.d234.s0.e2", "normalized": [] }, { "id": "BioInfer.d234.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d234.s0.e1", "arg2_id": "BioInfer.d234.s0.e3", "normalized": [] }, { "id": "BioInfer.d234.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d234.s0.e1", "arg2_id": "BioInfer.d234.s0.e5", "normalized": [] } ]

[ { "id": "BioInfer.d236.s0__text", "type": "Sentence", "text": [ "Hence, we conclude that in its dimeric form, which is used in actin and lipid binding, talin is a dumbbell-shaped molecule built of two antiparallel subunits." ], "offsets": [ [ 0, 158 ] ] } ]

[ { "id": "BioInfer.d236.s0.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 62, 67 ] ], "normalized": [] }, { "id": "BioInfer.d236.s0.e1", "type": "Individual_protein", "text": [ "talin" ], "offsets": [ [ 87, 92 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d236.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d236.s0.e0", "arg2_id": "BioInfer.d236.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d236.s1__text", "type": "Sentence", "text": [ "The talin dimer, which is crucial for actin and lipid binding, is built of a backbone containing the 200 kDa rod portions, at both ends of which a 47 kDa globular domain is attached." ], "offsets": [ [ 0, 182 ] ] } ]

[ { "id": "BioInfer.d236.s1.e0", "type": "Individual_protein", "text": [ "talin" ], "offsets": [ [ 4, 9 ] ], "normalized": [] }, { "id": "BioInfer.d236.s1.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 38, 43 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d236.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d236.s1.e0", "arg2_id": "BioInfer.d236.s1.e1", "normalized": [] } ]

[ { "id": "BioInfer.d237.s0__text", "type": "Sentence", "text": [ "Here, specific interactions between human RAD51 and RAD52 proteins are demonstrated both in vivo, using the yeast two-hybrid system and immunoprecipitation of insect cells co-infected with RAD51 and RAD52 recombinant viruses, and in vitro, using affinity chromatography with purified recombinant proteins." ], "offsets": [ [ 0, 305 ] ] } ]

[ { "id": "BioInfer.d237.s0.e0", "type": "Gene/protein/RNA", "text": [ "RAD52" ], "offsets": [ [ 199, 204 ] ], "normalized": [] }, { "id": "BioInfer.d237.s0.e1", "type": "Gene/protein/RNA", "text": [ "RAD51" ], "offsets": [ [ 189, 194 ] ], "normalized": [] }, { "id": "BioInfer.d237.s0.e2", "type": "Gene", "text": [ "RAD52" ], "offsets": [ [ 52, 57 ] ], "normalized": [] }, { "id": "BioInfer.d237.s0.e3", "type": "Gene", "text": [ "RAD51" ], "offsets": [ [ 42, 47 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d237.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d237.s0.e2", "arg2_id": "BioInfer.d237.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d237.s1__text", "type": "Sentence", "text": [ "Interaction of the yeast RAD51 and RAD52 proteins plays a crucial role in yeast DNA homologous recombination and DNA double-strand break repair." ], "offsets": [ [ 0, 144 ] ] } ]

[ { "id": "BioInfer.d237.s1.e0", "type": "Individual_protein", "text": [ "RAD51" ], "offsets": [ [ 25, 30 ] ], "normalized": [] }, { "id": "BioInfer.d237.s1.e1", "type": "Individual_protein", "text": [ "RAD52" ], "offsets": [ [ 35, 40 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d237.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d237.s1.e0", "arg2_id": "BioInfer.d237.s1.e1", "normalized": [] } ]

[ { "id": "BioInfer.d237.s2__text", "type": "Sentence", "text": [ "Specific interactions between the human RAD51 and RAD52 proteins." ], "offsets": [ [ 0, 65 ] ] } ]

[ { "id": "BioInfer.d237.s2.e0", "type": "Individual_protein", "text": [ "RAD52" ], "offsets": [ [ 50, 55 ] ], "normalized": [] }, { "id": "BioInfer.d237.s2.e1", "type": "Individual_protein", "text": [ "RAD51" ], "offsets": [ [ 40, 45 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d237.s2.i0", "type": "PPI", "arg1_id": "BioInfer.d237.s2.e0", "arg2_id": "BioInfer.d237.s2.e1", "normalized": [] } ]

[ { "id": "BioInfer.d237.s3__text", "type": "Sentence", "text": [ "The RAD51-interacting region (amino acids 291-330) of the human RAD52 protein shows no homology with the yeast RAD52 protein, indicating that the interaction between RAD51 and RAD52 is species-specific." ], "offsets": [ [ 0, 202 ] ] } ]

[ { "id": "BioInfer.d237.s3.e0", "type": "Individual_protein", "text": [ "RAD52" ], "offsets": [ [ 111, 116 ] ], "normalized": [] }, { "id": "BioInfer.d237.s3.e1", "type": "Individual_protein", "text": [ "RAD52" ], "offsets": [ [ 64, 69 ] ], "normalized": [] }, { "id": "BioInfer.d237.s3.e2", "type": "Individual_protein", "text": [ "RAD51" ], "offsets": [ [ 166, 171 ] ], "normalized": [] }, { "id": "BioInfer.d237.s3.e3", "type": "Individual_protein", "text": [ "RAD52" ], "offsets": [ [ 176, 181 ] ], "normalized": [] }, { "id": "BioInfer.d237.s3.e4", "type": "Individual_protein", "text": [ "RAD51" ], "offsets": [ [ 4, 9 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d237.s3.i0", "type": "PPI", "arg1_id": "BioInfer.d237.s3.e0", "arg2_id": "BioInfer.d237.s3.e1", "normalized": [] }, { "id": "BioInfer.d237.s3.i1", "type": "PPI", "arg1_id": "BioInfer.d237.s3.e1", "arg2_id": "BioInfer.d237.s3.e4", "normalized": [] }, { "id": "BioInfer.d237.s3.i2", "type": "PPI", "arg1_id": "BioInfer.d237.s3.e2", "arg2_id": "BioInfer.d237.s3.e3", "normalized": [] } ]

[ { "id": "BioInfer.d237.s4__text", "type": "Sentence", "text": [ "These results suggest that RAD52 may modulate the catalytic activities of RAD51 protein such as homologous pairing and strand exchange through a direct physical interaction." ], "offsets": [ [ 0, 173 ] ] } ]

[ { "id": "BioInfer.d237.s4.e0", "type": "Gene", "text": [ "RAD52" ], "offsets": [ [ 27, 32 ] ], "normalized": [] }, { "id": "BioInfer.d237.s4.e1", "type": "Gene", "text": [ "RAD51" ], "offsets": [ [ 74, 79 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d237.s4.i0", "type": "PPI", "arg1_id": "BioInfer.d237.s4.e0", "arg2_id": "BioInfer.d237.s4.e1", "normalized": [] } ]

[ { "id": "BioInfer.d238.s0__text", "type": "Sentence", "text": [ "Here we demonstrate that accessory receptor triggering induces the transient association of cofilin with the actin cytoskeleton." ], "offsets": [ [ 0, 128 ] ] } ]

[ { "id": "BioInfer.d238.s0.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 109, 114 ] ], "normalized": [] }, { "id": "BioInfer.d238.s0.e1", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 92, 99 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d238.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d238.s0.e0", "arg2_id": "BioInfer.d238.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d238.s1__text", "type": "Sentence", "text": [ "Recently, we have shown that the small actin-depolymerizing protein cofilin represents a component of a co-stimulatory signaling pathway in human T cells." ], "offsets": [ [ 0, 154 ] ] } ]

[ { "id": "BioInfer.d238.s1.e0", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 68, 75 ] ], "normalized": [] }, { "id": "BioInfer.d238.s1.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 39, 44 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d238.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d238.s1.e0", "arg2_id": "BioInfer.d238.s1.e1", "normalized": [] } ]

[ { "id": "BioInfer.d238.s2__text", "type": "Sentence", "text": [ "These results suggest that cofilin provides an as yet missing link between functionally crucial T cell surface receptors and rearrangements of the actin cytoskeleton." ], "offsets": [ [ 0, 166 ] ] } ]

[ { "id": "BioInfer.d238.s2.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 147, 152 ] ], "normalized": [] }, { "id": "BioInfer.d238.s2.e1", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 27, 34 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d238.s2.i0", "type": "PPI", "arg1_id": "BioInfer.d238.s2.e0", "arg2_id": "BioInfer.d238.s2.e1", "normalized": [] } ]

[ { "id": "BioInfer.d239.s0__text", "type": "Sentence", "text": [ "Here we demonstrate that growth arrest and differentiation of NT2/D1 cells induced by HMBA involve increased expression of the cyclin-dependent kinase inhibitor p27, enhanced association of p27 with cyclin E/CDK2 complexes and suppression of kinase activity associated to cyclin E/CDK2 (but not to cyclin D3/CDK4)." ], "offsets": [ [ 0, 314 ] ] } ]

[ { "id": "BioInfer.d239.s0.e0", "type": "Individual_protein", "text": [ "CDK4" ], "offsets": [ [ 308, 312 ] ], "normalized": [] }, { "id": "BioInfer.d239.s0.e1", "type": "Individual_protein", "text": [ "p27" ], "offsets": [ [ 161, 164 ] ], "normalized": [] }, { "id": "BioInfer.d239.s0.e2", "type": "Individual_protein", "text": [ "CDK2" ], "offsets": [ [ 281, 285 ] ], "normalized": [] }, { "id": "BioInfer.d239.s0.e3", "type": "Protein_family_or_group", "text": [ "cyclin-dependent kinase inhibitor" ], "offsets": [ [ 127, 160 ] ], "normalized": [] }, { "id": "BioInfer.d239.s0.e4", "type": "Individual_protein", "text": [ "cyclin E" ], "offsets": [ [ 272, 280 ] ], "normalized": [] }, { "id": "BioInfer.d239.s0.e5", "type": "Individual_protein", "text": [ "CDK2" ], "offsets": [ [ 208, 212 ] ], "normalized": [] }, { "id": "BioInfer.d239.s0.e6", "type": "Individual_protein", "text": [ "cyclin D3" ], "offsets": [ [ 298, 307 ] ], "normalized": [] }, { "id": "BioInfer.d239.s0.e7", "type": "Individual_protein", "text": [ "cyclin E" ], "offsets": [ [ 199, 207 ] ], "normalized": [] }, { "id": "BioInfer.d239.s0.e8", "type": "Individual_protein", "text": [ "p27" ], "offsets": [ [ 190, 193 ] ], "normalized": [] }, { "id": "BioInfer.d239.s0.e9", "type": "Protein_family_or_group", "text": [ "kinase" ], "offsets": [ [ 242, 248 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d239.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d239.s0.e0", "arg2_id": "BioInfer.d239.s0.e6", "normalized": [] }, { "id": "BioInfer.d239.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d239.s0.e0", "arg2_id": "BioInfer.d239.s0.e9", "normalized": [] }, { "id": "BioInfer.d239.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d239.s0.e1", "arg2_id": "BioInfer.d239.s0.e3", "normalized": [] }, { "id": "BioInfer.d239.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d239.s0.e2", "arg2_id": "BioInfer.d239.s0.e4", "normalized": [] }, { "id": "BioInfer.d239.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d239.s0.e2", "arg2_id": "BioInfer.d239.s0.e9", "normalized": [] }, { "id": "BioInfer.d239.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d239.s0.e4", "arg2_id": "BioInfer.d239.s0.e9", "normalized": [] }, { "id": "BioInfer.d239.s0.i6", "type": "PPI", "arg1_id": "BioInfer.d239.s0.e5", "arg2_id": "BioInfer.d239.s0.e7", "normalized": [] }, { "id": "BioInfer.d239.s0.i7", "type": "PPI", "arg1_id": "BioInfer.d239.s0.e5", "arg2_id": "BioInfer.d239.s0.e8", "normalized": [] }, { "id": "BioInfer.d239.s0.i8", "type": "PPI", "arg1_id": "BioInfer.d239.s0.e6", "arg2_id": "BioInfer.d239.s0.e9", "normalized": [] }, { "id": "BioInfer.d239.s0.i9", "type": "PPI", "arg1_id": "BioInfer.d239.s0.e7", "arg2_id": "BioInfer.d239.s0.e8", "normalized": [] } ]

[ { "id": "BioInfer.d240.s0__text", "type": "Sentence", "text": [ "Here we demonstrate that type XIII collagen is concentrated in cultured skin fibroblasts and several other human mesenchymal cell lines in the focal adhesions at the ends of actin stress fibers, co-localizing with the known focal adhesion components talin and vinculin." ], "offsets": [ [ 0, 269 ] ] } ]

[ { "id": "BioInfer.d240.s0.e0", "type": "Individual_protein", "text": [ "type XIII collagen" ], "offsets": [ [ 25, 43 ] ], "normalized": [] }, { "id": "BioInfer.d240.s0.e1", "type": "Individual_protein", "text": [ "talin" ], "offsets": [ [ 250, 255 ] ], "normalized": [] }, { "id": "BioInfer.d240.s0.e2", "type": "Individual_protein", "text": [ "vinculin" ], "offsets": [ [ 260, 268 ] ], "normalized": [] }, { "id": "BioInfer.d240.s0.e3", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 174, 179 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d240.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d240.s0.e0", "arg2_id": "BioInfer.d240.s0.e1", "normalized": [] }, { "id": "BioInfer.d240.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d240.s0.e0", "arg2_id": "BioInfer.d240.s0.e2", "normalized": [] }, { "id": "BioInfer.d240.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d240.s0.e0", "arg2_id": "BioInfer.d240.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d241.s0__text", "type": "Sentence", "text": [ "Here, we describe proline-rich proteins involved in regulating actin polymerization and classify them according to their role in recruiting profilin to the membrane." ], "offsets": [ [ 0, 165 ] ] } ]

[ { "id": "BioInfer.d241.s0.e0", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 63, 68 ] ], "normalized": [] }, { "id": "BioInfer.d241.s0.e1", "type": "Gene/protein/RNA", "text": [ "profilin" ], "offsets": [ [ 140, 148 ] ], "normalized": [] } ]

[]

[]

[]

[ { "id": "BioInfer.d242.s0__text", "type": "Sentence", "text": [ "Here we describe the TNF-dependent activation of acid SMase (A-SMase) through the p55 TNF receptor-associated proteins TRADD and FADD." ], "offsets": [ [ 0, 134 ] ] } ]

[ { "id": "BioInfer.d242.s0.e0", "type": "Individual_protein", "text": [ "TRADD" ], "offsets": [ [ 119, 124 ] ], "normalized": [] }, { "id": "BioInfer.d242.s0.e1", "type": "Individual_protein", "text": [ "FADD" ], "offsets": [ [ 129, 133 ] ], "normalized": [] }, { "id": "BioInfer.d242.s0.e2", "type": "Individual_protein", "text": [ "TNF" ], "offsets": [ [ 21, 24 ] ], "normalized": [] }, { "id": "BioInfer.d242.s0.e3", "type": "Individual_protein", "text": [ "p55" ], "offsets": [ [ 82, 85 ] ], "normalized": [] }, { "id": "BioInfer.d242.s0.e4", "type": "Protein_family_or_group", "text": [ "TNF receptor" ], "offsets": [ [ 86, 98 ] ], "normalized": [] }, { "id": "BioInfer.d242.s0.e5", "type": "Individual_protein", "text": [ "acid SMase" ], "offsets": [ [ 49, 59 ] ], "normalized": [] }, { "id": "BioInfer.d242.s0.e6", "type": "Individual_protein", "text": [ "A-SMase" ], "offsets": [ [ 61, 68 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d242.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d242.s0.e0", "arg2_id": "BioInfer.d242.s0.e3", "normalized": [] }, { "id": "BioInfer.d242.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d242.s0.e0", "arg2_id": "BioInfer.d242.s0.e5", "normalized": [] }, { "id": "BioInfer.d242.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d242.s0.e0", "arg2_id": "BioInfer.d242.s0.e6", "normalized": [] }, { "id": "BioInfer.d242.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d242.s0.e1", "arg2_id": "BioInfer.d242.s0.e3", "normalized": [] }, { "id": "BioInfer.d242.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d242.s0.e1", "arg2_id": "BioInfer.d242.s0.e5", "normalized": [] }, { "id": "BioInfer.d242.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d242.s0.e1", "arg2_id": "BioInfer.d242.s0.e6", "normalized": [] }, { "id": "BioInfer.d242.s0.i6", "type": "PPI", "arg1_id": "BioInfer.d242.s0.e2", "arg2_id": "BioInfer.d242.s0.e5", "normalized": [] }, { "id": "BioInfer.d242.s0.i7", "type": "PPI", "arg1_id": "BioInfer.d242.s0.e2", "arg2_id": "BioInfer.d242.s0.e6", "normalized": [] }, { "id": "BioInfer.d242.s0.i8", "type": "PPI", "arg1_id": "BioInfer.d242.s0.e3", "arg2_id": "BioInfer.d242.s0.e4", "normalized": [] } ]

[ { "id": "BioInfer.d242.s1__text", "type": "Sentence", "text": [ "TNF receptor death domain-associated proteins TRADD and FADD signal activation of acid sphingomyelinase." ], "offsets": [ [ 0, 104 ] ] } ]

[ { "id": "BioInfer.d242.s1.e0", "type": "Individual_protein", "text": [ "TRADD" ], "offsets": [ [ 46, 51 ] ], "normalized": [] }, { "id": "BioInfer.d242.s1.e1", "type": "Individual_protein", "text": [ "acid sphingomyelinase" ], "offsets": [ [ 82, 103 ] ], "normalized": [] }, { "id": "BioInfer.d242.s1.e2", "type": "Individual_protein", "text": [ "FADD" ], "offsets": [ [ 56, 60 ] ], "normalized": [] }, { "id": "BioInfer.d242.s1.e3", "type": "Individual_protein", "text": [ "TNF receptor" ], "offsets": [ [ 0, 12 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d242.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d242.s1.e0", "arg2_id": "BioInfer.d242.s1.e1", "normalized": [] }, { "id": "BioInfer.d242.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d242.s1.e0", "arg2_id": "BioInfer.d242.s1.e3", "normalized": [] }, { "id": "BioInfer.d242.s1.i2", "type": "PPI", "arg1_id": "BioInfer.d242.s1.e1", "arg2_id": "BioInfer.d242.s1.e2", "normalized": [] }, { "id": "BioInfer.d242.s1.i3", "type": "PPI", "arg1_id": "BioInfer.d242.s1.e2", "arg2_id": "BioInfer.d242.s1.e3", "normalized": [] } ]

[ { "id": "BioInfer.d243.s0__text", "type": "Sentence", "text": [ "Here, we designed a genetic screen for mutant strains defective for filamentous growth (dfg) to identify novel targets of the filamentation signaling pathway, and we thereby identified 16 different genes, CDC39, STE12, TEC1, WHI3, NAB1, DBR1, CDC55, SRV2, TPM1, SPA2, BNI1, DFG5, DFG9, DFG10, BUD8 and DFG16, mutations that block filamentous growth." ], "offsets": [ [ 0, 349 ] ] } ]

[ { "id": "BioInfer.d243.s0.e0", "type": "Gene/protein/RNA", "text": [ "BUD8" ], "offsets": [ [ 293, 297 ] ], "normalized": [] }, { "id": "BioInfer.d243.s0.e1", "type": "Gene/protein/RNA", "text": [ "TEC1" ], "offsets": [ [ 219, 223 ] ], "normalized": [] }, { "id": "BioInfer.d243.s0.e2", "type": "Gene/protein/RNA", "text": [ "CDC39" ], "offsets": [ [ 205, 210 ] ], "normalized": [] }, { "id": "BioInfer.d243.s0.e3", "type": "Gene/protein/RNA", "text": [ "NAB1" ], "offsets": [ [ 231, 235 ] ], "normalized": [] }, { "id": "BioInfer.d243.s0.e4", "type": "Gene/protein/RNA", "text": [ "STE12" ], "offsets": [ [ 212, 217 ] ], "normalized": [] }, { "id": "BioInfer.d243.s0.e5", "type": "Gene/protein/RNA", "text": [ "CDC55" ], "offsets": [ [ 243, 248 ] ], "normalized": [] }, { "id": "BioInfer.d243.s0.e6", "type": "Gene/protein/RNA", "text": [ "WHI3" ], "offsets": [ [ 225, 229 ] ], "normalized": [] }, { "id": "BioInfer.d243.s0.e7", "type": "Gene/protein/RNA", "text": [ "TPM1" ], "offsets": [ [ 256, 260 ] ], "normalized": [] }, { "id": "BioInfer.d243.s0.e8", "type": "Gene/protein/RNA", "text": [ "DBR1" ], "offsets": [ [ 237, 241 ] ], "normalized": [] }, { "id": "BioInfer.d243.s0.e9", "type": "Gene/protein/RNA", "text": [ "BNI1" ], "offsets": [ [ 268, 272 ] ], "normalized": [] }, { "id": "BioInfer.d243.s0.e10", "type": "Gene/protein/RNA", "text": [ "DFG10" ], "offsets": [ [ 286, 291 ] ], "normalized": [] }, { "id": "BioInfer.d243.s0.e11", "type": "Gene/protein/RNA", "text": [ "DFG16" ], "offsets": [ [ 302, 307 ] ], "normalized": [] }, { "id": "BioInfer.d243.s0.e12", "type": "Gene/protein/RNA", "text": [ "DFG9" ], "offsets": [ [ 280, 284 ] ], "normalized": [] }, { "id": "BioInfer.d243.s0.e13", "type": "Gene/protein/RNA", "text": [ "SPA2" ], "offsets": [ [ 262, 266 ] ], "normalized": [] }, { "id": "BioInfer.d243.s0.e14", "type": "Gene/protein/RNA", "text": [ "SRV2" ], "offsets": [ [ 250, 254 ] ], "normalized": [] }, { "id": "BioInfer.d243.s0.e15", "type": "Gene/protein/RNA", "text": [ "DFG5" ], "offsets": [ [ 274, 278 ] ], "normalized": [] } ]

[]

[]

[]

[ { "id": "BioInfer.d244.s0__text", "type": "Sentence", "text": [ "Here, we have detected a polypeptide in rat rod outer segments that is recognized by myosin heavy chain antibodies and was found to possess other characteristics of conventional non-muscle myosin heavy chain: it comigrates in SDS-PAGE with non-muscle myosin heavy chain; it associates with the cytoskeleton of rod outer segments in an ATP-sensitive manner; and it binds to purified actin filaments in the absence of ATP." ], "offsets": [ [ 0, 420 ] ] } ]

[ { "id": "BioInfer.d244.s0.e0", "type": "Gene/protein/RNA", "text": [ "non-muscle myosin heavy chain" ], "offsets": [ [ 240, 269 ] ], "normalized": [] }, { "id": "BioInfer.d244.s0.e1", "type": "Gene/protein/RNA", "text": [ "myosin heavy chain" ], "offsets": [ [ 85, 103 ] ], "normalized": [] }, { "id": "BioInfer.d244.s0.e2", "type": "Individual_protein", "text": [ "non-muscle myosin heavy chain" ], "offsets": [ [ 178, 207 ] ], "normalized": [] }, { "id": "BioInfer.d244.s0.e3", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 382, 387 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d244.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d244.s0.e2", "arg2_id": "BioInfer.d244.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d245.s0__text", "type": "Sentence", "text": [ "Here we have now identified the reciprocal complementary binding site in alpha-catenin which mediates its interaction with beta-catenin and plakoglobin." ], "offsets": [ [ 0, 152 ] ] } ]

[ { "id": "BioInfer.d245.s0.e0", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 73, 86 ] ], "normalized": [] }, { "id": "BioInfer.d245.s0.e1", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 123, 135 ] ], "normalized": [] }, { "id": "BioInfer.d245.s0.e2", "type": "Individual_protein", "text": [ "plakoglobin" ], "offsets": [ [ 140, 151 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d245.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d245.s0.e0", "arg2_id": "BioInfer.d245.s0.e1", "normalized": [] }, { "id": "BioInfer.d245.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d245.s0.e0", "arg2_id": "BioInfer.d245.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d245.s1__text", "type": "Sentence", "text": [ "It is well established that the cytoplasmic domain of E-cadherin binds either beta-catenin or plakoglobin, which both can assemble alpha-catenin into the complex." ], "offsets": [ [ 0, 162 ] ] } ]

[ { "id": "BioInfer.d245.s1.e0", "type": "Individual_protein", "text": [ "plakoglobin" ], "offsets": [ [ 94, 105 ] ], "normalized": [] }, { "id": "BioInfer.d245.s1.e1", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 131, 144 ] ], "normalized": [] }, { "id": "BioInfer.d245.s1.e2", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 78, 90 ] ], "normalized": [] }, { "id": "BioInfer.d245.s1.e3", "type": "Individual_protein", "text": [ "E-cadherin" ], "offsets": [ [ 54, 64 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d245.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d245.s1.e0", "arg2_id": "BioInfer.d245.s1.e1", "normalized": [] }, { "id": "BioInfer.d245.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d245.s1.e0", "arg2_id": "BioInfer.d245.s1.e3", "normalized": [] }, { "id": "BioInfer.d245.s1.i2", "type": "PPI", "arg1_id": "BioInfer.d245.s1.e1", "arg2_id": "BioInfer.d245.s1.e2", "normalized": [] }, { "id": "BioInfer.d245.s1.i3", "type": "PPI", "arg1_id": "BioInfer.d245.s1.e1", "arg2_id": "BioInfer.d245.s1.e3", "normalized": [] }, { "id": "BioInfer.d245.s1.i4", "type": "PPI", "arg1_id": "BioInfer.d245.s1.e2", "arg2_id": "BioInfer.d245.s1.e3", "normalized": [] } ]

[ { "id": "BioInfer.d245.s2__text", "type": "Sentence", "text": [ "Recently we have identified an alpha-catenin binding site in beta-catenin and plakoglobin and postulated, based on sequence analysis, that these protein-protein interactions are mediated by a hydrophobic interaction mechanism." ], "offsets": [ [ 0, 226 ] ] } ]

[ { "id": "BioInfer.d245.s2.e0", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 31, 44 ] ], "normalized": [] }, { "id": "BioInfer.d245.s2.e1", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 61, 73 ] ], "normalized": [] }, { "id": "BioInfer.d245.s2.e2", "type": "Individual_protein", "text": [ "plakoglobin" ], "offsets": [ [ 78, 89 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d245.s2.i0", "type": "PPI", "arg1_id": "BioInfer.d245.s2.e0", "arg2_id": "BioInfer.d245.s2.e1", "normalized": [] }, { "id": "BioInfer.d245.s2.i1", "type": "PPI", "arg1_id": "BioInfer.d245.s2.e0", "arg2_id": "BioInfer.d245.s2.e2", "normalized": [] } ]

[ { "id": "BioInfer.d246.s0__text", "type": "Sentence", "text": [ "Here we identify a pathway for the regulation of cofilin, a ubiquitous actin-binding protein that is essential for effective depolymerization of actin filaments." ], "offsets": [ [ 0, 161 ] ] } ]

[ { "id": "BioInfer.d246.s0.e0", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 49, 56 ] ], "normalized": [] }, { "id": "BioInfer.d246.s0.e1", "type": "Protein_family_or_group", "text": [ "actin-binding protein" ], "offsets": [ [ 71, 92 ] ], "normalized": [] }, { "id": "BioInfer.d246.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 145, 150 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d246.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d246.s0.e0", "arg2_id": "BioInfer.d246.s0.e1", "normalized": [] }, { "id": "BioInfer.d246.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d246.s0.e0", "arg2_id": "BioInfer.d246.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d246.s1__text", "type": "Sentence", "text": [ "Our results define a mechanism for the regulation of cofilin and hence of actin dynamics in vivo." ], "offsets": [ [ 0, 97 ] ] } ]

[ { "id": "BioInfer.d246.s1.e0", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 74, 79 ] ], "normalized": [] }, { "id": "BioInfer.d246.s1.e1", "type": "Gene/protein/RNA", "text": [ "cofilin" ], "offsets": [ [ 53, 60 ] ], "normalized": [] } ]

[]

[]

[]

[ { "id": "BioInfer.d246.s2__text", "type": "Sentence", "text": [ "Phosphorylation by LIM-kinase 1 inactivates cofilin, leading to accumulation of actin filaments." ], "offsets": [ [ 0, 96 ] ] } ]

[ { "id": "BioInfer.d246.s2.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 80, 85 ] ], "normalized": [] }, { "id": "BioInfer.d246.s2.e1", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 44, 51 ] ], "normalized": [] }, { "id": "BioInfer.d246.s2.e2", "type": "Individual_protein", "text": [ "LIM-kinase 1" ], "offsets": [ [ 19, 31 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d246.s2.i0", "type": "PPI", "arg1_id": "BioInfer.d246.s2.e0", "arg2_id": "BioInfer.d246.s2.e1", "normalized": [] }, { "id": "BioInfer.d246.s2.i1", "type": "PPI", "arg1_id": "BioInfer.d246.s2.e0", "arg2_id": "BioInfer.d246.s2.e2", "normalized": [] }, { "id": "BioInfer.d246.s2.i2", "type": "PPI", "arg1_id": "BioInfer.d246.s2.e1", "arg2_id": "BioInfer.d246.s2.e2", "normalized": [] } ]

[ { "id": "BioInfer.d246.s3__text", "type": "Sentence", "text": [ "Regulation of actin dynamics through phosphorylation of cofilin by LIM-kinase." ], "offsets": [ [ 0, 78 ] ] } ]

[ { "id": "BioInfer.d246.s3.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 14, 19 ] ], "normalized": [] }, { "id": "BioInfer.d246.s3.e1", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 56, 63 ] ], "normalized": [] }, { "id": "BioInfer.d246.s3.e2", "type": "Individual_protein", "text": [ "LIM-kinase" ], "offsets": [ [ 67, 77 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d246.s3.i0", "type": "PPI", "arg1_id": "BioInfer.d246.s3.e0", "arg2_id": "BioInfer.d246.s3.e1", "normalized": [] }, { "id": "BioInfer.d246.s3.i1", "type": "PPI", "arg1_id": "BioInfer.d246.s3.e0", "arg2_id": "BioInfer.d246.s3.e2", "normalized": [] }, { "id": "BioInfer.d246.s3.i2", "type": "PPI", "arg1_id": "BioInfer.d246.s3.e1", "arg2_id": "BioInfer.d246.s3.e2", "normalized": [] } ]

[ { "id": "BioInfer.d247.s0__text", "type": "Sentence", "text": [ "Here, we prepared a profilin mutant (H119E) defective in actin binding, but retaining the ability to bind to other proteins." ], "offsets": [ [ 0, 124 ] ] } ]

[ { "id": "BioInfer.d247.s0.e0", "type": "Individual_protein", "text": [ "profilin", "H119E" ], "offsets": [ [ 20, 28 ], [ 37, 42 ] ], "normalized": [] }, { "id": "BioInfer.d247.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 57, 62 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d247.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d247.s0.e0", "arg2_id": "BioInfer.d247.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d247.s1__text", "type": "Sentence", "text": [ "The essential role of profilin in the assembly of actin for microspike formation." ], "offsets": [ [ 0, 81 ] ] } ]

[ { "id": "BioInfer.d247.s1.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 50, 55 ] ], "normalized": [] }, { "id": "BioInfer.d247.s1.e1", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 22, 30 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d247.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d247.s1.e0", "arg2_id": "BioInfer.d247.s1.e1", "normalized": [] } ]

[ { "id": "BioInfer.d247.s2__text", "type": "Sentence", "text": [ "These findings provide the first evidence that profilin is a key molecule linking a signaling network to rapid actin polymerization in microspike formation." ], "offsets": [ [ 0, 156 ] ] } ]

[ { "id": "BioInfer.d247.s2.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 111, 116 ] ], "normalized": [] }, { "id": "BioInfer.d247.s2.e1", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 47, 55 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d247.s2.i0", "type": "PPI", "arg1_id": "BioInfer.d247.s2.e0", "arg2_id": "BioInfer.d247.s2.e1", "normalized": [] } ]

[ { "id": "BioInfer.d247.s3__text", "type": "Sentence", "text": [ "This mutant profilin I suppresses actin polymerization in microspike formation induced by N-WASP, the essential factor in microspike formation." ], "offsets": [ [ 0, 143 ] ] } ]

[ { "id": "BioInfer.d247.s3.e0", "type": "Individual_protein", "text": [ "profilin I" ], "offsets": [ [ 12, 22 ] ], "normalized": [] }, { "id": "BioInfer.d247.s3.e1", "type": "Individual_protein", "text": [ "N-WASP" ], "offsets": [ [ 90, 96 ] ], "normalized": [] }, { "id": "BioInfer.d247.s3.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 34, 39 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d247.s3.i0", "type": "PPI", "arg1_id": "BioInfer.d247.s3.e0", "arg2_id": "BioInfer.d247.s3.e1", "normalized": [] }, { "id": "BioInfer.d247.s3.i1", "type": "PPI", "arg1_id": "BioInfer.d247.s3.e0", "arg2_id": "BioInfer.d247.s3.e2", "normalized": [] }, { "id": "BioInfer.d247.s3.i2", "type": "PPI", "arg1_id": "BioInfer.d247.s3.e1", "arg2_id": "BioInfer.d247.s3.e2", "normalized": [] } ]

[ { "id": "BioInfer.d248.s0__text", "type": "Sentence", "text": [ "Here we report that p120 associates with a complex containing E-cadherin, alpha-catenin, beta-catenin, and plakoglobin." ], "offsets": [ [ 0, 119 ] ] } ]

[ { "id": "BioInfer.d248.s0.e0", "type": "Individual_protein", "text": [ "E-cadherin" ], "offsets": [ [ 62, 72 ] ], "normalized": [] }, { "id": "BioInfer.d248.s0.e1", "type": "Individual_protein", "text": [ "p120" ], "offsets": [ [ 20, 24 ] ], "normalized": [] }, { "id": "BioInfer.d248.s0.e2", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 74, 87 ] ], "normalized": [] }, { "id": "BioInfer.d248.s0.e3", "type": "Individual_protein", "text": [ "plakoglobin" ], "offsets": [ [ 107, 118 ] ], "normalized": [] }, { "id": "BioInfer.d248.s0.e4", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 89, 101 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d248.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d248.s0.e0", "arg2_id": "BioInfer.d248.s0.e1", "normalized": [] }, { "id": "BioInfer.d248.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d248.s0.e0", "arg2_id": "BioInfer.d248.s0.e2", "normalized": [] }, { "id": "BioInfer.d248.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d248.s0.e0", "arg2_id": "BioInfer.d248.s0.e3", "normalized": [] }, { "id": "BioInfer.d248.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d248.s0.e0", "arg2_id": "BioInfer.d248.s0.e4", "normalized": [] }, { "id": "BioInfer.d248.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d248.s0.e1", "arg2_id": "BioInfer.d248.s0.e2", "normalized": [] }, { "id": "BioInfer.d248.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d248.s0.e1", "arg2_id": "BioInfer.d248.s0.e3", "normalized": [] }, { "id": "BioInfer.d248.s0.i6", "type": "PPI", "arg1_id": "BioInfer.d248.s0.e1", "arg2_id": "BioInfer.d248.s0.e4", "normalized": [] }, { "id": "BioInfer.d248.s0.i7", "type": "PPI", "arg1_id": "BioInfer.d248.s0.e2", "arg2_id": "BioInfer.d248.s0.e3", "normalized": [] }, { "id": "BioInfer.d248.s0.i8", "type": "PPI", "arg1_id": "BioInfer.d248.s0.e2", "arg2_id": "BioInfer.d248.s0.e4", "normalized": [] }, { "id": "BioInfer.d248.s0.i9", "type": "PPI", "arg1_id": "BioInfer.d248.s0.e3", "arg2_id": "BioInfer.d248.s0.e4", "normalized": [] } ]

[ { "id": "BioInfer.d249.s0__text", "type": "Sentence", "text": [ "Here we report the functional importance of profilin in various actin-mediated morphological changes using H119E mutant profilin I, which is deficient only in actin binding." ], "offsets": [ [ 0, 173 ] ] } ]

[ { "id": "BioInfer.d249.s0.e0", "type": "Individual_protein", "text": [ "H119E", "profilin I" ], "offsets": [ [ 107, 112 ], [ 120, 130 ] ], "normalized": [] }, { "id": "BioInfer.d249.s0.e1", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 44, 52 ] ], "normalized": [] }, { "id": "BioInfer.d249.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 64, 69 ] ], "normalized": [] }, { "id": "BioInfer.d249.s0.e3", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 159, 164 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d249.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d249.s0.e0", "arg2_id": "BioInfer.d249.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d250.s0__text", "type": "Sentence", "text": [ "Here we show that cdc12p is a member of a family of proteins including Drosophila diaphanous, Saccharomyces cerevisiae BNI1, and S. pombe fus1, which are involved in cytokinesis or other actin-mediated processes." ], "offsets": [ [ 0, 212 ] ] } ]

[ { "id": "BioInfer.d250.s0.e0", "type": "Individual_protein", "text": [ "cdc12p" ], "offsets": [ [ 18, 24 ] ], "normalized": [] }, { "id": "BioInfer.d250.s0.e1", "type": "Individual_protein", "text": [ "fus1" ], "offsets": [ [ 138, 142 ] ], "normalized": [] }, { "id": "BioInfer.d250.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 187, 192 ] ], "normalized": [] }, { "id": "BioInfer.d250.s0.e3", "type": "Individual_protein", "text": [ "BNI1" ], "offsets": [ [ 119, 123 ] ], "normalized": [] }, { "id": "BioInfer.d250.s0.e4", "type": "Individual_protein", "text": [ "diaphanous" ], "offsets": [ [ 82, 92 ] ], "normalized": [] } ]

[]

[]

[]

[ { "id": "BioInfer.d251.s0__text", "type": "Sentence", "text": [ "Here, we show that EID-1 is a potent inhibitor of differentiation and link this activity to its ability to inhibit p300 (and the highly related molecule, CREB-binding protein, or CBP) histone acetylation activity." ], "offsets": [ [ 0, 213 ] ] } ]

[ { "id": "BioInfer.d251.s0.e0", "type": "Individual_protein", "text": [ "p300" ], "offsets": [ [ 115, 119 ] ], "normalized": [] }, { "id": "BioInfer.d251.s0.e1", "type": "Protein_family_or_group", "text": [ "histone" ], "offsets": [ [ 184, 191 ] ], "normalized": [] }, { "id": "BioInfer.d251.s0.e2", "type": "Individual_protein", "text": [ "CREB-binding protein" ], "offsets": [ [ 154, 174 ] ], "normalized": [] }, { "id": "BioInfer.d251.s0.e3", "type": "Individual_protein", "text": [ "CBP" ], "offsets": [ [ 179, 182 ] ], "normalized": [] }, { "id": "BioInfer.d251.s0.e4", "type": "Individual_protein", "text": [ "EID-1" ], "offsets": [ [ 19, 24 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d251.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d251.s0.e0", "arg2_id": "BioInfer.d251.s0.e1", "normalized": [] }, { "id": "BioInfer.d251.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d251.s0.e0", "arg2_id": "BioInfer.d251.s0.e2", "normalized": [] }, { "id": "BioInfer.d251.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d251.s0.e0", "arg2_id": "BioInfer.d251.s0.e3", "normalized": [] }, { "id": "BioInfer.d251.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d251.s0.e1", "arg2_id": "BioInfer.d251.s0.e2", "normalized": [] }, { "id": "BioInfer.d251.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d251.s0.e1", "arg2_id": "BioInfer.d251.s0.e3", "normalized": [] }, { "id": "BioInfer.d251.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d251.s0.e1", "arg2_id": "BioInfer.d251.s0.e4", "normalized": [] } ]

[ { "id": "BioInfer.d252.s0__text", "type": "Sentence", "text": [ "Here we show that the N-terminal domain of ActA binds one actin monomer, in a profilin-like fashion, and Arp2/3 complex and mimics the C-terminal domain of WASp family proteins in catalyzing filament barbed end branching by Arp2/3 complex." ], "offsets": [ [ 0, 239 ] ] } ]

[ { "id": "BioInfer.d252.s0.e0", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 78, 86 ] ], "normalized": [] }, { "id": "BioInfer.d252.s0.e1", "type": "Individual_protein", "text": [ "Arp2" ], "offsets": [ [ 105, 109 ] ], "normalized": [] }, { "id": "BioInfer.d252.s0.e2", "type": "Individual_protein", "text": [ "Arp2" ], "offsets": [ [ 224, 228 ] ], "normalized": [] }, { "id": "BioInfer.d252.s0.e3", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 58, 63 ] ], "normalized": [] }, { "id": "BioInfer.d252.s0.e4", "type": "Individual_protein", "text": [ "Arp", "3" ], "offsets": [ [ 105, 108 ], [ 110, 111 ] ], "normalized": [] }, { "id": "BioInfer.d252.s0.e5", "type": "Individual_protein", "text": [ "Arp", "3" ], "offsets": [ [ 224, 227 ], [ 229, 230 ] ], "normalized": [] }, { "id": "BioInfer.d252.s0.e6", "type": "Individual_protein", "text": [ "WASp" ], "offsets": [ [ 156, 160 ] ], "normalized": [] }, { "id": "BioInfer.d252.s0.e7", "type": "Individual_protein", "text": [ "ActA" ], "offsets": [ [ 43, 47 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d252.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d252.s0.e0", "arg2_id": "BioInfer.d252.s0.e7", "normalized": [] }, { "id": "BioInfer.d252.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d252.s0.e1", "arg2_id": "BioInfer.d252.s0.e4", "normalized": [] }, { "id": "BioInfer.d252.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d252.s0.e1", "arg2_id": "BioInfer.d252.s0.e7", "normalized": [] }, { "id": "BioInfer.d252.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d252.s0.e2", "arg2_id": "BioInfer.d252.s0.e5", "normalized": [] }, { "id": "BioInfer.d252.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d252.s0.e3", "arg2_id": "BioInfer.d252.s0.e7", "normalized": [] }, { "id": "BioInfer.d252.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d252.s0.e4", "arg2_id": "BioInfer.d252.s0.e7", "normalized": [] } ]

[ { "id": "BioInfer.d254.s0__text", "type": "Sentence", "text": [ "Here, we show that the x-ray sensitivity of rad55 and rad57 mutant strains is suppressible by overexpression of RAD51 or RAD52." ], "offsets": [ [ 0, 127 ] ] } ]

[ { "id": "BioInfer.d254.s0.e0", "type": "Gene", "text": [ "rad57" ], "offsets": [ [ 54, 59 ] ], "normalized": [] }, { "id": "BioInfer.d254.s0.e1", "type": "Individual_protein", "text": [ "RAD51" ], "offsets": [ [ 112, 117 ] ], "normalized": [] }, { "id": "BioInfer.d254.s0.e2", "type": "Gene", "text": [ "rad55" ], "offsets": [ [ 44, 49 ] ], "normalized": [] }, { "id": "BioInfer.d254.s0.e3", "type": "Individual_protein", "text": [ "RAD52" ], "offsets": [ [ 121, 126 ] ], "normalized": [] } ]

[]

[]

[]

[ { "id": "BioInfer.d255.s0__text", "type": "Sentence", "text": [ "alpha-SNAP binds to predicted alpha-helical coiled-coil regions of syntaxin and SNAP-25, shown previously to be engaged in their direct interaction." ], "offsets": [ [ 0, 148 ] ] } ]

[ { "id": "BioInfer.d255.s0.e0", "type": "Individual_protein", "text": [ "syntaxin" ], "offsets": [ [ 67, 75 ] ], "normalized": [] }, { "id": "BioInfer.d255.s0.e1", "type": "Individual_protein", "text": [ "alpha-SNAP" ], "offsets": [ [ 0, 10 ] ], "normalized": [] }, { "id": "BioInfer.d255.s0.e2", "type": "Individual_protein", "text": [ "SNAP-25" ], "offsets": [ [ 80, 87 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d255.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d255.s0.e0", "arg2_id": "BioInfer.d255.s0.e1", "normalized": [] }, { "id": "BioInfer.d255.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d255.s0.e0", "arg2_id": "BioInfer.d255.s0.e2", "normalized": [] }, { "id": "BioInfer.d255.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d255.s0.e1", "arg2_id": "BioInfer.d255.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d256.s0__text", "type": "Sentence", "text": [ "Here, we sought to determine the spatial distributions of E-cadherin, alpha-catenin, beta-catenin, and plakoglobin, and whether different complexes of these proteins accumulate at steady state in polarized Madin-Darby canine kidney cells." ], "offsets": [ [ 0, 238 ] ] } ]

[ { "id": "BioInfer.d256.s0.e0", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 85, 97 ] ], "normalized": [] }, { "id": "BioInfer.d256.s0.e1", "type": "Individual_protein", "text": [ "E-cadherin" ], "offsets": [ [ 58, 68 ] ], "normalized": [] }, { "id": "BioInfer.d256.s0.e2", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 70, 83 ] ], "normalized": [] }, { "id": "BioInfer.d256.s0.e3", "type": "Individual_protein", "text": [ "plakoglobin" ], "offsets": [ [ 103, 114 ] ], "normalized": [] } ]

[]

[]

[]

[ { "id": "BioInfer.d257.s0__text", "type": "Sentence", "text": [ "Herpes simplex virus type 1 encodes a heterotrimeric helicase-primase complex that is composed of the products of the UL5, UL52, and UL8 genes." ], "offsets": [ [ 0, 143 ] ] } ]

[ { "id": "BioInfer.d257.s0.e0", "type": "Gene", "text": [ "UL52" ], "offsets": [ [ 123, 127 ] ], "normalized": [] }, { "id": "BioInfer.d257.s0.e1", "type": "Protein_complex", "text": [ "helicase-primase" ], "offsets": [ [ 53, 69 ] ], "normalized": [] }, { "id": "BioInfer.d257.s0.e2", "type": "Gene", "text": [ "UL5" ], "offsets": [ [ 118, 121 ] ], "normalized": [] }, { "id": "BioInfer.d257.s0.e3", "type": "Gene", "text": [ "UL8" ], "offsets": [ [ 133, 136 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d257.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d257.s0.e0", "arg2_id": "BioInfer.d257.s0.e1", "normalized": [] }, { "id": "BioInfer.d257.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d257.s0.e0", "arg2_id": "BioInfer.d257.s0.e2", "normalized": [] }, { "id": "BioInfer.d257.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d257.s0.e0", "arg2_id": "BioInfer.d257.s0.e3", "normalized": [] }, { "id": "BioInfer.d257.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d257.s0.e1", "arg2_id": "BioInfer.d257.s0.e2", "normalized": [] }, { "id": "BioInfer.d257.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d257.s0.e1", "arg2_id": "BioInfer.d257.s0.e3", "normalized": [] }, { "id": "BioInfer.d257.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d257.s0.e2", "arg2_id": "BioInfer.d257.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d258.s0__text", "type": "Sentence", "text": [ "Herpes simplex virus type 1 expresses a heterotrimeric helicase-primase, the subunits of which are encoded by the viral UL5, UL8 and UL52 genes." ], "offsets": [ [ 0, 144 ] ] } ]

[ { "id": "BioInfer.d258.s0.e0", "type": "Gene", "text": [ "UL8" ], "offsets": [ [ 125, 128 ] ], "normalized": [] }, { "id": "BioInfer.d258.s0.e1", "type": "Gene", "text": [ "UL5" ], "offsets": [ [ 120, 123 ] ], "normalized": [] }, { "id": "BioInfer.d258.s0.e2", "type": "Protein_complex", "text": [ "helicase-primase" ], "offsets": [ [ 55, 71 ] ], "normalized": [] }, { "id": "BioInfer.d258.s0.e3", "type": "Gene", "text": [ "UL52" ], "offsets": [ [ 133, 137 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d258.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d258.s0.e0", "arg2_id": "BioInfer.d258.s0.e2", "normalized": [] }, { "id": "BioInfer.d258.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d258.s0.e1", "arg2_id": "BioInfer.d258.s0.e2", "normalized": [] }, { "id": "BioInfer.d258.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d258.s0.e2", "arg2_id": "BioInfer.d258.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d258.s1__text", "type": "Sentence", "text": [ "The interactions of the UL52 protein with the UL8 and UL5 proteins were analysed by using the yeast two-hybrid system." ], "offsets": [ [ 0, 118 ] ] } ]

[ { "id": "BioInfer.d258.s1.e0", "type": "Individual_protein", "text": [ "UL5" ], "offsets": [ [ 54, 57 ] ], "normalized": [] }, { "id": "BioInfer.d258.s1.e1", "type": "Individual_protein", "text": [ "UL8" ], "offsets": [ [ 46, 49 ] ], "normalized": [] }, { "id": "BioInfer.d258.s1.e2", "type": "Individual_protein", "text": [ "UL52" ], "offsets": [ [ 24, 28 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d258.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d258.s1.e0", "arg2_id": "BioInfer.d258.s1.e2", "normalized": [] }, { "id": "BioInfer.d258.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d258.s1.e1", "arg2_id": "BioInfer.d258.s1.e2", "normalized": [] } ]

[ { "id": "BioInfer.d258.s2__text", "type": "Sentence", "text": [ "Two-hybrid analysis of the interaction between the UL52 and UL8 subunits of the herpes simplex virus type 1 helicase-primase." ], "offsets": [ [ 0, 125 ] ] } ]

[ { "id": "BioInfer.d258.s2.e0", "type": "Protein_complex", "text": [ "helicase-primase" ], "offsets": [ [ 108, 124 ] ], "normalized": [] } ]

[]

[]

[]

[ { "id": "BioInfer.d259.s0__text", "type": "Sentence", "text": [ "Herpes simplex virus type 1 (HSV-1) encodes a helicase-primase that consists of the products of the UL5, UL8, and UL52 genes (Crute, J. J., Tsurumi, T., Zhu, L., Weller, S. K., Olivo, P. D., Challberg, M. D., Mocarski, E. S. and Lehman, I. R. (1989) Proc. Natl. Acad. Sci. U. S. A. 86, 2186-2189)." ], "offsets": [ [ 0, 297 ] ] } ]

[ { "id": "BioInfer.d259.s0.e0", "type": "Gene", "text": [ "UL8" ], "offsets": [ [ 105, 108 ] ], "normalized": [] }, { "id": "BioInfer.d259.s0.e1", "type": "Gene", "text": [ "UL52" ], "offsets": [ [ 114, 118 ] ], "normalized": [] }, { "id": "BioInfer.d259.s0.e2", "type": "Protein_complex", "text": [ "helicase-primase" ], "offsets": [ [ 46, 62 ] ], "normalized": [] }, { "id": "BioInfer.d259.s0.e3", "type": "Gene", "text": [ "UL5" ], "offsets": [ [ 100, 103 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d259.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d259.s0.e0", "arg2_id": "BioInfer.d259.s0.e1", "normalized": [] }, { "id": "BioInfer.d259.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d259.s0.e0", "arg2_id": "BioInfer.d259.s0.e2", "normalized": [] }, { "id": "BioInfer.d259.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d259.s0.e0", "arg2_id": "BioInfer.d259.s0.e3", "normalized": [] }, { "id": "BioInfer.d259.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d259.s0.e1", "arg2_id": "BioInfer.d259.s0.e2", "normalized": [] }, { "id": "BioInfer.d259.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d259.s0.e1", "arg2_id": "BioInfer.d259.s0.e3", "normalized": [] }, { "id": "BioInfer.d259.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d259.s0.e2", "arg2_id": "BioInfer.d259.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d260.s0__text", "type": "Sentence", "text": [ "Herpes simplex virus type 1 (HSV-1) encodes a helicase-primase that consists of three polypeptides encoded by the UL5, UL8, and UL52 genes (Crute, J.J., Tsurumi, T., Zhu, L., Weller, S.K., Olivo, P.D., Challberg, M.D., Mocarski, E.S., and Lehman, I.R. (1989) Proc. Natl." ], "offsets": [ [ 0, 270 ] ] } ]

[ { "id": "BioInfer.d260.s0.e0", "type": "Individual_protein", "text": [ "helicase-primase" ], "offsets": [ [ 46, 62 ] ], "normalized": [] }, { "id": "BioInfer.d260.s0.e1", "type": "Gene", "text": [ "UL8" ], "offsets": [ [ 119, 122 ] ], "normalized": [] }, { "id": "BioInfer.d260.s0.e2", "type": "Gene", "text": [ "UL5" ], "offsets": [ [ 114, 117 ] ], "normalized": [] }, { "id": "BioInfer.d260.s0.e3", "type": "Gene", "text": [ "UL52" ], "offsets": [ [ 128, 132 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d260.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d260.s0.e0", "arg2_id": "BioInfer.d260.s0.e1", "normalized": [] }, { "id": "BioInfer.d260.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d260.s0.e0", "arg2_id": "BioInfer.d260.s0.e2", "normalized": [] }, { "id": "BioInfer.d260.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d260.s0.e0", "arg2_id": "BioInfer.d260.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d261.s0__text", "type": "Sentence", "text": [ "Herpes simplex virus type 1 (HSV-1) encodes a heterotrimeric helicase-primase composed of the products of the three DNA replication-specific genes UL5, UL8, and UL52 (Crute, J. J., and Lehman, I. R. (1991) J. Biol. Chem. 266, 4484-4488)." ], "offsets": [ [ 0, 237 ] ] } ]

[ { "id": "BioInfer.d261.s0.e0", "type": "Gene", "text": [ "UL8" ], "offsets": [ [ 152, 155 ] ], "normalized": [] }, { "id": "BioInfer.d261.s0.e1", "type": "Protein_complex", "text": [ "helicase-primase" ], "offsets": [ [ 61, 77 ] ], "normalized": [] }, { "id": "BioInfer.d261.s0.e2", "type": "Gene", "text": [ "UL5" ], "offsets": [ [ 147, 150 ] ], "normalized": [] }, { "id": "BioInfer.d261.s0.e3", "type": "Gene", "text": [ "UL52" ], "offsets": [ [ 161, 165 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d261.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d261.s0.e0", "arg2_id": "BioInfer.d261.s0.e1", "normalized": [] }, { "id": "BioInfer.d261.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d261.s0.e0", "arg2_id": "BioInfer.d261.s0.e2", "normalized": [] }, { "id": "BioInfer.d261.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d261.s0.e0", "arg2_id": "BioInfer.d261.s0.e3", "normalized": [] }, { "id": "BioInfer.d261.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d261.s0.e1", "arg2_id": "BioInfer.d261.s0.e2", "normalized": [] }, { "id": "BioInfer.d261.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d261.s0.e1", "arg2_id": "BioInfer.d261.s0.e3", "normalized": [] }, { "id": "BioInfer.d261.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d261.s0.e2", "arg2_id": "BioInfer.d261.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d262.s0__text", "type": "Sentence", "text": [ "HGF/SF treatment of LoVo reduced the amount of alpha-catenin complexed with E-cadherin more markedly than in L-10, but in both cell lines this reduction was not accompanied by increased tyrosine phosphorylation of beta-catenin, suggesting the presence of a mechanism other than phosphorylation for release from cell-cell adhesion during cell motility." ], "offsets": [ [ 0, 351 ] ] } ]

[ { "id": "BioInfer.d262.s0.e0", "type": "Individual_protein", "text": [ "SF" ], "offsets": [ [ 4, 6 ] ], "normalized": [] }, { "id": "BioInfer.d262.s0.e1", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 47, 60 ] ], "normalized": [] }, { "id": "BioInfer.d262.s0.e2", "type": "Individual_protein", "text": [ "E-cadherin" ], "offsets": [ [ 76, 86 ] ], "normalized": [] }, { "id": "BioInfer.d262.s0.e3", "type": "Individual_protein", "text": [ "HGF" ], "offsets": [ [ 0, 3 ] ], "normalized": [] }, { "id": "BioInfer.d262.s0.e4", "type": "Gene/protein/RNA", "text": [ "beta-catenin" ], "offsets": [ [ 214, 226 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d262.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d262.s0.e1", "arg2_id": "BioInfer.d262.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d263.s0__text", "type": "Sentence", "text": [ "High levels of profilin suppress the lethality caused by overproduction of actin in yeast cells." ], "offsets": [ [ 0, 96 ] ] } ]

[ { "id": "BioInfer.d263.s0.e0", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 15, 23 ] ], "normalized": [] }, { "id": "BioInfer.d263.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 75, 80 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d263.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d263.s0.e0", "arg2_id": "BioInfer.d263.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d263.s1__text", "type": "Sentence", "text": [ "In contrast, overexpression of the profilin gene, PFY1, encoding an actin-binding protein, leads to no very obvious phenotype." ], "offsets": [ [ 0, 126 ] ] } ]

[ { "id": "BioInfer.d263.s1.e0", "type": "Individual_protein", "text": [ "actin-binding protein" ], "offsets": [ [ 68, 89 ] ], "normalized": [] }, { "id": "BioInfer.d263.s1.e1", "type": "Gene", "text": [ "PFY1" ], "offsets": [ [ 50, 54 ] ], "normalized": [] }, { "id": "BioInfer.d263.s1.e2", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 35, 43 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d263.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d263.s1.e0", "arg2_id": "BioInfer.d263.s1.e1", "normalized": [] }, { "id": "BioInfer.d263.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d263.s1.e0", "arg2_id": "BioInfer.d263.s1.e2", "normalized": [] } ]

[ { "id": "BioInfer.d263.s2__text", "type": "Sentence", "text": [ "Interestingly, profilin overproduction can compensate for the deleterious effects of too much actin in a profilin concentration-dependent manner." ], "offsets": [ [ 0, 145 ] ] } ]

[ { "id": "BioInfer.d263.s2.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 94, 99 ] ], "normalized": [] }, { "id": "BioInfer.d263.s2.e1", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 105, 113 ] ], "normalized": [] }, { "id": "BioInfer.d263.s2.e2", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 15, 23 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d263.s2.i0", "type": "PPI", "arg1_id": "BioInfer.d263.s2.e0", "arg2_id": "BioInfer.d263.s2.e1", "normalized": [] }, { "id": "BioInfer.d263.s2.i1", "type": "PPI", "arg1_id": "BioInfer.d263.s2.e0", "arg2_id": "BioInfer.d263.s2.e2", "normalized": [] } ]

[ { "id": "BioInfer.d264.s0__text", "type": "Sentence", "text": [ "Histone H3 showed at least seven sites of acetylation, histone H2B.1 had six sites and histone H4 had five sites." ], "offsets": [ [ 0, 113 ] ] } ]

[ { "id": "BioInfer.d264.s0.e0", "type": "Protein_family_or_group", "text": [ "histone" ], "offsets": [ [ 87, 94 ] ], "normalized": [] }, { "id": "BioInfer.d264.s0.e1", "type": "Protein_family_or_group", "text": [ "Histone" ], "offsets": [ [ 0, 7 ] ], "normalized": [] }, { "id": "BioInfer.d264.s0.e2", "type": "Individual_protein", "text": [ "H2B.1" ], "offsets": [ [ 63, 68 ] ], "normalized": [] }, { "id": "BioInfer.d264.s0.e3", "type": "Protein_family_or_group", "text": [ "histone" ], "offsets": [ [ 55, 62 ] ], "normalized": [] }, { "id": "BioInfer.d264.s0.e4", "type": "Individual_protein", "text": [ "H4" ], "offsets": [ [ 95, 97 ] ], "normalized": [] }, { "id": "BioInfer.d264.s0.e5", "type": "Individual_protein", "text": [ "H3" ], "offsets": [ [ 8, 10 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d264.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d264.s0.e0", "arg2_id": "BioInfer.d264.s0.e4", "normalized": [] }, { "id": "BioInfer.d264.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d264.s0.e1", "arg2_id": "BioInfer.d264.s0.e5", "normalized": [] }, { "id": "BioInfer.d264.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d264.s0.e2", "arg2_id": "BioInfer.d264.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d266.s0__text", "type": "Sentence", "text": [ "However, although expression of Ras alone will not induce G1 CDK activity or S phase, coexpression of Ras with Myc allows the generation of cyclin E-dependent kinase activity and the induction of S phase, coincident with the loss of the p27 cyclin-dependent kinase inhibitor (CKI)." ], "offsets": [ [ 0, 281 ] ] } ]

[ { "id": "BioInfer.d266.s0.e0", "type": "Protein_family_or_group", "text": [ "cyclin-dependent kinase inhibitor" ], "offsets": [ [ 241, 274 ] ], "normalized": [] }, { "id": "BioInfer.d266.s0.e1", "type": "Protein_family_or_group", "text": [ "CKI" ], "offsets": [ [ 276, 279 ] ], "normalized": [] }, { "id": "BioInfer.d266.s0.e2", "type": "Individual_protein", "text": [ "Myc" ], "offsets": [ [ 111, 114 ] ], "normalized": [] }, { "id": "BioInfer.d266.s0.e3", "type": "Individual_protein", "text": [ "Ras" ], "offsets": [ [ 102, 105 ] ], "normalized": [] }, { "id": "BioInfer.d266.s0.e4", "type": "Individual_protein", "text": [ "CDK" ], "offsets": [ [ 61, 64 ] ], "normalized": [] }, { "id": "BioInfer.d266.s0.e5", "type": "Individual_protein", "text": [ "Ras" ], "offsets": [ [ 32, 35 ] ], "normalized": [] }, { "id": "BioInfer.d266.s0.e6", "type": "Individual_protein", "text": [ "p27" ], "offsets": [ [ 237, 240 ] ], "normalized": [] }, { "id": "BioInfer.d266.s0.e7", "type": "Individual_protein", "text": [ "cyclin E-dependent kinase" ], "offsets": [ [ 140, 165 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d266.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d266.s0.e0", "arg2_id": "BioInfer.d266.s0.e6", "normalized": [] }, { "id": "BioInfer.d266.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d266.s0.e1", "arg2_id": "BioInfer.d266.s0.e6", "normalized": [] }, { "id": "BioInfer.d266.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d266.s0.e2", "arg2_id": "BioInfer.d266.s0.e3", "normalized": [] }, { "id": "BioInfer.d266.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d266.s0.e2", "arg2_id": "BioInfer.d266.s0.e7", "normalized": [] }, { "id": "BioInfer.d266.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d266.s0.e3", "arg2_id": "BioInfer.d266.s0.e7", "normalized": [] }, { "id": "BioInfer.d266.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d266.s0.e4", "arg2_id": "BioInfer.d266.s0.e5", "normalized": [] }, { "id": "BioInfer.d266.s0.i6", "type": "PPI", "arg1_id": "BioInfer.d266.s0.e6", "arg2_id": "BioInfer.d266.s0.e7", "normalized": [] } ]

[ { "id": "BioInfer.d267.s0__text", "type": "Sentence", "text": [ "However, a number of mammalian DNA repair proteins lack NLS clusters; these proteins include ERCC1, ERCC2 (XPD), mouse RAD51, and the HHR23B/p58 and HHR23A subunits of XPC." ], "offsets": [ [ 0, 172 ] ] } ]

[ { "id": "BioInfer.d267.s0.e0", "type": "Protein_complex", "text": [ "XPC" ], "offsets": [ [ 168, 171 ] ], "normalized": [] }, { "id": "BioInfer.d267.s0.e1", "type": "Individual_protein", "text": [ "XPD" ], "offsets": [ [ 107, 110 ] ], "normalized": [] }, { "id": "BioInfer.d267.s0.e2", "type": "Individual_protein", "text": [ "HHR23B" ], "offsets": [ [ 134, 140 ] ], "normalized": [] }, { "id": "BioInfer.d267.s0.e3", "type": "Individual_protein", "text": [ "p58" ], "offsets": [ [ 141, 144 ] ], "normalized": [] }, { "id": "BioInfer.d267.s0.e4", "type": "Individual_protein", "text": [ "HHR23A" ], "offsets": [ [ 149, 155 ] ], "normalized": [] }, { "id": "BioInfer.d267.s0.e5", "type": "Gene/protein/RNA", "text": [ "ERCC1" ], "offsets": [ [ 93, 98 ] ], "normalized": [] }, { "id": "BioInfer.d267.s0.e6", "type": "Individual_protein", "text": [ "ERCC2" ], "offsets": [ [ 100, 105 ] ], "normalized": [] }, { "id": "BioInfer.d267.s0.e7", "type": "Gene/protein/RNA", "text": [ "RAD51" ], "offsets": [ [ 119, 124 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d267.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d267.s0.e0", "arg2_id": "BioInfer.d267.s0.e2", "normalized": [] }, { "id": "BioInfer.d267.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d267.s0.e0", "arg2_id": "BioInfer.d267.s0.e3", "normalized": [] }, { "id": "BioInfer.d267.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d267.s0.e0", "arg2_id": "BioInfer.d267.s0.e4", "normalized": [] }, { "id": "BioInfer.d267.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d267.s0.e2", "arg2_id": "BioInfer.d267.s0.e3", "normalized": [] }, { "id": "BioInfer.d267.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d267.s0.e2", "arg2_id": "BioInfer.d267.s0.e4", "normalized": [] }, { "id": "BioInfer.d267.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d267.s0.e3", "arg2_id": "BioInfer.d267.s0.e4", "normalized": [] } ]

[ { "id": "BioInfer.d267.s1__text", "type": "Sentence", "text": [ "NLS-less S.cerevisiae proteins include both RAD51 and RAD52 that function in the recombination and in the repair of double-strand breaks as well as the RAD23 and HRR25 molecules." ], "offsets": [ [ 0, 178 ] ] } ]

[ { "id": "BioInfer.d267.s1.e0", "type": "Gene/protein/RNA", "text": [ "HRR25" ], "offsets": [ [ 162, 167 ] ], "normalized": [] }, { "id": "BioInfer.d267.s1.e1", "type": "Gene/protein/RNA", "text": [ "RAD52" ], "offsets": [ [ 54, 59 ] ], "normalized": [] }, { "id": "BioInfer.d267.s1.e2", "type": "Gene/protein/RNA", "text": [ "RAD23" ], "offsets": [ [ 152, 157 ] ], "normalized": [] }, { "id": "BioInfer.d267.s1.e3", "type": "Gene/protein/RNA", "text": [ "RAD51" ], "offsets": [ [ 44, 49 ] ], "normalized": [] } ]

[]

[]

[]

[ { "id": "BioInfer.d268.s0__text", "type": "Sentence", "text": [ "However, disassembly of the actin cytoskeleton using Latrunculin-A does not alter verprolin's location, indicating that verprolin establishes and maintains its location independent of the actin cytoskeleton." ], "offsets": [ [ 0, 207 ] ] } ]

[ { "id": "BioInfer.d268.s0.e0", "type": "Individual_protein", "text": [ "verprolin" ], "offsets": [ [ 120, 129 ] ], "normalized": [] }, { "id": "BioInfer.d268.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 188, 193 ] ], "normalized": [] }, { "id": "BioInfer.d268.s0.e2", "type": "Individual_protein", "text": [ "verprolin" ], "offsets": [ [ 82, 91 ] ], "normalized": [] }, { "id": "BioInfer.d268.s0.e3", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 28, 33 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d268.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d268.s0.e0", "arg2_id": "BioInfer.d268.s0.e1", "normalized": [] }, { "id": "BioInfer.d268.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d268.s0.e2", "arg2_id": "BioInfer.d268.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d268.s1__text", "type": "Sentence", "text": [ "Using the two-hybrid system, we show that verprolin binds actin." ], "offsets": [ [ 0, 64 ] ] } ]

[ { "id": "BioInfer.d268.s1.e0", "type": "Individual_protein", "text": [ "verprolin" ], "offsets": [ [ 42, 51 ] ], "normalized": [] }, { "id": "BioInfer.d268.s1.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 58, 63 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d268.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d268.s1.e0", "arg2_id": "BioInfer.d268.s1.e1", "normalized": [] } ]

[ { "id": "BioInfer.d269.s0__text", "type": "Sentence", "text": [ "However, immunofluorescence staining revealed a similar organisation of actin microfilaments, talin and phosphotyrosyl-containing proteins on both substrates." ], "offsets": [ [ 0, 158 ] ] } ]

[ { "id": "BioInfer.d269.s0.e0", "type": "Gene/protein/RNA", "text": [ "talin" ], "offsets": [ [ 94, 99 ] ], "normalized": [] }, { "id": "BioInfer.d269.s0.e1", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 72, 77 ] ], "normalized": [] } ]

[]

[]

[]

[ { "id": "BioInfer.d270.s0__text", "type": "Sentence", "text": [ "However, increases were also selective in nature, with increases in certain individual proteins, including actin (twofold to threefold), vimentin (2.5-fold to sevenfold), tropomyosin (threefold to sixfold), and myosin heavy chain, far exceeding overall increases in cellular protein content (20-40%)." ], "offsets": [ [ 0, 300 ] ] } ]

[ { "id": "BioInfer.d270.s0.e0", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 107, 112 ] ], "normalized": [] }, { "id": "BioInfer.d270.s0.e1", "type": "Gene/protein/RNA", "text": [ "tropomyosin" ], "offsets": [ [ 171, 182 ] ], "normalized": [] }, { "id": "BioInfer.d270.s0.e2", "type": "Gene/protein/RNA", "text": [ "vimentin" ], "offsets": [ [ 137, 145 ] ], "normalized": [] }, { "id": "BioInfer.d270.s0.e3", "type": "Gene/protein/RNA", "text": [ "myosin heavy chain" ], "offsets": [ [ 211, 229 ] ], "normalized": [] } ]

[]

[]

[]

[ { "id": "BioInfer.d272.s0__text", "type": "Sentence", "text": [ "However, once initiated, the synthesis of muscle tropomyosin mRNA continued in the presence of cycloheximide, while the expression of muscle actin, myosin heavy chain, and myogenin mRNA was abolished." ], "offsets": [ [ 0, 200 ] ] } ]

[ { "id": "BioInfer.d272.s0.e0", "type": "Gene/protein/RNA", "text": [ "muscle", "myosin heavy chain" ], "offsets": [ [ 134, 140 ], [ 148, 166 ] ], "normalized": [] }, { "id": "BioInfer.d272.s0.e1", "type": "Gene/protein/RNA", "text": [ "muscle tropomyosin" ], "offsets": [ [ 42, 60 ] ], "normalized": [] }, { "id": "BioInfer.d272.s0.e2", "type": "Gene/protein/RNA", "text": [ "muscle", "myogenin" ], "offsets": [ [ 134, 140 ], [ 172, 180 ] ], "normalized": [] }, { "id": "BioInfer.d272.s0.e3", "type": "Gene/protein/RNA", "text": [ "muscle actin" ], "offsets": [ [ 134, 146 ] ], "normalized": [] } ]

[]

[]

[]

[ { "id": "BioInfer.d272.s1__text", "type": "Sentence", "text": [ "These results suggest that muscle-specific processing of tropomyosin transcripts can continue to occur in the absence of myogenin expression unlike the expression of muscle actin and myosin heavy chain mRNAs." ], "offsets": [ [ 0, 208 ] ] } ]

[ { "id": "BioInfer.d272.s1.e0", "type": "Individual_protein", "text": [ "muscle actin" ], "offsets": [ [ 166, 178 ] ], "normalized": [] }, { "id": "BioInfer.d272.s1.e1", "type": "Individual_protein", "text": [ "myogenin" ], "offsets": [ [ 121, 129 ] ], "normalized": [] }, { "id": "BioInfer.d272.s1.e2", "type": "Individual_protein", "text": [ "myosin heavy chain" ], "offsets": [ [ 183, 201 ] ], "normalized": [] }, { "id": "BioInfer.d272.s1.e3", "type": "Individual_protein", "text": [ "tropomyosin" ], "offsets": [ [ 57, 68 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d272.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d272.s1.e1", "arg2_id": "BioInfer.d272.s1.e3", "normalized": [] } ]

[ { "id": "BioInfer.d274.s0__text", "type": "Sentence", "text": [ "However, similar to utrophin, alpha-syntrophin is only present at the neuromuscular junction in mdx mouse muscle in which dystrophin is absent." ], "offsets": [ [ 0, 143 ] ] } ]

[ { "id": "BioInfer.d274.s0.e0", "type": "Individual_protein", "text": [ "alpha-syntrophin" ], "offsets": [ [ 30, 46 ] ], "normalized": [] }, { "id": "BioInfer.d274.s0.e1", "type": "Gene/protein/RNA", "text": [ "dystrophin" ], "offsets": [ [ 122, 132 ] ], "normalized": [] }, { "id": "BioInfer.d274.s0.e2", "type": "Individual_protein", "text": [ "utrophin" ], "offsets": [ [ 20, 28 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d274.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d274.s0.e0", "arg2_id": "BioInfer.d274.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d274.s1__text", "type": "Sentence", "text": [ "Identification of alpha-syntrophin binding to syntrophin triplet, dystrophin, and utrophin." ], "offsets": [ [ 0, 91 ] ] } ]

[ { "id": "BioInfer.d274.s1.e0", "type": "Individual_protein", "text": [ "alpha-syntrophin" ], "offsets": [ [ 18, 34 ] ], "normalized": [] }, { "id": "BioInfer.d274.s1.e1", "type": "Individual_protein", "text": [ "dystrophin" ], "offsets": [ [ 66, 76 ] ], "normalized": [] }, { "id": "BioInfer.d274.s1.e2", "type": "Individual_protein", "text": [ "syntrophin triplet" ], "offsets": [ [ 46, 64 ] ], "normalized": [] }, { "id": "BioInfer.d274.s1.e3", "type": "Individual_protein", "text": [ "utrophin" ], "offsets": [ [ 82, 90 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d274.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d274.s1.e0", "arg2_id": "BioInfer.d274.s1.e1", "normalized": [] }, { "id": "BioInfer.d274.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d274.s1.e0", "arg2_id": "BioInfer.d274.s1.e2", "normalized": [] }, { "id": "BioInfer.d274.s1.i2", "type": "PPI", "arg1_id": "BioInfer.d274.s1.e0", "arg2_id": "BioInfer.d274.s1.e3", "normalized": [] } ]

[ { "id": "BioInfer.d275.s0__text", "type": "Sentence", "text": [ "However, smooth muscle contents of actin (26.0 +/- 1.8 vs. 19.1 +/- 2.2 micrograms/mg wet wt) and myosin heavy chain (5.5 +/- 0.4 vs. 2.0 +/- 0.3 microgram/mg wet wt) were greater (P < 0.04) in myometrium from late-pregnant vs. nonpregnant ewes." ], "offsets": [ [ 0, 245 ] ] } ]

[ { "id": "BioInfer.d275.s0.e0", "type": "Gene/protein/RNA", "text": [ "myosin heavy chain" ], "offsets": [ [ 98, 116 ] ], "normalized": [] }, { "id": "BioInfer.d275.s0.e1", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 35, 40 ] ], "normalized": [] } ]

[]

[]

[]

[ { "id": "BioInfer.d276.s0__text", "type": "Sentence", "text": [ "However, some proteins (e.g., profilin) and other agents (e.g., cytochalasin D) that bind to actin are affected by the presence of fluorescent labels, making actin intrinsic fluorescence potentially useful in investigating the interaction of these agents with actin, and in validating data obtained using labeled actin." ], "offsets": [ [ 0, 319 ] ] } ]

[ { "id": "BioInfer.d276.s0.e0", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 30, 38 ] ], "normalized": [] }, { "id": "BioInfer.d276.s0.e1", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 158, 163 ] ], "normalized": [] }, { "id": "BioInfer.d276.s0.e2", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 313, 318 ] ], "normalized": [] }, { "id": "BioInfer.d276.s0.e3", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 260, 265 ] ], "normalized": [] }, { "id": "BioInfer.d276.s0.e4", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 93, 98 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d276.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d276.s0.e0", "arg2_id": "BioInfer.d276.s0.e3", "normalized": [] }, { "id": "BioInfer.d276.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d276.s0.e0", "arg2_id": "BioInfer.d276.s0.e4", "normalized": [] } ]

[ { "id": "BioInfer.d278.s0__text", "type": "Sentence", "text": [ "However, these rod structures were not observed in response to TSH, forskolin, or TPA, suggesting that dephosphorylation of cofilin correlates with the reorganization of actin microfilaments but not with the nuclear transport of cofilin." ], "offsets": [ [ 0, 237 ] ] } ]

[ { "id": "BioInfer.d278.s0.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 170, 175 ] ], "normalized": [] }, { "id": "BioInfer.d278.s0.e1", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 229, 236 ] ], "normalized": [] }, { "id": "BioInfer.d278.s0.e2", "type": "Gene/protein/RNA", "text": [ "TSH" ], "offsets": [ [ 63, 66 ] ], "normalized": [] }, { "id": "BioInfer.d278.s0.e3", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 124, 131 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d278.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d278.s0.e0", "arg2_id": "BioInfer.d278.s0.e3", "normalized": [] }, { "id": "BioInfer.d278.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d278.s0.e1", "arg2_id": "BioInfer.d278.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d278.s1__text", "type": "Sentence", "text": [ "This suggests that dephosphorylation of cofilin and destrin/ADF by TSH could be implicated in the disruption of actin-containing stress fibers and in the reorganization of microfilaments induced by this hormone." ], "offsets": [ [ 0, 211 ] ] } ]

[ { "id": "BioInfer.d278.s1.e0", "type": "Individual_protein", "text": [ "ADF" ], "offsets": [ [ 60, 63 ] ], "normalized": [] }, { "id": "BioInfer.d278.s1.e1", "type": "Individual_protein", "text": [ "TSH" ], "offsets": [ [ 67, 70 ] ], "normalized": [] }, { "id": "BioInfer.d278.s1.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 112, 117 ] ], "normalized": [] }, { "id": "BioInfer.d278.s1.e3", "type": "Individual_protein", "text": [ "destrin" ], "offsets": [ [ 52, 59 ] ], "normalized": [] }, { "id": "BioInfer.d278.s1.e4", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 40, 47 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d278.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d278.s1.e0", "arg2_id": "BioInfer.d278.s1.e1", "normalized": [] }, { "id": "BioInfer.d278.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d278.s1.e0", "arg2_id": "BioInfer.d278.s1.e2", "normalized": [] }, { "id": "BioInfer.d278.s1.i2", "type": "PPI", "arg1_id": "BioInfer.d278.s1.e1", "arg2_id": "BioInfer.d278.s1.e2", "normalized": [] }, { "id": "BioInfer.d278.s1.i3", "type": "PPI", "arg1_id": "BioInfer.d278.s1.e1", "arg2_id": "BioInfer.d278.s1.e3", "normalized": [] }, { "id": "BioInfer.d278.s1.i4", "type": "PPI", "arg1_id": "BioInfer.d278.s1.e1", "arg2_id": "BioInfer.d278.s1.e4", "normalized": [] }, { "id": "BioInfer.d278.s1.i5", "type": "PPI", "arg1_id": "BioInfer.d278.s1.e2", "arg2_id": "BioInfer.d278.s1.e3", "normalized": [] }, { "id": "BioInfer.d278.s1.i6", "type": "PPI", "arg1_id": "BioInfer.d278.s1.e2", "arg2_id": "BioInfer.d278.s1.e4", "normalized": [] } ]

[ { "id": "BioInfer.d279.s0__text", "type": "Sentence", "text": [ "However, upon treatment with DMSO, cytoplasmic actin filaments were disrupted and intranuclear rod structures containing cofilin and actin were apparently larger and thicker in cells overexpressing cofilin than in normal cells." ], "offsets": [ [ 0, 227 ] ] } ]

[ { "id": "BioInfer.d279.s0.e0", "type": "Gene/protein/RNA", "text": [ "cofilin" ], "offsets": [ [ 198, 205 ] ], "normalized": [] }, { "id": "BioInfer.d279.s0.e1", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 121, 128 ] ], "normalized": [] }, { "id": "BioInfer.d279.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 133, 138 ] ], "normalized": [] }, { "id": "BioInfer.d279.s0.e3", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 47, 52 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d279.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d279.s0.e1", "arg2_id": "BioInfer.d279.s0.e2", "normalized": [] } ]