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1.0alpha7.train.200
3655981
[ { "id": "1.0alpha7.train.200.sent", "type": "sentence", "text": [ "Furthermore, G6P binding to GS induces a conformational change, increasing its susceptibility to dephosphorylation ( 5, 6)." ], "offsets": [ [ 0, 123 ] ] } ]
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[]
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1.0alpha7.train.201
9270266
[ { "id": "1.0alpha7.train.201.sent", "type": "sentence", "text": [ "(A) The peptide analogous to the wild-type N terminus of KCNK9 (and KCNK3) binds beta-COP from rat brain, while peptides with the NQ mutation do not (left)." ], "offsets": [ [ 0, 156 ] ] } ]
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[]
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1.0alpha7.train.202
9539483
[ { "id": "1.0alpha7.train.202.sent", "type": "sentence", "text": [ "On the other hand, the SH2 domain of Crk can potentially bind to both p130Cas and paxillin." ], "offsets": [ [ 0, 91 ] ] } ]
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[]
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1.0alpha7.train.203
1814820
[ { "id": "1.0alpha7.train.203.sent", "type": "sentence", "text": [ "TAFII250 binds directly to TBP and multiple other TAFIIs, thus serving as a potential scaffold for the multiprotein complex ( 28, 29)." ], "offsets": [ [ 0, 134 ] ] } ]
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[]
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1.0alpha7.train.204
10947020
[ { "id": "1.0alpha7.train.204.sent", "type": "sentence", "text": [ "Since TSA induced Sp1 binding to Sp1 consensus sequences in Hep3B cells, we investigated whether TSA affected Sp1 phosphorylation, a possible cause for the increase of Sp1 binding to its consensus DNA sequences." ], "offsets": [ [ 0, 211 ] ] } ]
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[]
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1.0alpha7.train.205
21745005
[ { "id": "1.0alpha7.train.205.sent", "type": "sentence", "text": [ "Systemic administration of 3-NPA (30 mg kg-1 per day for 3 days) induced a 170% increase in [3]- PK 11195 binding, and expression of HSP27." ], "offsets": [ [ 0, 139 ] ] } ]
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[]
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[]
1.0alpha7.train.206
22146010
[ { "id": "1.0alpha7.train.206.sent", "type": "sentence", "text": [ "This interpretation is consistent with stopped flow experiments on the formation of the catalytic complex, which were interpreted as evidence that the second dIII binds to the dI dimer with a Kd of 20-50 M [ 24]." ], "offsets": [ [ 0, 212 ] ] } ]
[ { "id": "1.0alpha7.train.206.ent0_0", "type": "protein", "text": [ "dI" ], "offsets": [ [ 176, 178 ] ], "normalized": [] }, { "id": "1.0alpha7.train.206.ent1_0", "type": "protein", "text": [ "dIII" ], "offsets": [ [ 158, 162 ] ], "normalized": [] } ]
[]
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1.0alpha7.train.207
10369809
[ { "id": "1.0alpha7.train.207.sent", "type": "sentence", "text": [ "75 89 90 91 Two of them, A63V and K70T, are located in exon 2b within the consensus pattern of sequence repeats of alpha-TM and could alter tropomyosin binding to actin." ], "offsets": [ [ 0, 169 ] ] } ]
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[]
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1.0alpha7.train.208
639982
[ { "id": "1.0alpha7.train.208.sent", "type": "sentence", "text": [ "The majority of gp160 remained bound to calreticulin despite addition of ATP (not shown)." ], "offsets": [ [ 0, 89 ] ] } ]
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[]
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1.0alpha7.train.209
23900170
[ { "id": "1.0alpha7.train.209.sent", "type": "sentence", "text": [ "Because PIP2 was added in the form of micelles, the effects of actin and PIP2 on profilin binding to gephyrin cannot be compared in terms of affinities." ], "offsets": [ [ 0, 152 ] ] } ]
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[]
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1.0alpha7.train.210
9126838
[ { "id": "1.0alpha7.train.210.sent", "type": "sentence", "text": [ "This situation is similar to that of pI cells, where overexpression of the GTP-bound form of Galphai, GalphaiQ205L, also influences the orientation of the spindle." ], "offsets": [ [ 0, 163 ] ] } ]
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[]
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1.0alpha7.train.211
5293344
[ { "id": "1.0alpha7.train.211.sent", "type": "sentence", "text": [ "Therefore, we hypothesized that co-stimulatory molecules that preferentially bind CD28 or CTLA-4 would have dramatically altered biological properties." ], "offsets": [ [ 0, 151 ] ] } ]
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[]
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[]
1.0alpha7.train.212
9255615
[ { "id": "1.0alpha7.train.212.sent", "type": "sentence", "text": [ "Using electrophoretic mobility shift assays (EMSA), we found that Dfd binds to this fragment ( S3/240bpwt; Figure 5D)." ], "offsets": [ [ 0, 118 ] ] } ]
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[]
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[]
1.0alpha7.train.213
1356396
[ { "id": "1.0alpha7.train.213.sent", "type": "sentence", "text": [ "The INK family has a specificity for the early G1 kinases Cdk4 and Cdk6 complexed with D-type cyclins, while the CIP family is partial to Cdk2 bound to either cyclin A or E." ], "offsets": [ [ 0, 173 ] ] } ]
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[]
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1.0alpha7.train.214
19530807
[ { "id": "1.0alpha7.train.214.sent", "type": "sentence", "text": [ "These results suggest that most of the synergistic coactivation by CRP2 requires efficient binding of SRF to multiple SREs." ], "offsets": [ [ 0, 123 ] ] } ]
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[]
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1.0alpha7.train.215
7548236
[ { "id": "1.0alpha7.train.215.sent", "type": "sentence", "text": [ "These membrane lipids bind to the actin-binding domains of AC ( Yonezawa et al 1991a, Kusano et al 1999) and are capable of inhibiting AC binding to actin in vitro." ], "offsets": [ [ 0, 164 ] ] } ]
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[]
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1.0alpha7.train.216
2066872
[ { "id": "1.0alpha7.train.216.sent", "type": "sentence", "text": [ "In addition, Redlitz et al. (10) showed that activated pro-plasma carboxypeptidase B and plasma carboxypeptidase N diminish the binding of plasminogen to U937 cells and that fibrinolysis occurs more rapidly in pro-plasma carboxypeptidase B (TAFI)-deficient compared with normal plasma." ], "offsets": [ [ 0, 285 ] ] } ]
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[]
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[]
1.0alpha7.train.217
206727
[ { "id": "1.0alpha7.train.217.sent", "type": "sentence", "text": [ "Tyrosine Phosphorylation of p190 Correlates with Enhanced p120 GAP Binding in Vivo; Because p120 protein preferentially binds phosphorylated p190 in vitro, we compared the levels of native p120•p190 complex formation in normal 3Y1 rat fibroblasts and v-Src-transformed 3Y1 cells (SR3Y1)." ], "offsets": [ [ 0, 287 ] ] } ]
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[]
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1.0alpha7.train.218
3554320
[ { "id": "1.0alpha7.train.218.sent", "type": "sentence", "text": [ "Furthermore, we determined that this regionalized editing of the collagen substrate was orchestrated by the stimulated expression of collagenase-1, which was bound to the SMC plasma membrane." ], "offsets": [ [ 0, 191 ] ] } ]
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[]
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[]
1.0alpha7.train.219
15995413
[ { "id": "1.0alpha7.train.219.sent", "type": "sentence", "text": [ "After transfection of vectors expressing MUC1 and GSK3beta, 293 cells were subjected to immunoprecipitation with anti-MUC1 and the precipitates were analyzed for binding of MUC1 to beta-catenin." ], "offsets": [ [ 0, 194 ] ] } ]
[ { "id": "1.0alpha7.train.219.ent0_0", "type": "protein", "text": [ "beta-catenin" ], "offsets": [ [ 181, 193 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "1499" }, { "db_name": "hgnc", "db_id": "CTNNB1" }, { "db_name": "uniprot", "db_id": "P35222" } ] }, { "id": "1.0alpha7.train.219.ent1_0", "type": "protein", "text": [ "MUC1" ], "offsets": [ [ 41, 45 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "4582" }, { "db_name": "hgnc", "db_id": "MUC1" } ] }, { "id": "1.0alpha7.train.219.ent2_1", "type": "protein", "text": [ "MUC1" ], "offsets": [ [ 118, 122 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "4582" }, { "db_name": "hgnc", "db_id": "MUC1" } ] }, { "id": "1.0alpha7.train.219.ent3_2", "type": "protein", "text": [ "MUC1" ], "offsets": [ [ 173, 177 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "4582" }, { "db_name": "hgnc", "db_id": "MUC1" } ] }, { "id": "1.0alpha7.train.219.ent4_0", "type": "reagent", "text": [ "anti-MUC1" ], "offsets": [ [ 113, 122 ] ], "normalized": [] }, { "id": "1.0alpha7.train.219.ent5_0", "type": "protein", "text": [ "GSK3beta" ], "offsets": [ [ 50, 58 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "2932" }, { "db_name": "hgnc", "db_id": "GSK3B" }, { "db_name": "uniprot", "db_id": "P49841" } ] } ]
[]
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[]
1.0alpha7.train.220
20571476
[ { "id": "1.0alpha7.train.220.sent", "type": "sentence", "text": [ "This orientation shows the actin-binding surface of profilin [14,15] , which is predominately composed of the C-terminal helix (H3) and the bottom three strands ( 4, 5 and 6) of the central sheet." ], "offsets": [ [ 0, 196 ] ] } ]
[ { "id": "1.0alpha7.train.220.ent0_0", "type": "protein-family", "text": [ "actin" ], "offsets": [ [ 27, 32 ] ], "normalized": [ { "db_name": "pfam", "db_id": "PF00022" } ] }, { "id": "1.0alpha7.train.220.ent1_0", "type": "protein-family", "text": [ "profilin" ], "offsets": [ [ 52, 60 ] ], "normalized": [ { "db_name": "interpro", "db_id": "IPR005455" } ] } ]
[]
[ { "id": "1.0alpha7.train.220.coref0", "entity_ids": [ "1.0alpha7.train.220.ent0_0" ] }, { "id": "1.0alpha7.train.220.coref1", "entity_ids": [ "1.0alpha7.train.220.ent1_0" ] } ]
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1.0alpha7.train.221
19503598
[ { "id": "1.0alpha7.train.221.sent", "type": "sentence", "text": [ "Binding of Cdc20 and Cdh1 to the APC is differentially regulated." ], "offsets": [ [ 0, 65 ] ] } ]
[ { "id": "1.0alpha7.train.221.ent0_0", "type": "protein", "text": [ "Cdh1" ], "offsets": [ [ 21, 25 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "999" }, { "db_name": "hgnc", "db_id": "CDH1" }, { "db_name": "uniprot", "db_id": "P12830" } ] }, { "id": "1.0alpha7.train.221.ent1_0", "type": "protein", "text": [ "APC" ], "offsets": [ [ 33, 36 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "324" }, { "db_name": "hgnc", "db_id": "APC" } ] }, { "id": "1.0alpha7.train.221.ent2_0", "type": "protein", "text": [ "Cdc20" ], "offsets": [ [ 11, 16 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "991" }, { "db_name": "hgnc", "db_id": "CDC20" }, { "db_name": "uniprot", "db_id": "Q12834" } ] } ]
[]
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1.0alpha7.train.222
12684514
[ { "id": "1.0alpha7.train.222.sent", "type": "sentence", "text": [ "With the goal of learning more about the mechanisms responsible for insulating activity, we have identified and characterized SBP ( scs binding protein), a protein component of the scs nucleoprotein complex." ], "offsets": [ [ 0, 207 ] ] } ]
[ { "id": "1.0alpha7.train.222.ent0_0", "type": "protein", "text": [ "SBP" ], "offsets": [ [ 126, 129 ] ], "normalized": [] }, { "id": "1.0alpha7.train.222.ent1_0", "type": "protein", "text": [ "scs binding protein" ], "offsets": [ [ 132, 151 ] ], "normalized": [] }, { "id": "1.0alpha7.train.222.ent2_0", "type": "protein-complex", "text": [ "scs" ], "offsets": [ [ 132, 135 ] ], "normalized": [] }, { "id": "1.0alpha7.train.222.ent3_1", "type": "protein-complex", "text": [ "scs" ], "offsets": [ [ 181, 184 ] ], "normalized": [] } ]
[]
[ { "id": "1.0alpha7.train.222.coref0", "entity_ids": [ "1.0alpha7.train.222.ent0_0", "1.0alpha7.train.222.ent1_0" ] }, { "id": "1.0alpha7.train.222.coref1", "entity_ids": [ "1.0alpha7.train.222.ent2_0", "1.0alpha7.train.222.ent3_1" ] } ]
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1.0alpha7.train.223
4871993
[ { "id": "1.0alpha7.train.223.sent", "type": "sentence", "text": [ "Thus, the binding of Porc with Wg appears to be necessary for the stimulation of the N-glycosylation of Wg." ], "offsets": [ [ 0, 107 ] ] } ]
[ { "id": "1.0alpha7.train.223.ent0_0", "type": "protein", "text": [ "Wg" ], "offsets": [ [ 31, 33 ] ], "normalized": [ { "db_name": "uniprot", "db_id": "P09615" } ] }, { "id": "1.0alpha7.train.223.ent1_1", "type": "protein", "text": [ "Wg" ], "offsets": [ [ 104, 106 ] ], "normalized": [ { "db_name": "uniprot", "db_id": "P09615" } ] }, { "id": "1.0alpha7.train.223.ent2_0", "type": "protein", "text": [ "Porc" ], "offsets": [ [ 21, 25 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "3145" }, { "db_name": "hgnc", "db_id": "HMBS" }, { "db_name": "uniprot", "db_id": "P08397" } ] } ]
[]
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1.0alpha7.train.224
19761788
[ { "id": "1.0alpha7.train.224.sent", "type": "sentence", "text": [ "Pals1 (or Sdt) binds to the Crb-PBM motif (CrbPBM) via its single PDZ domain." ], "offsets": [ [ 0, 77 ] ] } ]
[ { "id": "1.0alpha7.train.224.ent0_0", "type": "protein", "text": [ "Sdt" ], "offsets": [ [ 10, 13 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "64398" }, { "db_name": "hgnc", "db_id": "MPP5" }, { "db_name": "uniprot", "db_id": "Q8N3R9" } ] }, { "id": "1.0alpha7.train.224.ent1_0", "type": "protein", "text": [ "Pals1" ], "offsets": [ [ 0, 5 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "64398" }, { "db_name": "hgnc", "db_id": "MPP5" }, { "db_name": "uniprot", "db_id": "Q8N3R9" } ] }, { "id": "1.0alpha7.train.224.ent2_0", "type": "protein-motif", "text": [ "CrbPBM" ], "offsets": [ [ 43, 49 ] ], "normalized": [] }, { "id": "1.0alpha7.train.224.ent3_0", "type": "protein-motif", "text": [ "Crb-PBM motif" ], "offsets": [ [ 28, 41 ] ], "normalized": [] }, { "id": "1.0alpha7.train.224.ent4_0", "type": "protein-domain", "text": [ "PDZ" ], "offsets": [ [ 66, 69 ] ], "normalized": [ { "db_name": "interpro", "db_id": "IPR001478" } ] } ]
[]
[ { "id": "1.0alpha7.train.224.coref0", "entity_ids": [ "1.0alpha7.train.224.ent0_0", "1.0alpha7.train.224.ent1_0" ] }, { "id": "1.0alpha7.train.224.coref1", "entity_ids": [ "1.0alpha7.train.224.ent2_0", "1.0alpha7.train.224.ent3_0" ] }, { "id": "1.0alpha7.train.224.coref2", "entity_ids": [ "1.0alpha7.train.224.ent4_0" ] } ]
[]
1.0alpha7.train.225
13846927
[ { "id": "1.0alpha7.train.225.sent", "type": "sentence", "text": [ "Under these conditions, Hbp binds heme in a 1:1 molar ratio (unpublished data)." ], "offsets": [ [ 0, 79 ] ] } ]
[ { "id": "1.0alpha7.train.225.ent0_0", "type": "protein", "text": [ "Hbp" ], "offsets": [ [ 24, 27 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "566" }, { "db_name": "hgnc", "db_id": "AZU1" }, { "db_name": "uniprot", "db_id": "P20160" } ] }, { "id": "1.0alpha7.train.225.ent1_0", "type": "chemical", "text": [ "heme" ], "offsets": [ [ 34, 38 ] ], "normalized": [ { "db_name": "pubchem:compound", "db_id": "26945" } ] } ]
[]
[ { "id": "1.0alpha7.train.225.coref0", "entity_ids": [ "1.0alpha7.train.225.ent0_0" ] }, { "id": "1.0alpha7.train.225.coref1", "entity_ids": [ "1.0alpha7.train.225.ent1_0" ] } ]
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1.0alpha7.train.226
3506549
[ { "id": "1.0alpha7.train.226.sent", "type": "sentence", "text": [ "Both Axin and Axil bind not only to GSK-3beta but also to beta-catenin and APC ( 14-20) and promote GSK-3beta-dependent phosphorylation of beta-catenin and APC ( 14, 15, 19, 21, 22)." ], "offsets": [ [ 0, 182 ] ] } ]
[ { "id": "1.0alpha7.train.226.ent0_0", "type": "protein", "text": [ "Axil" ], "offsets": [ [ 14, 18 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "8313" }, { "db_name": "hgnc", "db_id": "AXIN2" }, { "db_name": "uniprot", "db_id": "A0A087WXP8" } ] }, { "id": "1.0alpha7.train.226.ent1_0", "type": "protein", "text": [ "beta-catenin" ], "offsets": [ [ 58, 70 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "1499" }, { "db_name": "hgnc", "db_id": "CTNNB1" }, { "db_name": "uniprot", "db_id": "P35222" } ] }, { "id": "1.0alpha7.train.226.ent2_1", "type": "protein", "text": [ "beta-catenin" ], "offsets": [ [ 139, 151 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "1499" }, { "db_name": "hgnc", "db_id": "CTNNB1" }, { "db_name": "uniprot", "db_id": "P35222" } ] }, { "id": "1.0alpha7.train.226.ent3_0", "type": "protein", "text": [ "Axin" ], "offsets": [ [ 5, 9 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "8312" }, { "db_name": "hgnc", "db_id": "AXIN1" }, { "db_name": "uniprot", "db_id": "O15169" } ] }, { "id": "1.0alpha7.train.226.ent4_0", "type": "protein", "text": [ "GSK-3beta" ], "offsets": [ [ 36, 45 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "2932" }, { "db_name": "hgnc", "db_id": "GSK3B" }, { "db_name": "uniprot", "db_id": "P49841" } ] }, { "id": "1.0alpha7.train.226.ent5_1", "type": "protein", "text": [ "GSK-3beta" ], "offsets": [ [ 100, 109 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "2932" }, { "db_name": "hgnc", "db_id": "GSK3B" }, { "db_name": "uniprot", "db_id": "P49841" } ] }, { "id": "1.0alpha7.train.226.ent6_0", "type": "protein", "text": [ "APC" ], "offsets": [ [ 75, 78 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "324" }, { "db_name": "hgnc", "db_id": "APC" } ] }, { "id": "1.0alpha7.train.226.ent7_1", "type": "protein", "text": [ "APC" ], "offsets": [ [ 156, 159 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "324" }, { "db_name": "hgnc", "db_id": "APC" } ] } ]
[]
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1.0alpha7.train.227
11347599
[ { "id": "1.0alpha7.train.227.sent", "type": "sentence", "text": [ "Even though transportin can bind an M9 signal and the BIB domain simultaneously, it appears unlikely that transportin normally would import the two substrates at the same time: import of the trimeric M9-transportin-BIB complex is apparently much less efficient than import of, for example, an M9-transportin complex (not shown)." ], "offsets": [ [ 0, 328 ] ] } ]
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[]
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1.0alpha7.train.228
19530653
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[]
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1.0alpha7.train.229
11405650
[ { "id": "1.0alpha7.train.229.sent", "type": "sentence", "text": [ "Nature, 377, 246-248 [Medline] orlich, D. , Henklein, P. , Laskey, R.A. and Hartmann, E. (1996a) A 41 amino acid motif in importin alpha confers binding to importin beta and hence transit into the nucleus." ], "offsets": [ [ 0, 205 ] ] } ]
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[]
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1.0alpha7.train.230
1570746
[ { "id": "1.0alpha7.train.230.sent", "type": "sentence", "text": [ "In addition, we show that the gelsolin S1 peptide PS1 does not hinder binding of cofilin or PS2 to F-actin; this also argues against the model proposed by Hatanaka et al. ( 24)." ], "offsets": [ [ 0, 177 ] ] } ]
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[]
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1.0alpha7.train.231
15937016
[ { "id": "1.0alpha7.train.231.sent", "type": "sentence", "text": [ "Furthermore, it has been shown that GSK-3beta phosphorylates APC and that the phosphorylation enhances the binding of APC to beta-catenin ( 37)." ], "offsets": [ [ 0, 144 ] ] } ]
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[]
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1.0alpha7.train.232
9049233
[ { "id": "1.0alpha7.train.232.sent", "type": "sentence", "text": [ "Binding of FasL to Fas or cross-linking Fas with agonistic antibodies (IgM class anti-Fas antibody, or IgG3 class anti-APO1 antibody) induces apoptosis in Fas-bearing cells (Trauth et al., 1989 ; Yonehara et al., 1989 ; Itoh et al., 1991 )." ], "offsets": [ [ 0, 240 ] ] } ]
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[]
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1.0alpha7.train.233
6238942
[ { "id": "1.0alpha7.train.233.sent", "type": "sentence", "text": [ "( B) ELISA demonstrating the reduced binding of the Ab to BDNF after modification with the caging group and its successful reactivation by UV light." ], "offsets": [ [ 0, 148 ] ] } ]
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[]
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[]
1.0alpha7.train.234
4397443
[ { "id": "1.0alpha7.train.234.sent", "type": "sentence", "text": [ "Immunoprecipitation of p53 was followed by Western blot analysis to determine the type and level of Mdm2 bound to p53 under each of these conditions." ], "offsets": [ [ 0, 149 ] ] } ]
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[]
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1.0alpha7.train.235
2477089
[ { "id": "1.0alpha7.train.235.sent", "type": "sentence", "text": [ "Binding of E1A to CBP amino acids 1805-1891 prevents binding of the histone acetyltransferase P/CAF, whereas E1A binding to CBP amino acids 2058-2163 prevents binding of the co-activator P/CIP ( 5, 12)." ], "offsets": [ [ 0, 202 ] ] } ]
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[]
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1.0alpha7.train.236
3115715
[ { "id": "1.0alpha7.train.236.sent", "type": "sentence", "text": [ "As expected, conversion of the TAGA element into a consensus TATA box increased f:TFIID binding to the LRP-2 promoter, leading to increased protection of the TATA box region and downstream promoter sequences (Fig. 4 B, comparelanes 1–4 with lanes 5–8). " ], "offsets": [ [ 0, 253 ] ] } ]
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[]
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1.0alpha7.train.237
1544583
[ { "id": "1.0alpha7.train.237.sent", "type": "sentence", "text": [ "The mutation replacing Ser-39 with Ala eliminated the phosphorylation-dependent regulation of actin binding of fascin, indicating that phosphorylation at this site regulates the actin binding ability of fascin." ], "offsets": [ [ 0, 210 ] ] } ]
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[]
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1.0alpha7.train.238
9128447
[ { "id": "1.0alpha7.train.238.sent", "type": "sentence", "text": [ "Slit significantly increased the binding of srGAP1 to Robo1 ( Figure 4C, lane 2, compared to lane 1)." ], "offsets": [ [ 0, 101 ] ] } ]
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[]
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1.0alpha7.train.239
22183532
[ { "id": "1.0alpha7.train.239.sent", "type": "sentence", "text": [ "The heparin-binding property of apoE plays an important role in the sequestration step of the heparan sulfate proteoglycan (HSPG)/ LRP metabolic pathway as well as in the independent HSPG pathway [ 5." ], "offsets": [ [ 0, 200 ] ] } ]
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[]
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1.0alpha7.train.240
992182
[ { "id": "1.0alpha7.train.240.sent", "type": "sentence", "text": [ "Full-length p21, which binds to both Cdk-cyclin and PCNA, effectively inhibits DNA replication (Fig. 7 A), whereas GST control protein is not inhibitory." ], "offsets": [ [ 0, 153 ] ] } ]
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[]
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1.0alpha7.train.241
23035520
[ { "id": "1.0alpha7.train.241.sent", "type": "sentence", "text": [ "Thus several different mutations that disrupt calcium binding and calcium-dependent syntaxin 1A binding to the C2A domain of synaptotagmin 1 do not reverse the inhibitory effect of microinjected C2A fragments on calcium-regulated secretion from PC12 cells." ], "offsets": [ [ 0, 256 ] ] } ]
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[]
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1.0alpha7.train.242
16028298
[ { "id": "1.0alpha7.train.242.sent", "type": "sentence", "text": [ "The relative proportion of TBP bound to GST-TADIV of the total present in the crude extract (Fig. 2) was found to be about 1/10 of that of the TAFIIs as determined by densitometric analysis (data not shown)." ], "offsets": [ [ 0, 207 ] ] } ]
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[]
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1.0alpha7.train.243
888051
[ { "id": "1.0alpha7.train.243.sent", "type": "sentence", "text": [ "These findings suggest a complex reciprocal relationship between regulation of adducin function by calmodulin binding and phosphorylation by PKA and PKC." ], "offsets": [ [ 0, 153 ] ] } ]
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[]
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1.0alpha7.train.244
18055440
[ { "id": "1.0alpha7.train.244.sent", "type": "sentence", "text": [ "At present, we do not know whether Arp11 binds directly to Arp1 or actin." ], "offsets": [ [ 0, 73 ] ] } ]
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[]
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[]
1.0alpha7.train.245
19306498
[ { "id": "1.0alpha7.train.245.sent", "type": "sentence", "text": [ "In vivo binding of hAxin to APC, -catenin and GSK3 ." ], "offsets": [ [ 0, 52 ] ] } ]
[ { "id": "1.0alpha7.train.245.ent0_0", "type": "protein", "text": [ "APC" ], "offsets": [ [ 28, 31 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "324" }, { "db_name": "hgnc", "db_id": "APC" } ] }, { "id": "1.0alpha7.train.245.ent1_0", "type": "protein", "text": [ "hAxin" ], "offsets": [ [ 19, 24 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "8312" }, { "db_name": "hgnc", "db_id": "AXIN1" }, { "db_name": "uniprot", "db_id": "O15169" } ] }, { "id": "1.0alpha7.train.245.ent2_0", "type": "protein", "text": [ "catenin" ], "offsets": [ [ 34, 41 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "1495" }, { "db_name": "hgnc", "db_id": "CTNNA1" }, { "db_name": "uniprot", "db_id": "P35221" } ] }, { "id": "1.0alpha7.train.245.ent3_0", "type": "protein", "text": [ "GSK3" ], "offsets": [ [ 46, 50 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "2931" }, { "db_name": "hgnc", "db_id": "GSK3A" }, { "db_name": "uniprot", "db_id": "P49840" } ] } ]
[]
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1.0alpha7.train.246
11440019
[ { "id": "1.0alpha7.train.246.sent", "type": "sentence", "text": [ "The ATP-bound form of Hsp70 binds and releases peptides rapidly, whereas the ADP-bound form binds and releases them slowly (Palleros et al., 1991 ; Schmid et al., 1994 ; Szabo et al., 1994 )." ], "offsets": [ [ 0, 191 ] ] } ]
[ { "id": "1.0alpha7.train.246.ent0_0", "type": "protein", "text": [ "Hsp70" ], "offsets": [ [ 22, 27 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "3308" }, { "db_name": "hgnc", "db_id": "HSPA4" }, { "db_name": "uniprot", "db_id": "P34932" } ] }, { "id": "1.0alpha7.train.246.ent1_0", "type": "protein", "text": [ "ADP-bound form" ], "offsets": [ [ 77, 91 ] ], "normalized": [] }, { "id": "1.0alpha7.train.246.ent2_0", "type": "protein", "text": [ "ATP-bound form of Hsp70" ], "offsets": [ [ 4, 27 ] ], "normalized": [] }, { "id": "1.0alpha7.train.246.ent3_0", "type": "chemical", "text": [ "ADP" ], "offsets": [ [ 77, 80 ] ], "normalized": [ { "db_name": "pubchem:compound", "db_id": "6022" } ] }, { "id": "1.0alpha7.train.246.ent4_0", "type": "chemical", "text": [ "ATP" ], "offsets": [ [ 4, 7 ] ], "normalized": [ { "db_name": "pubchem:compound", "db_id": "5957" } ] } ]
[]
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1.0alpha7.train.247
15546592
[ { "id": "1.0alpha7.train.247.sent", "type": "sentence", "text": [ "To confirm the specificity for interaction between EID-1 and Rb in vivo, we tested the binding of endogenous Rb to wild-type EID-1 versus the C180G mutation in transfected mammalian cells." ], "offsets": [ [ 0, 188 ] ] } ]
[ { "id": "1.0alpha7.train.247.ent0_0", "type": "protein", "text": [ "EID-1" ], "offsets": [ [ 51, 56 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "23741" }, { "db_name": "hgnc", "db_id": "EID1" }, { "db_name": "uniprot", "db_id": "Q9Y6B2" } ] }, { "id": "1.0alpha7.train.247.ent1_1", "type": "protein", "text": [ "EID-1" ], "offsets": [ [ 125, 130 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "23741" }, { "db_name": "hgnc", "db_id": "EID1" }, { "db_name": "uniprot", "db_id": "Q9Y6B2" } ] }, { "id": "1.0alpha7.train.247.ent2_0", "type": "protein", "text": [ "Rb" ], "offsets": [ [ 61, 63 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "5925" }, { "db_name": "hgnc", "db_id": "RB1" }, { "db_name": "uniprot", "db_id": "P06400" } ] }, { "id": "1.0alpha7.train.247.ent3_1", "type": "protein", "text": [ "Rb" ], "offsets": [ [ 109, 111 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "5925" }, { "db_name": "hgnc", "db_id": "RB1" }, { "db_name": "uniprot", "db_id": "P06400" } ] } ]
[]
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1.0alpha7.train.248
18222181
[ { "id": "1.0alpha7.train.248.sent", "type": "sentence", "text": [ "None of the mutations affected the binding of APC11 to APC2 (our unpublished data)." ], "offsets": [ [ 0, 83 ] ] } ]
[ { "id": "1.0alpha7.train.248.ent0_0", "type": "protein", "text": [ "APC2" ], "offsets": [ [ 55, 59 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "10297" }, { "db_name": "hgnc", "db_id": "APC2" } ] }, { "id": "1.0alpha7.train.248.ent1_0", "type": "protein", "text": [ "APC11" ], "offsets": [ [ 46, 51 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "51529" }, { "db_name": "hgnc", "db_id": "ANAPC11" }, { "db_name": "uniprot", "db_id": "Q9NYG5" } ] } ]
[]
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1.0alpha7.train.249
9490745
[ { "id": "1.0alpha7.train.249.sent", "type": "sentence", "text": [ "In parallel control experiments, all TRP tails failed to bind INAD from InaDP215 head extracts." ], "offsets": [ [ 0, 95 ] ] } ]
[ { "id": "1.0alpha7.train.249.ent0_0", "type": "protein-family", "text": [ "TRP" ], "offsets": [ [ 37, 40 ] ], "normalized": [ { "db_name": "interpro", "db_id": "IPR010308" } ] }, { "id": "1.0alpha7.train.249.ent1_0", "type": "protein", "text": [ "INAD" ], "offsets": [ [ 62, 66 ] ], "normalized": [ { "db_name": "uniprot", "db_id": "Q24008" } ] }, { "id": "1.0alpha7.train.249.ent2_0", "type": "gene", "text": [ "InaDP215" ], "offsets": [ [ 72, 80 ] ], "normalized": [] } ]
[]
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1.0alpha7.train.250
15406395
[ { "id": "1.0alpha7.train.250.sent", "type": "sentence", "text": [ "Interestingly, we saw strong binding of Gal4 to the GC-rich region, even in the absence of galactose, which agrees with previous work by others, showing that the transcriptional activity of Gal4 is not regulated by its DNA-binding activity but rather by the action of Gal80 and Gal3 (for examples, see references 7 and 31)." ], "offsets": [ [ 0, 323 ] ] } ]
[ { "id": "1.0alpha7.train.250.ent0_0", "type": "protein", "text": [ "Gal4" ], "offsets": [ [ 40, 44 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "3960" }, { "db_name": "hgnc", "db_id": "LGALS4" }, { "db_name": "uniprot", "db_id": "P56470" } ] }, { "id": "1.0alpha7.train.250.ent1_1", "type": "protein", "text": [ "Gal4" ], "offsets": [ [ 190, 194 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "3960" }, { "db_name": "hgnc", "db_id": "LGALS4" }, { "db_name": "uniprot", "db_id": "P56470" } ] }, { "id": "1.0alpha7.train.250.ent2_0", "type": "chemical", "text": [ "galactose" ], "offsets": [ [ 91, 100 ] ], "normalized": [ { "db_name": "pubchem:compound", "db_id": "6036" } ] }, { "id": "1.0alpha7.train.250.ent3_0", "type": "DNA", "text": [ "DNA" ], "offsets": [ [ 219, 222 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "25782" }, { "db_name": "hgnc", "db_id": "RAB3GAP2" }, { "db_name": "uniprot", "db_id": "Q9H2M9" } ] }, { "id": "1.0alpha7.train.250.ent4_0", "type": "protein", "text": [ "Gal3" ], "offsets": [ [ 278, 282 ] ], "normalized": [ { "db_name": "uniprot", "db_id": "P13045" } ] }, { "id": "1.0alpha7.train.250.ent5_0", "type": "protein", "text": [ "Gal80" ], "offsets": [ [ 268, 273 ] ], "normalized": [ { "db_name": "uniprot", "db_id": "P04387" } ] }, { "id": "1.0alpha7.train.250.ent6_0", "type": "DNA", "text": [ "GC-rich region" ], "offsets": [ [ 52, 66 ] ], "normalized": [] } ]
[]
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1.0alpha7.train.251
25223190
[ { "id": "1.0alpha7.train.251.sent", "type": "sentence", "text": [ "Blockade of either VASP binding to ActA ( Smith et al. 1996 ) or Profilin binding to VASP ( Kang et al. 1997 ) impairs Listeria motility, implying a role for Profilin in accelerating the actin-dependent motility." ], "offsets": [ [ 0, 212 ] ] } ]
[ { "id": "1.0alpha7.train.251.ent0_0", "type": "protein", "text": [ "ActA" ], "offsets": [ [ 35, 39 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "58" }, { "db_name": "hgnc", "db_id": "ACTA1" }, { "db_name": "uniprot", "db_id": "P68133" } ] }, { "id": "1.0alpha7.train.251.ent1_0", "type": "protein", "text": [ "VASP" ], "offsets": [ [ 19, 23 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "7408" }, { "db_name": "hgnc", "db_id": "VASP" }, { "db_name": "uniprot", "db_id": "P50552" } ] }, { "id": "1.0alpha7.train.251.ent2_1", "type": "protein", "text": [ "VASP" ], "offsets": [ [ 85, 89 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "7408" }, { "db_name": "hgnc", "db_id": "VASP" }, { "db_name": "uniprot", "db_id": "P50552" } ] }, { "id": "1.0alpha7.train.251.ent3_0", "type": "protein-family", "text": [ "actin" ], "offsets": [ [ 187, 192 ] ], "normalized": [ { "db_name": "pfam", "db_id": "PF00022" } ] }, { "id": "1.0alpha7.train.251.ent4_0", "type": "protein-family", "text": [ "Profilin" ], "offsets": [ [ 65, 73 ] ], "normalized": [ { "db_name": "interpro", "db_id": "IPR005455" } ] }, { "id": "1.0alpha7.train.251.ent5_1", "type": "protein-family", "text": [ "Profilin" ], "offsets": [ [ 158, 166 ] ], "normalized": [ { "db_name": "interpro", "db_id": "IPR005455" } ] } ]
[]
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1.0alpha7.train.252
5301491
[ { "id": "1.0alpha7.train.252.sent", "type": "sentence", "text": [ "The presence of similar motifs to those found in all known GTPases suggests that menin could similarly exhibit GTP binding activity as well as GTP-hydrolyzing activity." ], "offsets": [ [ 0, 168 ] ] } ]
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[]
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1.0alpha7.train.253
5301491
[ { "id": "1.0alpha7.train.253.sent", "type": "sentence", "text": [ "Menin Binds GTP" ], "offsets": [ [ 0, 15 ] ] } ]
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[]
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1.0alpha7.train.254
3099102
[ { "id": "1.0alpha7.train.254.sent", "type": "sentence", "text": [ "The finding that SLB can bind to Lhx3 and Lhx4 suggests a possible role in modulating transcription." ], "offsets": [ [ 0, 100 ] ] } ]
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[]
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1.0alpha7.train.255
5161992
[ { "id": "1.0alpha7.train.255.sent", "type": "sentence", "text": [ "We show that Hsp70 binding is regulated by the phosphorylation state of the turn motif, one of the two conserved carboxyl-terminal phosphorylation sites, and that Hsp70 binds mature PKC that has become dephosphorylated, rather than newly synthesized PKC that has yet to be phosphorylated." ], "offsets": [ [ 0, 288 ] ] } ]
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[]
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1.0alpha7.train.256
3367575
[ { "id": "1.0alpha7.train.256.sent", "type": "sentence", "text": [ "However, affinity chromatography experiments showed that Tm bound to acidic TnT with a greater affinity than to basic TnT, consistent with the significantly higher maximal binding of acidic TnT to Tm in solid phase binding assays." ], "offsets": [ [ 0, 230 ] ] } ]
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[]
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1.0alpha7.train.257
25166232
[ { "id": "1.0alpha7.train.257.sent", "type": "sentence", "text": [ "Ca2+-Dependent Binding of Syntaxin 1a to the C2A Domain Demonstrated by 1H-15N HSQC Spectroscopy" ], "offsets": [ [ 0, 96 ] ] } ]
[ { "id": "1.0alpha7.train.257.ent0_0", "type": "assay", "text": [ "1H-15N HSQC Spectroscopy" ], "offsets": [ [ 72, 96 ] ], "normalized": [] }, { "id": "1.0alpha7.train.257.ent1_0", "type": "chemical", "text": [ "Ca2+" ], "offsets": [ [ 0, 4 ] ], "normalized": [ { "db_name": "pubchem:compound", "db_id": "5460341" } ] }, { "id": "1.0alpha7.train.257.ent2_0", "type": "protein-domain", "text": [ "C2A" ], "offsets": [ [ 45, 48 ] ], "normalized": [] }, { "id": "1.0alpha7.train.257.ent3_0", "type": "protein", "text": [ "Syntaxin 1a" ], "offsets": [ [ 26, 37 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "6804" }, { "db_name": "hgnc", "db_id": "STX1A" }, { "db_name": "uniprot", "db_id": "Q16623" } ] } ]
[]
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1.0alpha7.train.258
563208
[ { "id": "1.0alpha7.train.258.sent", "type": "sentence", "text": [ "Adducin is a membrane skeleton protein originally described in human erythrocytes that promotes the binding of spectrin to actin and also binds directly to actin and bundles actin filaments." ], "offsets": [ [ 0, 190 ] ] } ]
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[]
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1.0alpha7.train.259
6233645
[ { "id": "1.0alpha7.train.259.sent", "type": "sentence", "text": [ "In conjunction with peptide-binding and genetic studies, atomic modeling of fimbrin binding to F-actin strongly suggests that the F-actin-binding residues in the CH domain are concentrated in its C-terminal portion ( 23)." ], "offsets": [ [ 0, 221 ] ] } ]
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1.0alpha7.train.260
5676496
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1.0alpha7.train.261
3506818
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1.0alpha7.train.262
4281828
[ { "id": "1.0alpha7.train.262.sent", "type": "sentence", "text": [ "Specific binding of Sp1 and Smad3 was inhibited with an excess of 100x unlabeled oligonucleotide ( Competitor)." ], "offsets": [ [ 0, 111 ] ] } ]
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[]
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1.0alpha7.train.263
3533947
[ { "id": "1.0alpha7.train.263.sent", "type": "sentence", "text": [ "This indicates that the binding of GSK-3beta to Axin is essential for its activity to degrade beta-catenin, consistent with the observation that AxindeltaGSK-3beta does not enhance the phosphorylation of beta-catenin even in the presence of APC-(1211-2075)." ], "offsets": [ [ 0, 257 ] ] } ]
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[]
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1.0alpha7.train.264
25751449
[ { "id": "1.0alpha7.train.264.sent", "type": "sentence", "text": [ "N.N. Dewji and S.J. Singer, Specific transcellular binding between membrane proteins crucial to Alzheimer disease." ], "offsets": [ [ 0, 114 ] ] } ]
[]
[]
[]
[]
1.0alpha7.train.265
16335607
[ { "id": "1.0alpha7.train.265.sent", "type": "sentence", "text": [ "We tested seven mAbs derived from an HIV-2-infected human for their ability to inhibit SIVmac239 gp120 binding to CCR5rh in HEK293 cells in the presence and absence of sCD4." ], "offsets": [ [ 0, 173 ] ] } ]
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[]
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1.0alpha7.train.266
3181409
[ { "id": "1.0alpha7.train.266.sent", "type": "sentence", "text": [ "After extensive washing, the amount of MyD118/Gadd45 protein bound to PCNA was assessed using either MyD118- or Gadd45-specific antibodies, which, in turn, were reacted with HRP-coupled secondary antibody." ], "offsets": [ [ 0, 205 ] ] } ]
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[]
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1.0alpha7.train.267
15268425
[ { "id": "1.0alpha7.train.267.sent", "type": "sentence", "text": [ "Given the observation that CRT binds to SL structures with GC-rich stems (7, 16, 24, 27), we searched for the secondary structures with GC-rich stems within the C/EBPα mRNA and found two possible SL organizations containing GC-rich regions within the stem (Fig. ​7B)." ], "offsets": [ [ 0, 267 ] ] } ]
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[]
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[]
1.0alpha7.train.268
25166292
[ { "id": "1.0alpha7.train.268.sent", "type": "sentence", "text": [ "These observations strongly suggest that electrostatic interactions provide a main driving force for the Ca2+-dependent binding of the C2A domain to syntaxin." ], "offsets": [ [ 0, 158 ] ] } ]
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[]
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1.0alpha7.train.269
20479913
[ { "id": "1.0alpha7.train.269.sent", "type": "sentence", "text": [ "In this report, we show that AlF-C1 and AlF-C2 bind directly to Orc1, a subunit of ORC, and discuss that in mammalian cells, sequence-specific DNA-binding proteins might be involved in recruiting ORC to regulate replication initiation and/or transcription repression." ], "offsets": [ [ 0, 267 ] ] } ]
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[]
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1.0alpha7.train.270
15937374
[ { "id": "1.0alpha7.train.270.sent", "type": "sentence", "text": [ "It has been shown that APC makes a complex with beta-catenin and that the phosphorylation of APC by GSK-3beta increases the binding of APC to beta-catenin ( 37)." ], "offsets": [ [ 0, 161 ] ] } ]
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[]
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1.0alpha7.train.271
3129207
[ { "id": "1.0alpha7.train.271.sent", "type": "sentence", "text": [ "Interestingly, dTAFII110 also bound GST-IIAτ more abundantly than it bound to GST-αβ (Fig.4 C, lane 4)." ], "offsets": [ [ 0, 103 ] ] } ]
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[]
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1.0alpha7.train.272
19640896
[ { "id": "1.0alpha7.train.272.sent", "type": "sentence", "text": [ "Hes6 binds to an Enhancer of Split E box and mediates transcriptional repression" ], "offsets": [ [ 0, 80 ] ] } ]
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[]
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1.0alpha7.train.273
19640896
[ { "id": "1.0alpha7.train.273.sent", "type": "sentence", "text": [ "Hes6 has been shown to act indirectly by binding other orange domain-containing proteins, rather than by acting as a DNA-binding transcription factor (Bae et al., 2000; Koyano-Nakagawa et al., 2000)." ], "offsets": [ [ 0, 199 ] ] } ]
[ { "id": "1.0alpha7.train.273.ent0_0", "type": "DNA", "text": [ "DNA" ], "offsets": [ [ 117, 120 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "25782" }, { "db_name": "hgnc", "db_id": "RAB3GAP2" }, { "db_name": "uniprot", "db_id": "Q9H2M9" } ] }, { "id": "1.0alpha7.train.273.ent1_0", "type": "protein", "text": [ "Hes6" ], "offsets": [ [ 0, 4 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "55502" }, { "db_name": "hgnc", "db_id": "HES6" }, { "db_name": "uniprot", "db_id": "B8ZZP9" } ] } ]
[]
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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 ] ] } ]
[ { "id": "1.0alpha7.train.274.ent0_0", "type": "protein-family", "text": [ "dynein" ], "offsets": [ [ 45, 51 ] ], "normalized": [] }, { "id": "1.0alpha7.train.274.ent1_1", "type": "protein-family", "text": [ "dynein" ], "offsets": [ [ 172, 178 ] ], "normalized": [] }, { "id": "1.0alpha7.train.274.ent2_0", "type": "protein", "text": [ "dynein binding subunit" ], "offsets": [ [ 172, 194 ] ], "normalized": [] }, { "id": "1.0alpha7.train.274.ent3_0", "type": "protein", "text": [ "p150 Glued" ], "offsets": [ [ 197, 207 ] ], "normalized": [] }, { "id": "1.0alpha7.train.274.ent4_0", "type": "protein-complex", "text": [ "dynactin" ], "offsets": [ [ 137, 145 ] ], "normalized": [] } ]
[]
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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 ] ] } ]
[ { "id": "1.0alpha7.train.278.ent0_0", "type": "protein", "text": [ "BMP-7" ], "offsets": [ [ 18, 23 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "655" }, { "db_name": "hgnc", "db_id": "BMP7" }, { "db_name": "uniprot", "db_id": "P18075" } ] }, { "id": "1.0alpha7.train.278.ent1_0", "type": "cell", "text": [ "ROS 17/2" ], "offsets": [ [ 35, 43 ] ], "normalized": [] } ]
[]
[ { "id": "1.0alpha7.train.278.coref0", "entity_ids": [ "1.0alpha7.train.278.ent0_0" ] }, { "id": "1.0alpha7.train.278.coref1", "entity_ids": [ "1.0alpha7.train.278.ent1_0" ] } ]
[]
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 ] ] } ]
[ { "id": "1.0alpha7.train.279.ent0_0", "type": "DNA", "text": [ "ESEs" ], "offsets": [ [ 43, 47 ] ], "normalized": [] }, { "id": "1.0alpha7.train.279.ent1_0", "type": "protein-family", "text": [ "SR" ], "offsets": [ [ 183, 185 ] ], "normalized": [] }, { "id": "1.0alpha7.train.279.ent2_0", "type": "protein", "text": [ "U2AF65" ], "offsets": [ [ 354, 360 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "11338" }, { "db_name": "hgnc", "db_id": "U2AF2" }, { "db_name": "uniprot", "db_id": "P26368" } ] }, { "id": "1.0alpha7.train.279.ent3_0", "type": "protein-complex", "text": [ "U2AF" ], "offsets": [ [ 322, 326 ] ], "normalized": [] }, { "id": "1.0alpha7.train.279.ent4_0", "type": "protein", "text": [ "U2AF35" ], "offsets": [ [ 51, 57 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "7307" }, { "db_name": "hgnc", "db_id": "U2AF1" }, { "db_name": "uniprot", "db_id": "Q01081" } ] }, { "id": "1.0alpha7.train.279.ent5_1", "type": "protein", "text": [ "U2AF35" ], "offsets": [ [ 270, 276 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "7307" }, { "db_name": "hgnc", "db_id": "U2AF1" }, { "db_name": "uniprot", "db_id": "Q01081" } ] }, { "id": "1.0alpha7.train.279.ent6_0", "type": "DNA", "text": [ "Py tract" ], "offsets": [ [ 376, 384 ] ], "normalized": [] } ]
[]
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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 ] ] } ]
[ { "id": "1.0alpha7.train.280.ent0_0", "type": "protein", "text": [ "HtsRC" ], "offsets": [ [ 47, 52 ] ], "normalized": [] }, { "id": "1.0alpha7.train.280.ent1_1", "type": "protein", "text": [ "HtsRC" ], "offsets": [ [ 86, 91 ] ], "normalized": [] }, { "id": "1.0alpha7.train.280.ent2_0", "type": "protein-family", "text": [ "actin" ], "offsets": [ [ 30, 35 ] ], "normalized": [ { "db_name": "pfam", "db_id": "PF00022" } ] }, { "id": "1.0alpha7.train.280.ent3_1", "type": "protein-family", "text": [ "actin" ], "offsets": [ [ 113, 118 ] ], "normalized": [ { "db_name": "pfam", "db_id": "PF00022" } ] } ]
[]
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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 ] ] } ]
[ { "id": "1.0alpha7.train.281.ent0_0", "type": "protein", "text": [ "Ubc9" ], "offsets": [ [ 8, 12 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "7329" }, { "db_name": "hgnc", "db_id": "UBE2I" }, { "db_name": "uniprot", "db_id": "P63279" } ] }, { "id": "1.0alpha7.train.281.ent1_1", "type": "protein", "text": [ "Ubc9" ], "offsets": [ [ 95, 99 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "7329" }, { "db_name": "hgnc", "db_id": "UBE2I" }, { "db_name": "uniprot", "db_id": "P63279" } ] }, { "id": "1.0alpha7.train.281.ent2_0", "type": "protein-motif", "text": [ "NLS" ], "offsets": [ [ 27, 30 ] ], "normalized": [] } ]
[]
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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 ] ] } ]
[ { "id": "1.0alpha7.train.282.ent0_0", "type": "protein", "text": [ "dSlo" ], "offsets": [ [ 96, 100 ] ], "normalized": [ { "db_name": "uniprot", "db_id": "Q03720" } ] }, { "id": "1.0alpha7.train.282.ent1_0", "type": "protein", "text": [ "PKAc" ], "offsets": [ [ 105, 109 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "5566" }, { "db_name": "hgnc", "db_id": "PRKACA" }, { "db_name": "uniprot", "db_id": "P17612" } ] } ]
[]
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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
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[]
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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 ] ] } ]
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[]
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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 ] ] } ]
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[]
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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 ] ] } ]
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[]
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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.289
4211455
[ { "id": "1.0alpha7.train.289.sent", "type": "sentence", "text": [ "Experiments using equilibrium dialysis (39) and protein fluorescence quenching (11) showed that NADH binds to isolated R. rubrum dI protein with a K d≈ 20 μM. " ], "offsets": [ [ 0, 159 ] ] } ]
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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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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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