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1.0alpha7.train.274
4115477
[ { "id": "1.0alpha7.train.274.sent", "type": "sentence", "text": [ "This model is supported by the inhibition of dynein-mediated transport by p50(dynamitin) expression ( 20, 28, 29), which dissociates the dynactin complex and separates the dynein binding subunit ( p150 Glued) from membrane binding subunits ( 30, 31)." ], "offsets": [ [ 0, 250 ] ] } ]
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[]
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1.0alpha7.train.275
20230417
[ { "id": "1.0alpha7.train.275.sent", "type": "sentence", "text": [ "LZ and PNT both directly bind to the pros promoter/enhancer region and pros expression occurs only when PNT and LZ have bound simultaneously to the pros enhancer/promoter." ], "offsets": [ [ 0, 171 ] ] } ]
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[]
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1.0alpha7.train.276
4912938
[ { "id": "1.0alpha7.train.276.sent", "type": "sentence", "text": [ "HIP1 and HIP12 display differential binding to F-actin, AP2, and clathrin." ], "offsets": [ [ 0, 74 ] ] } ]
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[]
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1.0alpha7.train.277
2434981
[ { "id": "1.0alpha7.train.277.sent", "type": "sentence", "text": [ "In this study, we identified binding domains of GSK-3β and β-catenin in Axin." ], "offsets": [ [ 0, 77 ] ] } ]
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[]
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1.0alpha7.train.278
11107237
[ { "id": "1.0alpha7.train.278.sent", "type": "sentence", "text": [ "(A) Inhibition of BMP-7 binding to ROS 17/2." ], "offsets": [ [ 0, 44 ] ] } ]
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[]
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[]
1.0alpha7.train.279
15373484
[ { "id": "1.0alpha7.train.279.sent", "type": "sentence", "text": [ "To further investigate a possible role for ESEs in U2AF35-dependent splicing, an experiment was designed to test a critical tenet of the recruitment model for exon enhancer function: SR proteins bound to the enhancer sequence establish protein-protein interactions with U2AF35 that increase the local concentration of the U2AF heterodimer and facilitate U2AF65 binding to the Py tract (13)." ], "offsets": [ [ 0, 390 ] ] } ]
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[]
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1.0alpha7.train.280
19339178
[ { "id": "1.0alpha7.train.280.sent", "type": "sentence", "text": [ "Further indirect evidence for actin binding by HtsRC comes from cher mutants in which HtsRC is redirected to the actin-rich nurse-cell plasma membrane [15] ." ], "offsets": [ [ 0, 157 ] ] } ]
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[]
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1.0alpha7.train.281
6392213
[ { "id": "1.0alpha7.train.281.sent", "type": "sentence", "text": [ "Because Ubc9 binds such an NLS sequence, we propose three potential mechanisms for the role of Ubc9 in nuclear import." ], "offsets": [ [ 0, 118 ] ] } ]
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[]
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[]
1.0alpha7.train.282
23643688
[ { "id": "1.0alpha7.train.282.sent", "type": "sentence", "text": [ "As shown in Figure 7 A, deletion of these 35 amino acids results in the loss of binding between dSlo and PKAc." ], "offsets": [ [ 0, 110 ] ] } ]
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[]
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1.0alpha7.train.283
15370882
[ { "id": "1.0alpha7.train.283.sent", "type": "sentence", "text": [ "(B) Binding of a NES to CRM1 occurs in a tripartite complex with RanGTP." ], "offsets": [ [ 0, 72 ] ] } ]
[ { "id": "1.0alpha7.train.283.ent0_0", "type": "protein", "text": [ "CRM1" ], "offsets": [ [ 24, 28 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "7514" }, { "db_name": "hgnc", "db_id": "XPO1" }, { "db_name": "uniprot", "db_id": "O14980" } ] }, { "id": "1.0alpha7.train.283.ent1_0", "type": "protein", "text": [ "RanGTP" ], "offsets": [ [ 65, 71 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "5901" }, { "db_name": "hgnc", "db_id": "RAN" }, { "db_name": "uniprot", "db_id": "P62826" } ] }, { "id": "1.0alpha7.train.283.ent2_0", "type": "protein-motif", "text": [ "NES" ], "offsets": [ [ 17, 20 ] ], "normalized": [] } ]
[]
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[]
1.0alpha7.train.284
123458
[ { "id": "1.0alpha7.train.284.sent", "type": "sentence", "text": [ "For in vitro kinase assays, 15 μl of GST or GST-Cx43CT bound to glutathione-Sepharose 4B beads (washed once in kinase buffer) were incubated with purified kinase-active pp60 c-src, kinase buffer (20 mM HEPES (pH 7.4), 12 mM MnCl2, 1 mM dithothreitol, 100 μM Na2VO4) and 10 μCi of ATP (DuPont NEN, NEG-002Z, 6000 Ci/mmol) in a total volume of 40 μl for 15 min at room temperature." ], "offsets": [ [ 0, 379 ] ] } ]
[ { "id": "1.0alpha7.train.284.ent0_0", "type": "experiment-tag", "text": [ "GST" ], "offsets": [ [ 37, 40 ] ], "normalized": [ { "db_name": "intenz", "db_id": "2.5.1.18" } ] }, { "id": "1.0alpha7.train.284.ent1_1", "type": "experiment-tag", "text": [ "GST" ], "offsets": [ [ 44, 47 ] ], "normalized": [ { "db_name": "intenz", "db_id": "2.5.1.18" } ] }, { "id": "1.0alpha7.train.284.ent2_0", "type": "reagent", "text": [ "HEPES" ], "offsets": [ [ 202, 207 ] ], "normalized": [] }, { "id": "1.0alpha7.train.284.ent3_0", "type": "reagent", "text": [ "kinase-active pp60" ], "offsets": [ [ 155, 173 ] ], "normalized": [] }, { "id": "1.0alpha7.train.284.ent4_0", "type": "reagent", "text": [ "ATP" ], "offsets": [ [ 280, 283 ] ], "normalized": [] }, { "id": "1.0alpha7.train.284.ent5_0", "type": "experimental-construct", "text": [ "GST-Cx43CT" ], "offsets": [ [ 44, 54 ] ], "normalized": [] }, { "id": "1.0alpha7.train.284.ent6_0", "type": "reagent", "text": [ "glutathione-Sepharose 4B" ], "offsets": [ [ 64, 88 ] ], "normalized": [] } ]
[]
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[]
1.0alpha7.train.285
13126995
[ { "id": "1.0alpha7.train.285.sent", "type": "sentence", "text": [ "In the absence of calcium, TnI binding to actin holds the Tm-Tn complex in the \"`closed\"` state in which the myosin-binding site is occluded, preventing myosin from binding actin." ], "offsets": [ [ 0, 179 ] ] } ]
[ { "id": "1.0alpha7.train.285.ent0_0", "type": "chemical", "text": [ "calcium" ], "offsets": [ [ 18, 25 ] ], "normalized": [ { "db_name": "pubchem:compound", "db_id": "5460341" } ] }, { "id": "1.0alpha7.train.285.ent1_0", "type": "protein-complex", "text": [ "Tm-Tn" ], "offsets": [ [ 58, 63 ] ], "normalized": [] }, { "id": "1.0alpha7.train.285.ent2_0", "type": "protein-complex", "text": [ "myosin" ], "offsets": [ [ 109, 115 ] ], "normalized": [] }, { "id": "1.0alpha7.train.285.ent3_1", "type": "protein-complex", "text": [ "myosin" ], "offsets": [ [ 153, 159 ] ], "normalized": [] }, { "id": "1.0alpha7.train.285.ent4_0", "type": "protein", "text": [ "TnI" ], "offsets": [ [ 27, 30 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "7134" }, { "db_name": "hgnc", "db_id": "TNNC1" }, { "db_name": "uniprot", "db_id": "P63316" } ] }, { "id": "1.0alpha7.train.285.ent5_0", "type": "protein-family", "text": [ "actin" ], "offsets": [ [ 42, 47 ] ], "normalized": [ { "db_name": "pfam", "db_id": "PF00022" } ] }, { "id": "1.0alpha7.train.285.ent6_1", "type": "protein-family", "text": [ "actin" ], "offsets": [ [ 173, 178 ] ], "normalized": [ { "db_name": "pfam", "db_id": "PF00022" } ] } ]
[]
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1.0alpha7.train.286
16243889
[ { "id": "1.0alpha7.train.286.sent", "type": "sentence", "text": [ "The 2.8 angstrom crystal structure of ZAG resembles a class I major histocompatibility complex (MHC) heavy chain, but ZAG does not bind the class I light chain beta2-microglobulin. " ], "offsets": [ [ 0, 181 ] ] } ]
[ { "id": "1.0alpha7.train.286.ent0_0", "type": "protein", "text": [ "ZAG" ], "offsets": [ [ 38, 41 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "563" }, { "db_name": "hgnc", "db_id": "AZGP1" }, { "db_name": "uniprot", "db_id": "P25311" } ] }, { "id": "1.0alpha7.train.286.ent1_1", "type": "protein", "text": [ "ZAG" ], "offsets": [ [ 118, 121 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "563" }, { "db_name": "hgnc", "db_id": "AZGP1" }, { "db_name": "uniprot", "db_id": "P25311" } ] }, { "id": "1.0alpha7.train.286.ent2_0", "type": "protein", "text": [ "beta2-microglobulin" ], "offsets": [ [ 160, 179 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "567" }, { "db_name": "hgnc", "db_id": "B2M" }, { "db_name": "uniprot", "db_id": "P61769" } ] }, { "id": "1.0alpha7.train.286.ent3_0", "type": "protein-family", "text": [ "MHC" ], "offsets": [ [ 96, 99 ] ], "normalized": [] }, { "id": "1.0alpha7.train.286.ent4_0", "type": "protein-family", "text": [ "class I major histocompatibility complex" ], "offsets": [ [ 54, 94 ] ], "normalized": [] } ]
[]
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1.0alpha7.train.287
11474448
[ { "id": "1.0alpha7.train.287.sent", "type": "sentence", "text": [ " Precursor proteins that do not bind to MSF, or that bind preferentially to hsp70, bypass the Tom70-Tom37 complex and are targeted directly to Tom20-Tom22 (Hachiya et al., 1995 ). " ], "offsets": [ [ 0, 187 ] ] } ]
[ { "id": "1.0alpha7.train.287.ent0_0", "type": "protein-complex", "text": [ "Tom70-Tom37" ], "offsets": [ [ 97, 108 ] ], "normalized": [] }, { "id": "1.0alpha7.train.287.ent1_0", "type": "protein-complex", "text": [ "Tom20-Tom22" ], "offsets": [ [ 147, 158 ] ], "normalized": [] }, { "id": "1.0alpha7.train.287.ent2_0", "type": "protein", "text": [ "Tom70" ], "offsets": [ [ 97, 102 ] ], "normalized": [ { "db_name": "uniprot", "db_id": "P07213" } ] }, { "id": "1.0alpha7.train.287.ent3_0", "type": "protein-family", "text": [ "hsp70" ], "offsets": [ [ 78, 83 ] ], "normalized": [ { "db_name": "interpro", "db_id": "IPR013126" } ] }, { "id": "1.0alpha7.train.287.ent4_0", "type": "protein", "text": [ "MSF" ], "offsets": [ [ 41, 44 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "10801" }, { "db_name": "hgnc", "db_id": "SEPT9" }, { "db_name": "uniprot", "db_id": "Q9UHD8" } ] }, { "id": "1.0alpha7.train.287.ent5_0", "type": "protein", "text": [ "Tom20" ], "offsets": [ [ 147, 152 ] ], "normalized": [ { "db_name": "uniprot", "db_id": "P35180" } ] }, { "id": "1.0alpha7.train.287.ent6_0", "type": "protein", "text": [ "Tom22" ], "offsets": [ [ 153, 158 ] ], "normalized": [ { "db_name": "uniprot", "db_id": "P49334" } ] }, { "id": "1.0alpha7.train.287.ent7_0", "type": "protein", "text": [ "Tom37" ], "offsets": [ [ 103, 108 ] ], "normalized": [ { "db_name": "uniprot", "db_id": "P50110" } ] } ]
[]
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1.0alpha7.train.288
4211455
[ { "id": "1.0alpha7.train.288.sent", "type": "sentence", "text": [ "The Effect of dI2dIII1 Complex Formation on NADH Binding to dI" ], "offsets": [ [ 0, 62 ] ] } ]
[ { "id": "1.0alpha7.train.288.ent0_0", "type": "protein", "text": [ "dI" ], "offsets": [ [ 60, 62 ] ], "normalized": [] }, { "id": "1.0alpha7.train.288.ent1_0", "type": "chemical", "text": [ "NADH" ], "offsets": [ [ 44, 48 ] ], "normalized": [ { "db_name": "pubchem:compound", "db_id": "439153" } ] }, { "id": "1.0alpha7.train.288.ent2_0", "type": "protein-complex", "text": [ "dI2dIII1 Complex" ], "offsets": [ [ 14, 30 ] ], "normalized": [] } ]
[]
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1.0alpha7.train.290
16065821
[ { "id": "1.0alpha7.train.290.sent", "type": "sentence", "text": [ " As the binding of ORC and MCM proteins occurs at or very near the origin, we determined the genome-wide locations of ORC- and MCM-binding sites to identify the positions of potential DNA replication origins across the S. cerevisiae genome. " ], "offsets": [ [ 0, 248 ] ] } ]
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[]
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1.0alpha7.train.291
24668077
[ { "id": "1.0alpha7.train.291.sent", "type": "sentence", "text": [ " Moreover, the insulin-induced increase in GTP bound Rheb, but not that of Ras, is blocked by wortmannin, whereas both increases are resistant to rapamycin (Figure 2A). " ], "offsets": [ [ 0, 175 ] ] } ]
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[]
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1.0alpha7.train.292
19076092
[ { "id": "1.0alpha7.train.292.sent", "type": "sentence", "text": [ " CtBP binds with HPC2 and XPc through the same conserved amino acid motif, PI/LDL. " ], "offsets": [ [ 0, 86 ] ] } ]
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[]
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1.0alpha7.train.293
2028459
[ { "id": "1.0alpha7.train.293.sent", "type": "sentence", "text": [ " Mg2+ inhibited but did not abolish ATPgammaS binding to both synapsin C-domains, similar to its effect on GTP binding to Rab proteins (Fig. 1) ( 25). " ], "offsets": [ [ 0, 156 ] ] } ]
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[]
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1.0alpha7.train.294
15642360
[ { "id": "1.0alpha7.train.294.sent", "type": "sentence", "text": [ "We note that CKIɛ, CKI∂, and the kinase domain fragment of CKIɛ bound to mPER1 whereas CKIα2 did not, consistent with the mPER1 interaction taking place via the kinase domain and not via the carboxy-terminal regulatory domain." ], "offsets": [ [ 0, 226 ] ] } ]
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[]
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1.0alpha7.train.295
5336609
[ { "id": "1.0alpha7.train.295.sent", "type": "sentence", "text": [ " Combining GST-Smad-4 with the probe, however, produced two shifted bands, indicating that the Hex BRE binds purified Smad4 but not Smad1. " ], "offsets": [ [ 0, 144 ] ] } ]
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[]
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1.0alpha7.train.296
11772169
[ { "id": "1.0alpha7.train.296.sent", "type": "sentence", "text": [ "A third important feature of the mechanism of transcriptional activation is the synergy in binding between Sp1 and Smad2 (and to some extent Smad4)." ], "offsets": [ [ 0, 151 ] ] } ]
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[]
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1.0alpha7.train.297
676131
[ { "id": "1.0alpha7.train.297.sent", "type": "sentence", "text": [ " There is solid evidence that Mas70p is a component of the mitochondrial receptor machinery for protein import ( 46), and we asked if Mas70p would bind to hsp90. " ], "offsets": [ [ 0, 167 ] ] } ]
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[]
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1.0alpha7.train.298
933939
[ { "id": "1.0alpha7.train.298.sent", "type": "sentence", "text": [ " Previously, assay of the reduction in the EDTA-ATPase activity of S-1 in the supernatant when S-1.MgADP.Pi is cosedimented with actin has been used to measure the weak binding of myosin to actin ( 37). " ], "offsets": [ [ 0, 209 ] ] } ]
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[]
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1.0alpha7.train.299
22277185
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[]
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1.0alpha7.train.300
3654233
[ { "id": "1.0alpha7.train.300.sent", "type": "sentence", "text": [ "We showed previously that MEKK1 binds directly to JNK/SAPK." ], "offsets": [ [ 0, 61 ] ] } ]
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[]
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1.0alpha7.train.301
20457160
[ { "id": "1.0alpha7.train.301.sent", "type": "sentence", "text": [ "By extension of studies of the Rad3 ATPase (15), mutation of the conserved lysine residue in the Walker domain to alanine (K→A) in Rad54 is thought to prevent ATP binding, whereas mutation of lysine to arginine (K→R) is expected to prevent ATP hydrolysis but not ATP binding." ], "offsets": [ [ 0, 275 ] ] } ]
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[]
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1.0alpha7.train.302
15776300
[ { "id": "1.0alpha7.train.302.sent", "type": "sentence", "text": [ " Note that cyclin E binds to both forms of Cdk2, whereas cyclin A binds only the activated form of Cdk2. " ], "offsets": [ [ 0, 110 ] ] } ]
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[]
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1.0alpha7.train.303
1810686
[ { "id": "1.0alpha7.train.303.sent", "type": "sentence", "text": [ "Binding of GST537C and GST547C to hsp90 after their translation in reticulocyte lysate." ], "offsets": [ [ 0, 90 ] ] } ]
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[]
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1.0alpha7.train.304
18797540
[ { "id": "1.0alpha7.train.304.sent", "type": "sentence", "text": [ " Thus, for example, Hairy binds dCtBP strongly but hCtBP weakly, confirming the specificity of the binding sites. " ], "offsets": [ [ 0, 117 ] ] } ]
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[]
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1.0alpha7.train.305
1929398
[ { "id": "1.0alpha7.train.305.sent", "type": "sentence", "text": [ " To ascertain the binding affinity of Pitx2 for the bicoid element, an EMSA DNA titration experiment was performed. " ], "offsets": [ [ 0, 126 ] ] } ]
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[]
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1.0alpha7.train.306
11059909
[ { "id": "1.0alpha7.train.306.sent", "type": "sentence", "text": [ "Axin binds to not only GSK3 and DCAP but also Arrow/LRP5." ], "offsets": [ [ 0, 57 ] ] } ]
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1.0alpha7.train.307
13021306
[ { "id": "1.0alpha7.train.307.sent", "type": "sentence", "text": [ " W EN et al. 1995 ; P OTEET-SMITH et al. 1997 ), we conclude that PKAr* must bind PKAc to activate Hh target genes. " ], "offsets": [ [ 0, 127 ] ] } ]
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[]
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1.0alpha7.train.308
24638134
[ { "id": "1.0alpha7.train.308.sent", "type": "sentence", "text": [ "The CtBP structure reveals a bound acetate ion (right panel)." ], "offsets": [ [ 0, 62 ] ] } ]
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[]
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1.0alpha7.train.309
20295885
[ { "id": "1.0alpha7.train.309.sent", "type": "sentence", "text": [ " We propose that this is where CstF-64 binds to CstF-77, and this is supported by in vitro experiments with the human protein (Y.Takagaki and J.L.Manley, submitted). " ], "offsets": [ [ 0, 171 ] ] } ]
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[]
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1.0alpha7.train.310
14471508
[ { "id": "1.0alpha7.train.310.sent", "type": "sentence", "text": [ " From these results, we can reasonably conclude that IntI1 bound both ds and ss attI but that only ss attC was efficiently bound by IntI1 in vitro. " ], "offsets": [ [ 0, 151 ] ] } ]
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[]
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1.0alpha7.train.311
4519188
[ { "id": "1.0alpha7.train.311.sent", "type": "sentence", "text": [ "Our observation that binding of eIF4A to eIF4G is cooperative could explain these results by ensuring a higher affinity interaction between eIF4G and eIF4A." ], "offsets": [ [ 0, 160 ] ] } ]
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[]
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1.0alpha7.train.312
18356833
[ { "id": "1.0alpha7.train.312.sent", "type": "sentence", "text": [ "This inhibition is mediated through the Pnt domain-dependent binding of Mae to Yan (compare lanes 7 and 10)." ], "offsets": [ [ 0, 111 ] ] } ]
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[]
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1.0alpha7.train.313
15500140
[ { "id": "1.0alpha7.train.313.sent", "type": "sentence", "text": [ " However, it remained to be shown whether Aos binds directly to DER. " ], "offsets": [ [ 0, 72 ] ] } ]
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[]
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1.0alpha7.train.314
8951536
[ { "id": "1.0alpha7.train.314.sent", "type": "sentence", "text": [ " Deletion mutagenesis also indicated that Leu-20, Phe-25, and Glu-70 in dTAFII230 are important for TBP binding and inhibition of TBP-promoter interaction. " ], "offsets": [ [ 0, 163 ] ] } ]
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[]
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1.0alpha7.train.315
15791822
[ { "id": "1.0alpha7.train.315.sent", "type": "sentence", "text": [ "That occupation of the ATP/ADP binding pocket of Hsp90 by GA results in dissociation of the protein from Raf-1 is consistent with the notion that alternating cycles of ATP and ADP binding regulate Hsp90 conformation and, in turn, its ability to mediate the formation of productive signaling heterocomplexes (7, 22, 55, 72)." ], "offsets": [ [ 0, 323 ] ] } ]
[ { "id": "1.0alpha7.train.315.ent0_0", "type": "chemical", "text": [ "ATP" ], "offsets": [ [ 23, 26 ] ], "normalized": [ { "db_name": "pubchem:compound", "db_id": "5957" } ] }, { "id": "1.0alpha7.train.315.ent1_1", "type": "chemical", "text": [ "ATP" ], "offsets": [ [ 168, 171 ] ], "normalized": [ { "db_name": "pubchem:compound", "db_id": "5957" } ] }, { "id": "1.0alpha7.train.315.ent2_0", "type": "chemical", "text": [ "ADP" ], "offsets": [ [ 27, 30 ] ], "normalized": [ { "db_name": "pubchem:compound", "db_id": "6022" } ] }, { "id": "1.0alpha7.train.315.ent3_1", "type": "chemical", "text": [ "ADP" ], "offsets": [ [ 176, 179 ] ], "normalized": [ { "db_name": "pubchem:compound", "db_id": "6022" } ] }, { "id": "1.0alpha7.train.315.ent4_0", "type": "protein", "text": [ "Hsp90" ], "offsets": [ [ 49, 54 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "3320" }, { "db_name": "hgnc", "db_id": "HSP90AA1" }, { "db_name": "uniprot", "db_id": "P07900" } ] }, { "id": "1.0alpha7.train.315.ent5_1", "type": "protein", "text": [ "Hsp90" ], "offsets": [ [ 197, 202 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "3320" }, { "db_name": "hgnc", "db_id": "HSP90AA1" }, { "db_name": "uniprot", "db_id": "P07900" } ] }, { "id": "1.0alpha7.train.315.ent6_0", "type": "chemical", "text": [ "GA" ], "offsets": [ [ 58, 60 ] ], "normalized": [] }, { "id": "1.0alpha7.train.315.ent7_0", "type": "protein", "text": [ "Raf-1" ], "offsets": [ [ 105, 110 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "5894" }, { "db_name": "hgnc", "db_id": "RAF1" }, { "db_name": "uniprot", "db_id": "P04049" } ] } ]
[]
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1.0alpha7.train.316
24614174
[ { "id": "1.0alpha7.train.316.sent", "type": "sentence", "text": [ "Despite the higher abundance of PTBΔ in the IP pellet (Figure 6B, compare lane 12 to lane 10), no binding of PTBΔ to MSE1-4 RNA could be detected by UV crosslinking, while binding of PTB was clearly and consistently detected (Figure 6B, compare lanes 4 and 6)." ], "offsets": [ [ 0, 260 ] ] } ]
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[]
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1.0alpha7.train.317
16308908
[ { "id": "1.0alpha7.train.317.sent", "type": "sentence", "text": [ "The behavior in the motility assay suggested that AS-2 may interfere with MT binding to kinesin." ], "offsets": [ [ 0, 98 ] ] } ]
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[]
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1.0alpha7.train.318
11347530
[ { "id": "1.0alpha7.train.318.sent", "type": "sentence", "text": [ " It should be noted that importin alpha binding was strictly dependent on the presence of importin beta (not shown), as if the importin alpha/ beta heterodimer would bind rpL23a only via the beta subunit. " ], "offsets": [ [ 0, 211 ] ] } ]
[ { "id": "1.0alpha7.train.318.ent0_0", "type": "protein-family", "text": [ "importin alpha" ], "offsets": [ [ 26, 40 ] ], "normalized": [ { "db_name": "interpro", "db_id": "IPR040122" } ] }, { "id": "1.0alpha7.train.318.ent1_1", "type": "protein-family", "text": [ "importin alpha" ], "offsets": [ [ 130, 144 ] ], "normalized": [ { "db_name": "interpro", "db_id": "IPR040122" } ] }, { "id": "1.0alpha7.train.318.ent2_0", "type": "protein-complex", "text": [ "importin alpha/ beta" ], "offsets": [ [ 130, 150 ] ], "normalized": [] }, { "id": "1.0alpha7.train.318.ent3_0", "type": "protein-family", "text": [ "importin beta" ], "offsets": [ [ 92, 105 ] ], "normalized": [ { "db_name": "interpro", "db_id": "IPR040122" } ] }, { "id": "1.0alpha7.train.318.ent4_0", "type": "protein", "text": [ "rpL23a" ], "offsets": [ [ 175, 181 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "6147" }, { "db_name": "hgnc", "db_id": "RPL23A" }, { "db_name": "uniprot", "db_id": "P62750" } ] } ]
[]
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1.0alpha7.train.319
9149598
[ { "id": "1.0alpha7.train.319.sent", "type": "sentence", "text": [ " When HH binds to Ptc, Smo accumulates in the membrane in a highly phosphorylated state and HH targets are activated. " ], "offsets": [ [ 0, 126 ] ] } ]
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[]
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1.0alpha7.train.320
1749030
[ { "id": "1.0alpha7.train.320.sent", "type": "sentence", "text": [ " Both Hsp70 and Hsp88 bound to Hsp30 in preference to other proteins, but binding of Hsp88 was more selective for Hsp30, and a direct interaction was observed. " ], "offsets": [ [ 0, 166 ] ] } ]
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[]
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1.0alpha7.train.321
15788776
[ { "id": "1.0alpha7.train.321.sent", "type": "sentence", "text": [ " CBP and p300 bind many other transcription factors, including p53, NF-kappaB p65, and RAR, and the association with CBP has been shown to correlate with transcription activation function ( 26, 30, 43, 53, 71). " ], "offsets": [ [ 0, 222 ] ] } ]
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[]
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1.0alpha7.train.322
19992155
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[]
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1.0alpha7.train.323
1559257
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[]
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1.0alpha7.train.324
762216
[ { "id": "1.0alpha7.train.324.sent", "type": "sentence", "text": [ " The Raf 23-284 mutant contains the amino-terminal Ras-binding sequence of Raf, but lacks the carboxyl-terminal kinase domain ( 34). " ], "offsets": [ [ 0, 137 ] ] } ]
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[]
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1.0alpha7.train.325
2465578
[ { "id": "1.0alpha7.train.325.sent", "type": "sentence", "text": [ " The 12V35S (Gly-12 Val, Thr-35 Ser) mutant retains the Raf-1 binding site and thus can activate the Raf-1/MEK/MAPK pathway. " ], "offsets": [ [ 0, 132 ] ] } ]
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[]
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[]
1.0alpha7.train.326
24668031
[ { "id": "1.0alpha7.train.326.sent", "type": "sentence", "text": [ "Therefore, Rheb was immunoprecipitated from either [32P]-labeled, serum-starved TSC2+/+ MEFs or TSC2−/− MEFs, and the ratio of GTP to GDP bound Rheb was determined by one-dimensional thin-layer chromatography. " ], "offsets": [ [ 0, 210 ] ] } ]
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[]
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1.0alpha7.train.327
9541801
[ { "id": "1.0alpha7.train.327.sent", "type": "sentence", "text": [ " Therefore, Axin and GBP both bind to GSK-3, but have opposite effects on its activity. " ], "offsets": [ [ 0, 92 ] ] } ]
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[]
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1.0alpha7.train.328
15036857
[ { "id": "1.0alpha7.train.328.sent", "type": "sentence", "text": [ " As shown in Fig. 4D (lower panel), wt p53 showed strong binding to Sp1. " ], "offsets": [ [ 0, 77 ] ] } ]
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[]
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1.0alpha7.train.329
15768212
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1.0alpha7.train.330
9401270
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[]
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1.0alpha7.train.331
8467741
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[]
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1.0alpha7.train.332
19102273
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[]
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1.0alpha7.train.333
11880697
[ { "id": "1.0alpha7.train.333.sent", "type": "sentence", "text": [ "Rab3a Q81L, which is locked in the GTP‐bound form (Brondyk et al., 1993), was capable of interacting with Ca2+/CaM as well as wild‐type Rab3a (not shown), confirming that Ca2+/CaM is able to complex to both the GDP‐ and the GTP‐bound form of Rab3a (Park et al., 1997). " ], "offsets": [ [ 0, 269 ] ] } ]
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"1.0alpha7.train.333.rel4s1.0alpha7.train.333.ent0_0.o1.0alpha7.train.333.ent1_0", "type": "bind", "arg1_id": "1.0alpha7.train.333.ent0_0", "arg2_id": "1.0alpha7.train.333.ent1_0", "normalized": [] }, { "id": "1.0alpha7.train.333.rel4s1.0alpha7.train.333.ent0_0.o1.0alpha7.train.333.ent2_1", "type": "bind", "arg1_id": "1.0alpha7.train.333.ent0_0", "arg2_id": "1.0alpha7.train.333.ent2_1", "normalized": [] }, { "id": "1.0alpha7.train.333.rel4s1.0alpha7.train.333.ent0_0.o1.0alpha7.train.333.ent3_2", "type": "bind", "arg1_id": "1.0alpha7.train.333.ent0_0", "arg2_id": "1.0alpha7.train.333.ent3_2", "normalized": [] }, { "id": "1.0alpha7.train.333.rel5s1.0alpha7.train.333.ent1_0.o1.0alpha7.train.333.ent4_0", "type": "bind", "arg1_id": "1.0alpha7.train.333.ent1_0", "arg2_id": "1.0alpha7.train.333.ent4_0", "normalized": [] }, { "id": "1.0alpha7.train.333.rel5s1.0alpha7.train.333.ent1_0.o1.0alpha7.train.333.ent5_1", "type": "bind", "arg1_id": "1.0alpha7.train.333.ent1_0", "arg2_id": "1.0alpha7.train.333.ent5_1", "normalized": [] }, { "id": "1.0alpha7.train.333.rel5s1.0alpha7.train.333.ent2_1.o1.0alpha7.train.333.ent4_0", "type": "bind", "arg1_id": "1.0alpha7.train.333.ent2_1", "arg2_id": "1.0alpha7.train.333.ent4_0", "normalized": [] }, { "id": "1.0alpha7.train.333.rel5s1.0alpha7.train.333.ent2_1.o1.0alpha7.train.333.ent5_1", "type": "bind", "arg1_id": "1.0alpha7.train.333.ent2_1", "arg2_id": "1.0alpha7.train.333.ent5_1", "normalized": [] }, { "id": "1.0alpha7.train.333.rel5s1.0alpha7.train.333.ent3_2.o1.0alpha7.train.333.ent4_0", "type": "bind", "arg1_id": "1.0alpha7.train.333.ent3_2", "arg2_id": "1.0alpha7.train.333.ent4_0", "normalized": [] }, { "id": "1.0alpha7.train.333.rel5s1.0alpha7.train.333.ent3_2.o1.0alpha7.train.333.ent5_1", "type": "bind", "arg1_id": "1.0alpha7.train.333.ent3_2", "arg2_id": "1.0alpha7.train.333.ent5_1", "normalized": [] }, { "id": "1.0alpha7.train.333.rel6s1.0alpha7.train.333.ent1_0.o1.0alpha7.train.333.ent4_0", "type": "bind", "arg1_id": "1.0alpha7.train.333.ent1_0", "arg2_id": "1.0alpha7.train.333.ent4_0", "normalized": [] }, { "id": "1.0alpha7.train.333.rel6s1.0alpha7.train.333.ent1_0.o1.0alpha7.train.333.ent5_1", "type": "bind", "arg1_id": "1.0alpha7.train.333.ent1_0", "arg2_id": "1.0alpha7.train.333.ent5_1", "normalized": [] }, { "id": "1.0alpha7.train.333.rel6s1.0alpha7.train.333.ent2_1.o1.0alpha7.train.333.ent4_0", "type": "bind", "arg1_id": "1.0alpha7.train.333.ent2_1", "arg2_id": "1.0alpha7.train.333.ent4_0", "normalized": [] }, { "id": "1.0alpha7.train.333.rel6s1.0alpha7.train.333.ent2_1.o1.0alpha7.train.333.ent5_1", "type": "bind", "arg1_id": "1.0alpha7.train.333.ent2_1", "arg2_id": "1.0alpha7.train.333.ent5_1", "normalized": [] }, { "id": "1.0alpha7.train.333.rel6s1.0alpha7.train.333.ent3_2.o1.0alpha7.train.333.ent4_0", "type": "bind", "arg1_id": "1.0alpha7.train.333.ent3_2", "arg2_id": "1.0alpha7.train.333.ent4_0", "normalized": [] }, { "id": "1.0alpha7.train.333.rel6s1.0alpha7.train.333.ent3_2.o1.0alpha7.train.333.ent5_1", "type": "bind", "arg1_id": "1.0alpha7.train.333.ent3_2", "arg2_id": "1.0alpha7.train.333.ent5_1", "normalized": [] } ]
1.0alpha7.train.334
9641340
[ { "id": "1.0alpha7.train.334.sent", "type": "sentence", "text": [ "To determine if this was the case, we produced a recombinant mutant of cyclin B1 previously reported to lack the ability to interact with Cdc2 (cyclin B1 121-373; Stewart et al., 1994) and an analogous mutant of cyclin E unable to bind Cdk2 (cyclin E 1-338; Fig. ​Fig.55 A). " ], "offsets": [ [ 0, 275 ] ] } ]
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[]
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1.0alpha7.train.335
4884022
[ { "id": "1.0alpha7.train.335.sent", "type": "sentence", "text": [ "IGFBP-5 was captured by FHL2 covalently bound to pre-activated ProteinChip array." ], "offsets": [ [ 0, 84 ] ] } ]
[ { "id": "1.0alpha7.train.335.ent0_0", "type": "protein", "text": [ "FHL2" ], "offsets": [ [ 26, 30 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "2274" }, { "db_name": "hgnc", "db_id": "FHL2" }, { "db_name": "uniprot", "db_id": "E9PKF4" } ] }, { "id": "1.0alpha7.train.335.ent1_0", "type": "protein", "text": [ "IGFBP-5" ], "offsets": [ [ 0, 7 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "3488" }, { "db_name": "hgnc", "db_id": "IGFBP5" }, { "db_name": "uniprot", "db_id": "P24593" } ] } ]
[]
[ { "id": "1.0alpha7.train.335.coref0", "entity_ids": [ "1.0alpha7.train.335.ent0_0" ] }, { "id": "1.0alpha7.train.335.coref1", "entity_ids": [ "1.0alpha7.train.335.ent1_0" ] } ]
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1.0alpha7.train.336
4050199
[ { "id": "1.0alpha7.train.336.sent", "type": "sentence", "text": [ " This suggests that, even in the absence of Ca2+, CEB does not bind GTP. " ], "offsets": [ [ 0, 79 ] ] } ]
[ { "id": "1.0alpha7.train.336.ent0_0", "type": "chemical", "text": [ "GTP" ], "offsets": [ [ 69, 72 ] ], "normalized": [ { "db_name": "pubchem:compound", "db_id": "135398633" } ] }, { "id": "1.0alpha7.train.336.ent1_0", "type": "chemical", "text": [ "Ca2+" ], "offsets": [ [ 44, 48 ] ], "normalized": [ { "db_name": "pubchem:compound", "db_id": "5460341" } ] }, { "id": "1.0alpha7.train.336.ent2_0", "type": "protein", "text": [ "CEB" ], "offsets": [ [ 51, 54 ] ], "normalized": [] } ]
[]
[ { "id": "1.0alpha7.train.336.coref0", "entity_ids": [ "1.0alpha7.train.336.ent0_0" ] }, { "id": "1.0alpha7.train.336.coref1", "entity_ids": [ "1.0alpha7.train.336.ent1_0" ] }, { "id": "1.0alpha7.train.336.coref2", "entity_ids": [ "1.0alpha7.train.336.ent2_0" ] } ]
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1.0alpha7.train.337
225487
[ { "id": "1.0alpha7.train.337.sent", "type": "sentence", "text": [ " Adducin has been seen to promote the binding of spectrin to F-actin (5, Fig.9 A). " ], "offsets": [ [ 0, 88 ] ] } ]
[ { "id": "1.0alpha7.train.337.ent0_0", "type": "protein-family", "text": [ "spectrin" ], "offsets": [ [ 51, 59 ] ], "normalized": [ { "db_name": "interpro", "db_id": "IPR002017" } ] }, { "id": "1.0alpha7.train.337.ent1_0", "type": "protein", "text": [ "F-actin" ], "offsets": [ [ 64, 71 ] ], "normalized": [] }, { "id": "1.0alpha7.train.337.ent2_0", "type": "protein-family", "text": [ "actin" ], "offsets": [ [ 66, 71 ] ], "normalized": [ { "db_name": "interpro", "db_id": "IPR004000" } ] }, { "id": "1.0alpha7.train.337.ent3_0", "type": "protein-family", "text": [ "Adducin" ], "offsets": [ [ 1, 8 ] ], "normalized": [] } ]
[]
[ { "id": "1.0alpha7.train.337.coref0", "entity_ids": [ "1.0alpha7.train.337.ent0_0" ] }, { "id": "1.0alpha7.train.337.coref1", "entity_ids": [ "1.0alpha7.train.337.ent1_0" ] }, { "id": "1.0alpha7.train.337.coref2", "entity_ids": [ "1.0alpha7.train.337.ent2_0" ] }, { "id": "1.0alpha7.train.337.coref3", "entity_ids": [ "1.0alpha7.train.337.ent3_0" ] } ]
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1.0alpha7.train.338
5443867
[ { "id": "1.0alpha7.train.338.sent", "type": "sentence", "text": [ "ICAP-1alpha competes with talin but not with alpha-actinin binding to the beta1 cytoplasmic domain." ], "offsets": [ [ 0, 102 ] ] } ]
[ { "id": "1.0alpha7.train.338.ent0_0", "type": "protein", "text": [ "ICAP-1alpha" ], "offsets": [ [ 0, 11 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "9270" }, { "db_name": "hgnc", "db_id": "ITGB1BP1" }, { "db_name": "uniprot", "db_id": "O14713" } ] }, { "id": "1.0alpha7.train.338.ent1_0", "type": "protein-family", "text": [ "alpha-actinin" ], "offsets": [ [ 47, 60 ] ], "normalized": [ { "db_name": "interpro", "db_id": "IPR026921" } ] }, { "id": "1.0alpha7.train.338.ent2_0", "type": "protein", "text": [ "talin" ], "offsets": [ [ 27, 32 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "7094" }, { "db_name": "hgnc", "db_id": "TLN1" }, { "db_name": "uniprot", "db_id": "Q9Y490" } ] }, { "id": "1.0alpha7.train.338.ent3_0", "type": "protein-domain", "text": [ "beta1 cytoplasmic domain" ], "offsets": [ [ 77, 101 ] ], "normalized": [] } ]
[]
[ { "id": "1.0alpha7.train.338.coref0", "entity_ids": [ "1.0alpha7.train.338.ent0_0" ] }, { "id": "1.0alpha7.train.338.coref1", "entity_ids": [ "1.0alpha7.train.338.ent1_0" ] }, { "id": "1.0alpha7.train.338.coref2", "entity_ids": [ "1.0alpha7.train.338.ent2_0" ] }, { "id": "1.0alpha7.train.338.coref3", "entity_ids": [ "1.0alpha7.train.338.ent3_0" ] } ]
[]
1.0alpha7.train.339
6265431
[ { "id": "1.0alpha7.train.339.sent", "type": "sentence", "text": [ "( B) Deletion of the p300-binding region of SRC-1 abolished the interaction between p300 and SRC-1." ], "offsets": [ [ 0, 103 ] ] } ]
[ { "id": "1.0alpha7.train.339.ent0_0", "type": "protein", "text": [ "SRC-1" ], "offsets": [ [ 46, 51 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "8648" }, { "db_name": "hgnc", "db_id": "NCOA1" }, { "db_name": "uniprot", "db_id": "Q15788" } ] }, { "id": "1.0alpha7.train.339.ent1_1", "type": "protein", "text": [ "SRC-1" ], "offsets": [ [ 97, 102 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "8648" }, { "db_name": "hgnc", "db_id": "NCOA1" }, { "db_name": "uniprot", "db_id": "Q15788" } ] }, { "id": "1.0alpha7.train.339.ent2_0", "type": "protein", "text": [ "p300" ], "offsets": [ [ 22, 26 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "2033" }, { "db_name": "hgnc", "db_id": "EP300" }, { "db_name": "uniprot", "db_id": "Q09472" } ] }, { "id": "1.0alpha7.train.339.ent3_1", "type": "protein", "text": [ "p300" ], "offsets": [ [ 87, 91 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "2033" }, { "db_name": "hgnc", "db_id": "EP300" }, { "db_name": "uniprot", "db_id": "Q09472" } ] } ]
[]
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1.0alpha7.train.340
4585296
[ { "id": "1.0alpha7.train.340.sent", "type": "sentence", "text": [ " However, the binding affinity of MKP3 with ERK2 decreases 16-fold when both Leu167 and Leu170 are replaced by Ala residues. " ], "offsets": [ [ 0, 129 ] ] } ]
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1.0alpha7.train.341
38544
[ { "id": "1.0alpha7.train.341.sent", "type": "sentence", "text": [ " However, the present findings suggest that such a simple model is probably not correct and provide strong evidence that the binding of CBP to CREB is not sufficient for transcriptional activation. " ], "offsets": [ [ 0, 204 ] ] } ]
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1.0alpha7.train.342
9170179
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1.0alpha7.train.343
3506574
[ { "id": "1.0alpha7.train.343.sent", "type": "sentence", "text": [ " PP2A binds to Axin ( 22, 30), and it dephosphorylates APC and Axin ( 22). " ], "offsets": [ [ 0, 80 ] ] } ]
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1.0alpha7.train.344
285199
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1.0alpha7.train.345
12692946
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1.0alpha7.train.346
9843494
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1.0alpha7.train.347
6656120
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1.0alpha7.train.348
38547
[ { "id": "1.0alpha7.train.348.sent", "type": "sentence", "text": [ " If binding of CBP to CREB is not sufficient for transcriptional activation, what essential step in the PKA-mediated response is disrupted by replacement of Ser of CREB with Asp? " ], "offsets": [ [ 0, 190 ] ] } ]
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1.0alpha7.train.349
54804
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[]
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[]
1.0alpha7.train.350
2873562
[ { "id": "1.0alpha7.train.350.sent", "type": "sentence", "text": [ " The actin-binding properties of neurabin and spinophilin likely account, at least in part, for their enrichment in isolated postsynaptic densities ( 13), which contain significant amounts of actin ( 39). " ], "offsets": [ [ 0, 210 ] ] } ]
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[]
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1.0alpha7.train.351
7465567
[ { "id": "1.0alpha7.train.351.sent", "type": "sentence", "text": [ "Dimerization of RBP1 as detected in the two-hybrid system is consistent with earlier indications for cooperative binding of RBP1 to multiple RBP1 RNA target sequences and with evidence for oligomerization of RBP1 in gel-shift experiments ( 15)." ], "offsets": [ [ 0, 248 ] ] } ]
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[]
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1.0alpha7.train.352
1266444
[ { "id": "1.0alpha7.train.352.sent", "type": "sentence", "text": [ " Following probing with the anti-wheat PABP antibodies, PABP was detected bound to eIF-4B, eIF-4F, eIF-iso4F, and recombinant eIF-iso4G, but not to eIF-iso4E or eIF-4A (Fig. 2 A). " ], "offsets": [ [ 0, 190 ] ] } ]
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[]
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1.0alpha7.train.353
4050089
[ { "id": "1.0alpha7.train.353.sent", "type": "sentence", "text": [ "CEB does not bind GTP." ], "offsets": [ [ 0, 23 ] ] } ]
[ { "id": "1.0alpha7.train.353.ent0_0", "type": "chemical", "text": [ "GTP" ], "offsets": [ [ 19, 22 ] ], "normalized": [ { "db_name": "pubchem:compound", "db_id": "135398633" } ] }, { "id": "1.0alpha7.train.353.ent1_0", "type": "protein", "text": [ "CEB" ], "offsets": [ [ 0, 3 ] ], "normalized": [] } ]
[]
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1.0alpha7.train.354
1418578
[ { "id": "1.0alpha7.train.354.sent", "type": "sentence", "text": [ "The results of this study suggest that the third positive response element at bp 125 also binds Sp1." ], "offsets": [ [ 0, 103 ] ] } ]
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[]
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[]
1.0alpha7.train.355
11787607
[ { "id": "1.0alpha7.train.355.sent", "type": "sentence", "text": [ " Collectively, these findings indicate that cyt c and Hsp90 bind competitively to Apaf-1. " ], "offsets": [ [ 0, 93 ] ] } ]
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[]
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1.0alpha7.train.356
15642343
[ { "id": "1.0alpha7.train.356.sent", "type": "sentence", "text": [ "Interestingly, CKIepsilon binds to mPER1 in a region that has no obvious sequence similarity to the suggested DBT-binding region of dPER (27)." ], "offsets": [ [ 0, 142 ] ] } ]
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[]
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1.0alpha7.train.357
1696390
[ { "id": "1.0alpha7.train.357.sent", "type": "sentence", "text": [ "Inhibiting CREB phosphorylation would thus inhibit CREB binding to CREB-binding protein and may inhibit TGF-beta-induced stimulation of fibronectin gene transcription." ], "offsets": [ [ 0, 171 ] ] } ]
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1.0alpha7.train.358
24079081
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1.0alpha7.train.359
88734
[ { "id": "1.0alpha7.train.359.sent", "type": "sentence", "text": [ " Binding of Rb to E2F, which represses E2F-dependent transcription, increases the half-life of E2F-DNA complexes 10-15-fold ( 58) . " ], "offsets": [ [ 0, 140 ] ] } ]
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1.0alpha7.train.360
4249933
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[]
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1.0alpha7.train.361
11479130
[ { "id": "1.0alpha7.train.361.sent", "type": "sentence", "text": [ " Cell, 78, 761-771 [Medline] ubinfeld, B. , Albert, I. , Porfiri, E. , Fiol, C. , Munemitso, S. and Polakis, P. (1996) Binding of GSK3beta to the APC-beta-catenin complex and regulation of complex assembly. " ], "offsets": [ [ 0, 223 ] ] } ]
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[]
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1.0alpha7.train.362
795524
[ { "id": "1.0alpha7.train.362.sent", "type": "sentence", "text": [ " These results suggest that p62 binds noncovalently to ubiquitin, rather than forming a thioester or an isopeptide bond. " ], "offsets": [ [ 0, 124 ] ] } ]
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[]
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1.0alpha7.train.363
24638155
[ { "id": "1.0alpha7.train.363.sent", "type": "sentence", "text": [ "These data strongly imply that NAD+ binding to CtBP causes a conformational change necessary for binding of the PXDLS motif." ], "offsets": [ [ 0, 125 ] ] } ]
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[]
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1.0alpha7.train.364
5566793
[ { "id": "1.0alpha7.train.364.sent", "type": "sentence", "text": [ "Note that the LRR-to-EEE conversion altered the Rab binding specificity of Rim2." ], "offsets": [ [ 0, 83 ] ] } ]
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[]
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1.0alpha7.train.365
1712609
[ { "id": "1.0alpha7.train.365.sent", "type": "sentence", "text": [ "Binding of Numb PTB domain to LNX." ], "offsets": [ [ 0, 36 ] ] } ]
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[]
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1.0alpha7.train.366
25785588
[ { "id": "1.0alpha7.train.366.sent", "type": "sentence", "text": [ "We observed changes in the CRE-DNA binding of CREB after the ME ( Fig. 2B and E)." ], "offsets": [ [ 0, 84 ] ] } ]
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[]
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1.0alpha7.train.367
23431474
[ { "id": "1.0alpha7.train.367.sent", "type": "sentence", "text": [ " A neurobeachin isoform that does not bind RII, beige-like protein (BGL), is expressed in many tissues. " ], "offsets": [ [ 0, 107 ] ] } ]
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[]
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1.0alpha7.train.368
4287973
[ { "id": "1.0alpha7.train.368.sent", "type": "sentence", "text": [ " Use of this approach showed that ZAG can bind several different types of fatty acids, all of which are abundant in human tissues. " ], "offsets": [ [ 0, 135 ] ] } ]
[ { "id": "1.0alpha7.train.368.ent0_0", "type": "protein", "text": [ "ZAG" ], "offsets": [ [ 35, 38 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "563" }, { "db_name": "hgnc", "db_id": "AZGP1" }, { "db_name": "uniprot", "db_id": "P25311" } ] }, { "id": "1.0alpha7.train.368.ent1_0", "type": "chemical", "text": [ "fatty acids" ], "offsets": [ [ 76, 87 ] ], "normalized": [] } ]
[]
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1.0alpha7.train.369
25318960
[ { "id": "1.0alpha7.train.369.sent", "type": "sentence", "text": [ "(B) PlexB binds to Rac in a GTP-dependent manner." ], "offsets": [ [ 0, 52 ] ] } ]
[ { "id": "1.0alpha7.train.369.ent0_0", "type": "chemical", "text": [ "GTP" ], "offsets": [ [ 31, 34 ] ], "normalized": [ { "db_name": "pubchem:compound", "db_id": "135398633" } ] }, { "id": "1.0alpha7.train.369.ent1_0", "type": "protein", "text": [ "Rac" ], "offsets": [ [ 21, 24 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "5879" }, { "db_name": "hgnc", "db_id": "RAC1" }, { "db_name": "uniprot", "db_id": "P63000" } ] }, { "id": "1.0alpha7.train.369.ent2_0", "type": "protein", "text": [ "PlexB" ], "offsets": [ [ 5, 10 ] ], "normalized": [ { "db_name": "uniprot", "db_id": "Q9V4A7" } ] } ]
[]
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1.0alpha7.train.370
11356552
[ { "id": "1.0alpha7.train.370.sent", "type": "sentence", "text": [ "In in vitro assays, Su(fu) can bind directly to Fu and to Ci; since there is no evidence for a direct interaction between the latter proteins or indeed between them and Cos‐2, it may be that Su(fu) forms a bridge between them, stabilizing their association with one another and with Cos-2 (Monnier et al., 1998) (Figure 1). " ], "offsets": [ [ 0, 324 ] ] } ]
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[]
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1.0alpha7.train.371
2399738
[ { "id": "1.0alpha7.train.371.sent", "type": "sentence", "text": [ " Taken together, these results strongly implicate a role for PI3K in the facilitation of FAK-promoted cell migration and suggest that the binding of Src and p130Cas to FAK may not be sufficient for this process. " ], "offsets": [ [ 0, 218 ] ] } ]
[ { "id": "1.0alpha7.train.371.ent0_0", "type": "protein", "text": [ "FAK" ], "offsets": [ [ 91, 94 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "5747" }, { "db_name": "hgnc", "db_id": "PTK2" }, { "db_name": "uniprot", "db_id": "Q05397" } ] }, { "id": "1.0alpha7.train.371.ent1_1", "type": "protein", "text": [ "FAK" ], "offsets": [ [ 173, 176 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "5747" }, { "db_name": "hgnc", "db_id": "PTK2" }, { "db_name": "uniprot", "db_id": "Q05397" } ] }, { "id": "1.0alpha7.train.371.ent2_0", "type": "protein", "text": [ "Src" ], "offsets": [ [ 152, 155 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "6714" }, { "db_name": "hgnc", "db_id": "SRC" }, { "db_name": "uniprot", "db_id": "P12931" } ] }, { "id": "1.0alpha7.train.371.ent3_0", "type": "protein", "text": [ "p130Cas" ], "offsets": [ [ 161, 168 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "9564" }, { "db_name": "hgnc", "db_id": "BCAR1" }, { "db_name": "uniprot", "db_id": "P56945" } ] }, { "id": "1.0alpha7.train.371.ent4_0", "type": "protein-family", "text": [ "PI3K" ], "offsets": [ [ 62, 66 ] ], "normalized": [ { "db_name": "pfam", "db_id": "PF00454" } ] } ]
[]
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1.0alpha7.train.372
340366
[ { "id": "1.0alpha7.train.372.sent", "type": "sentence", "text": [ "The IL-11-inducible binding of Syp to both gp130 and JAK2 was shown by reciprocal immunoprecipitations." ], "offsets": [ [ 0, 109 ] ] } ]
[ { "id": "1.0alpha7.train.372.ent0_0", "type": "protein", "text": [ "Syp" ], "offsets": [ [ 34, 37 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "6855" }, { "db_name": "hgnc", "db_id": "SYP" }, { "db_name": "uniprot", "db_id": "P08247" } ] }, { "id": "1.0alpha7.train.372.ent1_0", "type": "protein", "text": [ "JAK2" ], "offsets": [ [ 58, 62 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "3717" }, { "db_name": "hgnc", "db_id": "JAK2" } ] }, { "id": "1.0alpha7.train.372.ent2_0", "type": "protein", "text": [ "gp130" ], "offsets": [ [ 47, 52 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "3572" }, { "db_name": "hgnc", "db_id": "IL6ST" }, { "db_name": "uniprot", "db_id": "P40189" } ] }, { "id": "1.0alpha7.train.372.ent3_0", "type": "protein", "text": [ "IL-11" ], "offsets": [ [ 5, 10 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "3589" }, { "db_name": "hgnc", "db_id": "IL11" }, { "db_name": "uniprot", "db_id": "P20809" } ] } ]
[]
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1.0alpha7.train.373
25302485
[ { "id": "1.0alpha7.train.373.sent", "type": "sentence", "text": [ " It has been shown, by in vitro binding assay, that Ldb proteins only binds to the first LIM domain of Islet-1 and not to the second LIM domain (Jurata et al., 1996 ), leaving room for the second LIM domain to interact with some other cofactors. " ], "offsets": [ [ 0, 254 ] ] } ]
[ { "id": "1.0alpha7.train.373.ent0_0", "type": "protein-family", "text": [ "Ldb" ], "offsets": [ [ 53, 56 ] ], "normalized": [ { "db_name": "interpro", "db_id": "IPR030174" } ] }, { "id": "1.0alpha7.train.373.ent1_0", "type": "protein", "text": [ "Islet-1" ], "offsets": [ [ 106, 113 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "3670" }, { "db_name": "hgnc", "db_id": "ISL1" }, { "db_name": "uniprot", "db_id": "P61371" } ] }, { "id": "1.0alpha7.train.373.ent2_0", "type": "protein-domain", "text": [ "LIM" ], "offsets": [ [ 91, 94 ] ], "normalized": [] }, { "id": "1.0alpha7.train.373.ent3_1", "type": "protein-domain", "text": [ "LIM" ], "offsets": [ [ 137, 140 ] ], "normalized": [] }, { "id": "1.0alpha7.train.373.ent4_2", "type": "protein-domain", "text": [ "LIM" ], "offsets": [ [ 203, 206 ] ], "normalized": [] } ]
[]
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1.0alpha7.train.374
12492614
[ { "id": "1.0alpha7.train.374.sent", "type": "sentence", "text": [ "The RGS domain of Axin binds APC (Behrens et al. 1998; Kishida et al. 1998), defined domains of Axin are required for binding GSK3β and β-catenin (Behrens et al. 1998; Ikeda et al. 1998; Sakanaka et al. 1998; Hedgepeth et al. 1999) and the carboxy-terminal DIX domain and more internal sequences are required for Axin homodimerization and binding to Dsh and LRP/Arrow (Hsu et al. 1999; Kishida et al. 1999; Li et al. 1999; Smalley et al. 1999; Mao et al. 2001). " ], "offsets": [ [ 0, 462 ] ] } ]
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[]
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