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800
BioInfer.d721.s0
[ { "id": "BioInfer.d721.s0__text", "type": "Sentence", "text": [ "The sizes and characteristics of each of the proteins determined from various radiolabelling experiments allowed preliminary identification of the proteins as the large (L; 190 kDa), haemagglutinin neuraminidase (HN; 74 kDa), nucleocapsid (N; 66 kDa), fusion (F0; 63 kDa), phosphoprotein (P; 49 kDa), matrix (M; 43 kDa) and non-structural (V; 35 kDa) proteins." ], "offsets": [ [ 0, 360 ] ] } ]
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[]
[]
[]
801
BioInfer.d722.s0
[ { "id": "BioInfer.d722.s0__text", "type": "Sentence", "text": [ "The Src homology domain 3 (SH3) of a yeast type I myosin, Myo5p, binds to verprolin and is required for targeting to sites of actin polarization." ], "offsets": [ [ 0, 145 ] ] } ]
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[]
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802
BioInfer.d723.s0
[ { "id": "BioInfer.d723.s0__text", "type": "Sentence", "text": [ "The structural homology between cofilin and gelsolin segment-1 binding to actin was confirmed experimentally by two types of competitive binding assays." ], "offsets": [ [ 0, 152 ] ] } ]
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[]
[]
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803
BioInfer.d724.s0
[ { "id": "BioInfer.d724.s0__text", "type": "Sentence", "text": [ "The structure of an actin-crosslinking domain from human fimbrin." ], "offsets": [ [ 0, 65 ] ] } ]
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[]
[]
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804
BioInfer.d725.s0
[ { "id": "BioInfer.d725.s0__text", "type": "Sentence", "text": [ "The structure of Ykt6pN differed entirely from that of syntaxin and resembled the overall fold of the actin regulatory protein, profilin." ], "offsets": [ [ 0, 137 ] ] } ]
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[]
[]
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805
BioInfer.d726.s0
[ { "id": "BioInfer.d726.s0__text", "type": "Sentence", "text": [ "The Tetrahymena fimbrin has two actin-binding domains, but lacks the EF-hand Ca(2+)-binding motif, suggesting that Tetrahymena fimbrin probably cross-links actin filaments in a Ca(2+)- insensitive manner during cytokinesis." ], "offsets": [ [ 0, 223 ] ] } ]
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[]
[]
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806
BioInfer.d727.s0
[ { "id": "BioInfer.d727.s0__text", "type": "Sentence", "text": [ "The tumor necrosis factor receptor 1 (TNFR1) and the Fas receptor recruit complexes formed by the interactions between RIP kinase, TRADD, FADD and RAIDD - adaptor proteins that contain death domains - which in turn recruit other proteins to initiate signaling [1][2][3][4][5]." ], "offsets": [ [ 0, 276 ] ] } ]
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[]
[]
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807
BioInfer.d728.s0
[ { "id": "BioInfer.d728.s0__text", "type": "Sentence", "text": [ "The two cardiac myosin heavy chain isoforms, alpha and beta, differ functionally, alpha Myosin exhibits higher actin-activated ATPase than does beta myosin, and hearts expressing alpha myosin exhibit increased contractility relative to hearts expressing beta myosin." ], "offsets": [ [ 0, 266 ] ] } ]
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[]
[]
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808
BioInfer.d729.s0
[ { "id": "BioInfer.d729.s0__text", "type": "Sentence", "text": [ "The two proteins were found to differ in their interaction with actin, like destrin and cofilin isolated from porcine brain." ], "offsets": [ [ 0, 124 ] ] } ]
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[]
[]
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809
BioInfer.d730.s0
[ { "id": "BioInfer.d730.s0__text", "type": "Sentence", "text": [ "The undifferentiated cells (a) were unable to spread on gelatin or laminin and grew as rounded colonies, although they were able to spread on fibronectin (b) showed reduced adhesion to laminin, but not fibronectin (c) expressed much reduced levels of beta1 integrin, although levels of alpha5 and alphaV were wild-type (d) were less polarized with increased membrane protrusions compared with a vinculin (-/-) ES cell mutant (e) were unable to assemble vinculin or paxillin-containing focal adhesions or actin stress fibers on fibronectin, whereas vinculin (-/-) ES cells were able to assemble talin-containing focal adhesions." ], "offsets": [ [ 0, 627 ] ] } ]
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[]
[]
[]
810
BioInfer.d731.s0
[ { "id": "BioInfer.d731.s0__text", "type": "Sentence", "text": [ "The vaccinia virus E3L gene product, pE3, is a dsRNA binding protein that prevents activation of the interferon-induced, dsRNA-activated protein kinase, PKR." ], "offsets": [ [ 0, 157 ] ] } ]
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811
BioInfer.d732.s0
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812
BioInfer.d733.s0
[ { "id": "BioInfer.d733.s0__text", "type": "Sentence", "text": [ "They exhibited strong synergistic increases in CAN1 duplication mutations, intrachromosomal and interchromosomal recombination, and required the wild-type double-strand break repair genes RAD50, RAD51, and RAD52 for viability." ], "offsets": [ [ 0, 226 ] ] } ]
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[]
[]
[]
813
BioInfer.d734.s0
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[]
[]
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814
BioInfer.d735.s0
[ { "id": "BioInfer.d735.s0__text", "type": "Sentence", "text": [ "This activity is independent of FADD-DN's ability to bind to three known interacting proteins, Fas, TRADD or RIP suggesting that it is distinct from FADD's functions at activated death receptors." ], "offsets": [ [ 0, 195 ] ] } ]
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[]
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815
BioInfer.d736.s0
[ { "id": "BioInfer.d736.s0__text", "type": "Sentence", "text": [ "This approach is based on the assumption that an actin mutation that specifically impairs the interaction with an actin-binding protein will cause a phenotype similar to a null mutation in the gene that encodes the actin-binding protein." ], "offsets": [ [ 0, 237 ] ] } ]
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[]
[]
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816
BioInfer.d736.s1
[ { "id": "BioInfer.d736.s1__text", "type": "Sentence", "text": [ "21 actin mutations were analyzed in budding yeast, and specific regions of actin subdomain 1 were implicated in the interaction with fimbrin, an actin filament-bundling protein." ], "offsets": [ [ 0, 177 ] ] } ]
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[]
[]
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817
BioInfer.d737.s0
[ { "id": "BioInfer.d737.s0__text", "type": "Sentence", "text": [ "This arrest can be suppressed by mutations in RAD51, RAD52, and RAD57, suggesting that the cell cycle defect in sgs1 srs2 mutants results from inappropriate homologous recombination." ], "offsets": [ [ 0, 182 ] ] } ]
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[]
[]
[]
818
BioInfer.d739.s0
[ { "id": "BioInfer.d739.s0__text", "type": "Sentence", "text": [ "This filament growth is driven by a large storage pool of actin bound to the sequestering protein, profilin." ], "offsets": [ [ 0, 108 ] ] } ]
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[]
[]
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819
BioInfer.d740.s0
[ { "id": "BioInfer.d740.s0__text", "type": "Sentence", "text": [ "This is consistent with cofilin activation being required for actin reorganization during exocytosis." ], "offsets": [ [ 0, 101 ] ] } ]
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[]
[]
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820
BioInfer.d741.s0
[ { "id": "BioInfer.d741.s0__text", "type": "Sentence", "text": [ "This is the first report describing the coexistence of profilin with actin filaments in the division furrow, implying the possible involvement of profilin in assembly and disassembly of contractile ring microfilaments in the process of cytokinesis." ], "offsets": [ [ 0, 248 ] ] } ]
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[]
[]
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821
BioInfer.d742.s0
[ { "id": "BioInfer.d742.s0__text", "type": "Sentence", "text": [ "This novel mutation was predicted to disrupt the binding of beta-catenin to alpha-catenin and may be related to the diffuse type morphology." ], "offsets": [ [ 0, 140 ] ] } ]
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[]
[]
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822
BioInfer.d746.s0
[ { "id": "BioInfer.d746.s0__text", "type": "Sentence", "text": [ "This shows that structural changes in the poly(L-proline)-binding region of profilin can affect the distantly located actin-binding site." ], "offsets": [ [ 0, 137 ] ] } ]
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[]
[]
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823
BioInfer.d747.s0
[ { "id": "BioInfer.d747.s0__text", "type": "Sentence", "text": [ "This technique was employed to quantify changes caused by the lack of talin, a protein that couples the actin network to the plasma membrane, or by the lack of cortexillin I or II, two isoforms of the actin-bundling protein cortexillin." ], "offsets": [ [ 0, 236 ] ] } ]
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[]
[]
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824
BioInfer.d749.s0
[ { "id": "BioInfer.d749.s0__text", "type": "Sentence", "text": [ "Three actin-associated proteins, actin-binding protein, gelsolin, and profilin, influence gelation, solation, and polymerization, respectively, of actin in vitro." ], "offsets": [ [ 0, 162 ] ] } ]
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[]
[]
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825
BioInfer.d750.s0
[ { "id": "BioInfer.d750.s0__text", "type": "Sentence", "text": [ "Three components of Drosophila adherens junctions, analogous to those in vertebrates, have been identified: Armadillo (homolog of beta-catenin), Drosophila E-cadherin (DE-cadherin), and alpha-catenin." ], "offsets": [ [ 0, 200 ] ] } ]
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[]
[]
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826
BioInfer.d751.s0
[ { "id": "BioInfer.d751.s0__text", "type": "Sentence", "text": [ "Thus, actin was found in association with fimbrin in the mechanoreceptive region of hair cells, whereas supporting cells, although rich in actin, did not reveal fimbrin." ], "offsets": [ [ 0, 169 ] ] } ]
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[]
[]
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827
BioInfer.d752.s0
[ { "id": "BioInfer.d752.s0__text", "type": "Sentence", "text": [ "Thus, beta-catenin, E-cadherin, and alpha-catenin have similar prognostic values." ], "offsets": [ [ 0, 81 ] ] } ]
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[]
[]
[]
828
BioInfer.d755.s0
[ { "id": "BioInfer.d755.s0__text", "type": "Sentence", "text": [ "Thus, mHip1R contains an NH(2)-terminal domain homologous to that implicated in Sla2p's endocytic function, three predicted coiled-coils, a leucine zipper, and a talin-like actin-binding domain at the COOH terminus." ], "offsets": [ [ 0, 215 ] ] } ]
[ { "id": "BioInfer.d755.s0.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 173, 178 ] ], "normalized": [] }, { "id": "BioInfer.d755.s0.e1", "type": "Individual_protein", "text": [ "Sla2p" ], "offsets": [ [ 80, 85 ] ], "normalized": [] }, { "id": "BioInfer.d755.s0.e2", "type": "Individual_protein", "text": [ "talin" ], "offsets": [ [ 162, 167 ] ], "normalized": [] }, { "id": "BioInfer.d755.s0.e3", "type": "Individual_protein", "text": [ "mHip1R" ], "offsets": [ [ 6, 12 ] ], "normalized": [] } ]
[]
[]
[ { "id": "BioInfer.d755.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d755.s0.e0", "arg2_id": "BioInfer.d755.s0.e3", "normalized": [] }, { "id": "BioInfer.d755.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d755.s0.e1", "arg2_id": "BioInfer.d755.s0.e3", "normalized": [] }, { "id": "BioInfer.d755.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d755.s0.e2", "arg2_id": "BioInfer.d755.s0.e3", "normalized": [] } ]
829
BioInfer.d756.s0
[ { "id": "BioInfer.d756.s0__text", "type": "Sentence", "text": [ "Thus, poly-L-proline binding, actin binding, and actin nucleotide exchange are each independent requirements for profilin function in fission yeast." ], "offsets": [ [ 0, 148 ] ] } ]
[ { "id": "BioInfer.d756.s0.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 30, 35 ] ], "normalized": [] }, { "id": "BioInfer.d756.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 49, 54 ] ], "normalized": [] }, { "id": "BioInfer.d756.s0.e2", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 113, 121 ] ], "normalized": [] } ]
[]
[]
[ { "id": "BioInfer.d756.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d756.s0.e0", "arg2_id": "BioInfer.d756.s0.e2", "normalized": [] }, { "id": "BioInfer.d756.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d756.s0.e1", "arg2_id": "BioInfer.d756.s0.e2", "normalized": [] } ]
830
BioInfer.d757.s0
[ { "id": "BioInfer.d757.s0__text", "type": "Sentence", "text": [ "Thus, the actin-binding dodecapeptide sequence of cofilin may constitute a multifunctional domain in cofilin." ], "offsets": [ [ 0, 109 ] ] } ]
[ { "id": "BioInfer.d757.s0.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 10, 15 ] ], "normalized": [] }, { "id": "BioInfer.d757.s0.e1", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 50, 57 ] ], "normalized": [] }, { "id": "BioInfer.d757.s0.e2", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 101, 108 ] ], "normalized": [] } ]
[]
[]
[ { "id": "BioInfer.d757.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d757.s0.e0", "arg2_id": "BioInfer.d757.s0.e1", "normalized": [] } ]
831
BioInfer.d757.s1
[ { "id": "BioInfer.d757.s1__text", "type": "Sentence", "text": [ "We have previously shown that the synthetic dodecapeptide corresponding to Trp104-Met115 of cofilin is a potent inhibitor of actin polymerization (Yonezawa, N., Nishida, E., Iida, K., Kumagai, H., Yahara, I., and Sakai, H. (1991) J. Biol. Chem. 266, 10485-10489)." ], "offsets": [ [ 0, 263 ] ] } ]
[ { "id": "BioInfer.d757.s1.e0", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 92, 99 ] ], "normalized": [] }, { "id": "BioInfer.d757.s1.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 125, 130 ] ], "normalized": [] } ]
[]
[]
[ { "id": "BioInfer.d757.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d757.s1.e0", "arg2_id": "BioInfer.d757.s1.e1", "normalized": [] } ]
832
BioInfer.d758.s0
[ { "id": "BioInfer.d758.s0__text", "type": "Sentence", "text": [ "TNF also inhibited muscle differentiation as measured by several parameters, including cell fusion and the expression of other muscle-specific genes, such as alpha-skeletal actin and myosin heavy chain." ], "offsets": [ [ 0, 202 ] ] } ]
[ { "id": "BioInfer.d758.s0.e0", "type": "Gene/protein/RNA", "text": [ "TNF" ], "offsets": [ [ 0, 3 ] ], "normalized": [] }, { "id": "BioInfer.d758.s0.e1", "type": "Gene/protein/RNA", "text": [ "myosin heavy chain" ], "offsets": [ [ 183, 201 ] ], "normalized": [] }, { "id": "BioInfer.d758.s0.e2", "type": "Gene/protein/RNA", "text": [ "alpha-skeletal actin" ], "offsets": [ [ 158, 178 ] ], "normalized": [] } ]
[]
[]
[]
833
BioInfer.d760.s0
[ { "id": "BioInfer.d760.s0__text", "type": "Sentence", "text": [ "To characterize the AAV functions mediating this effect, cloned AAV type 2 wild-type or mutant genomes were transfected into simian virus 40 (SV40)-transformed hamster cells together with the six HSV replication genes (encoding UL5, UL8, major DNA-binding protein, DNA polymerase, UL42, and UL52) which together are necessary and sufficient for the induction of SV40 DNA amplification (R. Heilbronn and H. zur Hausen, J. Virol. 63:3683-3692, 1989)." ], "offsets": [ [ 0, 448 ] ] } ]
[ { "id": "BioInfer.d760.s0.e0", "type": "Gene/protein/RNA", "text": [ "DNA polymerase" ], "offsets": [ [ 265, 279 ] ], "normalized": [] }, { "id": "BioInfer.d760.s0.e1", "type": "Gene/protein/RNA", "text": [ "major DNA-binding protein" ], "offsets": [ [ 238, 263 ] ], "normalized": [] }, { "id": "BioInfer.d760.s0.e2", "type": "Gene/protein/RNA", "text": [ "UL8" ], "offsets": [ [ 233, 236 ] ], "normalized": [] }, { "id": "BioInfer.d760.s0.e3", "type": "Gene/protein/RNA", "text": [ "UL5" ], "offsets": [ [ 228, 231 ] ], "normalized": [] }, { "id": "BioInfer.d760.s0.e4", "type": "Gene/protein/RNA", "text": [ "UL52" ], "offsets": [ [ 291, 295 ] ], "normalized": [] }, { "id": "BioInfer.d760.s0.e5", "type": "Gene/protein/RNA", "text": [ "UL42" ], "offsets": [ [ 281, 285 ] ], "normalized": [] } ]
[]
[]
[]
834
BioInfer.d761.s0
[ { "id": "BioInfer.d761.s0__text", "type": "Sentence", "text": [ "To characterize the phenotypic alteration in mesangial cells in human glomerulonephritis, we investigated the expression of nonmuscle-type myosin heavy chain, SMemb, and alpha-smooth muscle actin (alpha-SM actin) in IgA nephropathy." ], "offsets": [ [ 0, 232 ] ] } ]
[ { "id": "BioInfer.d761.s0.e0", "type": "Gene/protein/RNA", "text": [ "IgA" ], "offsets": [ [ 216, 219 ] ], "normalized": [] }, { "id": "BioInfer.d761.s0.e1", "type": "Individual_protein", "text": [ "alpha-smooth muscle actin" ], "offsets": [ [ 170, 195 ] ], "normalized": [] }, { "id": "BioInfer.d761.s0.e2", "type": "Gene/protein/RNA", "text": [ "nonmuscle-type myosin heavy chain" ], "offsets": [ [ 124, 157 ] ], "normalized": [] }, { "id": "BioInfer.d761.s0.e3", "type": "Individual_protein", "text": [ "alpha-SM actin" ], "offsets": [ [ 197, 211 ] ], "normalized": [] }, { "id": "BioInfer.d761.s0.e4", "type": "Gene/protein/RNA", "text": [ "SMemb" ], "offsets": [ [ 159, 164 ] ], "normalized": [] } ]
[]
[]
[]
835
BioInfer.d762.s0
[ { "id": "BioInfer.d762.s0__text", "type": "Sentence", "text": [ "To check its applicability, well characterized, commercially available antibodies (against E-cadherin, alpha-catenin, and beta-catenin) were used on sections of human small intestine." ], "offsets": [ [ 0, 183 ] ] } ]
[ { "id": "BioInfer.d762.s0.e0", "type": "Gene/protein/RNA", "text": [ "alpha-catenin" ], "offsets": [ [ 103, 116 ] ], "normalized": [] }, { "id": "BioInfer.d762.s0.e1", "type": "Gene/protein/RNA", "text": [ "beta-catenin" ], "offsets": [ [ 122, 134 ] ], "normalized": [] }, { "id": "BioInfer.d762.s0.e2", "type": "Gene/protein/RNA", "text": [ "E-cadherin" ], "offsets": [ [ 91, 101 ] ], "normalized": [] } ]
[]
[]
[]
836
BioInfer.d763.s0
[ { "id": "BioInfer.d763.s0__text", "type": "Sentence", "text": [ "To clarify the relation between alteration of expression of cell adhesion molecules and progression of extrahepatic bile duct carcinomas 55 cases were immunohistochemically examined for E-cadherin, alpha-catenin, beta-catenin, and CD44, with additional reverse transcription-polymerase chain reaction and Southern blotting hybridization (RT-PCR/SBH) assays." ], "offsets": [ [ 0, 357 ] ] } ]
[ { "id": "BioInfer.d763.s0.e0", "type": "Gene/protein/RNA", "text": [ "CD44" ], "offsets": [ [ 231, 235 ] ], "normalized": [] }, { "id": "BioInfer.d763.s0.e1", "type": "Gene/protein/RNA", "text": [ "polymerase" ], "offsets": [ [ 275, 285 ] ], "normalized": [] }, { "id": "BioInfer.d763.s0.e2", "type": "Gene/protein/RNA", "text": [ "alpha-catenin" ], "offsets": [ [ 198, 211 ] ], "normalized": [] }, { "id": "BioInfer.d763.s0.e3", "type": "Gene/protein/RNA", "text": [ "cell adhesion molecules" ], "offsets": [ [ 60, 83 ] ], "normalized": [] }, { "id": "BioInfer.d763.s0.e4", "type": "Gene/protein/RNA", "text": [ "E-cadherin" ], "offsets": [ [ 186, 196 ] ], "normalized": [] }, { "id": "BioInfer.d763.s0.e5", "type": "Gene/protein/RNA", "text": [ "beta-catenin" ], "offsets": [ [ 213, 225 ] ], "normalized": [] } ]
[]
[]
[]
837
BioInfer.d764.s0
[ { "id": "BioInfer.d764.s0__text", "type": "Sentence", "text": [ "To determine the phenotypes of smooth muscle cells (SMCs) in such lesions, the authors conducted an immunohistochemical analysis of lung tissues from two patients with PPH, using two antimuscle actin antibodies, HHF35 and CGA7, and two anti-SMC myosin heavy chain markers, anti-SM1 and anti-SM2 antibodies and related antibodies." ], "offsets": [ [ 0, 329 ] ] } ]
[ { "id": "BioInfer.d764.s0.e0", "type": "Individual_protein", "text": [ "HHF35" ], "offsets": [ [ 212, 217 ] ], "normalized": [] }, { "id": "BioInfer.d764.s0.e1", "type": "Gene/protein/RNA", "text": [ "SM1" ], "offsets": [ [ 278, 281 ] ], "normalized": [] }, { "id": "BioInfer.d764.s0.e2", "type": "Gene/protein/RNA", "text": [ "SMC myosin heavy chain" ], "offsets": [ [ 241, 263 ] ], "normalized": [] }, { "id": "BioInfer.d764.s0.e3", "type": "Gene/protein/RNA", "text": [ "SM2" ], "offsets": [ [ 291, 294 ] ], "normalized": [] }, { "id": "BioInfer.d764.s0.e4", "type": "Individual_protein", "text": [ "CGA7" ], "offsets": [ [ 222, 226 ] ], "normalized": [] }, { "id": "BioInfer.d764.s0.e5", "type": "Individual_protein", "text": [ "muscle actin" ], "offsets": [ [ 187, 199 ] ], "normalized": [] } ]
[]
[]
[ { "id": "BioInfer.d764.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d764.s0.e0", "arg2_id": "BioInfer.d764.s0.e5", "normalized": [] }, { "id": "BioInfer.d764.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d764.s0.e4", "arg2_id": "BioInfer.d764.s0.e5", "normalized": [] } ]
838
BioInfer.d765.s0
[ { "id": "BioInfer.d765.s0__text", "type": "Sentence", "text": [ "To determine the relationship between cell cycle regulation and differentiation, the spatiotemporal expression of cyclin A, cyclin B1, cyclin D1, the cyclin-dependent kinase inhibitors (CKIs) p27 and p57, and markers of differentiating podocytes in developing human kidneys was investigated by immunohistochemistry." ], "offsets": [ [ 0, 315 ] ] } ]
[ { "id": "BioInfer.d765.s0.e0", "type": "Individual_protein", "text": [ "p27" ], "offsets": [ [ 192, 195 ] ], "normalized": [] }, { "id": "BioInfer.d765.s0.e1", "type": "Protein_family_or_group", "text": [ "CKIs" ], "offsets": [ [ 186, 190 ] ], "normalized": [] }, { "id": "BioInfer.d765.s0.e2", "type": "Protein_family_or_group", "text": [ "cyclin-dependent kinase inhibitors" ], "offsets": [ [ 150, 184 ] ], "normalized": [] }, { "id": "BioInfer.d765.s0.e3", "type": "Gene/protein/RNA", "text": [ "cyclin D1" ], "offsets": [ [ 135, 144 ] ], "normalized": [] }, { "id": "BioInfer.d765.s0.e4", "type": "Gene/protein/RNA", "text": [ "cyclin A" ], "offsets": [ [ 114, 122 ] ], "normalized": [] }, { "id": "BioInfer.d765.s0.e5", "type": "Gene/protein/RNA", "text": [ "cyclin B1" ], "offsets": [ [ 124, 133 ] ], "normalized": [] }, { "id": "BioInfer.d765.s0.e6", "type": "Individual_protein", "text": [ "p57" ], "offsets": [ [ 200, 203 ] ], "normalized": [] } ]
[]
[]
[ { "id": "BioInfer.d765.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d765.s0.e0", "arg2_id": "BioInfer.d765.s0.e1", "normalized": [] }, { "id": "BioInfer.d765.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d765.s0.e0", "arg2_id": "BioInfer.d765.s0.e2", "normalized": [] }, { "id": "BioInfer.d765.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d765.s0.e1", "arg2_id": "BioInfer.d765.s0.e6", "normalized": [] }, { "id": "BioInfer.d765.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d765.s0.e2", "arg2_id": "BioInfer.d765.s0.e6", "normalized": [] } ]
839
BioInfer.d766.s0
[ { "id": "BioInfer.d766.s0__text", "type": "Sentence", "text": [ "To determine the relative importance of protein degradation in the development of starvation-induced cardiac atrophy, in vivo fractional synthetic rates of total cardiac protein, myosin heavy chain, actin, light chain 1, and light chain 2 were measured in fed and fasted rabbits by continuous infusion of [3H] leucine." ], "offsets": [ [ 0, 318 ] ] } ]
[ { "id": "BioInfer.d766.s0.e0", "type": "Gene/protein/RNA", "text": [ "myosin", "light chain 2" ], "offsets": [ [ 179, 185 ], [ 225, 238 ] ], "normalized": [] }, { "id": "BioInfer.d766.s0.e1", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 199, 204 ] ], "normalized": [] }, { "id": "BioInfer.d766.s0.e2", "type": "Gene/protein/RNA", "text": [ "myosin", "light chain 1" ], "offsets": [ [ 179, 185 ], [ 206, 219 ] ], "normalized": [] }, { "id": "BioInfer.d766.s0.e3", "type": "Gene/protein/RNA", "text": [ "myosin heavy chain" ], "offsets": [ [ 179, 197 ] ], "normalized": [] } ]
[]
[]
[]
840
BioInfer.d767.s0
[ { "id": "BioInfer.d767.s0__text", "type": "Sentence", "text": [ "To determine whether alpha 1-adrenergic stimulation produced similar effects on the turnover of myofibrillar proteins, rates of synthesis and degradation were estimated for a myofibrillar-enriched protein fraction and for myosin heavy chain and actin." ], "offsets": [ [ 0, 251 ] ] } ]
[ { "id": "BioInfer.d767.s0.e0", "type": "Gene/protein/RNA", "text": [ "myosin heavy chain" ], "offsets": [ [ 222, 240 ] ], "normalized": [] }, { "id": "BioInfer.d767.s0.e1", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 245, 250 ] ], "normalized": [] } ]
[]
[]
[]
841
BioInfer.d768.s0
[ { "id": "BioInfer.d768.s0__text", "type": "Sentence", "text": [ "Together these results indicate that TGFbeta regulates clusterin gene expression through an AP-1 site and its cognate transcription factor AP-1, and requires the involvement of protein kinase C." ], "offsets": [ [ 0, 194 ] ] } ]
[ { "id": "BioInfer.d768.s0.e0", "type": "Individual_protein", "text": [ "TGFbeta" ], "offsets": [ [ 37, 44 ] ], "normalized": [] }, { "id": "BioInfer.d768.s0.e1", "type": "Individual_protein", "text": [ "clusterin" ], "offsets": [ [ 55, 64 ] ], "normalized": [] }, { "id": "BioInfer.d768.s0.e2", "type": "Individual_protein", "text": [ "AP-1" ], "offsets": [ [ 139, 143 ] ], "normalized": [] }, { "id": "BioInfer.d768.s0.e3", "type": "Individual_protein", "text": [ "AP-1" ], "offsets": [ [ 92, 96 ] ], "normalized": [] }, { "id": "BioInfer.d768.s0.e4", "type": "Individual_protein", "text": [ "protein kinase C" ], "offsets": [ [ 177, 193 ] ], "normalized": [] } ]
[]
[]
[ { "id": "BioInfer.d768.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d768.s0.e0", "arg2_id": "BioInfer.d768.s0.e1", "normalized": [] }, { "id": "BioInfer.d768.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d768.s0.e0", "arg2_id": "BioInfer.d768.s0.e2", "normalized": [] }, { "id": "BioInfer.d768.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d768.s0.e0", "arg2_id": "BioInfer.d768.s0.e3", "normalized": [] }, { "id": "BioInfer.d768.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d768.s0.e0", "arg2_id": "BioInfer.d768.s0.e4", "normalized": [] }, { "id": "BioInfer.d768.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d768.s0.e1", "arg2_id": "BioInfer.d768.s0.e2", "normalized": [] }, { "id": "BioInfer.d768.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d768.s0.e1", "arg2_id": "BioInfer.d768.s0.e3", "normalized": [] }, { "id": "BioInfer.d768.s0.i6", "type": "PPI", "arg1_id": "BioInfer.d768.s0.e2", "arg2_id": "BioInfer.d768.s0.e3", "normalized": [] } ]
842
BioInfer.d769.s0
[ { "id": "BioInfer.d769.s0__text", "type": "Sentence", "text": [ "To improve our ability to study these proteins, we have expressed UL5, UL8, UL9, and UL52 in insect cells by using the baculovirus expression system." ], "offsets": [ [ 0, 149 ] ] } ]
[ { "id": "BioInfer.d769.s0.e0", "type": "Gene/protein/RNA", "text": [ "UL5" ], "offsets": [ [ 66, 69 ] ], "normalized": [] }, { "id": "BioInfer.d769.s0.e1", "type": "Gene/protein/RNA", "text": [ "UL9" ], "offsets": [ [ 76, 79 ] ], "normalized": [] }, { "id": "BioInfer.d769.s0.e2", "type": "Gene/protein/RNA", "text": [ "UL8" ], "offsets": [ [ 71, 74 ] ], "normalized": [] }, { "id": "BioInfer.d769.s0.e3", "type": "Gene/protein/RNA", "text": [ "UL52" ], "offsets": [ [ 85, 89 ] ], "normalized": [] } ]
[]
[]
[]
843
BioInfer.d769.s1
[ { "id": "BioInfer.d769.s1__text", "type": "Sentence", "text": [ "Various immunological assays suggest that four of these proteins (UL5, UL8, UL9, and UL52) are made in infected cells in very low abundance relative to the other three." ], "offsets": [ [ 0, 168 ] ] } ]
[ { "id": "BioInfer.d769.s1.e0", "type": "Gene/protein/RNA", "text": [ "UL52" ], "offsets": [ [ 85, 89 ] ], "normalized": [] }, { "id": "BioInfer.d769.s1.e1", "type": "Gene/protein/RNA", "text": [ "UL8" ], "offsets": [ [ 71, 74 ] ], "normalized": [] }, { "id": "BioInfer.d769.s1.e2", "type": "Gene/protein/RNA", "text": [ "UL9" ], "offsets": [ [ 76, 79 ] ], "normalized": [] }, { "id": "BioInfer.d769.s1.e3", "type": "Gene/protein/RNA", "text": [ "UL5" ], "offsets": [ [ 66, 69 ] ], "normalized": [] } ]
[]
[]
[]
844
BioInfer.d772.s0
[ { "id": "BioInfer.d772.s0__text", "type": "Sentence", "text": [ "Transcriptional expression of TNFR1(p55), as well as that of FLICE, Fas, FADD, DR3, FAF, TRADD, and RIP was similar in these cell lines, indicating that the susceptibility to TNFalpha-induced apoptosis may not be determined by the constitutive expression level of these factors." ], "offsets": [ [ 0, 278 ] ] } ]
[ { "id": "BioInfer.d772.s0.e0", "type": "Individual_protein", "text": [ "FLICE" ], "offsets": [ [ 61, 66 ] ], "normalized": [] }, { "id": "BioInfer.d772.s0.e1", "type": "Individual_protein", "text": [ "TRADD" ], "offsets": [ [ 89, 94 ] ], "normalized": [] }, { "id": "BioInfer.d772.s0.e2", "type": "Individual_protein", "text": [ "FADD" ], "offsets": [ [ 73, 77 ] ], "normalized": [] }, { "id": "BioInfer.d772.s0.e3", "type": "Individual_protein", "text": [ "TNFalpha" ], "offsets": [ [ 175, 183 ] ], "normalized": [] }, { "id": "BioInfer.d772.s0.e4", "type": "Individual_protein", "text": [ "FAF" ], "offsets": [ [ 84, 87 ] ], "normalized": [] }, { "id": "BioInfer.d772.s0.e5", "type": "Individual_protein", "text": [ "TNFR1" ], "offsets": [ [ 30, 35 ] ], "normalized": [] }, { "id": "BioInfer.d772.s0.e6", "type": "Individual_protein", "text": [ "DR3" ], "offsets": [ [ 79, 82 ] ], "normalized": [] }, { "id": "BioInfer.d772.s0.e7", "type": "Individual_protein", "text": [ "Fas" ], "offsets": [ [ 68, 71 ] ], "normalized": [] }, { "id": "BioInfer.d772.s0.e8", "type": "Individual_protein", "text": [ "p55" ], "offsets": [ [ 36, 39 ] ], "normalized": [] }, { "id": "BioInfer.d772.s0.e9", "type": "Individual_protein", "text": [ "RIP" ], "offsets": [ [ 100, 103 ] ], "normalized": [] } ]
[]
[]
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845
BioInfer.d773.s0
[ { "id": "BioInfer.d773.s0__text", "type": "Sentence", "text": [ "Transcriptional regulation in the galactose regulon of yeast is determined by an interplay between a positive regulatory protein, GAL4, and a negative regulatory protein, GAL80." ], "offsets": [ [ 0, 177 ] ] } ]
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[]
[]
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846
BioInfer.d774.s0
[ { "id": "BioInfer.d774.s0__text", "type": "Sentence", "text": [ "Transfection of alpha-catenin-deficient colon carcinoma cells recruited E-cadherin and beta-catenin to cell-cell contacts and functional cadherin-mediated cell-cell adhesion was restored in this way." ], "offsets": [ [ 0, 199 ] ] } ]
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[]
[]
[]
847
BioInfer.d776.s0
[ { "id": "BioInfer.d776.s0__text", "type": "Sentence", "text": [ "Treatment of cells with gamma linolenic acid (GLA) increased alpha catenin expression in most cell lines, while beta catenin levels were reduced, and gamma catenin expression was unchanged." ], "offsets": [ [ 0, 189 ] ] } ]
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[]
[]
[]
848
BioInfer.d777.s0
[ { "id": "BioInfer.d777.s0__text", "type": "Sentence", "text": [ "Treatment with HNE resulted in activation of extracellular signal-regulated protein kinases ERK1 and ERK2, induction of c-fos and c-jun protein expression, and an increase in transcription factor AP-1 DNA binding activity." ], "offsets": [ [ 0, 222 ] ] } ]
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[]
[]
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849
BioInfer.d779.s0
[ { "id": "BioInfer.d779.s0__text", "type": "Sentence", "text": [ "Two cDNAs, isolated from a Xenopus laevis embryonic library, encode proteins of 168 amino acids, both of which are 77% identical to chick cofilin and 66% identical to chick actin-depolymerizing factor (ADF), two structurally and functionally related proteins." ], "offsets": [ [ 0, 259 ] ] } ]
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[]
[]
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850
BioInfer.d781.s0
[ { "id": "BioInfer.d781.s0__text", "type": "Sentence", "text": [ "Under all conditions, platelets retained 40-50% of their total actin and greater than 70% of their actin-binding protein (ABP) but lost greater than 80% of talin and myosin to the supernatant." ], "offsets": [ [ 0, 192 ] ] } ]
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[]
[]
[]
851
BioInfer.d782.s0
[ { "id": "BioInfer.d782.s0__text", "type": "Sentence", "text": [ "Unexpectedly, treatment with the actin-depolymerizing drug latrunculin-A disrupted the medial region targeting pattern, and cells deficient in the actin-binding proteins tropomyosin and profilin also did not exhibit medial GFP-Cdc42p staining." ], "offsets": [ [ 0, 243 ] ] } ]
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[]
[]
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852
BioInfer.d783.s0
[ { "id": "BioInfer.d783.s0__text", "type": "Sentence", "text": [ "Unlike fimbrin, L-plastin's actin-bundling action was strictly calcium-dependent: the bundles were formed at pCa 7, but not at pCa 6." ], "offsets": [ [ 0, 133 ] ] } ]
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[]
[]
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853
BioInfer.d784.s0
[ { "id": "BioInfer.d784.s0__text", "type": "Sentence", "text": [ "Unmasking of this site serves as a molecular switch that initiates assembly of an actin-based motility complex containing VASP and profilin." ], "offsets": [ [ 0, 140 ] ] } ]
[ { "id": "BioInfer.d784.s0.e0", "type": "Individual_protein", "text": [ "VASP" ], "offsets": [ [ 122, 126 ] ], "normalized": [] }, { "id": "BioInfer.d784.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 82, 87 ] ], "normalized": [] }, { "id": "BioInfer.d784.s0.e2", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 131, 139 ] ], "normalized": [] } ]
[]
[]
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854
BioInfer.d786.s0
[ { "id": "BioInfer.d786.s0__text", "type": "Sentence", "text": [ "Using a complementary sequence or antipeptide to selectively neutralize the stretch of residues 633-642 of skeletal myosin heavy chain, we recently demonstrated that this segment is an actin binding site operating in the absence as in the presence of nucleotide and that this stretch 633-642 is not part of the nucleotide binding site [Chaussepied & Morales (1988) Proc. Natl. Acad. Sci. U.S.A. 85, 7471-7475]." ], "offsets": [ [ 0, 410 ] ] } ]
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[]
[]
[ { "id": "BioInfer.d786.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d786.s0.e0", "arg2_id": "BioInfer.d786.s0.e1", "normalized": [] } ]
855
BioInfer.d787.s0
[ { "id": "BioInfer.d787.s0__text", "type": "Sentence", "text": [ "Using ITP (a substrate for myosin II ATPase) and/or ATP gamma S (a substrate for myosin II heavy-chain kinase [MHCK]), we demonstrated that phosphorylation of myosin heavy chains occurred at the foci within the actin network, a result that suggests that MHCK was localized at the foci." ], "offsets": [ [ 0, 285 ] ] } ]
[ { "id": "BioInfer.d787.s0.e0", "type": "Individual_protein", "text": [ "MHCK" ], "offsets": [ [ 111, 115 ] ], "normalized": [] }, { "id": "BioInfer.d787.s0.e1", "type": "Protein_family_or_group", "text": [ "ATPase" ], "offsets": [ [ 37, 43 ] ], "normalized": [] }, { "id": "BioInfer.d787.s0.e2", "type": "Individual_protein", "text": [ "myosin II" ], "offsets": [ [ 27, 36 ] ], "normalized": [] }, { "id": "BioInfer.d787.s0.e3", "type": "Individual_protein", "text": [ "MHCK" ], "offsets": [ [ 254, 258 ] ], "normalized": [] }, { "id": "BioInfer.d787.s0.e4", "type": "Individual_protein", "text": [ "myosin II heavy-chain kinase" ], "offsets": [ [ 81, 109 ] ], "normalized": [] }, { "id": "BioInfer.d787.s0.e5", "type": "Individual_protein", "text": [ "myosin heavy chains" ], "offsets": [ [ 159, 178 ] ], "normalized": [] }, { "id": "BioInfer.d787.s0.e6", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 211, 216 ] ], "normalized": [] } ]
[]
[]
[ { "id": "BioInfer.d787.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d787.s0.e1", "arg2_id": "BioInfer.d787.s0.e2", "normalized": [] } ]
856
BioInfer.d788.s0
[ { "id": "BioInfer.d788.s0__text", "type": "Sentence", "text": [ "Using the known three-dimensional structure of the homologous actin-binding domain of fimbrin, these results have enabled us to determine the likely orientation of the utrophin actin-binding domain with respect to the actin filament." ], "offsets": [ [ 0, 233 ] ] } ]
[ { "id": "BioInfer.d788.s0.e0", "type": "Individual_protein", "text": [ "utrophin" ], "offsets": [ [ 168, 176 ] ], "normalized": [] }, { "id": "BioInfer.d788.s0.e1", "type": "Individual_protein", "text": [ "fimbrin" ], "offsets": [ [ 86, 93 ] ], "normalized": [] }, { "id": "BioInfer.d788.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 218, 223 ] ], "normalized": [] }, { "id": "BioInfer.d788.s0.e3", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 177, 182 ] ], "normalized": [] }, { "id": "BioInfer.d788.s0.e4", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 62, 67 ] ], "normalized": [] } ]
[]
[]
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857
BioInfer.d789.s0
[ { "id": "BioInfer.d789.s0__text", "type": "Sentence", "text": [ "Using the 'nuclear displacement assay' as a measure of the integrity of the actin cytoskeleton in living stamen hair cells, we demonstrated that AtFim1 protects actin filaments in these cells from Z. mays profilin (ZmPRO5)-induced depolymerization, in a dose-dependent manner." ], "offsets": [ [ 0, 276 ] ] } ]
[ { "id": "BioInfer.d789.s0.e0", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 205, 213 ] ], "normalized": [] }, { "id": "BioInfer.d789.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 161, 166 ] ], "normalized": [] }, { "id": "BioInfer.d789.s0.e2", "type": "Individual_protein", "text": [ "AtFim1" ], "offsets": [ [ 145, 151 ] ], "normalized": [] }, { "id": "BioInfer.d789.s0.e3", "type": "Individual_protein", "text": [ "ZmPRO5" ], "offsets": [ [ 215, 221 ] ], "normalized": [] }, { "id": "BioInfer.d789.s0.e4", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 76, 81 ] ], "normalized": [] } ]
[]
[]
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858
BioInfer.d790.s0
[ { "id": "BioInfer.d790.s0__text", "type": "Sentence", "text": [ "Using these methods, we confirm previous reports that intact talin induces cross-linking as well as filament shortening on actin networks." ], "offsets": [ [ 0, 138 ] ] } ]
[ { "id": "BioInfer.d790.s0.e0", "type": "Individual_protein", "text": [ "talin" ], "offsets": [ [ 61, 66 ] ], "normalized": [] }, { "id": "BioInfer.d790.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 123, 128 ] ], "normalized": [] } ]
[]
[]
[ { "id": "BioInfer.d790.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d790.s0.e0", "arg2_id": "BioInfer.d790.s0.e1", "normalized": [] } ]
859
BioInfer.d791.s0
[ { "id": "BioInfer.d791.s0__text", "type": "Sentence", "text": [ "Vascular endothelial cadherin (VE-cadherin) clusters were co-localized with beta-catenin, an important signal transduction ligand, and with alpha-catenin, which is thought to link the complex to the peri-junctional actin." ], "offsets": [ [ 0, 221 ] ] } ]
[ { "id": "BioInfer.d791.s0.e0", "type": "Individual_protein", "text": [ "VE-cadherin" ], "offsets": [ [ 31, 42 ] ], "normalized": [] }, { "id": "BioInfer.d791.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 215, 220 ] ], "normalized": [] }, { "id": "BioInfer.d791.s0.e2", "type": "Individual_protein", "text": [ "Vascular endothelial cadherin" ], "offsets": [ [ 0, 29 ] ], "normalized": [] }, { "id": "BioInfer.d791.s0.e3", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 140, 153 ] ], "normalized": [] }, { "id": "BioInfer.d791.s0.e4", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 76, 88 ] ], "normalized": [] } ]
[]
[]
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860
BioInfer.d792.s0
[ { "id": "BioInfer.d792.s0__text", "type": "Sentence", "text": [ "VASP, in turn, provides the ABM-2 sequences [XPPPPP, X = G, P, L, S, A] for binding profilin, an actin-regulatory protein that stimulates actin filament assembly." ], "offsets": [ [ 0, 162 ] ] } ]
[ { "id": "BioInfer.d792.s0.e0", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 84, 92 ] ], "normalized": [] }, { "id": "BioInfer.d792.s0.e1", "type": "Individual_protein", "text": [ "VASP" ], "offsets": [ [ 0, 4 ] ], "normalized": [] }, { "id": "BioInfer.d792.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 97, 102 ] ], "normalized": [] }, { "id": "BioInfer.d792.s0.e3", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 138, 143 ] ], "normalized": [] } ]
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861
BioInfer.d793.s0
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862
BioInfer.d795.s0
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863
BioInfer.d796.s0
[ { "id": "BioInfer.d796.s0__text", "type": "Sentence", "text": [ "We also analysed NHEJ in other DNA damage response mutants and showed that the checkpoint mutant rad3-d and two recombination mutants defective in rhp51 and rhp54 (homologues of S.cerevisiae RAD51 and RAD54, respectively) are not affected." ], "offsets": [ [ 0, 239 ] ] } ]
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864
BioInfer.d797.s0
[ { "id": "BioInfer.d797.s0__text", "type": "Sentence", "text": [ "We believe that this complex may mediate the cortical functions of profilin at actin patches in S. pombe." ], "offsets": [ [ 0, 105 ] ] } ]
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865
BioInfer.d799.s0
[ { "id": "BioInfer.d799.s0__text", "type": "Sentence", "text": [ "We constructed recombinant viruses based on the herpes simplex virus type 1 mutant tsK which individually were able to express the products of four viral DNA replication genes (UL5, UL8, UL9 and UL52) in the absence of any of the other proteins required for viral DNA synthesis." ], "offsets": [ [ 0, 278 ] ] } ]
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[]
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866
BioInfer.d800.s0
[ { "id": "BioInfer.d800.s0__text", "type": "Sentence", "text": [ "We describe the localization of cadherin-11 and N-cadherin along the cell margins of mouse osteoblast-like cells, the colocalization of \"pancadherin\" with alpha-catenin, beta-catenin, p120, and vinculin, and the association of these complexes with the actin microfilaments." ], "offsets": [ [ 0, 273 ] ] } ]
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867
BioInfer.d801.s0
[ { "id": "BioInfer.d801.s0__text", "type": "Sentence", "text": [ "We determined whether short-term weight-lifting exercise increases the synthesis rate of the major contractile proteins, myosin heavy chain (MHC), actin, and mixed muscle proteins in nonfrail elders and younger women and men." ], "offsets": [ [ 0, 225 ] ] } ]
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868
BioInfer.d802.s0
[ { "id": "BioInfer.d802.s0__text", "type": "Sentence", "text": [ "We examined whether levels of alpha-smooth-muscle actin or proliferating cell nuclear antigen correlated with myosin heavy-chain levels in the glomeruli of rats with puromycin aminonucleoside nephrosis." ], "offsets": [ [ 0, 202 ] ] } ]
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869
BioInfer.d803.s0
[ { "id": "BioInfer.d803.s0__text", "type": "Sentence", "text": [ "We find that profilin and cofilin regulate actin-filament formation throughout the cell cortex." ], "offsets": [ [ 0, 95 ] ] } ]
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[]
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870
BioInfer.d804.s0
[ { "id": "BioInfer.d804.s0__text", "type": "Sentence", "text": [ "We find that profilin contributes in several ways to Cdc42-induced nucleation of actin filaments in high speed supernatant of lysed neutrophils." ], "offsets": [ [ 0, 144 ] ] } ]
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[]
[]
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871
BioInfer.d805.s0
[ { "id": "BioInfer.d805.s0__text", "type": "Sentence", "text": [ "We found normal levels of alpha-catenin and beta-catenin in BT549 and HS578t cells; however, low levels of plakoglobin were expressed in these cells compared to those found in weakly invasive MCF-7 cells." ], "offsets": [ [ 0, 204 ] ] } ]
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[]
[]
[]
872
BioInfer.d807.s0
[ { "id": "BioInfer.d807.s0__text", "type": "Sentence", "text": [ "We have analyzed the expression levels of the genes encoding alpha-catenin, beta-catenin and plakoglobin in correlation to the E-cadherin expression levels in cell lines derived from human cervical carcinomas." ], "offsets": [ [ 0, 209 ] ] } ]
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[]
[]
[]
873
BioInfer.d809.s0
[ { "id": "BioInfer.d809.s0__text", "type": "Sentence", "text": [ "We have characterized this actin with respect to its ability to interact with yeast profilin and tropomyosin, the only yeast actin-binding proteins so far purified and characterized." ], "offsets": [ [ 0, 182 ] ] } ]
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[]
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874
BioInfer.d809.s1
[ { "id": "BioInfer.d809.s1__text", "type": "Sentence", "text": [ "Yeast profilin can sequester yeast actin monomers and thereby reduce the ability of yeast actin to polymerize, whereas it has little effect on the degree of polymerization of rabbit skeletal muscle actin." ], "offsets": [ [ 0, 204 ] ] } ]
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875
BioInfer.d810.s0
[ { "id": "BioInfer.d810.s0__text", "type": "Sentence", "text": [ "We have cloned a Saccharomyces cerevisiae gene (COF1) encoding a low-M(r) actin-binding protein of 143 amino acid (aa) residues (yeast cofilin; Cof); its aa sequence is 35% identical to porcine Cof." ], "offsets": [ [ 0, 198 ] ] } ]
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[]
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876
BioInfer.d812.s0
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[]
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877
BioInfer.d813.s0
[ { "id": "BioInfer.d813.s0__text", "type": "Sentence", "text": [ "We have found that cofilin, a 21-kDa actin-binding protein, is a component of these rods." ], "offsets": [ [ 0, 89 ] ] } ]
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[]
[]
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878
BioInfer.d814.s0
[ { "id": "BioInfer.d814.s0__text", "type": "Sentence", "text": [ "We have shown that the FH proteins Bni1p and Bnr1p are potential targets of the Rho family small GTP-binding proteins and bind to an actin-binding protein, profilin, at their proline-rich FH1 domains to regulate reorganization of the actin cytoskeleton in the yeast Saccharomyces cerevisiae." ], "offsets": [ [ 0, 291 ] ] } ]
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[]
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879
BioInfer.d815.s0
[ { "id": "BioInfer.d815.s0__text", "type": "Sentence", "text": [ "We have shown that these proteins are indeed nuclear basic proteins: the 14 kd is the histone H4, the 19 kd is the histone H3, and the 25 kd is the sperm-specific protein SP2." ], "offsets": [ [ 0, 175 ] ] } ]
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[]
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880
BioInfer.d817.s0
[ { "id": "BioInfer.d817.s0__text", "type": "Sentence", "text": [ "We previously showed that actin is transported in an unassembled form with its associated proteins actin depolymerizing factor, cofilin, and profilin." ], "offsets": [ [ 0, 150 ] ] } ]
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[]
[]
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881
BioInfer.d819.s0
[ { "id": "BioInfer.d819.s0__text", "type": "Sentence", "text": [ "We report here that tropomyosin, which is found in the rootlet but not in the microvillus core, can bind to and saturate the actin of isolated cores, and can cause the dissociation of up to 30% of the villin and fimbrin from the cores but does not affect actin binding by 110-kD calmodulin." ], "offsets": [ [ 0, 290 ] ] } ]
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[]
[]
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882
BioInfer.d821.s0
[ { "id": "BioInfer.d821.s0__text", "type": "Sentence", "text": [ "We show that the HSV-1 UL5, UL8, UL29, UL30, UL42, and UL52 gene products along with the AAV Rep68 protein are sufficient to initiate replication on duplex DNA containing the AAV origins of replication, resulting in products several hundred nucleotides in length." ], "offsets": [ [ 0, 263 ] ] } ]
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[]
[]
[]
883
BioInfer.d822.s0
[ { "id": "BioInfer.d822.s0__text", "type": "Sentence", "text": [ "We speculate that fimbrin may help maintain the parallel growth of actin filaments within the stereocilia." ], "offsets": [ [ 0, 106 ] ] } ]
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[]
[]
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884
BioInfer.d823.s0
[ { "id": "BioInfer.d823.s0__text", "type": "Sentence", "text": [ "Western analysis of gel-purified USF-nucleosome and GAL4-AH-nucleosome complexes demonstrated the predominant presence of acetylated histone H4 relative to acetylated histone H3." ], "offsets": [ [ 0, 178 ] ] } ]
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[]
[]
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885
BioInfer.d827.s0
[ { "id": "BioInfer.d827.s0__text", "type": "Sentence", "text": [ "We then compared colorectal cancers with 'mild' RER (n = 15), and those with 'severe' RER without (n = 11) or with (n = 22) detectable mutations in MSH2 or MLH1 to assess the involvement of mononucleotide repeats contained in the coding regions of MSH3, MSH6, BAX, and TGFbeta RII." ], "offsets": [ [ 0, 281 ] ] } ]
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[]
[]
[]
886
BioInfer.d828.s0
[ { "id": "BioInfer.d828.s0__text", "type": "Sentence", "text": [ "We used yeast as a model to test this hypothesis and found that chromosome deletion of any known nuclear mitotic mismatch repair genes, including MLH1, MSH2, MSH3, MSH6, and PMS1, did not rescue mgt1delta O6 MeG DNA repair methyltransferase-deficient cells from killing by MNNG." ], "offsets": [ [ 0, 278 ] ] } ]
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[]
[]
[]
887
BioInfer.d829.s0
[ { "id": "BioInfer.d829.s0__text", "type": "Sentence", "text": [ "When a lyophilized Mf and AO mixture was incubated at 40 degrees C and 65% relative humidity, the conjugation of AO was confirmed at myosin heavy chain, actin, and tropomyosin." ], "offsets": [ [ 0, 176 ] ] } ]
[ { "id": "BioInfer.d829.s0.e0", "type": "Gene/protein/RNA", "text": [ "tropomyosin" ], "offsets": [ [ 164, 175 ] ], "normalized": [] }, { "id": "BioInfer.d829.s0.e1", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 153, 158 ] ], "normalized": [] }, { "id": "BioInfer.d829.s0.e2", "type": "Gene/protein/RNA", "text": [ "myosin heavy chain" ], "offsets": [ [ 133, 151 ] ], "normalized": [] } ]
[]
[]
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888
BioInfer.d830.s0
[ { "id": "BioInfer.d830.s0__text", "type": "Sentence", "text": [ "When the actin monomer pool in untransfected myoblasts is increased 70% by treatment with latrunculin A, synthesis of ADF and actin are down-regulated compared with cofilin and 19 other proteins selected at random." ], "offsets": [ [ 0, 214 ] ] } ]
[ { "id": "BioInfer.d830.s0.e0", "type": "Gene/protein/RNA", "text": [ "ADF" ], "offsets": [ [ 118, 121 ] ], "normalized": [] }, { "id": "BioInfer.d830.s0.e1", "type": "Gene/protein/RNA", "text": [ "cofilin" ], "offsets": [ [ 165, 172 ] ], "normalized": [] }, { "id": "BioInfer.d830.s0.e2", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 9, 14 ] ], "normalized": [] }, { "id": "BioInfer.d830.s0.e3", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 126, 131 ] ], "normalized": [] } ]
[]
[]
[]
889
BioInfer.d831.s0
[ { "id": "BioInfer.d831.s0__text", "type": "Sentence", "text": [ "While levels of most of these proteins decrease, accumulation of cyclin D1 and the cyclin-dependent kinase inhibitor p21 Cip1/WAF1 is observed." ], "offsets": [ [ 0, 143 ] ] } ]
[ { "id": "BioInfer.d831.s0.e0", "type": "Individual_protein", "text": [ "WAF1" ], "offsets": [ [ 126, 130 ] ], "normalized": [] }, { "id": "BioInfer.d831.s0.e1", "type": "Individual_protein", "text": [ "p21" ], "offsets": [ [ 117, 120 ] ], "normalized": [] }, { "id": "BioInfer.d831.s0.e2", "type": "Gene/protein/RNA", "text": [ "cyclin D1" ], "offsets": [ [ 65, 74 ] ], "normalized": [] }, { "id": "BioInfer.d831.s0.e3", "type": "Protein_family_or_group", "text": [ "cyclin-dependent kinase inhibitor" ], "offsets": [ [ 83, 116 ] ], "normalized": [] }, { "id": "BioInfer.d831.s0.e4", "type": "Individual_protein", "text": [ "Cip1" ], "offsets": [ [ 121, 125 ] ], "normalized": [] } ]
[]
[]
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890
BioInfer.d832.s0
[ { "id": "BioInfer.d832.s0__text", "type": "Sentence", "text": [ "While poly(ADP-ribose) effectively competed with DNA for binding of histone H4, it equally competed with DNA for binding of histone H3 and only inefficiently competed with DNA for binding of histone H1." ], "offsets": [ [ 0, 202 ] ] } ]
[ { "id": "BioInfer.d832.s0.e0", "type": "Protein_family_or_group", "text": [ "histone" ], "offsets": [ [ 124, 131 ] ], "normalized": [] }, { "id": "BioInfer.d832.s0.e1", "type": "Individual_protein", "text": [ "H3" ], "offsets": [ [ 132, 134 ] ], "normalized": [] }, { "id": "BioInfer.d832.s0.e2", "type": "Protein_family_or_group", "text": [ "histone" ], "offsets": [ [ 191, 198 ] ], "normalized": [] }, { "id": "BioInfer.d832.s0.e3", "type": "Protein_family_or_group", "text": [ "histone" ], "offsets": [ [ 68, 75 ] ], "normalized": [] }, { "id": "BioInfer.d832.s0.e4", "type": "Individual_protein", "text": [ "H4" ], "offsets": [ [ 76, 78 ] ], "normalized": [] }, { "id": "BioInfer.d832.s0.e5", "type": "Individual_protein", "text": [ "H1" ], "offsets": [ [ 199, 201 ] ], "normalized": [] } ]
[]
[]
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891
BioInfer.d833.s0
[ { "id": "BioInfer.d833.s0__text", "type": "Sentence", "text": [ "Within 1 hour of raising the concentration of calcium ions, integrins, cadherins, alpha-catenin, beta-catenin, plakoglobin, vinculin and alpha-actinin appeared to accumulate at cell-cell borders, whereas the focal contact proteins, paxillin and talin, did not." ], "offsets": [ [ 0, 260 ] ] } ]
[ { "id": "BioInfer.d833.s0.e0", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 97, 109 ] ], "normalized": [] }, { "id": "BioInfer.d833.s0.e1", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 82, 95 ] ], "normalized": [] }, { "id": "BioInfer.d833.s0.e2", "type": "Individual_protein", "text": [ "paxillin" ], "offsets": [ [ 232, 240 ] ], "normalized": [] }, { "id": "BioInfer.d833.s0.e3", "type": "Individual_protein", "text": [ "talin" ], "offsets": [ [ 245, 250 ] ], "normalized": [] }, { "id": "BioInfer.d833.s0.e4", "type": "Individual_protein", "text": [ "plakoglobin" ], "offsets": [ [ 111, 122 ] ], "normalized": [] }, { "id": "BioInfer.d833.s0.e5", "type": "Individual_protein", "text": [ "alpha-actinin" ], "offsets": [ [ 137, 150 ] ], "normalized": [] }, { "id": "BioInfer.d833.s0.e6", "type": "Individual_protein", "text": [ "vinculin" ], "offsets": [ [ 124, 132 ] ], "normalized": [] }, { "id": "BioInfer.d833.s0.e7", "type": "Individual_protein", "text": [ "cadherins" ], "offsets": [ [ 71, 80 ] ], "normalized": [] }, { "id": "BioInfer.d833.s0.e8", "type": "Individual_protein", "text": [ "integrins" ], "offsets": [ [ 60, 69 ] ], "normalized": [] } ]
[]
[]
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892
BioInfer.d834.s0
[ { "id": "BioInfer.d834.s0__text", "type": "Sentence", "text": [ "Within the sieve-tube exudate, profilin was present in 15-fold molar excess to actin." ], "offsets": [ [ 0, 85 ] ] } ]
[ { "id": "BioInfer.d834.s0.e0", "type": "Gene/protein/RNA", "text": [ "profilin" ], "offsets": [ [ 31, 39 ] ], "normalized": [] }, { "id": "BioInfer.d834.s0.e1", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 79, 84 ] ], "normalized": [] } ]
[]
[]
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893
BioInfer.d835.s0
[ { "id": "BioInfer.d835.s0__text", "type": "Sentence", "text": [ "YACs containing color vision red pigment gene DNA or 1.5 rDNA tandem repeat units were transformed into hosts bearing lesions at the RAD1, RAD6, RAD51, or RAD52 loci." ], "offsets": [ [ 0, 166 ] ] } ]
[ { "id": "BioInfer.d835.s0.e0", "type": "Gene/protein/RNA", "text": [ "RAD52" ], "offsets": [ [ 155, 160 ] ], "normalized": [] }, { "id": "BioInfer.d835.s0.e1", "type": "Gene/protein/RNA", "text": [ "color vision red pigment" ], "offsets": [ [ 16, 40 ] ], "normalized": [] }, { "id": "BioInfer.d835.s0.e2", "type": "Gene/protein/RNA", "text": [ "RAD6" ], "offsets": [ [ 139, 143 ] ], "normalized": [] }, { "id": "BioInfer.d835.s0.e3", "type": "Gene/protein/RNA", "text": [ "RAD51" ], "offsets": [ [ 145, 150 ] ], "normalized": [] }, { "id": "BioInfer.d835.s0.e4", "type": "Gene/protein/RNA", "text": [ "RAD1" ], "offsets": [ [ 133, 137 ] ], "normalized": [] } ]
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