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1.0alpha7.train.576
15191263
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1.0alpha7.train.577
15977843
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1.0alpha7.train.578
3405736
[ { "id": "1.0alpha7.train.578.sent", "type": "sentence", "text": [ " Residues implicated in catalysis are marked with asterisks, and Lys101 involved in binding of ATP and CoA is marked with a triangle. " ], "offsets": [ [ 0, 139 ] ] } ]
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[]
1.0alpha7.train.579
18008472
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1.0alpha7.train.580
5135328
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1.0alpha7.train.581
19446424
[ { "id": "1.0alpha7.train.581.sent", "type": "sentence", "text": [ " Several TRP channels bind to calmodulin [16] , raising the question as to whether activation of TRPM5 by Ca2+ occurs through calmodulin. " ], "offsets": [ [ 0, 145 ] ] } ]
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[]
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1.0alpha7.train.582
5860687
[ { "id": "1.0alpha7.train.582.sent", "type": "sentence", "text": [ " The corepressor protein CtBP, the PcG proteins HPC2 and BMI-1, and HDAC1 (or HDAC2) bind to the MLL repression domain. " ], "offsets": [ [ 0, 127 ] ] } ]
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[]
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1.0alpha7.train.583
8939507
[ { "id": "1.0alpha7.train.583.sent", "type": "sentence", "text": [ " As shown in Figure 8B, the 32P label was gradually lost during incubation, suggesting that the ATP bound to actin was hydrolyzed, most likely by the ATPase activity of actin itself. " ], "offsets": [ [ 0, 191 ] ] } ]
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1.0alpha7.train.584
1778461
[ { "id": "1.0alpha7.train.584.sent", "type": "sentence", "text": [ "Based on a sequence comparison between IP4-sensitive and -insensitive isoforms (Figs. 3 and 4 A) and deletion or mutational analysis of synaptotagmin III (Figs. 4 and 5), we propose that the primitive form of synaptotagmin originally bound IP4 and that, during the diversification of synaptotagmin in vertebrates, some isoforms (III, V, and X) lost their IP4 binding activity as a consequence of several amino acid substitutions mainly in the C-terminal region of the C2B domain, but not in the putative IP4-binding site itself." ], "offsets": [ [ 0, 528 ] ] } ]
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[]
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"1.0alpha7.train.584.ent6_0", "normalized": [] }, { "id": "1.0alpha7.train.584.rel0s1.0alpha7.train.584.ent4_1.o1.0alpha7.train.584.ent7_1", "type": "bind", "arg1_id": "1.0alpha7.train.584.ent4_1", "arg2_id": "1.0alpha7.train.584.ent7_1", "normalized": [] }, { "id": "1.0alpha7.train.584.rel0s1.0alpha7.train.584.ent4_1.o1.0alpha7.train.584.ent8_2", "type": "bind", "arg1_id": "1.0alpha7.train.584.ent4_1", "arg2_id": "1.0alpha7.train.584.ent8_2", "normalized": [] }, { "id": "1.0alpha7.train.584.rel0s1.0alpha7.train.584.ent4_1.o1.0alpha7.train.584.ent9_3", "type": "bind", "arg1_id": "1.0alpha7.train.584.ent4_1", "arg2_id": "1.0alpha7.train.584.ent9_3", "normalized": [] }, { "id": "1.0alpha7.train.584.rel0s1.0alpha7.train.584.ent5_2.o1.0alpha7.train.584.ent6_0", "type": "bind", "arg1_id": "1.0alpha7.train.584.ent5_2", "arg2_id": "1.0alpha7.train.584.ent6_0", "normalized": [] }, { "id": "1.0alpha7.train.584.rel0s1.0alpha7.train.584.ent5_2.o1.0alpha7.train.584.ent7_1", "type": "bind", "arg1_id": "1.0alpha7.train.584.ent5_2", "arg2_id": "1.0alpha7.train.584.ent7_1", "normalized": [] }, { "id": "1.0alpha7.train.584.rel0s1.0alpha7.train.584.ent5_2.o1.0alpha7.train.584.ent8_2", "type": "bind", "arg1_id": "1.0alpha7.train.584.ent5_2", "arg2_id": "1.0alpha7.train.584.ent8_2", "normalized": [] }, { "id": "1.0alpha7.train.584.rel0s1.0alpha7.train.584.ent5_2.o1.0alpha7.train.584.ent9_3", "type": "bind", "arg1_id": "1.0alpha7.train.584.ent5_2", "arg2_id": "1.0alpha7.train.584.ent9_3", "normalized": [] }, { "id": "1.0alpha7.train.584.rel1s1.0alpha7.train.584.ent0_0.o1.0alpha7.train.584.ent6_0", "type": "bind", "arg1_id": "1.0alpha7.train.584.ent0_0", "arg2_id": "1.0alpha7.train.584.ent6_0", "normalized": [] }, { "id": "1.0alpha7.train.584.rel1s1.0alpha7.train.584.ent0_0.o1.0alpha7.train.584.ent7_1", "type": "bind", "arg1_id": "1.0alpha7.train.584.ent0_0", "arg2_id": "1.0alpha7.train.584.ent7_1", "normalized": [] }, { "id": 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"arg1_id": "1.0alpha7.train.584.ent2_0", "arg2_id": "1.0alpha7.train.584.ent9_3", "normalized": [] }, { "id": "1.0alpha7.train.584.rel2s1.0alpha7.train.584.ent6_0.o1.0alpha7.train.584.ent10_0", "type": "bind", "arg1_id": "1.0alpha7.train.584.ent6_0", "arg2_id": "1.0alpha7.train.584.ent10_0", "normalized": [] }, { "id": "1.0alpha7.train.584.rel2s1.0alpha7.train.584.ent7_1.o1.0alpha7.train.584.ent10_0", "type": "bind", "arg1_id": "1.0alpha7.train.584.ent7_1", "arg2_id": "1.0alpha7.train.584.ent10_0", "normalized": [] }, { "id": "1.0alpha7.train.584.rel2s1.0alpha7.train.584.ent8_2.o1.0alpha7.train.584.ent10_0", "type": "bind", "arg1_id": "1.0alpha7.train.584.ent8_2", "arg2_id": "1.0alpha7.train.584.ent10_0", "normalized": [] }, { "id": "1.0alpha7.train.584.rel2s1.0alpha7.train.584.ent9_3.o1.0alpha7.train.584.ent10_0", "type": "bind", "arg1_id": "1.0alpha7.train.584.ent9_3", "arg2_id": "1.0alpha7.train.584.ent10_0", "normalized": [] }, { "id": "1.0alpha7.train.584.rel3s1.0alpha7.train.584.ent6_0.o1.0alpha7.train.584.ent11_0", "type": "bind", "arg1_id": "1.0alpha7.train.584.ent6_0", "arg2_id": "1.0alpha7.train.584.ent11_0", "normalized": [] }, { "id": "1.0alpha7.train.584.rel3s1.0alpha7.train.584.ent7_1.o1.0alpha7.train.584.ent11_0", "type": "bind", "arg1_id": "1.0alpha7.train.584.ent7_1", "arg2_id": "1.0alpha7.train.584.ent11_0", "normalized": [] }, { "id": "1.0alpha7.train.584.rel3s1.0alpha7.train.584.ent8_2.o1.0alpha7.train.584.ent11_0", "type": "bind", "arg1_id": "1.0alpha7.train.584.ent8_2", "arg2_id": "1.0alpha7.train.584.ent11_0", "normalized": [] }, { "id": "1.0alpha7.train.584.rel3s1.0alpha7.train.584.ent9_3.o1.0alpha7.train.584.ent11_0", "type": "bind", "arg1_id": "1.0alpha7.train.584.ent9_3", "arg2_id": "1.0alpha7.train.584.ent11_0", "normalized": [] } ]
1.0alpha7.train.585
15693525
[ { "id": "1.0alpha7.train.585.sent", "type": "sentence", "text": [ "NES sequences bind to CRM1 with different affinities." ], "offsets": [ [ 0, 54 ] ] } ]
[ { "id": "1.0alpha7.train.585.ent0_0", "type": "protein", "text": [ "CRM1" ], "offsets": [ [ 23, 27 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "7514" }, { "db_name": "hgnc", "db_id": "XPO1" }, { "db_name": "uniprot", "db_id": "O14980" } ] }, { "id": "1.0alpha7.train.585.ent1_0", "type": "protein-region", "text": [ "NES" ], "offsets": [ [ 0, 3 ] ], "normalized": [] } ]
[]
[ { "id": "1.0alpha7.train.585.coref0", "entity_ids": [ "1.0alpha7.train.585.ent0_0" ] }, { "id": "1.0alpha7.train.585.coref1", "entity_ids": [ "1.0alpha7.train.585.ent1_0" ] } ]
[]
1.0alpha7.train.586
3414531
[ { "id": "1.0alpha7.train.586.sent", "type": "sentence", "text": [ " However, this mutation abolished both the binding of soluble DI to DII-III in the presence of scuPA and the synergistic activation of scuPA mediated by DI and wild type DII-DIII. " ], "offsets": [ [ 0, 185 ] ] } ]
[ { "id": "1.0alpha7.train.586.ent0_0", "type": "protein-domain", "text": [ "DII-III" ], "offsets": [ [ 70, 77 ] ], "normalized": [] }, { "id": "1.0alpha7.train.586.ent1_0", "type": "protein", "text": [ "scuPA" ], "offsets": [ [ 97, 102 ] ], "normalized": [] }, { "id": "1.0alpha7.train.586.ent2_1", "type": "protein", "text": [ "scuPA" ], "offsets": [ [ 137, 142 ] ], "normalized": [] }, { "id": "1.0alpha7.train.586.ent3_0", "type": "protein-domain", "text": [ "DI" ], "offsets": [ [ 63, 65 ] ], "normalized": [] }, { "id": "1.0alpha7.train.586.ent4_1", "type": "protein-domain", "text": [ "DI" ], "offsets": [ [ 156, 158 ] ], "normalized": [] } ]
[]
[ { "id": "1.0alpha7.train.586.coref0", "entity_ids": [ "1.0alpha7.train.586.ent0_0" ] }, { "id": "1.0alpha7.train.586.coref1", "entity_ids": [ "1.0alpha7.train.586.ent1_0", "1.0alpha7.train.586.ent2_1" ] }, { "id": "1.0alpha7.train.586.coref2", "entity_ids": [ "1.0alpha7.train.586.ent3_0", "1.0alpha7.train.586.ent4_1" ] } ]
[ { "id": "1.0alpha7.train.586.rel0s1.0alpha7.train.586.ent0_0.o1.0alpha7.train.586.ent3_0", "type": "bind", "arg1_id": "1.0alpha7.train.586.ent0_0", "arg2_id": "1.0alpha7.train.586.ent3_0", "normalized": [] }, { "id": "1.0alpha7.train.586.rel0s1.0alpha7.train.586.ent0_0.o1.0alpha7.train.586.ent4_1", "type": "bind", "arg1_id": "1.0alpha7.train.586.ent0_0", "arg2_id": "1.0alpha7.train.586.ent4_1", "normalized": [] } ]
1.0alpha7.train.587
22269986
[ { "id": "1.0alpha7.train.587.sent", "type": "sentence", "text": [ "Electrophoretic mobility shift assay of HMG-D binding to the TAR RNA at (A) 20°C or (B) 4°C. " ], "offsets": [ [ 0, 93 ] ] } ]
[ { "id": "1.0alpha7.train.587.ent0_0", "type": "protein", "text": [ "HMG-D" ], "offsets": [ [ 40, 45 ] ], "normalized": [ { "db_name": "uniprot", "db_id": "Q05783" } ] }, { "id": "1.0alpha7.train.587.ent1_0", "type": "RNA", "text": [ "TAR RNA" ], "offsets": [ [ 61, 68 ] ], "normalized": [] } ]
[]
[ { "id": "1.0alpha7.train.587.coref0", "entity_ids": [ "1.0alpha7.train.587.ent0_0" ] }, { "id": "1.0alpha7.train.587.coref1", "entity_ids": [ "1.0alpha7.train.587.ent1_0" ] } ]
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1.0alpha7.train.588
7032085
[ { "id": "1.0alpha7.train.588.sent", "type": "sentence", "text": [ " Pontin52 binds beta-catenin in the region of Armadillo repeats 2-5 and, more importantly, also binds the TATA box binding protein. " ], "offsets": [ [ 0, 136 ] ] } ]
[ { "id": "1.0alpha7.train.588.ent0_0", "type": "protein-region", "text": [ "Armadillo repeats" ], "offsets": [ [ 48, 65 ] ], "normalized": [] }, { "id": "1.0alpha7.train.588.ent1_0", "type": "protein", "text": [ "Pontin52" ], "offsets": [ [ 1, 9 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "8607" }, { "db_name": "hgnc", "db_id": "RUVBL1" }, { "db_name": "uniprot", "db_id": "P60122" } ] }, { "id": "1.0alpha7.train.588.ent2_0", "type": "DNA", "text": [ "TATA box" ], "offsets": [ [ 109, 117 ] ], "normalized": [] }, { "id": "1.0alpha7.train.588.ent3_0", "type": "protein", "text": [ "TATA box binding protein" ], "offsets": [ [ 109, 133 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "6908" }, { "db_name": "hgnc", "db_id": "TBP" }, { "db_name": "uniprot", "db_id": "P20226" } ] }, { "id": "1.0alpha7.train.588.ent4_0", "type": "protein-family", "text": [ "beta-catenin" ], "offsets": [ [ 17, 29 ] ], "normalized": [ { "db_name": "interpro", "db_id": "IPR013284" } ] } ]
[]
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1.0alpha7.train.589
11699808
[ { "id": "1.0alpha7.train.589.sent", "type": "sentence", "text": [ " Also, we have been unable to observe consistent binding between Armadillo and Tsh in vitro (unpublished results), which suggests that the interaction between the two proteins would not be strong enough to account for Tsh recruitment. " ], "offsets": [ [ 0, 240 ] ] } ]
[ { "id": "1.0alpha7.train.589.ent0_0", "type": "protein-motif", "text": [ "Armadillo" ], "offsets": [ [ 66, 75 ] ], "normalized": [ { "db_name": "interpro", "db_id": "IPR000225" } ] }, { "id": "1.0alpha7.train.589.ent1_0", "type": "protein", "text": [ "Tsh" ], "offsets": [ [ 81, 84 ] ], "normalized": [ { "db_name": "uniprot", "db_id": "Q47692" } ] }, { "id": "1.0alpha7.train.589.ent2_1", "type": "protein", "text": [ "Tsh" ], "offsets": [ [ 222, 225 ] ], "normalized": [ { "db_name": "uniprot", "db_id": "Q47692" } ] } ]
[]
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1.0alpha7.train.590
11544085
[ { "id": "1.0alpha7.train.590.sent", "type": "sentence", "text": [ "These experiments suggest that RBP binds either Notch or SHARP exclusively." ], "offsets": [ [ 0, 77 ] ] } ]
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[]
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1.0alpha7.train.591
9801074
[ { "id": "1.0alpha7.train.591.sent", "type": "sentence", "text": [ "Disintegrin peptides from snake venom are known to bind to platelet integrin αIIbβ3 (GP IIb/IIIa) and prevent binding of fibrinogen and subsequent clotting (Adler et al., 1991; Beer et al., 1992)." ], "offsets": [ [ 0, 196 ] ] } ]
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[]
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1.0alpha7.train.592
20321780
[ { "id": "1.0alpha7.train.592.sent", "type": "sentence", "text": [ "Like VP16, ZF binds to HCF but not to the mutant HCF(P134S), as determined by GST pull-down assay (A and B) and by mammalian two-hybrid assay (C)." ], "offsets": [ [ 0, 146 ] ] } ]
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[]
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1.0alpha7.train.593
2790039
[ { "id": "1.0alpha7.train.593.sent", "type": "sentence", "text": [ "Numerous putative Rho effectors have been identified; PKN1 (4, 5), Rho-kinase/ROKα/ROCK II (6-8), myosin-binding subunit of myosin phosphatase (9), mDia1 (10), citron (11), citron kinase (12), rhophilin, rhotekin (11), Kv1.2 (13), and phospholipase D (14)." ], "offsets": [ [ 0, 256 ] ] } ]
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[]
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1.0alpha7.train.594
17987364
[ { "id": "1.0alpha7.train.594.sent", "type": "sentence", "text": [ "Reconstitution of the binding of alpha-actinin to VPMs in the presence of actin stress fibers." ], "offsets": [ [ 0, 97 ] ] } ]
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[]
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1.0alpha7.train.595
15031471
[ { "id": "1.0alpha7.train.595.sent", "type": "sentence", "text": [ " Consistent with this, both the wild-type and S101A mutant 4E-BP1 proteins were released from eIF4E in response to insulin, allowing insulin to promote assembly of eIF4F complexes, observed as increased binding of eIF4G to eIF4E (Fig. 2D). " ], "offsets": [ [ 0, 247 ] ] } ]
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[]
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1.0alpha7.train.596
9003371
[ { "id": "1.0alpha7.train.596.sent", "type": "sentence", "text": [ "Consistent with this idea, we have observed that in the presence of EXD and the appropriate HOX protein, HTH can bind some EXD-HOX binding sites, but not others (our unpublished data)." ], "offsets": [ [ 0, 184 ] ] } ]
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[]
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1.0alpha7.train.597
22878078
[ { "id": "1.0alpha7.train.597.sent", "type": "sentence", "text": [ " The sequence analysis also indicates that this region may be the target of a complex regulation by a number of other transcription factors; specifically, two putative SP1 binding sites exist that flank the AP-2 core sequence. " ], "offsets": [ [ 0, 231 ] ] } ]
[ { "id": "1.0alpha7.train.597.ent0_0", "type": "protein", "text": [ "SP1" ], "offsets": [ [ 170, 173 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "6667" }, { "db_name": "hgnc", "db_id": "SP1" }, { "db_name": "uniprot", "db_id": "P08047" } ] }, { "id": "1.0alpha7.train.597.ent1_0", "type": "protein-complex", "text": [ "AP-2" ], "offsets": [ [ 210, 214 ] ], "normalized": [] }, { "id": "1.0alpha7.train.597.ent2_0", "type": "DNA", "text": [ "SP1 binding sites" ], "offsets": [ [ 170, 187 ] ], "normalized": [] } ]
[]
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1.0alpha7.train.598
11332822
[ { "id": "1.0alpha7.train.598.sent", "type": "sentence", "text": [ "These dynamic changes in the binding of PC and TRX to PREs/REs and promoters of target genes may point to important transitions necessary for the establishment of the cellular memory mechanism supported by the PcG and trxG." ], "offsets": [ [ 0, 227 ] ] } ]
[ { "id": "1.0alpha7.train.598.ent0_0", "type": "protein", "text": [ "TRX" ], "offsets": [ [ 49, 52 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "7295" }, { "db_name": "hgnc", "db_id": "TXN" }, { "db_name": "uniprot", "db_id": "P10599" } ] }, { "id": "1.0alpha7.train.598.ent1_0", "type": "DNA", "text": [ "promoters" ], "offsets": [ [ 69, 78 ] ], "normalized": [] }, { "id": "1.0alpha7.train.598.ent2_0", "type": "protein", "text": [ "PC" ], "offsets": [ [ 41, 43 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "5091" }, { "db_name": "hgnc", "db_id": "PC" } ] }, { "id": "1.0alpha7.train.598.ent3_0", "type": "protein-family", "text": [ "trxG" ], "offsets": [ [ 222, 226 ] ], "normalized": [] }, { "id": "1.0alpha7.train.598.ent4_0", "type": "DNA", "text": [ "PREs/REs" ], "offsets": [ [ 56, 64 ] ], "normalized": [] }, { "id": "1.0alpha7.train.598.ent5_0", "type": "protein-family", "text": [ "PcG" ], "offsets": [ [ 214, 217 ] ], "normalized": [] } ]
[]
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1.0alpha7.train.599
11310237
[ { "id": "1.0alpha7.train.599.sent", "type": "sentence", "text": [ " Previous studies have shown that Grb2 binding to Shc is important for the transmission of integrin-stimulated signals to ERK2 (Wary et al., 1996 ; Mainiero et al., 1997 ; Schlaepfer et al., 1998 ). " ], "offsets": [ [ 0, 209 ] ] } ]
[ { "id": "1.0alpha7.train.599.ent0_0", "type": "protein", "text": [ "Shc" ], "offsets": [ [ 52, 55 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "6464" }, { "db_name": "hgnc", "db_id": "SHC1" }, { "db_name": "uniprot", "db_id": "P29353" } ] }, { "id": "1.0alpha7.train.599.ent1_0", "type": "protein", "text": [ "Grb2" ], "offsets": [ [ 35, 39 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "2885" }, { "db_name": "hgnc", "db_id": "GRB2" }, { "db_name": "uniprot", "db_id": "P62993" } ] }, { "id": "1.0alpha7.train.599.ent2_0", "type": "protein", "text": [ "ERK2" ], "offsets": [ [ 125, 129 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "5594" }, { "db_name": "hgnc", "db_id": "MAPK1" }, { "db_name": "uniprot", "db_id": "P28482" } ] }, { "id": "1.0alpha7.train.599.ent3_0", "type": "protein-family", "text": [ "integrin" ], "offsets": [ [ 93, 101 ] ], "normalized": [ { "db_name": "interpro", "db_id": "IPR032695" } ] } ]
[]
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1.0alpha7.train.600
11332746
[ { "id": "1.0alpha7.train.600.sent", "type": "sentence", "text": [ "To determine when TRX binds to the BX-C and whether its binding exhibits temporal changes during early development when PcG silencing is established, in vivo fixed chromatin was prepared from embryos of three different stages; 0-2, 2-5 and 5-8 h after egg laying." ], "offsets": [ [ 0, 263 ] ] } ]
[ { "id": "1.0alpha7.train.600.ent0_0", "type": "protein", "text": [ "TRX" ], "offsets": [ [ 18, 21 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "7295" }, { "db_name": "hgnc", "db_id": "TXN" }, { "db_name": "uniprot", "db_id": "P10599" } ] }, { "id": "1.0alpha7.train.600.ent1_0", "type": "protein-complex", "text": [ "BX-C" ], "offsets": [ [ 35, 39 ] ], "normalized": [] }, { "id": "1.0alpha7.train.600.ent2_0", "type": "protein-family", "text": [ "PcG" ], "offsets": [ [ 120, 123 ] ], "normalized": [] } ]
[]
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1.0alpha7.train.601
23643812
[ { "id": "1.0alpha7.train.601.sent", "type": "sentence", "text": [ " Using co-immunoprecipitation approaches, we showed that dSlo binds only to free PKAc but not to the PKA holoenzyme, and that both PKA regulatory subunit and PKI inhibit the association between dSlo and PKAc. " ], "offsets": [ [ 0, 217 ] ] } ]
[ { "id": "1.0alpha7.train.601.ent0_0", "type": "protein", "text": [ "dSlo" ], "offsets": [ [ 58, 62 ] ], "normalized": [ { "db_name": "uniprot", "db_id": "Q03720" } ] }, { "id": "1.0alpha7.train.601.ent1_1", "type": "protein", "text": [ "dSlo" ], "offsets": [ [ 200, 204 ] ], "normalized": [ { "db_name": "uniprot", "db_id": "Q03720" } ] }, { "id": "1.0alpha7.train.601.ent2_0", "type": "protein-family", "text": [ "PKI" ], "offsets": [ [ 163, 166 ] ], "normalized": [ { "db_name": "interpro", "db_id": "IPR004171" } ] }, { "id": "1.0alpha7.train.601.ent3_0", "type": "protein-complex", "text": [ "PKA regulatory subunit" ], "offsets": [ [ 135, 157 ] ], "normalized": [] }, { "id": "1.0alpha7.train.601.ent4_0", "type": "protein-complex", "text": [ "PKA holoenzyme" ], "offsets": [ [ 104, 118 ] ], "normalized": [] }, { "id": "1.0alpha7.train.601.ent5_0", "type": "protein", "text": [ "PKAc" ], "offsets": [ [ 83, 87 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "5566" }, { "db_name": "hgnc", "db_id": "PRKACA" }, { "db_name": "uniprot", "db_id": "P17612" } ] }, { "id": "1.0alpha7.train.601.ent6_1", "type": "protein", "text": [ "PKAc" ], "offsets": [ [ 210, 214 ] ], "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.602
1712717
[ { "id": "1.0alpha7.train.602.sent", "type": "sentence", "text": [ " However, unlike SHC, binding of Numb PTB domain to LNX does not require tyrosine phosphorylation. " ], "offsets": [ [ 0, 103 ] ] } ]
[ { "id": "1.0alpha7.train.602.ent0_0", "type": "protein-family", "text": [ "SHC" ], "offsets": [ [ 18, 21 ] ], "normalized": [ { "db_name": "interpro", "db_id": "IPR029586" } ] }, { "id": "1.0alpha7.train.602.ent1_0", "type": "protein-domain", "text": [ "PTB" ], "offsets": [ [ 40, 43 ] ], "normalized": [ { "db_name": "interpro", "db_id": "IPR006020" } ] }, { "id": "1.0alpha7.train.602.ent2_0", "type": "protein", "text": [ "Numb" ], "offsets": [ [ 35, 39 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "8650" }, { "db_name": "hgnc", "db_id": "NUMB" }, { "db_name": "uniprot", "db_id": "P49757" } ] }, { "id": "1.0alpha7.train.602.ent3_0", "type": "protein", "text": [ "LNX" ], "offsets": [ [ 55, 58 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "84708" }, { "db_name": "hgnc", "db_id": "LNX1" }, { "db_name": "uniprot", "db_id": "Q8TBB1" } ] } ]
[]
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1.0alpha7.train.603
6972368
[ { "id": "1.0alpha7.train.603.sent", "type": "sentence", "text": [ " As a result this protein lacks the sequences that are know to mediate either the transcriptional activation or pRB, p107, or p130 binding properties of the other E2F proteins. " ], "offsets": [ [ 0, 183 ] ] } ]
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[]
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1.0alpha7.train.604
22867040
[ { "id": "1.0alpha7.train.604.sent", "type": "sentence", "text": [ "This suggests that the binding of dynactin to MTs is modulated for different tasks in different neuronal locations." ], "offsets": [ [ 0, 117 ] ] } ]
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[]
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1.0alpha7.train.605
12551602
[ { "id": "1.0alpha7.train.605.sent", "type": "sentence", "text": [ "( B) Clathrin binding to amphiphysin." ], "offsets": [ [ 0, 39 ] ] } ]
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[]
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1.0alpha7.train.606
1266507
[ { "id": "1.0alpha7.train.606.sent", "type": "sentence", "text": [ " We observed PABP binding to eIF-4F, eIF-iso4F, or eIF-4B using a far Western assay and direct fluorescence measurements. " ], "offsets": [ [ 0, 127 ] ] } ]
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[]
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1.0alpha7.train.607
23700747
[ { "id": "1.0alpha7.train.607.sent", "type": "sentence", "text": [ "The L27 domains of PSD95β and SAP97 bind Hrs" ], "offsets": [ [ 0, 44 ] ] } ]
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[]
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1.0alpha7.train.608
25318924
[ { "id": "1.0alpha7.train.608.sent", "type": "sentence", "text": [ "But what is the in vivo function of PlexB binding to Rac?" ], "offsets": [ [ 0, 59 ] ] } ]
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[]
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1.0alpha7.train.609
466336
[ { "id": "1.0alpha7.train.609.sent", "type": "sentence", "text": [ "GST or the GST-fusion proteins were first bound to the Glutathione-agarose beads followed by the addition of purified PDI and centrifugation to collect the unbound material." ], "offsets": [ [ 0, 178 ] ] } ]
[ { "id": "1.0alpha7.train.609.ent0_0", "type": "reagent", "text": [ "Glutathione-agarose beads" ], "offsets": [ [ 58, 83 ] ], "normalized": [] }, { "id": "1.0alpha7.train.609.ent1_0", "type": "experiment-tag", "text": [ "GST" ], "offsets": [ [ 0, 3 ] ], "normalized": [ { "db_name": "intenz", "db_id": "2.5.1.18" } ] }, { "id": "1.0alpha7.train.609.ent2_1", "type": "experiment-tag", "text": [ "GST" ], "offsets": [ [ 12, 15 ] ], "normalized": [ { "db_name": "intenz", "db_id": "2.5.1.18" } ] }, { "id": "1.0alpha7.train.609.ent3_0", "type": "protein-family", "text": [ "PDI" ], "offsets": [ [ 122, 125 ] ], "normalized": [ { "db_name": "intenz", "db_id": "https://www.ebi.ac.uk/intenz/query?cmd" } ] } ]
[]
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[]
1.0alpha7.train.610
5411277
[ { "id": "1.0alpha7.train.610.sent", "type": "sentence", "text": [ "A short fragment of Vtg was aligned with the binding sequences of apoB and apoE." ], "offsets": [ [ 0, 83 ] ] } ]
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[]
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[]
1.0alpha7.train.611
2869449
[ { "id": "1.0alpha7.train.611.sent", "type": "sentence", "text": [ "On the other hand, our findings contrast with those of Kamata et al. (26), who reported that recombinant 125I-GST-α2-I domain bound to collagen in a metal-independent manner." ], "offsets": [ [ 0, 174 ] ] } ]
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[]
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1.0alpha7.train.612
4115418
[ { "id": "1.0alpha7.train.612.sent", "type": "sentence", "text": [ "These findings represent the first mapping of an intermediate chain phosphorylation site and suggest that this phosphorylation plays an important role in regulating the binding of cytoplasmic dynein to dynactin." ], "offsets": [ [ 0, 213 ] ] } ]
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[]
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1.0alpha7.train.613
4249850
[ { "id": "1.0alpha7.train.613.sent", "type": "sentence", "text": [ " B, comparative binding of HMG-1 and HMG-1(A-B) to TBP/TATA complex. " ], "offsets": [ [ 0, 73 ] ] } ]
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[]
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1.0alpha7.train.614
4251025
[ { "id": "1.0alpha7.train.614.sent", "type": "sentence", "text": [ "To explore whether proteins such as Hsp90 that bind the PAR-1 C-tail are important for signaling, human neuronal cells (Ad12HER10) were transfected with C-tail overexpression constructs to specifically disrupt the endogenous PAR-1 interaction with Hsp90. " ], "offsets": [ [ 0, 255 ] ] } ]
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[]
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1.0alpha7.train.615
4015562
[ { "id": "1.0alpha7.train.615.sent", "type": "sentence", "text": [ "However, although the armadillo domain is much more accessible, E-cadherin does not bind to phosphorylated β-catenin since the presence of a negative charge makes it difficult to establish the correct ion pairs required for the interaction between these two proteins (lower right). " ], "offsets": [ [ 0, 282 ] ] } ]
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[]
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1.0alpha7.train.616
1925497
[ { "id": "1.0alpha7.train.616.sent", "type": "sentence", "text": [ "It is possible that the insert mediates direct binding of MEK to ERK or that it binds other proteins that affect MEK-ERK coupling." ], "offsets": [ [ 0, 133 ] ] } ]
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[]
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1.0alpha7.train.617
6956340
[ { "id": "1.0alpha7.train.617.sent", "type": "sentence", "text": [ "The exchange of [3H]GDP bound to eIF2 for free GDP was measured as a decrease in the amount of eIF2.[3H]GDP retained on nitrocellulose filters at various times." ], "offsets": [ [ 0, 160 ] ] } ]
[ { "id": "1.0alpha7.train.617.ent0_0", "type": "chemical", "text": [ "GDP" ], "offsets": [ [ 20, 23 ] ], "normalized": [ { "db_name": "pubchem:compound", "db_id": "135398618" } ] }, { "id": "1.0alpha7.train.617.ent1_1", "type": "chemical", "text": [ "GDP" ], "offsets": [ [ 47, 50 ] ], "normalized": [ { "db_name": "pubchem:compound", "db_id": "135398618" } ] }, { "id": "1.0alpha7.train.617.ent2_2", "type": "chemical", "text": [ "GDP" ], "offsets": [ [ 104, 107 ] ], "normalized": [ { "db_name": "pubchem:compound", "db_id": "135398618" } ] }, { "id": "1.0alpha7.train.617.ent3_0", "type": "chemical", "text": [ "[3H]GDP" ], "offsets": [ [ 16, 23 ] ], "normalized": [] }, { "id": "1.0alpha7.train.617.ent4_1", "type": "chemical", "text": [ "[3H]GDP" ], "offsets": [ [ 100, 107 ] ], "normalized": [] }, { "id": "1.0alpha7.train.617.ent5_0", "type": "protein-complex", "text": [ "eIF2" ], "offsets": [ [ 33, 37 ] ], "normalized": [] }, { "id": "1.0alpha7.train.617.ent6_1", "type": "protein-complex", "text": [ "eIF2" ], "offsets": [ [ 95, 99 ] ], "normalized": [] }, { "id": "1.0alpha7.train.617.ent7_0", "type": "protein-complex", "text": [ "eIF2.[3H]GDP" ], "offsets": [ [ 95, 107 ] ], "normalized": [] } ]
[]
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1.0alpha7.train.618
4372400
[ { "id": "1.0alpha7.train.618.sent", "type": "sentence", "text": [ "This model is consistent with the results of earlier studies of the binding of heparin to apoE." ], "offsets": [ [ 0, 97 ] ] } ]
[ { "id": "1.0alpha7.train.618.ent0_0", "type": "chemical", "text": [ "heparin" ], "offsets": [ [ 80, 87 ] ], "normalized": [ { "db_name": "pubchem:compound", "db_id": "772" } ] }, { "id": "1.0alpha7.train.618.ent1_0", "type": "protein-family", "text": [ "apoE" ], "offsets": [ [ 92, 96 ] ], "normalized": [ { "db_name": "interpro", "db_id": "IPR000074" } ] } ]
[]
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1.0alpha7.train.619
11426730
[ { "id": "1.0alpha7.train.619.sent", "type": "sentence", "text": [ "Gel retardation assay of the binding of TR/RXR heterodimer to the TRE reconstituted into nucleosome in vitro" ], "offsets": [ [ 0, 108 ] ] } ]
[ { "id": "1.0alpha7.train.619.ent0_0", "type": "DNA", "text": [ "TRE" ], "offsets": [ [ 66, 69 ] ], "normalized": [] }, { "id": "1.0alpha7.train.619.ent1_0", "type": "protein-complex", "text": [ "TR/RXR" ], "offsets": [ [ 40, 46 ] ], "normalized": [] }, { "id": "1.0alpha7.train.619.ent2_0", "type": "protein-family", "text": [ "RXR" ], "offsets": [ [ 43, 46 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "6256" }, { "db_name": "hgnc", "db_id": "RXRA" }, { "db_name": "uniprot", "db_id": "P19793" } ] }, { "id": "1.0alpha7.train.619.ent3_0", "type": "protein", "text": [ "TR" ], "offsets": [ [ 40, 42 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "7067" }, { "db_name": "hgnc", "db_id": "THRA" }, { "db_name": "uniprot", "db_id": "P10827" } ] } ]
[]
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1.0alpha7.train.620
4576582
[ { "id": "1.0alpha7.train.620.sent", "type": "sentence", "text": [ "Git2 is highly homologous to p95PKL; and we indeed detected ternary complexes of paxillin α/Git2/βPIX, and Git2/βPIX/PAK3." ], "offsets": [ [ 0, 122 ] ] } ]
[ { "id": "1.0alpha7.train.620.ent0_0", "type": "protein-complex", "text": [ "paxillin α/Git2/βPIX" ], "offsets": [ [ 81, 101 ] ], "normalized": [] }, { "id": "1.0alpha7.train.620.ent1_0", "type": "protein", "text": [ "βPIX" ], "offsets": [ [ 97, 101 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "8874" }, { "db_name": "hgnc", "db_id": "ARHGEF7" }, { "db_name": "uniprot", "db_id": "Q14155" } ] }, { "id": "1.0alpha7.train.620.ent2_1", "type": "protein", "text": [ "βPIX" ], "offsets": [ [ 112, 116 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "8874" }, { "db_name": "hgnc", "db_id": "ARHGEF7" }, { "db_name": "uniprot", "db_id": "Q14155" } ] }, { "id": "1.0alpha7.train.620.ent3_0", "type": "protein", "text": [ "paxillin" ], "offsets": [ [ 81, 89 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "5829" }, { "db_name": "hgnc", "db_id": "PXN" }, { "db_name": "uniprot", "db_id": "P49023" } ] }, { "id": "1.0alpha7.train.620.ent4_0", "type": "protein", "text": [ "PAK3" ], "offsets": [ [ 117, 121 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "5063" }, { "db_name": "hgnc", "db_id": "PAK3" } ] }, { "id": "1.0alpha7.train.620.ent5_0", "type": "protein-complex", "text": [ "Git2/βPIX/PAK3" ], "offsets": [ [ 107, 121 ] ], "normalized": [] }, { "id": "1.0alpha7.train.620.ent6_0", "type": "protein-isoform", "text": [ "paxillin α" ], "offsets": [ [ 81, 91 ] ], "normalized": [] }, { "id": "1.0alpha7.train.620.ent7_0", "type": "protein", "text": [ "Git2" ], "offsets": [ [ 0, 4 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "9815" }, { "db_name": "hgnc", "db_id": "GIT2" }, { "db_name": "uniprot", "db_id": "Q14161" } ] }, { "id": "1.0alpha7.train.620.ent8_1", "type": "protein", "text": [ "Git2" ], "offsets": [ [ 92, 96 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "9815" }, { "db_name": "hgnc", "db_id": "GIT2" }, { "db_name": "uniprot", "db_id": "Q14161" } ] }, { "id": "1.0alpha7.train.620.ent9_2", "type": "protein", "text": [ "Git2" ], "offsets": [ [ 107, 111 ] ], "normalized": [ { "db_name": "NCBI gene", "db_id": "9815" }, { "db_name": "hgnc", "db_id": "GIT2" }, { "db_name": "uniprot", "db_id": "Q14161" } ] }, { "id": "1.0alpha7.train.620.ent10_0", "type": "protein", "text": [ "p95PKL" ], "offsets": [ [ 29, 35 ] ], "normalized": [] } ]
[]
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1.0alpha7.train.621
24658961
[ { "id": "1.0alpha7.train.621.sent", "type": "sentence", "text": [ "In previous studies, we found that the cytological locations of chromatin entry sites, visualized as partial MSL complex binding, were very similar in msl3, mle, or mof mutants Kageyama et al. 2001, Lyman et al. 1997, Meller et al. 2000." ], "offsets": [ [ 0, 237 ] ] } ]
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[]
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1.0alpha7.train.622
5316811
[ { "id": "1.0alpha7.train.622.sent", "type": "sentence", "text": [ " These results suggest that GSK-3beta, PKA, and PP1 bind to AKAP220 simultaneously and that they form a quaternary complex. " ], "offsets": [ [ 0, 129 ] ] } ]
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[]
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1.0alpha7.train.623
8385694
[ { "id": "1.0alpha7.train.623.sent", "type": "sentence", "text": [ " As detailed earlier, VASP is known to bind profilin, FP4-containing cytoskeletal proteins, and full-length VASP. " ], "offsets": [ [ 0, 119 ] ] } ]
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[]
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1.0alpha7.train.624
1213968
[ { "id": "1.0alpha7.train.624.sent", "type": "sentence", "text": [ "We next used a combinatorial peptide library approach to identify the preferred binding motif of the SH3 domain of amphiphysin and its relation to the binding region identified in dynamin I." ], "offsets": [ [ 0, 193 ] ] } ]
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[]
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1.0alpha7.train.625
19382486
[ { "id": "1.0alpha7.train.625.sent", "type": "sentence", "text": [ " However, recombinant mutant ORC, which was defective in the ATP binding Walker A motif of ORC1, did not bind the 304-bp ori fragment regardless of whether ATP- -S was added (data not shown). " ], "offsets": [ [ 0, 197 ] ] } ]
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[]
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1.0alpha7.train.626
1570383
[ { "id": "1.0alpha7.train.626.sent", "type": "sentence", "text": [ " When heat-shocked cells were also treated with rapamycin, an additive effect was observed such that rapamycin increased further both the amount of 4E-BP1 bound to eIF4E and the downward band shift caused by heat shock. " ], "offsets": [ [ 0, 224 ] ] } ]
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[]
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1.0alpha7.train.627
11927887
[ { "id": "1.0alpha7.train.627.sent", "type": "sentence", "text": [ "The EH domain of POB1 bound directly to Epsin and Eps15." ], "offsets": [ [ 0, 60 ] ] } ]
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[]
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1.0alpha7.train.628
18134608
[ { "id": "1.0alpha7.train.628.sent", "type": "sentence", "text": [ " Cyclin B1 import was stimulated by importin-β but insensitive to IBB, the amino-terminal domain of importin-α that binds importin-β and inhibits importin-α–mediated import α/β (Moore et al., 1999 blue right-pointing triangle; Takizawa et al., 1999 blue right-pointing triangle; Jackman, Kubota, Den Elzen, Hagting, and Pines, unpublished results)." ], "offsets": [ [ 0, 348 ] ] } ]
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[]
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1.0alpha7.train.629
20373691
[ { "id": "1.0alpha7.train.629.sent", "type": "sentence", "text": [ "Binding of Tcf with CBP ( 19) or CtBP ( 20) can lead to repression of the Wnt/Wingless response." ], "offsets": [ [ 0, 99 ] ] } ]
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[]
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1.0alpha7.train.630
3506691
[ { "id": "1.0alpha7.train.630.sent", "type": "sentence", "text": [ "Tcf-4 is a nuclear protein that binds to β-catenin, and hTcf-4-(1–80) interacts directly with the Armadillo repeats of β-catenin (7, 8)." ], "offsets": [ [ 0, 136 ] ] } ]
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1.0alpha7.train.631
6870589
[ { "id": "1.0alpha7.train.631.sent", "type": "sentence", "text": [ "Binding of actin to profilin was performed by using glutathione S-transferase fusion protein with human profilin [glutathione S-transferase (GST)-profilin coupled to glutathione Sepharose 4B beads (Amersham Pharmacia)." ], "offsets": [ [ 0, 222 ] ] } ]
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[]
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1.0alpha7.train.632
23645886
[ { "id": "1.0alpha7.train.632.sent", "type": "sentence", "text": [ " CREB binds to the cAMP response element ( CRE) present in many genes and, when phosphorylated, alters their transcription (Montminy, 1997 ; Shaywitz and Greenberg, 1999 ). " ], "offsets": [ [ 0, 176 ] ] } ]
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[]
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1.0alpha7.train.633
23643822
[ { "id": "1.0alpha7.train.633.sent", "type": "sentence", "text": [ " Moreover, our in vitro phosphorylation results suggest that binding of dSlo to PKAc does not prevent the enzyme from phosphorylating its substrates. " ], "offsets": [ [ 0, 154 ] ] } ]
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[]
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1.0alpha7.train.634
3194752
[ { "id": "1.0alpha7.train.634.sent", "type": "sentence", "text": [ "Overexpression in Chinese hamster ovary cells of an amphiphysin 1 fragment that binds both AP-2 and clathrin resulted in a segregation of clathrin, which acquired a diffuse distribution, from AP-2, which accumulated at patches also positive for Eps15." ], "offsets": [ [ 0, 251 ] ] } ]
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[]
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1.0alpha7.train.635
4311889
[ { "id": "1.0alpha7.train.635.sent", "type": "sentence", "text": [ " However, addition of a cold polypyrimidinic RNA (UCUU)3 did not have any effect on the binding of GST-TDP43 to (UG)12 (Fig. 1 B), confirming the high specificity of TDP-43 binding to UG-repeated motifs. " ], "offsets": [ [ 0, 209 ] ] } ]
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[]
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1.0alpha7.train.636
5999528
[ { "id": "1.0alpha7.train.636.sent", "type": "sentence", "text": [ "The kinetics provide a detailed picture of the threefold difference in affinity observed for estriol binding to beta ( KD = 5.6 nM) and alpha ( KD = 18 nM) isoforms of the receptor." ], "offsets": [ [ 0, 184 ] ] } ]
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[]
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1.0alpha7.train.637
25396938
[ { "id": "1.0alpha7.train.637.sent", "type": "sentence", "text": [ "35S-labeled Arr2 bound to PIP3 beads but not to control beads (Figure 2D)." ], "offsets": [ [ 0, 77 ] ] } ]
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[]
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1.0alpha7.train.638
1077088
[ { "id": "1.0alpha7.train.638.sent", "type": "sentence", "text": [ " Binding of 125I-bFGF to ECM produced in the presence of 30 mM chlorate was inhibited by 50-60%." ], "offsets": [ [ 0, 96 ] ] } ]
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[]
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1.0alpha7.train.639
1425792
[ { "id": "1.0alpha7.train.639.sent", "type": "sentence", "text": [ " These data suggest that the isolated mSos1 PH domain shows a specific interaction with PI(4,5)P2 and binds weakly to PI(4)P. " ], "offsets": [ [ 0, 128 ] ] } ]
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[]
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1.0alpha7.train.640
79307
[ { "id": "1.0alpha7.train.640.sent", "type": "sentence", "text": [ "Toth et al. ( 27) have shown that in Ad-infected cells transcription factors ML transcription factor and transcription factor IID bind to Ad ML promoter only in the late stage of infection." ], "offsets": [ [ 0, 197 ] ] } ]
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[]
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1.0alpha7.train.641
15854669
[ { "id": "1.0alpha7.train.641.sent", "type": "sentence", "text": [ " Taking these findings together with the results of Ikeda et al. ( 20), we conclude that the GID binds directly to GSK-3beta but does not inhibit its activity in vitro, in contrast to the robust inhibition seen in oocytes and embryos. " ], "offsets": [ [ 0, 238 ] ] } ]
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[]
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1.0alpha7.train.642
2892273
[ { "id": "1.0alpha7.train.642.sent", "type": "sentence", "text": [ "Immunoadsorption of FKBP52 from reticulocyte lysate also yields co-immunoadsorption of cytoplasmic dynein, and we show that co-immunoadsorption of dynein is competed by a fragment of FKBP52 containing its PPIase domain, but not by a TPR domain fragment that blocks FKBP52 binding to hsp90." ], "offsets": [ [ 0, 289 ] ] } ]
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[]
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1.0alpha7.train.643
25204644
[ { "id": "1.0alpha7.train.643.sent", "type": "sentence", "text": [ "Our data imply that among the typically used control reagents in phorbol ester experiments on PKC (C1-domain antagonists like calphostin C, inactive 4α phorbol esters, inhibitors of ATP binding like bisindolylmaleimide), only potent and selective inhibitors of ATP binding to PKC would allow one to distinguish phorbol ester-mediated effects on PKC from those on Munc13 proteins (assuming that Munc13s do not bind these ligands with a binding site outside the C1-domain)." ], "offsets": [ [ 0, 471 ] ] } ]
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[]
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1.0alpha7.train.644
5002058
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[]
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1.0alpha7.train.645
10525577
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[]
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1.0alpha7.train.646
1369099
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[]
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1.0alpha7.train.647
11309886
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[]
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1.0alpha7.train.648
18934905
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[]
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1.0alpha7.train.649
2873519
[ { "id": "1.0alpha7.train.649.sent", "type": "sentence", "text": [ " Therefore, we tested the binding of PP1 isoforms to recombinant spinophilin and neurabin. " ], "offsets": [ [ 0, 95 ] ] } ]
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[]
1.0alpha7.train.650
25032651
[ { "id": "1.0alpha7.train.650.sent", "type": "sentence", "text": [ "Although the authors claim that this effect is through disruption of PKC binding to RACK1, one of the residues converted to alanine was I236, a residue we now know to be essential for interaction with PDE4D5 (Buensuceso et al., 2001; Steele et al., 2001)." ], "offsets": [ [ 0, 255 ] ] } ]
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[]
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1.0alpha7.train.651
24822327
[ { "id": "1.0alpha7.train.651.sent", "type": "sentence", "text": [ " Dixon RAF, Sigal IS, Rands E, Register RB, Candelore MR, Blake AD and Strader CD (1987) Ligand binding to the beta-adrenergic receptor involves its rhodopsin-like core. " ], "offsets": [ [ 0, 179 ] ] } ]
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[]
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[]
1.0alpha7.train.652
4736764
[ { "id": "1.0alpha7.train.652.sent", "type": "sentence", "text": [ "The experiments described above show that alternative splicing of the VT motif determines binding of FRS2 to Fgfr1 (and presumably Fgfr2 and -3, which also exhibit VT splicing (23))." ], "offsets": [ [ 0, 182 ] ] } ]
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[]
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1.0alpha7.train.653
23330434
[ { "id": "1.0alpha7.train.653.sent", "type": "sentence", "text": [ " Growth cones were allowed to internalize anti-L1 Fab bound to L1 for 30 min, and the cell-surface Fab was blocked with unconjugated secondary antibody at 4 degrees C. " ], "offsets": [ [ 0, 171 ] ] } ]
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[]
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1.0alpha7.train.654
5102505
[ { "id": "1.0alpha7.train.654.sent", "type": "sentence", "text": [ " To further analyze the binding of c-Maf and Prox-1 to p300, a mammalian two-hybrid assay was established (Fig. 6). " ], "offsets": [ [ 0, 123 ] ] } ]
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[]
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1.0alpha7.train.655
9664392
[ { "id": "1.0alpha7.train.655.sent", "type": "sentence", "text": [ " With much lower affinity, kinesin also binds MTs at the physiologic pH 7.2-7.4 (Fig. 2 B), suggesting that kinesin could be purified at this pH if the concentrations of MTs and kinesin were sufficiently high. " ], "offsets": [ [ 0, 219 ] ] } ]
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[]
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1.0alpha7.train.656
23758093
[ { "id": "1.0alpha7.train.656.sent", "type": "sentence", "text": [ "BMP signaling is determined by expression patterns of BMPs, their receptors, and soluble BMP antagonists, such as noggin and follistatin, which directly bind BMPs and prevent functional receptor/ligand interaction (for review, see Cho and Blitz, 1998)." ], "offsets": [ [ 0, 252 ] ] } ]
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[]
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1.0alpha7.train.657
7365792
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[]
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1.0alpha7.train.658
2649983
[ { "id": "1.0alpha7.train.658.sent", "type": "sentence", "text": [ "Previous studies have shown that F-actin binds to the epidermal growth factor receptor at a site in its cytoplasmic domain similar to a peptide of profilin ( 56)." ], "offsets": [ [ 0, 165 ] ] } ]
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[]
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1.0alpha7.train.659
1393692
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[]
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1.0alpha7.train.660
1699365
[ { "id": "1.0alpha7.train.660.sent", "type": "sentence", "text": [ "REM-1 motifs appear to differ in their ability to discriminate between the GTP- and GDP-bound forms of RhoA.2 No sequence motifs common to other RhoA effectors have been identified, although the defined Rho-binding regions of Citron, Kinectin, and the ROCKs are all found in regions of extended α-helical coiled-coil structure." ], "offsets": [ [ 0, 327 ] ] } ]
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[]
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1.0alpha7.train.661
11521315
[ { "id": "1.0alpha7.train.661.sent", "type": "sentence", "text": [ " Since Cdt1(RLF-B), like Cdc6, is required for stable binding of Mcm proteins to ORC/chromatin sites, geminin inhibits binding of Mcm proteins to chromatin and prevents initiation of DNA replication. " ], "offsets": [ [ 0, 207 ] ] } ]
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[]
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1.0alpha7.train.662
11491345
[ { "id": "1.0alpha7.train.662.sent", "type": "sentence", "text": [ " We therefore examined whether p140mDia can bind to profilin and whether the binding of p140mDia to profilin is dependent on Rho, because the fragment isolated by Reinhard et al. (1995) corresponds to the C-terminal part of p140mDia. " ], "offsets": [ [ 0, 244 ] ] } ]
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[]
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1.0alpha7.train.663
17543578
[ { "id": "1.0alpha7.train.663.sent", "type": "sentence", "text": [ "The aim of the present study was to characterize the heme-binding properties of RFABG." ], "offsets": [ [ 0, 88 ] ] } ]
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[]
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1.0alpha7.train.664
3350378
[ { "id": "1.0alpha7.train.664.sent", "type": "sentence", "text": [ " Reciprocal coimmunoprecipitation studies revealed a similar result (Fig. 2), indicating that the binding of Dvl2 to Axin did not affect the interaction of Axin with MEKK1-C. " ], "offsets": [ [ 0, 181 ] ] } ]
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1.0alpha7.train.665
15500080
[ { "id": "1.0alpha7.train.665.sent", "type": "sentence", "text": [ "To determine whether Aos binds DER directly, a binding assay was performed with the baculovirus-generated DER-Fc recombinant protein (Fig. 1A). " ], "offsets": [ [ 0, 149 ] ] } ]
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1.0alpha7.train.666
2907803
[ { "id": "1.0alpha7.train.666.sent", "type": "sentence", "text": [ " To examine the possibility that delta S1 bound to actin without quenching the pyrene fluorescence, the binding of actin and S1 was directly determined by pelleting experiments (Fig. 3). " ], "offsets": [ [ 0, 194 ] ] } ]
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1.0alpha7.train.667
4221957
[ { "id": "1.0alpha7.train.667.sent", "type": "sentence", "text": [ "NIK Binds to NHE1" ], "offsets": [ [ 0, 17 ] ] } ]
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1.0alpha7.train.668
9155513
[ { "id": "1.0alpha7.train.668.sent", "type": "sentence", "text": [ " In this way, cadherins that are not bound to beta-catenin would be turned over rapidly, while cadherins bound to beta-catenin could proceed to the cell surface to participate in adherens junctions. " ], "offsets": [ [ 0, 208 ] ] } ]
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[]
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1.0alpha7.train.669
9040575
[ { "id": "1.0alpha7.train.669.sent", "type": "sentence", "text": [ "LEF-1 Binds to Armadillo" ], "offsets": [ [ 0, 24 ] ] } ]
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1.0alpha7.train.670
7548205
[ { "id": "1.0alpha7.train.670.sent", "type": "sentence", "text": [ " Because binding of AC and tropomyosin to actin filaments is mutually exclusive, the regulation of this conversion process is extremely important to understand. " ], "offsets": [ [ 0, 167 ] ] } ]
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1.0alpha7.train.671
19831887
[ { "id": "1.0alpha7.train.671.sent", "type": "sentence", "text": [ " The block A ( Fig. 4) contains the consensus sequence involved in the binding of the ADP moiety of FAD ( Wierenga et al., 1986). " ], "offsets": [ [ 0, 133 ] ] } ]
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[]
1.0alpha7.train.672
86387
[ { "id": "1.0alpha7.train.672.sent", "type": "sentence", "text": [ " Therefore, deactivation of CF1 in vivo probably involves an alternative form of regulation such as the binding of ADP to the β-subunit, which has previously been shown to deactivate CF1 enzymatic activity in the dark (16)." ], "offsets": [ [ 0, 223 ] ] } ]
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1.0alpha7.train.673
6510331
[ { "id": "1.0alpha7.train.673.sent", "type": "sentence", "text": [ " ( B) The transcriptional activation of the TCF reporter was inhibited by 12S E1A, but not by mutant E1A that does not bind p300. " ], "offsets": [ [ 0, 134 ] ] } ]
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[]
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1.0alpha7.train.674
24668037
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[]
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1.0alpha7.train.675
8713138
[ { "id": "1.0alpha7.train.675.sent", "type": "sentence", "text": [ "Studies have also shown that cyclin D1 can directly bind the estrogen receptor and enhance transcription of specific genes [ 53]." ], "offsets": [ [ 0, 131 ] ] } ]
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[]
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