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split_0_train_3400
split_0_train_3400
[ { "id": "split_0_train_3400_passage", "type": "progene_text", "text": [ "In addition , translation of the enterovirus and rhinovirus ( HRV ) subgroups requires cellular trans - acting factors that are absent from , or limiting in rabbit reticulocytes , but are more abundant in HeLa cell extracts ." ], "offsets": [ [ 0, 225 ] ] } ]
[]
[]
[]
[]
split_0_train_3401
split_0_train_3401
[ { "id": "split_0_train_3401_passage", "type": "progene_text", "text": [ "It has been shown previously that HeLa cells contain two separable activities , each of which independently stimulates HRV IRES - dependent translation when used to supplement reticulocyte lysate ; one of these activities was identified as polypyrimidine tract - binding protein ( PTB ) ." ], "offsets": [ [ 0, 288 ] ] } ]
[ { "id": "split_0_train_5510_entity", "type": "progene_text", "text": [ "polypyrimidine tract - binding protein" ], "offsets": [ [ 240, 278 ] ], "normalized": [] }, { "id": "split_0_train_5511_entity", "type": "progene_text", "text": [ "PTB" ], "offsets": [ [ 281, 284 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3402
split_0_train_3402
[ { "id": "split_0_train_3402_passage", "type": "progene_text", "text": [ "Here , the purification of the second activity is achieved by use of an RNA - affinity column based on the HRV 5' UTR ." ], "offsets": [ [ 0, 119 ] ] } ]
[]
[]
[]
[]
split_0_train_3403
split_0_train_3403
[ { "id": "split_0_train_3403_passage", "type": "progene_text", "text": [ "It comprises two components : a 38 - kD protein ( p38 ) , which is a novel member of the GH-WD repeat protein family and has no intrinsic RNA - binding activity ; and a 96 - to 97 - kD protein doublet , which was identified as unr , an RNA - binding protein with five cold - shock domains ." ], "offsets": [ [ 0, 290 ] ] } ]
[ { "id": "split_0_train_5512_entity", "type": "progene_text", "text": [ "p38" ], "offsets": [ [ 50, 53 ] ], "normalized": [] }, { "id": "split_0_train_5513_entity", "type": "progene_text", "text": [ "GH-WD repeat protein family" ], "offsets": [ [ 89, 116 ] ], "normalized": [] }, { "id": "split_0_train_5514_entity", "type": "progene_text", "text": [ "unr" ], "offsets": [ [ 227, 230 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3404
split_0_train_3404
[ { "id": "split_0_train_3404_passage", "type": "progene_text", "text": [ "Coimmunoprecipitation with antibodies against either protein shows that the two proteins interact with each other , and thus p38 is named unrip ( unr - interacting protein ) ." ], "offsets": [ [ 0, 175 ] ] } ]
[ { "id": "split_0_train_5515_entity", "type": "progene_text", "text": [ "p38" ], "offsets": [ [ 125, 128 ] ], "normalized": [] }, { "id": "split_0_train_5516_entity", "type": "progene_text", "text": [ "unrip" ], "offsets": [ [ 138, 143 ] ], "normalized": [] }, { "id": "split_0_train_5517_entity", "type": "progene_text", "text": [ "unr - interacting protein" ], "offsets": [ [ 146, 171 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3405
split_0_train_3405
[ { "id": "split_0_train_3405_passage", "type": "progene_text", "text": [ "Recombinant unr acts synergistically with recombinant PTB to stimulate translation dependent on the rhinovirus IRES ." ], "offsets": [ [ 0, 117 ] ] } ]
[ { "id": "split_0_train_5518_entity", "type": "progene_text", "text": [ "unr" ], "offsets": [ [ 12, 15 ] ], "normalized": [] }, { "id": "split_0_train_5519_entity", "type": "progene_text", "text": [ "PTB" ], "offsets": [ [ 54, 57 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3406
split_0_train_3406
[ { "id": "split_0_train_3406_passage", "type": "progene_text", "text": [ "In contrast , unr did not significantly augment the PTB - dependent stimulation of poliovirus IRES activity ." ], "offsets": [ [ 0, 109 ] ] } ]
[ { "id": "split_0_train_5520_entity", "type": "progene_text", "text": [ "unr" ], "offsets": [ [ 14, 17 ] ], "normalized": [] }, { "id": "split_0_train_5521_entity", "type": "progene_text", "text": [ "PTB" ], "offsets": [ [ 52, 55 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3407
split_0_train_3407
[ { "id": "split_0_train_3407_passage", "type": "progene_text", "text": [ "Control of the tissue inhibitor of metalloproteinases-1 promoter in culture - activated rat hepatic stellate cells : regulation by activator protein-1 DNA binding proteins ." ], "offsets": [ [ 0, 173 ] ] } ]
[ { "id": "split_0_train_5522_entity", "type": "progene_text", "text": [ "tissue inhibitor of metalloproteinases-1" ], "offsets": [ [ 15, 55 ] ], "normalized": [] }, { "id": "split_0_train_5523_entity", "type": "progene_text", "text": [ "activator protein-1" ], "offsets": [ [ 131, 150 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3408
split_0_train_3408
[ { "id": "split_0_train_3408_passage", "type": "progene_text", "text": [ "In the injured liver hepatic stellate cells ( HSCs ) undergo a dramatic phenotypic transformation known as \" activation \" in which they become myofibroblast - like and express high levels of the tissue inhibitor of metalloproteinase 1 ( TIMP-1 ) ." ], "offsets": [ [ 0, 247 ] ] } ]
[ { "id": "split_0_train_5524_entity", "type": "progene_text", "text": [ "tissue inhibitor of metalloproteinase 1" ], "offsets": [ [ 195, 234 ] ], "normalized": [] }, { "id": "split_0_train_5525_entity", "type": "progene_text", "text": [ "TIMP-1" ], "offsets": [ [ 237, 243 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3409
split_0_train_3409
[ { "id": "split_0_train_3409_passage", "type": "progene_text", "text": [ "HSC activation is accompanied by transactivation of the TIMP-1 promoter ." ], "offsets": [ [ 0, 73 ] ] } ]
[ { "id": "split_0_train_5526_entity", "type": "progene_text", "text": [ "TIMP-1" ], "offsets": [ [ 56, 62 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3410
split_0_train_3410
[ { "id": "split_0_train_3410_passage", "type": "progene_text", "text": [ "Truncation mutagenesis studies delineated a minimal active promoter consisting of nucleotides - 102 to + 60 relative to the major start site for transcription ." ], "offsets": [ [ 0, 160 ] ] } ]
[]
[]
[]
[]
split_0_train_3411
split_0_train_3411
[ { "id": "split_0_train_3411_passage", "type": "progene_text", "text": [ "Removal of an AP-1 site located at nucleotides - 93 to - 87 caused almost a complete loss of promoter activity ." ], "offsets": [ [ 0, 112 ] ] } ]
[ { "id": "split_0_train_5527_entity", "type": "progene_text", "text": [ "AP-1" ], "offsets": [ [ 14, 18 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3412
split_0_train_3412
[ { "id": "split_0_train_3412_passage", "type": "progene_text", "text": [ "Analysis of AP-1 DNA binding activities during culture activation of HSCs initially indicated transient expression of proteins capable of forming a low mobility AP-1 DNA binding complex ( LMAP-1 ) ." ], "offsets": [ [ 0, 198 ] ] } ]
[ { "id": "split_0_train_5528_entity", "type": "progene_text", "text": [ "AP-1" ], "offsets": [ [ 12, 16 ] ], "normalized": [] }, { "id": "split_0_train_5529_entity", "type": "progene_text", "text": [ "AP-1" ], "offsets": [ [ 161, 165 ] ], "normalized": [] }, { "id": "split_0_train_5530_entity", "type": "progene_text", "text": [ "LMAP-1" ], "offsets": [ [ 188, 194 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3413
split_0_train_3413
[ { "id": "split_0_train_3413_passage", "type": "progene_text", "text": [ "LMAP-1 was maximally induced at 24 hours of culture and then fell to undetectable levels at 120 hours ." ], "offsets": [ [ 0, 103 ] ] } ]
[ { "id": "split_0_train_5531_entity", "type": "progene_text", "text": [ "LMAP-1" ], "offsets": [ [ 0, 6 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3414
split_0_train_3414
[ { "id": "split_0_train_3414_passage", "type": "progene_text", "text": [ "Western blot studies showed that both c-Fos and c-Jun underwent similar transient inductions ." ], "offsets": [ [ 0, 94 ] ] } ]
[ { "id": "split_0_train_5532_entity", "type": "progene_text", "text": [ "c-Fos" ], "offsets": [ [ 38, 43 ] ], "normalized": [] }, { "id": "split_0_train_5533_entity", "type": "progene_text", "text": [ "c-Jun" ], "offsets": [ [ 48, 53 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3415
split_0_train_3415
[ { "id": "split_0_train_3415_passage", "type": "progene_text", "text": [ "These temporal changes in c-Fos and c-Jun activities were unexpected because TIMP-1 mRNA expression is not detected in HSCs until culture day 3 to 5 and is thereafter sustained at a high level ." ], "offsets": [ [ 0, 194 ] ] } ]
[ { "id": "split_0_train_5534_entity", "type": "progene_text", "text": [ "c-Fos" ], "offsets": [ [ 26, 31 ] ], "normalized": [] }, { "id": "split_0_train_5535_entity", "type": "progene_text", "text": [ "c-Jun" ], "offsets": [ [ 36, 41 ] ], "normalized": [] }, { "id": "split_0_train_5536_entity", "type": "progene_text", "text": [ "TIMP-1" ], "offsets": [ [ 77, 83 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3416
split_0_train_3416
[ { "id": "split_0_train_3416_passage", "type": "progene_text", "text": [ "Previous work in other cell lineages has established a key role for Pea3 binding proteins ( Ets-1 ) in AP-1 mediated transactivation of the TIMP-1 promoter ." ], "offsets": [ [ 0, 157 ] ] } ]
[ { "id": "split_0_train_5537_entity", "type": "progene_text", "text": [ "Pea3" ], "offsets": [ [ 68, 72 ] ], "normalized": [] }, { "id": "split_0_train_5538_entity", "type": "progene_text", "text": [ "Ets-1" ], "offsets": [ [ 92, 97 ] ], "normalized": [] }, { "id": "split_0_train_5539_entity", "type": "progene_text", "text": [ "AP-1" ], "offsets": [ [ 103, 107 ] ], "normalized": [] }, { "id": "split_0_train_5540_entity", "type": "progene_text", "text": [ "TIMP-1" ], "offsets": [ [ 140, 146 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3417
split_0_train_3417
[ { "id": "split_0_train_3417_passage", "type": "progene_text", "text": [ "We show that HSCs express relatively low levels Ets-1 and Ets-2 and show that mutagenesis of the Pea3 DNA binding site in the TIMP-1 promoter has less than a twofold effect on its activity in activated HSCs ." ], "offsets": [ [ 0, 208 ] ] } ]
[ { "id": "split_0_train_5541_entity", "type": "progene_text", "text": [ "Ets-1" ], "offsets": [ [ 48, 53 ] ], "normalized": [] }, { "id": "split_0_train_5542_entity", "type": "progene_text", "text": [ "Ets-2" ], "offsets": [ [ 58, 63 ] ], "normalized": [] }, { "id": "split_0_train_5543_entity", "type": "progene_text", "text": [ "Pea3" ], "offsets": [ [ 97, 101 ] ], "normalized": [] }, { "id": "split_0_train_5544_entity", "type": "progene_text", "text": [ "TIMP-1" ], "offsets": [ [ 126, 132 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3418
split_0_train_3418
[ { "id": "split_0_train_3418_passage", "type": "progene_text", "text": [ "Further analysis of AP-1 DNA binding activities in 7 - to 14 - day culture activated HSCs led to the discovery of high mobility AP-1 complexes ( HMAP-1 ) ." ], "offsets": [ [ 0, 155 ] ] } ]
[ { "id": "split_0_train_5545_entity", "type": "progene_text", "text": [ "AP-1" ], "offsets": [ [ 20, 24 ] ], "normalized": [] }, { "id": "split_0_train_5546_entity", "type": "progene_text", "text": [ "AP-1" ], "offsets": [ [ 128, 132 ] ], "normalized": [] }, { "id": "split_0_train_5547_entity", "type": "progene_text", "text": [ "HMAP-1" ], "offsets": [ [ 145, 151 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3419
split_0_train_3419
[ { "id": "split_0_train_3419_passage", "type": "progene_text", "text": [ "HMAP-1 DNA binding activities were sequence specific with respect to AP-1 and absent from freshly isolated HSCs ." ], "offsets": [ [ 0, 113 ] ] } ]
[ { "id": "split_0_train_5548_entity", "type": "progene_text", "text": [ "HMAP-1" ], "offsets": [ [ 0, 6 ] ], "normalized": [] }, { "id": "split_0_train_5549_entity", "type": "progene_text", "text": [ "AP-1" ], "offsets": [ [ 69, 73 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3420
split_0_train_3420
[ { "id": "split_0_train_3420_passage", "type": "progene_text", "text": [ "Supershift EMSA and Western blot studies identified JunD , Fra2 , and FosB as potential components of the HMAP-1 ." ], "offsets": [ [ 0, 114 ] ] } ]
[ { "id": "split_0_train_5550_entity", "type": "progene_text", "text": [ "JunD" ], "offsets": [ [ 52, 56 ] ], "normalized": [] }, { "id": "split_0_train_5551_entity", "type": "progene_text", "text": [ "Fra2" ], "offsets": [ [ 59, 63 ] ], "normalized": [] }, { "id": "split_0_train_5552_entity", "type": "progene_text", "text": [ "FosB" ], "offsets": [ [ 70, 74 ] ], "normalized": [] }, { "id": "split_0_train_5553_entity", "type": "progene_text", "text": [ "HMAP-1" ], "offsets": [ [ 106, 112 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3421
split_0_train_3421
[ { "id": "split_0_train_3421_passage", "type": "progene_text", "text": [ "Mutations of the AP-1 site of the TIMP-1 promoter that prevented formation of HMAP-1 caused a 70 % loss of activity in transfected activated HSCs ." ], "offsets": [ [ 0, 147 ] ] } ]
[ { "id": "split_0_train_5554_entity", "type": "progene_text", "text": [ "AP-1" ], "offsets": [ [ 17, 21 ] ], "normalized": [] }, { "id": "split_0_train_5555_entity", "type": "progene_text", "text": [ "TIMP-1" ], "offsets": [ [ 34, 40 ] ], "normalized": [] }, { "id": "split_0_train_5556_entity", "type": "progene_text", "text": [ "HMAP-1" ], "offsets": [ [ 78, 84 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3422
split_0_train_3422
[ { "id": "split_0_train_3422_passage", "type": "progene_text", "text": [ "Taken together the data indicate that sustained upregulation of TIMP-1 gene expression may be at least partially controlled by a novel AP-1 dependent regulation of TIMP-1 promoter activity ." ], "offsets": [ [ 0, 190 ] ] } ]
[ { "id": "split_0_train_5557_entity", "type": "progene_text", "text": [ "TIMP-1" ], "offsets": [ [ 64, 70 ] ], "normalized": [] }, { "id": "split_0_train_5558_entity", "type": "progene_text", "text": [ "AP-1" ], "offsets": [ [ 135, 139 ] ], "normalized": [] }, { "id": "split_0_train_5559_entity", "type": "progene_text", "text": [ "TIMP-1" ], "offsets": [ [ 164, 170 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3423
split_0_train_3423
[ { "id": "split_0_train_3423_passage", "type": "progene_text", "text": [ "The mouse genome contains two expressed intronless retroposed pseudogenes for the sentrin / sumo-1 / PIC1 conjugating enzyme Ubc9 ." ], "offsets": [ [ 0, 131 ] ] } ]
[ { "id": "split_0_train_5560_entity", "type": "progene_text", "text": [ "sentrin" ], "offsets": [ [ 82, 89 ] ], "normalized": [] }, { "id": "split_0_train_5561_entity", "type": "progene_text", "text": [ "sumo-1" ], "offsets": [ [ 92, 98 ] ], "normalized": [] }, { "id": "split_0_train_5562_entity", "type": "progene_text", "text": [ "PIC1" ], "offsets": [ [ 101, 105 ] ], "normalized": [] }, { "id": "split_0_train_5563_entity", "type": "progene_text", "text": [ "Ubc9" ], "offsets": [ [ 125, 129 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3424
split_0_train_3424
[ { "id": "split_0_train_3424_passage", "type": "progene_text", "text": [ "The ubiquitin conjugating ( ubc ) E2 enzyme ubc-9 conjugates the ubiquitin - like peptide sentrin / SUMO-1 / PIC1 to target proteins which include the Fas antigen ." ], "offsets": [ [ 0, 164 ] ] } ]
[ { "id": "split_0_train_5564_entity", "type": "progene_text", "text": [ "ubiquitin conjugating ( ubc ) E2 enzyme" ], "offsets": [ [ 4, 43 ] ], "normalized": [] }, { "id": "split_0_train_5565_entity", "type": "progene_text", "text": [ "ubc-9" ], "offsets": [ [ 44, 49 ] ], "normalized": [] }, { "id": "split_0_train_5566_entity", "type": "progene_text", "text": [ "ubiquitin" ], "offsets": [ [ 65, 74 ] ], "normalized": [] }, { "id": "split_0_train_5567_entity", "type": "progene_text", "text": [ "sentrin" ], "offsets": [ [ 90, 97 ] ], "normalized": [] }, { "id": "split_0_train_5568_entity", "type": "progene_text", "text": [ "SUMO-1" ], "offsets": [ [ 100, 106 ] ], "normalized": [] }, { "id": "split_0_train_5569_entity", "type": "progene_text", "text": [ "PIC1" ], "offsets": [ [ 109, 113 ] ], "normalized": [] }, { "id": "split_0_train_5570_entity", "type": "progene_text", "text": [ "Fas" ], "offsets": [ [ 151, 154 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3425
split_0_train_3425
[ { "id": "split_0_train_3425_passage", "type": "progene_text", "text": [ "We show that the mouse genome contains four copies of the ubc-9 gene ." ], "offsets": [ [ 0, 70 ] ] } ]
[ { "id": "split_0_train_5571_entity", "type": "progene_text", "text": [ "ubc-9" ], "offsets": [ [ 58, 63 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3426
split_0_train_3426
[ { "id": "split_0_train_3426_passage", "type": "progene_text", "text": [ "These include a structural ubc-9 gene consisting of seven exons which encode a protein identical to human ubc-9 , and three intronless processed pseudogenes ." ], "offsets": [ [ 0, 158 ] ] } ]
[ { "id": "split_0_train_5572_entity", "type": "progene_text", "text": [ "ubc-9" ], "offsets": [ [ 27, 32 ] ], "normalized": [] }, { "id": "split_0_train_5573_entity", "type": "progene_text", "text": [ "ubc-9" ], "offsets": [ [ 106, 111 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3427
split_0_train_3427
[ { "id": "split_0_train_3427_passage", "type": "progene_text", "text": [ "The open reading frames ( ORF ) of two of the pseudogenes , ubc9 - psi1 and ubc9 - psi2 , correspond to the cDNA of ubc-9 and encode for proteins which differ from ubc9 by three and one amino acid substitutions respectively ." ], "offsets": [ [ 0, 225 ] ] } ]
[ { "id": "split_0_train_5574_entity", "type": "progene_text", "text": [ "ubc9" ], "offsets": [ [ 60, 64 ] ], "normalized": [] }, { "id": "split_0_train_5575_entity", "type": "progene_text", "text": [ "ubc9" ], "offsets": [ [ 76, 80 ] ], "normalized": [] }, { "id": "split_0_train_5576_entity", "type": "progene_text", "text": [ "ubc-9" ], "offsets": [ [ 116, 121 ] ], "normalized": [] }, { "id": "split_0_train_5577_entity", "type": "progene_text", "text": [ "ubc9" ], "offsets": [ [ 164, 168 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3428
split_0_train_3428
[ { "id": "split_0_train_3428_passage", "type": "progene_text", "text": [ "The third pseudogene , ubc9 - psi3 , contains many mutations and stop codons ." ], "offsets": [ [ 0, 78 ] ] } ]
[ { "id": "split_0_train_5578_entity", "type": "progene_text", "text": [ "ubc9" ], "offsets": [ [ 23, 27 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3429
split_0_train_3429
[ { "id": "split_0_train_3429_passage", "type": "progene_text", "text": [ "ubc9 - psi1 and ubc9 - psi2 are flanked by 5' - and 3' - untranslated ( UT ) regions homologous to those of the structural ubc-9 gene ." ], "offsets": [ [ 0, 135 ] ] } ]
[ { "id": "split_0_train_5579_entity", "type": "progene_text", "text": [ "ubc9" ], "offsets": [ [ 0, 4 ] ], "normalized": [] }, { "id": "split_0_train_5580_entity", "type": "progene_text", "text": [ "ubc9" ], "offsets": [ [ 16, 20 ] ], "normalized": [] }, { "id": "split_0_train_5581_entity", "type": "progene_text", "text": [ "ubc-9" ], "offsets": [ [ 123, 128 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3430
split_0_train_3430
[ { "id": "split_0_train_3430_passage", "type": "progene_text", "text": [ "Both genes contain a polyA tail and direct repeats at both ends suggesting that they arose by mRNA retroposition ." ], "offsets": [ [ 0, 114 ] ] } ]
[]
[]
[]
[]
split_0_train_3431
split_0_train_3431
[ { "id": "split_0_train_3431_passage", "type": "progene_text", "text": [ "Both ubc9 - psi1 and ubc9 - psi2 are transcribed into mRNA in murine cells ." ], "offsets": [ [ 0, 76 ] ] } ]
[ { "id": "split_0_train_5582_entity", "type": "progene_text", "text": [ "ubc9" ], "offsets": [ [ 5, 9 ] ], "normalized": [] }, { "id": "split_0_train_5583_entity", "type": "progene_text", "text": [ "ubc9" ], "offsets": [ [ 21, 25 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3432
split_0_train_3432
[ { "id": "split_0_train_3432_passage", "type": "progene_text", "text": [ "In contrast to ubc9 , the protein products of ubc9 - psil and ubc9 - psi2 fail to bind Fas and to complement an yeast conditional ubc9 mutant ." ], "offsets": [ [ 0, 143 ] ] } ]
[ { "id": "split_0_train_5584_entity", "type": "progene_text", "text": [ "ubc9" ], "offsets": [ [ 15, 19 ] ], "normalized": [] }, { "id": "split_0_train_5585_entity", "type": "progene_text", "text": [ "ubc9" ], "offsets": [ [ 46, 50 ] ], "normalized": [] }, { "id": "split_0_train_5586_entity", "type": "progene_text", "text": [ "ubc9" ], "offsets": [ [ 62, 66 ] ], "normalized": [] }, { "id": "split_0_train_5587_entity", "type": "progene_text", "text": [ "Fas" ], "offsets": [ [ 87, 90 ] ], "normalized": [] }, { "id": "split_0_train_5588_entity", "type": "progene_text", "text": [ "ubc9" ], "offsets": [ [ 130, 134 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3433
split_0_train_3433
[ { "id": "split_0_train_3433_passage", "type": "progene_text", "text": [ "These results suggest that ubc9 - psi1 and ubc9 - psi2 encode for proteins that may interact with targets that differ from those recognized by ubc-9 ." ], "offsets": [ [ 0, 150 ] ] } ]
[ { "id": "split_0_train_5589_entity", "type": "progene_text", "text": [ "ubc9" ], "offsets": [ [ 27, 31 ] ], "normalized": [] }, { "id": "split_0_train_5590_entity", "type": "progene_text", "text": [ "ubc9" ], "offsets": [ [ 43, 47 ] ], "normalized": [] }, { "id": "split_0_train_5591_entity", "type": "progene_text", "text": [ "ubc-9" ], "offsets": [ [ 143, 148 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3434
split_0_train_3434
[ { "id": "split_0_train_3434_passage", "type": "progene_text", "text": [ "Genomic organization and mutational analysis of the human UCP2 gene , a prime candidate gene for human obesity ." ], "offsets": [ [ 0, 112 ] ] } ]
[ { "id": "split_0_train_5592_entity", "type": "progene_text", "text": [ "UCP2" ], "offsets": [ [ 58, 62 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3435
split_0_train_3435
[ { "id": "split_0_train_3435_passage", "type": "progene_text", "text": [ "Uncoupling proteins ( UCPs ) are mitochondrial membrane transporters which are involved in dissipating the proton electrochemical gradient thereby releasing stored energy as heat ." ], "offsets": [ [ 0, 180 ] ] } ]
[ { "id": "split_0_train_5593_entity", "type": "progene_text", "text": [ "Uncoupling proteins" ], "offsets": [ [ 0, 19 ] ], "normalized": [] }, { "id": "split_0_train_5594_entity", "type": "progene_text", "text": [ "UCPs" ], "offsets": [ [ 22, 26 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3436
split_0_train_3436
[ { "id": "split_0_train_3436_passage", "type": "progene_text", "text": [ "This implies a major role of UCPs in energy metabolism and thermogenesis which when deregulated are key risk factors for the development of obesity and other eating disorders ." ], "offsets": [ [ 0, 176 ] ] } ]
[ { "id": "split_0_train_5595_entity", "type": "progene_text", "text": [ "UCPs" ], "offsets": [ [ 29, 33 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3437
split_0_train_3437
[ { "id": "split_0_train_3437_passage", "type": "progene_text", "text": [ "Recent studies have shown that the sympathetic nervous system , via norepinephrine ( beta-adrenoceptors ) and cAMP , as well as thyroid hormones and PPAR gamma ligands seem to be major regulators of UCP expression ." ], "offsets": [ [ 0, 215 ] ] } ]
[ { "id": "split_0_train_5596_entity", "type": "progene_text", "text": [ "PPAR gamma" ], "offsets": [ [ 149, 159 ] ], "normalized": [] }, { "id": "split_0_train_5597_entity", "type": "progene_text", "text": [ "UCP" ], "offsets": [ [ 199, 202 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3438
split_0_train_3438
[ { "id": "split_0_train_3438_passage", "type": "progene_text", "text": [ "From the three different UCPs identified so far by gene cloning UCP1 is expressed exclusively in brown adipocytes while UCP2 is widely expressed ." ], "offsets": [ [ 0, 146 ] ] } ]
[ { "id": "split_0_train_5598_entity", "type": "progene_text", "text": [ "UCPs" ], "offsets": [ [ 25, 29 ] ], "normalized": [] }, { "id": "split_0_train_5599_entity", "type": "progene_text", "text": [ "UCP1" ], "offsets": [ [ 64, 68 ] ], "normalized": [] }, { "id": "split_0_train_5600_entity", "type": "progene_text", "text": [ "UCP2" ], "offsets": [ [ 120, 124 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3439
split_0_train_3439
[ { "id": "split_0_train_3439_passage", "type": "progene_text", "text": [ "The third analogue , UCP3 , is expressed predominantly in human skeletal muscle and was found to exist in a long and a short form ." ], "offsets": [ [ 0, 131 ] ] } ]
[ { "id": "split_0_train_5601_entity", "type": "progene_text", "text": [ "UCP3" ], "offsets": [ [ 21, 25 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3440
split_0_train_3440
[ { "id": "split_0_train_3440_passage", "type": "progene_text", "text": [ "At the amino acid level UCP2 has about 59 % homology to UCP1 while UCP3 is 73 % identical to UCP2 ." ], "offsets": [ [ 0, 99 ] ] } ]
[ { "id": "split_0_train_5602_entity", "type": "progene_text", "text": [ "UCP2" ], "offsets": [ [ 24, 28 ] ], "normalized": [] }, { "id": "split_0_train_5603_entity", "type": "progene_text", "text": [ "UCP1" ], "offsets": [ [ 56, 60 ] ], "normalized": [] }, { "id": "split_0_train_5604_entity", "type": "progene_text", "text": [ "UCP3" ], "offsets": [ [ 67, 71 ] ], "normalized": [] }, { "id": "split_0_train_5605_entity", "type": "progene_text", "text": [ "UCP2" ], "offsets": [ [ 93, 97 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3441
split_0_train_3441
[ { "id": "split_0_train_3441_passage", "type": "progene_text", "text": [ "Both UCP2 and UCP3 were mapped in close proximity ( 75 - 150 kb ) to regions of human chromosome 11 ( 11q13 ) that have been linked to obesity and hyper - insulinaemia ." ], "offsets": [ [ 0, 169 ] ] } ]
[ { "id": "split_0_train_5606_entity", "type": "progene_text", "text": [ "UCP2" ], "offsets": [ [ 5, 9 ] ], "normalized": [] }, { "id": "split_0_train_5607_entity", "type": "progene_text", "text": [ "UCP3" ], "offsets": [ [ 14, 18 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3442
split_0_train_3442
[ { "id": "split_0_train_3442_passage", "type": "progene_text", "text": [ "Furthermore , there is strong evidence that UCP2 , by virtue of its ubiquitous expression , may be important for determining basal metabolic rate ." ], "offsets": [ [ 0, 147 ] ] } ]
[ { "id": "split_0_train_5608_entity", "type": "progene_text", "text": [ "UCP2" ], "offsets": [ [ 44, 48 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3443
split_0_train_3443
[ { "id": "split_0_train_3443_passage", "type": "progene_text", "text": [ "Based on the published full - length cDNA sequence we have deduced the genomic structure of the human UCP2 ( hUCP2 ) gene by PCR and direct sequence analysis ." ], "offsets": [ [ 0, 159 ] ] } ]
[ { "id": "split_0_train_5609_entity", "type": "progene_text", "text": [ "UCP2" ], "offsets": [ [ 102, 106 ] ], "normalized": [] }, { "id": "split_0_train_5610_entity", "type": "progene_text", "text": [ "hUCP2" ], "offsets": [ [ 109, 114 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3444
split_0_train_3444
[ { "id": "split_0_train_3444_passage", "type": "progene_text", "text": [ "The hUCP2 gene spans over 8.4 kb distributed on 8 exons ." ], "offsets": [ [ 0, 57 ] ] } ]
[ { "id": "split_0_train_5611_entity", "type": "progene_text", "text": [ "hUCP2" ], "offsets": [ [ 4, 9 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3445
split_0_train_3445
[ { "id": "split_0_train_3445_passage", "type": "progene_text", "text": [ "The localization of the exon / intron boundaries within the coding region matches precisely the one found in the human UCP1 gene and is almost conserved in the recently discovered UCP3 gene as well ." ], "offsets": [ [ 0, 199 ] ] } ]
[ { "id": "split_0_train_5612_entity", "type": "progene_text", "text": [ "UCP1" ], "offsets": [ [ 119, 123 ] ], "normalized": [] }, { "id": "split_0_train_5613_entity", "type": "progene_text", "text": [ "UCP3" ], "offsets": [ [ 180, 184 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3446
split_0_train_3446
[ { "id": "split_0_train_3446_passage", "type": "progene_text", "text": [ "However , the size of each of the introns in the hUCP2 gene differs from its UCP1 and UCP3 counterparts ." ], "offsets": [ [ 0, 105 ] ] } ]
[ { "id": "split_0_train_5614_entity", "type": "progene_text", "text": [ "hUCP2" ], "offsets": [ [ 49, 54 ] ], "normalized": [] }, { "id": "split_0_train_5615_entity", "type": "progene_text", "text": [ "UCP1" ], "offsets": [ [ 77, 81 ] ], "normalized": [] }, { "id": "split_0_train_5616_entity", "type": "progene_text", "text": [ "UCP3" ], "offsets": [ [ 86, 90 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3447
split_0_train_3447
[ { "id": "split_0_train_3447_passage", "type": "progene_text", "text": [ "It varies from 81 bp ( intron 5 ) to about 3 kb ( intron 2 ) ." ], "offsets": [ [ 0, 62 ] ] } ]
[]
[]
[]
[]
split_0_train_3448
split_0_train_3448
[ { "id": "split_0_train_3448_passage", "type": "progene_text", "text": [ "The high degree of homology at the nucleotide level and the conservation of the exon / intron boundaries among the three UCP genes suggests that they may have evolved from a common ancestor or are the result from gene duplication events ." ], "offsets": [ [ 0, 238 ] ] } ]
[ { "id": "split_0_train_5617_entity", "type": "progene_text", "text": [ "UCP" ], "offsets": [ [ 121, 124 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3449
split_0_train_3449
[ { "id": "split_0_train_3449_passage", "type": "progene_text", "text": [ "Mutational analysis of the hUCP2 gene in a cohort of 25 children of caucasian origin ( aged 7 - 13 ) characterized by low BMR values revealed a point mutation in exon 4 ( C to T transition at position 164 of the corresponding cDNA resulting in the substitution of an alanine residue by a valine at codon 55 ) and an insertion polymorphism in exon 8 ." ], "offsets": [ [ 0, 350 ] ] } ]
[ { "id": "split_0_train_5618_entity", "type": "progene_text", "text": [ "hUCP2" ], "offsets": [ [ 27, 32 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3450
split_0_train_3450
[ { "id": "split_0_train_3450_passage", "type": "progene_text", "text": [ "The insertion polymorphism consists of a 45 bp repeat located 150 bp downstream of the stop codon in the 3'-UTR ." ], "offsets": [ [ 0, 113 ] ] } ]
[]
[]
[]
[]
split_0_train_3451
split_0_train_3451
[ { "id": "split_0_train_3451_passage", "type": "progene_text", "text": [ "The allele frequencies were 0.61 and 0.39 for the alanine and valine encoded alleles , respectively , and 0.71 versus 0.29 for the insertion polymorphism ." ], "offsets": [ [ 0, 155 ] ] } ]
[]
[]
[]
[]
split_0_train_3452
split_0_train_3452
[ { "id": "split_0_train_3452_passage", "type": "progene_text", "text": [ "Expression studies of the wildtype and mutant forms of UCP2 should clarify the functional consequences these mutations may have on energy metabolism and body weight regulation ." ], "offsets": [ [ 0, 177 ] ] } ]
[ { "id": "split_0_train_5619_entity", "type": "progene_text", "text": [ "UCP2" ], "offsets": [ [ 55, 59 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3453
split_0_train_3453
[ { "id": "split_0_train_3453_passage", "type": "progene_text", "text": [ "In addition , mapping of the promoter region and the identification of putative promoter regulatory sequences should give insight into the transcriptional regulation of UCP2 expression - - in particular by anyone of the above mentioned factors - - in vitro and in vivo ." ], "offsets": [ [ 0, 270 ] ] } ]
[ { "id": "split_0_train_5620_entity", "type": "progene_text", "text": [ "UCP2" ], "offsets": [ [ 169, 173 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3454
split_0_train_3454
[ { "id": "split_0_train_3454_passage", "type": "progene_text", "text": [ "A new pathway for mitogen - dependent cdk2 regulation uncovered in p27 ( Kip1 ) - deficient cells ." ], "offsets": [ [ 0, 99 ] ] } ]
[ { "id": "split_0_train_5621_entity", "type": "progene_text", "text": [ "cdk2" ], "offsets": [ [ 38, 42 ] ], "normalized": [] }, { "id": "split_0_train_5622_entity", "type": "progene_text", "text": [ "p27 ( Kip1 )" ], "offsets": [ [ 67, 79 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3455
split_0_train_3455
[ { "id": "split_0_train_3455_passage", "type": "progene_text", "text": [ "BACKGROUND :" ], "offsets": [ [ 0, 12 ] ] } ]
[]
[]
[]
[]
split_0_train_3456
split_0_train_3456
[ { "id": "split_0_train_3456_passage", "type": "progene_text", "text": [ "The ability of cyclin - dependent kinases ( CDKs ) to promote cell proliferation is opposed by cyclin - dependent kinase inhibitors ( CKIs ) , proteins that bind tightly to cyclin - CDK complexes and block the phosphorylation of exogenous substrates ." ], "offsets": [ [ 0, 251 ] ] } ]
[ { "id": "split_0_train_5623_entity", "type": "progene_text", "text": [ "cyclin - dependent kinases" ], "offsets": [ [ 15, 41 ] ], "normalized": [] }, { "id": "split_0_train_5624_entity", "type": "progene_text", "text": [ "CDKs" ], "offsets": [ [ 44, 48 ] ], "normalized": [] }, { "id": "split_0_train_5625_entity", "type": "progene_text", "text": [ "cyclin - dependent kinase inhibitors" ], "offsets": [ [ 95, 131 ] ], "normalized": [] }, { "id": "split_0_train_5626_entity", "type": "progene_text", "text": [ "CKIs" ], "offsets": [ [ 134, 138 ] ], "normalized": [] }, { "id": "split_0_train_5627_entity", "type": "progene_text", "text": [ "cyclin" ], "offsets": [ [ 173, 179 ] ], "normalized": [] }, { "id": "split_0_train_5628_entity", "type": "progene_text", "text": [ "CDK" ], "offsets": [ [ 182, 185 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3457
split_0_train_3457
[ { "id": "split_0_train_3457_passage", "type": "progene_text", "text": [ "Mice with targeted CKI gene deletions have only subtle proliferative abnormalities , however , and cells prepared from these mice seem remarkably normal when grown in vitro ." ], "offsets": [ [ 0, 174 ] ] } ]
[ { "id": "split_0_train_5629_entity", "type": "progene_text", "text": [ "CKI" ], "offsets": [ [ 19, 22 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3458
split_0_train_3458
[ { "id": "split_0_train_3458_passage", "type": "progene_text", "text": [ "One explanation may be the operation of compensatory pathways that control CDK activity and cell proliferation when normal pathways are inactivated ." ], "offsets": [ [ 0, 149 ] ] } ]
[ { "id": "split_0_train_5630_entity", "type": "progene_text", "text": [ "CDK" ], "offsets": [ [ 75, 78 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3459
split_0_train_3459
[ { "id": "split_0_train_3459_passage", "type": "progene_text", "text": [ "We have used mice lacking the CKIs p21 ( Cip1 ) and p27 ( Kip1 ) to investigate this issue , specifically with respect to CDK regulation by mitogens ." ], "offsets": [ [ 0, 150 ] ] } ]
[ { "id": "split_0_train_5631_entity", "type": "progene_text", "text": [ "CKIs" ], "offsets": [ [ 30, 34 ] ], "normalized": [] }, { "id": "split_0_train_5632_entity", "type": "progene_text", "text": [ "p21 ( Cip1 )" ], "offsets": [ [ 35, 47 ] ], "normalized": [] }, { "id": "split_0_train_5633_entity", "type": "progene_text", "text": [ "p27 ( Kip1 )" ], "offsets": [ [ 52, 64 ] ], "normalized": [] }, { "id": "split_0_train_5634_entity", "type": "progene_text", "text": [ "CDK" ], "offsets": [ [ 122, 125 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3460
split_0_train_3460
[ { "id": "split_0_train_3460_passage", "type": "progene_text", "text": [ "RESULTS :" ], "offsets": [ [ 0, 9 ] ] } ]
[]
[]
[]
[]
split_0_train_3461
split_0_train_3461
[ { "id": "split_0_train_3461_passage", "type": "progene_text", "text": [ "We show that p27 is the major inhibitor of Cdk2 activity in mitogen - starved wild - type murine embryonic fibroblasts ( MEFs ) ." ], "offsets": [ [ 0, 129 ] ] } ]
[ { "id": "split_0_train_5635_entity", "type": "progene_text", "text": [ "p27" ], "offsets": [ [ 13, 16 ] ], "normalized": [] }, { "id": "split_0_train_5636_entity", "type": "progene_text", "text": [ "Cdk2" ], "offsets": [ [ 43, 47 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3462
split_0_train_3462
[ { "id": "split_0_train_3462_passage", "type": "progene_text", "text": [ "Nevertheless , inactivation of the cyclin E - Cdk2 complex in response to mitogen starvation occurs normally in MEFs that have a homozygous deletion of the p27 gene ." ], "offsets": [ [ 0, 166 ] ] } ]
[ { "id": "split_0_train_5637_entity", "type": "progene_text", "text": [ "cyclin E" ], "offsets": [ [ 35, 43 ] ], "normalized": [] }, { "id": "split_0_train_5638_entity", "type": "progene_text", "text": [ "Cdk2" ], "offsets": [ [ 46, 50 ] ], "normalized": [] }, { "id": "split_0_train_5639_entity", "type": "progene_text", "text": [ "p27" ], "offsets": [ [ 156, 159 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3463
split_0_train_3463
[ { "id": "split_0_train_3463_passage", "type": "progene_text", "text": [ "Moreover , CDK regulation by mitogens is also not affected by the absence of both p27 and p21 ." ], "offsets": [ [ 0, 95 ] ] } ]
[ { "id": "split_0_train_5640_entity", "type": "progene_text", "text": [ "CDK" ], "offsets": [ [ 11, 14 ] ], "normalized": [] }, { "id": "split_0_train_5641_entity", "type": "progene_text", "text": [ "p27" ], "offsets": [ [ 82, 85 ] ], "normalized": [] }, { "id": "split_0_train_5642_entity", "type": "progene_text", "text": [ "p21" ], "offsets": [ [ 90, 93 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3464
split_0_train_3464
[ { "id": "split_0_train_3464_passage", "type": "progene_text", "text": [ "A titratable Cdk2 inhibitor compensates for the absence of both CKIs , and we identify this inhibitor as p130 , a protein related to the retinoblastoma gene product Rb ." ], "offsets": [ [ 0, 169 ] ] } ]
[ { "id": "split_0_train_5643_entity", "type": "progene_text", "text": [ "Cdk2" ], "offsets": [ [ 13, 17 ] ], "normalized": [] }, { "id": "split_0_train_5644_entity", "type": "progene_text", "text": [ "CKIs" ], "offsets": [ [ 64, 68 ] ], "normalized": [] }, { "id": "split_0_train_5645_entity", "type": "progene_text", "text": [ "p130" ], "offsets": [ [ 105, 109 ] ], "normalized": [] }, { "id": "split_0_train_5646_entity", "type": "progene_text", "text": [ "retinoblastoma" ], "offsets": [ [ 137, 151 ] ], "normalized": [] }, { "id": "split_0_train_5647_entity", "type": "progene_text", "text": [ "Rb" ], "offsets": [ [ 165, 167 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3465
split_0_train_3465
[ { "id": "split_0_train_3465_passage", "type": "progene_text", "text": [ "Thus , cyclin E - Cdk2 kinase activity cannot be inhibited by mitogen starvation of MEFs that lack both p27 and p130 ." ], "offsets": [ [ 0, 118 ] ] } ]
[ { "id": "split_0_train_5648_entity", "type": "progene_text", "text": [ "cyclin E" ], "offsets": [ [ 7, 15 ] ], "normalized": [] }, { "id": "split_0_train_5649_entity", "type": "progene_text", "text": [ "Cdk2" ], "offsets": [ [ 18, 22 ] ], "normalized": [] }, { "id": "split_0_train_5650_entity", "type": "progene_text", "text": [ "kinase" ], "offsets": [ [ 23, 29 ] ], "normalized": [] }, { "id": "split_0_train_5651_entity", "type": "progene_text", "text": [ "p27" ], "offsets": [ [ 104, 107 ] ], "normalized": [] }, { "id": "split_0_train_5652_entity", "type": "progene_text", "text": [ "p130" ], "offsets": [ [ 112, 116 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3466
split_0_train_3466
[ { "id": "split_0_train_3466_passage", "type": "progene_text", "text": [ "In addition , cell types that naturally express low amounts of p130 , such as T lymphocytes , are completely dependent on p27 for regulation of the cyclin E - Cdk2 complex by mitogens ." ], "offsets": [ [ 0, 185 ] ] } ]
[ { "id": "split_0_train_5653_entity", "type": "progene_text", "text": [ "p130" ], "offsets": [ [ 63, 67 ] ], "normalized": [] }, { "id": "split_0_train_5654_entity", "type": "progene_text", "text": [ "p27" ], "offsets": [ [ 122, 125 ] ], "normalized": [] }, { "id": "split_0_train_5655_entity", "type": "progene_text", "text": [ "cyclin E" ], "offsets": [ [ 148, 156 ] ], "normalized": [] }, { "id": "split_0_train_5656_entity", "type": "progene_text", "text": [ "Cdk2" ], "offsets": [ [ 159, 163 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3467
split_0_train_3467
[ { "id": "split_0_train_3467_passage", "type": "progene_text", "text": [ "CONCLUSIONS :" ], "offsets": [ [ 0, 13 ] ] } ]
[]
[]
[]
[]
split_0_train_3468
split_0_train_3468
[ { "id": "split_0_train_3468_passage", "type": "progene_text", "text": [ "Inhibition of Cdk2 activity in mitogen - starved fibroblasts is usually performed by the CKI p27 , and to a minor extent by p21 ." ], "offsets": [ [ 0, 129 ] ] } ]
[ { "id": "split_0_train_5657_entity", "type": "progene_text", "text": [ "Cdk2" ], "offsets": [ [ 14, 18 ] ], "normalized": [] }, { "id": "split_0_train_5658_entity", "type": "progene_text", "text": [ "CKI p27" ], "offsets": [ [ 89, 96 ] ], "normalized": [] }, { "id": "split_0_train_5659_entity", "type": "progene_text", "text": [ "p21" ], "offsets": [ [ 124, 127 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3469
split_0_train_3469
[ { "id": "split_0_train_3469_passage", "type": "progene_text", "text": [ "Remarkably p130 , a protein in the Rb family that is not related to either p21 or p27 , will directly substitute for the CKIs and restore normal CDK regulation by mitogens in cells lacking both p27 and p21 ." ], "offsets": [ [ 0, 207 ] ] } ]
[ { "id": "split_0_train_5660_entity", "type": "progene_text", "text": [ "p130" ], "offsets": [ [ 11, 15 ] ], "normalized": [] }, { "id": "split_0_train_5661_entity", "type": "progene_text", "text": [ "Rb family" ], "offsets": [ [ 35, 44 ] ], "normalized": [] }, { "id": "split_0_train_5662_entity", "type": "progene_text", "text": [ "p21" ], "offsets": [ [ 75, 78 ] ], "normalized": [] }, { "id": "split_0_train_5663_entity", "type": "progene_text", "text": [ "p27" ], "offsets": [ [ 82, 85 ] ], "normalized": [] }, { "id": "split_0_train_5664_entity", "type": "progene_text", "text": [ "CKIs" ], "offsets": [ [ 121, 125 ] ], "normalized": [] }, { "id": "split_0_train_5665_entity", "type": "progene_text", "text": [ "CDK" ], "offsets": [ [ 145, 148 ] ], "normalized": [] }, { "id": "split_0_train_5666_entity", "type": "progene_text", "text": [ "p27" ], "offsets": [ [ 194, 197 ] ], "normalized": [] }, { "id": "split_0_train_5667_entity", "type": "progene_text", "text": [ "p21" ], "offsets": [ [ 202, 205 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3470
split_0_train_3470
[ { "id": "split_0_train_3470_passage", "type": "progene_text", "text": [ "This compensatory pathway may be important in settings in which CKIs are not expressed at standard levels , as is the case in many human tumors ." ], "offsets": [ [ 0, 145 ] ] } ]
[ { "id": "split_0_train_5668_entity", "type": "progene_text", "text": [ "CKIs" ], "offsets": [ [ 64, 68 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3471
split_0_train_3471
[ { "id": "split_0_train_3471_passage", "type": "progene_text", "text": [ "Hypersensitive site 2 specifies a unique function within the human beta-globin locus control region to stimulate globin gene transcription ." ], "offsets": [ [ 0, 140 ] ] } ]
[ { "id": "split_0_train_5669_entity", "type": "progene_text", "text": [ "beta-globin" ], "offsets": [ [ 67, 78 ] ], "normalized": [] }, { "id": "split_0_train_5670_entity", "type": "progene_text", "text": [ "globin" ], "offsets": [ [ 113, 119 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3472
split_0_train_3472
[ { "id": "split_0_train_3472_passage", "type": "progene_text", "text": [ "The human beta-globin locus control region ( LCR ) harbors both strong chromatin opening and enhancer activity when assayed in transgenic mice ." ], "offsets": [ [ 0, 144 ] ] } ]
[ { "id": "split_0_train_5671_entity", "type": "progene_text", "text": [ "beta-globin" ], "offsets": [ [ 10, 21 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3473
split_0_train_3473
[ { "id": "split_0_train_3473_passage", "type": "progene_text", "text": [ "To understand the contribution of individual DNase I hypersensitive sites ( HS ) to the function of the human beta-globin LCR , we have mutated the core elements within the context of a yeast artificial chromosome ( YAC ) carrying the entire locus and then analyzed the effect of these mutations on the formation of LCR HS elements and expression of the genes in transgenic mice ." ], "offsets": [ [ 0, 380 ] ] } ]
[ { "id": "split_0_train_5672_entity", "type": "progene_text", "text": [ "DNase I" ], "offsets": [ [ 45, 52 ] ], "normalized": [] }, { "id": "split_0_train_5673_entity", "type": "progene_text", "text": [ "beta-globin" ], "offsets": [ [ 110, 121 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3474
split_0_train_3474
[ { "id": "split_0_train_3474_passage", "type": "progene_text", "text": [ "In the present study , we examined the consequences of two different HS2 mutations ." ], "offsets": [ [ 0, 84 ] ] } ]
[]
[]
[]
[]
split_0_train_3475
split_0_train_3475
[ { "id": "split_0_train_3475_passage", "type": "progene_text", "text": [ "We first generated seven YAC transgenic lines bearing a deletion of the 375 - bp core enhancer of HS2 ." ], "offsets": [ [ 0, 103 ] ] } ]
[]
[]
[]
[]
split_0_train_3476
split_0_train_3476
[ { "id": "split_0_train_3476_passage", "type": "progene_text", "text": [ "Single - copy HS2 deletion mutants exhibited severely depressed HS site formation and expression of all of the human beta-globin genes at every developmental stage , confirming that HS2 is a vital , integral component of the LCR ." ], "offsets": [ [ 0, 230 ] ] } ]
[ { "id": "split_0_train_5674_entity", "type": "progene_text", "text": [ "beta-globin" ], "offsets": [ [ 117, 128 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3477
split_0_train_3477
[ { "id": "split_0_train_3477_passage", "type": "progene_text", "text": [ "We also analyzed four transgenic lines in which the core element of HS2 was replaced by that of HS3 and found that while HS3 is able to restore the chromatin - opening activity of the LCR , it is not able to functionally replace HS2 in mediating high - level globin gene transcription ." ], "offsets": [ [ 0, 286 ] ] } ]
[ { "id": "split_0_train_5675_entity", "type": "progene_text", "text": [ "globin" ], "offsets": [ [ 259, 265 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3478
split_0_train_3478
[ { "id": "split_0_train_3478_passage", "type": "progene_text", "text": [ "These results continue to support the hypothesis that HS2 , HS3 , and HS4 act as a single , integral unit to regulate human globin gene transcription as a holocomplex , but they can also be interpreted to say that formation of a DNase I hypersensitive holocomplex alone is not sufficient for mediating high - level globin gene transcription ." ], "offsets": [ [ 0, 342 ] ] } ]
[ { "id": "split_0_train_5676_entity", "type": "progene_text", "text": [ "globin" ], "offsets": [ [ 124, 130 ] ], "normalized": [] }, { "id": "split_0_train_5677_entity", "type": "progene_text", "text": [ "DNase I" ], "offsets": [ [ 229, 236 ] ], "normalized": [] }, { "id": "split_0_train_5678_entity", "type": "progene_text", "text": [ "globin" ], "offsets": [ [ 315, 321 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3479
split_0_train_3479
[ { "id": "split_0_train_3479_passage", "type": "progene_text", "text": [ "We therefore propose that the core elements must productively interact with one another to generate a unique subdomain within the nucleoprotein holocomplex that interacts in a stage - specific manner with individual globin gene promoters ." ], "offsets": [ [ 0, 239 ] ] } ]
[ { "id": "split_0_train_5679_entity", "type": "progene_text", "text": [ "globin" ], "offsets": [ [ 216, 222 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3480
split_0_train_3480
[ { "id": "split_0_train_3480_passage", "type": "progene_text", "text": [ "MDS1 / EVI1 enhances TGF-beta1 signaling and strengthens its growth - inhibitory effect but the leukemia - associated fusion protein AML1 / MDS1 / EVI1 , product of the t ( 3 ; 21 ) , abrogates growth - inhibition in response to TGF-beta1 ." ], "offsets": [ [ 0, 240 ] ] } ]
[ { "id": "split_0_train_5680_entity", "type": "progene_text", "text": [ "MDS1" ], "offsets": [ [ 0, 4 ] ], "normalized": [] }, { "id": "split_0_train_5681_entity", "type": "progene_text", "text": [ "EVI1" ], "offsets": [ [ 7, 11 ] ], "normalized": [] }, { "id": "split_0_train_5682_entity", "type": "progene_text", "text": [ "TGF-beta1" ], "offsets": [ [ 21, 30 ] ], "normalized": [] }, { "id": "split_0_train_5683_entity", "type": "progene_text", "text": [ "AML1" ], "offsets": [ [ 133, 137 ] ], "normalized": [] }, { "id": "split_0_train_5684_entity", "type": "progene_text", "text": [ "MDS1" ], "offsets": [ [ 140, 144 ] ], "normalized": [] }, { "id": "split_0_train_5685_entity", "type": "progene_text", "text": [ "EVI1" ], "offsets": [ [ 147, 151 ] ], "normalized": [] }, { "id": "split_0_train_5686_entity", "type": "progene_text", "text": [ "TGF-beta1" ], "offsets": [ [ 229, 238 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3481
split_0_train_3481
[ { "id": "split_0_train_3481_passage", "type": "progene_text", "text": [ "MDS1 / EVI1 , located on chromosome 3 band q26 , encodes a zinc - finger DNA - binding transcription activator not detected in normal hematopoietic cells but expressed in several normal tissues ." ], "offsets": [ [ 0, 195 ] ] } ]
[ { "id": "split_0_train_5687_entity", "type": "progene_text", "text": [ "MDS1" ], "offsets": [ [ 0, 4 ] ], "normalized": [] }, { "id": "split_0_train_5688_entity", "type": "progene_text", "text": [ "EVI1" ], "offsets": [ [ 7, 11 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3482
split_0_train_3482
[ { "id": "split_0_train_3482_passage", "type": "progene_text", "text": [ "MDS1 / EVI1 is inappropriately activated in myeloid leukemias following chromosomal rearrangements involving band 3q26 ." ], "offsets": [ [ 0, 120 ] ] } ]
[ { "id": "split_0_train_5689_entity", "type": "progene_text", "text": [ "MDS1" ], "offsets": [ [ 0, 4 ] ], "normalized": [] }, { "id": "split_0_train_5690_entity", "type": "progene_text", "text": [ "EVI1" ], "offsets": [ [ 7, 11 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3483
split_0_train_3483
[ { "id": "split_0_train_3483_passage", "type": "progene_text", "text": [ "The rearrangements lead either to gene truncation , and to expression of the transcription repressor EVI1 , as seen in the t ( 3 ; 3 ) ( q21 ; q26 ) and inv ( 3 ) ( q21q26 ) , or to gene fusion , as seen in the t ( 3 ; 21 ) ( q26 ; q22 ) which results in the fusion protein AML1 / MDS1 / EVI1 ." ], "offsets": [ [ 0, 294 ] ] } ]
[ { "id": "split_0_train_5691_entity", "type": "progene_text", "text": [ "EVI1" ], "offsets": [ [ 101, 105 ] ], "normalized": [] }, { "id": "split_0_train_5692_entity", "type": "progene_text", "text": [ "inv" ], "offsets": [ [ 153, 156 ] ], "normalized": [] }, { "id": "split_0_train_5693_entity", "type": "progene_text", "text": [ "AML1" ], "offsets": [ [ 274, 278 ] ], "normalized": [] }, { "id": "split_0_train_5694_entity", "type": "progene_text", "text": [ "MDS1" ], "offsets": [ [ 281, 285 ] ], "normalized": [] }, { "id": "split_0_train_5695_entity", "type": "progene_text", "text": [ "EVI1" ], "offsets": [ [ 288, 292 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3484
split_0_train_3484
[ { "id": "split_0_train_3484_passage", "type": "progene_text", "text": [ "This fusion protein contains the DNA - binding domain of the transcription factor AML1 fused in-frame to the entire MDS1 / EVI1 with the exclusion of its first 12 amino acids ." ], "offsets": [ [ 0, 176 ] ] } ]
[ { "id": "split_0_train_5696_entity", "type": "progene_text", "text": [ "transcription factor" ], "offsets": [ [ 61, 81 ] ], "normalized": [] }, { "id": "split_0_train_5697_entity", "type": "progene_text", "text": [ "AML1" ], "offsets": [ [ 82, 86 ] ], "normalized": [] }, { "id": "split_0_train_5698_entity", "type": "progene_text", "text": [ "MDS1" ], "offsets": [ [ 116, 120 ] ], "normalized": [] }, { "id": "split_0_train_5699_entity", "type": "progene_text", "text": [ "EVI1" ], "offsets": [ [ 123, 127 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3485
split_0_train_3485
[ { "id": "split_0_train_3485_passage", "type": "progene_text", "text": [ "In this report , we have analyzed the response of the hematopoietic precursor cell line 32Dcl3 , expressing either the normal protein MDS1 / EVI1 or the fusion protein AML1 / MDS1 / EVI1 , to factors that control cell differentiation or cell replication ." ], "offsets": [ [ 0, 255 ] ] } ]
[ { "id": "split_0_train_5700_entity", "type": "progene_text", "text": [ "MDS1" ], "offsets": [ [ 134, 138 ] ], "normalized": [] }, { "id": "split_0_train_5701_entity", "type": "progene_text", "text": [ "EVI1" ], "offsets": [ [ 141, 145 ] ], "normalized": [] }, { "id": "split_0_train_5702_entity", "type": "progene_text", "text": [ "AML1" ], "offsets": [ [ 168, 172 ] ], "normalized": [] }, { "id": "split_0_train_5703_entity", "type": "progene_text", "text": [ "MDS1" ], "offsets": [ [ 175, 179 ] ], "normalized": [] }, { "id": "split_0_train_5704_entity", "type": "progene_text", "text": [ "EVI1" ], "offsets": [ [ 182, 186 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3486
split_0_train_3486
[ { "id": "split_0_train_3486_passage", "type": "progene_text", "text": [ "The 32Dcl3 cells are IL-3 - dependent for growth and they differentiate into granulocytes when exposed to G-CSF ." ], "offsets": [ [ 0, 113 ] ] } ]
[ { "id": "split_0_train_5705_entity", "type": "progene_text", "text": [ "IL-3" ], "offsets": [ [ 21, 25 ] ], "normalized": [] }, { "id": "split_0_train_5706_entity", "type": "progene_text", "text": [ "G-CSF" ], "offsets": [ [ 106, 111 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3487
split_0_train_3487
[ { "id": "split_0_train_3487_passage", "type": "progene_text", "text": [ "They are growth - inhibited by TGF-beta1 ." ], "offsets": [ [ 0, 42 ] ] } ]
[ { "id": "split_0_train_5707_entity", "type": "progene_text", "text": [ "TGF-beta1" ], "offsets": [ [ 31, 40 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3488
split_0_train_3488
[ { "id": "split_0_train_3488_passage", "type": "progene_text", "text": [ "We show that whereas the expression of MDS1 / EVI1 has no effect on granulocytic differentiation induced by G-CSF , expression of AML1 / MDS1 / EVI1 blocks differentiation resulting in cell death ." ], "offsets": [ [ 0, 197 ] ] } ]
[ { "id": "split_0_train_5708_entity", "type": "progene_text", "text": [ "MDS1" ], "offsets": [ [ 39, 43 ] ], "normalized": [] }, { "id": "split_0_train_5709_entity", "type": "progene_text", "text": [ "EVI1" ], "offsets": [ [ 46, 50 ] ], "normalized": [] }, { "id": "split_0_train_5710_entity", "type": "progene_text", "text": [ "G-CSF" ], "offsets": [ [ 108, 113 ] ], "normalized": [] }, { "id": "split_0_train_5711_entity", "type": "progene_text", "text": [ "AML1" ], "offsets": [ [ 130, 134 ] ], "normalized": [] }, { "id": "split_0_train_5712_entity", "type": "progene_text", "text": [ "MDS1" ], "offsets": [ [ 137, 141 ] ], "normalized": [] }, { "id": "split_0_train_5713_entity", "type": "progene_text", "text": [ "EVI1" ], "offsets": [ [ 144, 148 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3489
split_0_train_3489
[ { "id": "split_0_train_3489_passage", "type": "progene_text", "text": [ "This effect is similar to that previously described by others for 32Dcl3 cells that express transgenic Evil ." ], "offsets": [ [ 0, 109 ] ] } ]
[]
[]
[]
[]
split_0_train_3490
split_0_train_3490
[ { "id": "split_0_train_3490_passage", "type": "progene_text", "text": [ "Furthermore , we show that whereas the expression of the fusion protein AML1 / MDS1 / EVI1 completely abrogates the growth - inhibitory effect of TGF-beta1 and allows 32Dcl3 cells to proliferate , expression of the normal protein MDS1 / EVI1 has the opposite effect , and it strengthens the response of cells to the growth - inhibitory effect of TGF-beta1 ." ], "offsets": [ [ 0, 357 ] ] } ]
[ { "id": "split_0_train_5714_entity", "type": "progene_text", "text": [ "AML1" ], "offsets": [ [ 72, 76 ] ], "normalized": [] }, { "id": "split_0_train_5715_entity", "type": "progene_text", "text": [ "MDS1" ], "offsets": [ [ 79, 83 ] ], "normalized": [] }, { "id": "split_0_train_5716_entity", "type": "progene_text", "text": [ "EVI1" ], "offsets": [ [ 86, 90 ] ], "normalized": [] }, { "id": "split_0_train_5717_entity", "type": "progene_text", "text": [ "TGF-beta1" ], "offsets": [ [ 146, 155 ] ], "normalized": [] }, { "id": "split_0_train_5718_entity", "type": "progene_text", "text": [ "MDS1" ], "offsets": [ [ 230, 234 ] ], "normalized": [] }, { "id": "split_0_train_5719_entity", "type": "progene_text", "text": [ "EVI1" ], "offsets": [ [ 237, 241 ] ], "normalized": [] }, { "id": "split_0_train_5720_entity", "type": "progene_text", "text": [ "TGF-beta1" ], "offsets": [ [ 346, 355 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3491
split_0_train_3491
[ { "id": "split_0_train_3491_passage", "type": "progene_text", "text": [ "By using the yeast two - hybrid system , we also show that EVI1 ( contained in its entirety in MDS1 / EVI1 and AML1 / MDS1 / EVI1 ) physically interacts with SMAD3 , which is an intracellular mediator of TGF-beta1 signaling ." ], "offsets": [ [ 0, 225 ] ] } ]
[ { "id": "split_0_train_5721_entity", "type": "progene_text", "text": [ "EVI1" ], "offsets": [ [ 59, 63 ] ], "normalized": [] }, { "id": "split_0_train_5722_entity", "type": "progene_text", "text": [ "MDS1" ], "offsets": [ [ 95, 99 ] ], "normalized": [] }, { "id": "split_0_train_5723_entity", "type": "progene_text", "text": [ "EVI1" ], "offsets": [ [ 102, 106 ] ], "normalized": [] }, { "id": "split_0_train_5724_entity", "type": "progene_text", "text": [ "AML1" ], "offsets": [ [ 111, 115 ] ], "normalized": [] }, { "id": "split_0_train_5725_entity", "type": "progene_text", "text": [ "MDS1" ], "offsets": [ [ 118, 122 ] ], "normalized": [] }, { "id": "split_0_train_5726_entity", "type": "progene_text", "text": [ "EVI1" ], "offsets": [ [ 125, 129 ] ], "normalized": [] }, { "id": "split_0_train_5727_entity", "type": "progene_text", "text": [ "SMAD3" ], "offsets": [ [ 158, 163 ] ], "normalized": [] }, { "id": "split_0_train_5728_entity", "type": "progene_text", "text": [ "TGF-beta1" ], "offsets": [ [ 204, 213 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3492
split_0_train_3492
[ { "id": "split_0_train_3492_passage", "type": "progene_text", "text": [ "Finally , we have correlated the response of the cells to G-CSF or TGF-beta1 with the ability of the normal and fusion proteins to activate or repress promoters which they can directly regulate by binding to the promoter site ." ], "offsets": [ [ 0, 227 ] ] } ]
[ { "id": "split_0_train_5729_entity", "type": "progene_text", "text": [ "G-CSF" ], "offsets": [ [ 58, 63 ] ], "normalized": [] }, { "id": "split_0_train_5730_entity", "type": "progene_text", "text": [ "TGF-beta1" ], "offsets": [ [ 67, 76 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3493
split_0_train_3493
[ { "id": "split_0_train_3493_passage", "type": "progene_text", "text": [ "We propose that mutations of MDS1 / EVI1 either by gene truncation resulting in the transcription repressor EVI1 or by gene fusion to AML1 lead to an altered cellular response to growth and differentiation factors that could result in leukemic transformation ." ], "offsets": [ [ 0, 260 ] ] } ]
[ { "id": "split_0_train_5731_entity", "type": "progene_text", "text": [ "MDS1" ], "offsets": [ [ 29, 33 ] ], "normalized": [] }, { "id": "split_0_train_5732_entity", "type": "progene_text", "text": [ "EVI1" ], "offsets": [ [ 36, 40 ] ], "normalized": [] }, { "id": "split_0_train_5733_entity", "type": "progene_text", "text": [ "EVI1" ], "offsets": [ [ 108, 112 ] ], "normalized": [] }, { "id": "split_0_train_5734_entity", "type": "progene_text", "text": [ "AML1" ], "offsets": [ [ 134, 138 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3494
split_0_train_3494
[ { "id": "split_0_train_3494_passage", "type": "progene_text", "text": [ "The different response of myeloid cells ectopically expressing the normal or the fusion protein to G-CSF and TGF-beta1 could depend on the different transactivation properties of these proteins resulting in divergent expression of downstream genes regulated by the two proteins ." ], "offsets": [ [ 0, 279 ] ] } ]
[ { "id": "split_0_train_5735_entity", "type": "progene_text", "text": [ "G-CSF" ], "offsets": [ [ 99, 104 ] ], "normalized": [] }, { "id": "split_0_train_5736_entity", "type": "progene_text", "text": [ "TGF-beta1" ], "offsets": [ [ 109, 118 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3495
split_0_train_3495
[ { "id": "split_0_train_3495_passage", "type": "progene_text", "text": [ "Conformational aspects of HIV-1 integrase inhibition by a peptide derived from the enzyme central domain and by antibodies raised against this peptide ." ], "offsets": [ [ 0, 152 ] ] } ]
[ { "id": "split_0_train_5737_entity", "type": "progene_text", "text": [ "integrase" ], "offsets": [ [ 32, 41 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3496
split_0_train_3496
[ { "id": "split_0_train_3496_passage", "type": "progene_text", "text": [ "Monospecific antibodies were raised against a synthetic peptide K159 ( SQGVVESMNKELKKIIGQVRDQAEHLKTA ) reproducing the segment 147 - 175 of HIV-1 integrase ( IN ) ." ], "offsets": [ [ 0, 164 ] ] } ]
[ { "id": "split_0_train_5738_entity", "type": "progene_text", "text": [ "integrase" ], "offsets": [ [ 146, 155 ] ], "normalized": [] }, { "id": "split_0_train_5739_entity", "type": "progene_text", "text": [ "IN" ], "offsets": [ [ 158, 160 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_3497
split_0_train_3497
[ { "id": "split_0_train_3497_passage", "type": "progene_text", "text": [ "Synthesis of substituted and truncated analogs of K159 led us to identify the functional epitope reacting with antibodies within the C - terminal portion 163 - 175 of K159 ." ], "offsets": [ [ 0, 173 ] ] } ]
[]
[]
[]
[]
split_0_train_3498
split_0_train_3498
[ { "id": "split_0_train_3498_passage", "type": "progene_text", "text": [ "Conformational studies combining secondary structure predictions , CD and NMR spectroscopy together with ELISA assays , showed that the greater is the propensity of the epitope for helix formation the higher is the recognition by anti - K159 ." ], "offsets": [ [ 0, 243 ] ] } ]
[]
[]
[]
[]
split_0_train_3499
split_0_train_3499
[ { "id": "split_0_train_3499_passage", "type": "progene_text", "text": [ "Both the antibodies and the antigenic peptide K159 exhibited inhibitory activities against IN ." ], "offsets": [ [ 0, 95 ] ] } ]
[ { "id": "split_0_train_5740_entity", "type": "progene_text", "text": [ "IN" ], "offsets": [ [ 91, 93 ] ], "normalized": [] } ]
[]
[]
[]