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split_0_train_6000
split_0_train_6000
[ { "id": "split_0_train_6000_passage", "type": "progene_text", "text": [ "Furthermore , 11beta-HSD-1 activity assessed by measurement of the urinary ratio of ( tetrahydrocortisol ( THF ) + 5alphaTHF ) / ( tetrahydrocortisone ) was significantly increased after ACTH treatment compared with the control group ." ], "offsets": [ [ 0, 235 ] ] } ]
[ { "id": "split_0_train_9319_entity", "type": "progene_text", "text": [ "11beta-HSD-1" ], "offsets": [ [ 14, 26 ] ], "normalized": [] }, { "id": "split_0_train_9320_entity", "type": "progene_text", "text": [ "ACTH" ], "offsets": [ [ 187, 191 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6001
split_0_train_6001
[ { "id": "split_0_train_6001_passage", "type": "progene_text", "text": [ "Plasma levels of cortisol , cortisone , progesterone , 17-hydroxyprogesterone and androstenedione increased significantly following in vivo ACTH treatment ." ], "offsets": [ [ 0, 156 ] ] } ]
[ { "id": "split_0_train_9321_entity", "type": "progene_text", "text": [ "ACTH" ], "offsets": [ [ 140, 144 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6002
split_0_train_6002
[ { "id": "split_0_train_6002_passage", "type": "progene_text", "text": [ "The enhanced reductase activity of the hepatic and renal 11beta-HSD-1 is apparently caused by cortisol or other ACTH - dependent steroids rather than by ACTH itself ." ], "offsets": [ [ 0, 166 ] ] } ]
[ { "id": "split_0_train_9322_entity", "type": "progene_text", "text": [ "reductase" ], "offsets": [ [ 13, 22 ] ], "normalized": [] }, { "id": "split_0_train_9323_entity", "type": "progene_text", "text": [ "11beta-HSD-1" ], "offsets": [ [ 57, 69 ] ], "normalized": [] }, { "id": "split_0_train_9324_entity", "type": "progene_text", "text": [ "ACTH" ], "offsets": [ [ 112, 116 ] ], "normalized": [] }, { "id": "split_0_train_9325_entity", "type": "progene_text", "text": [ "ACTH" ], "offsets": [ [ 153, 157 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6003
split_0_train_6003
[ { "id": "split_0_train_6003_passage", "type": "progene_text", "text": [ "This may be an important fine regulation of the glucocorticoid tonus for stress adaptation in every organ , e.g. enhanced gluconeogenesis in liver ." ], "offsets": [ [ 0, 148 ] ] } ]
[]
[]
[]
[]
split_0_train_6004
split_0_train_6004
[ { "id": "split_0_train_6004_passage", "type": "progene_text", "text": [ "Cloning and sequence analysis of a mitochondrial gene cluster encoding cytochrome C oxidase subunit III from Trichoderma pseudokoningii ." ], "offsets": [ [ 0, 137 ] ] } ]
[ { "id": "split_0_train_9326_entity", "type": "progene_text", "text": [ "cytochrome C oxidase subunit III" ], "offsets": [ [ 71, 103 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6005
split_0_train_6005
[ { "id": "split_0_train_6005_passage", "type": "progene_text", "text": [ "A mitochondrial gene cluster encoding cytochrome c oxidase subunit III ( COX3 ) , an ORF ( called ORF250 ) similar to NADH dehydrogenase subunit VI ( ND6 ) , ten tRNA molecules , partial rRNA small subunit and rRNA large subunit from Trichoderma pseudokoningii S38 was cloned and sequenced ." ], "offsets": [ [ 0, 291 ] ] } ]
[ { "id": "split_0_train_9327_entity", "type": "progene_text", "text": [ "cytochrome c oxidase subunit III" ], "offsets": [ [ 38, 70 ] ], "normalized": [] }, { "id": "split_0_train_9328_entity", "type": "progene_text", "text": [ "COX3" ], "offsets": [ [ 73, 77 ] ], "normalized": [] }, { "id": "split_0_train_9329_entity", "type": "progene_text", "text": [ "NADH dehydrogenase subunit VI" ], "offsets": [ [ 118, 147 ] ], "normalized": [] }, { "id": "split_0_train_9330_entity", "type": "progene_text", "text": [ "ND6" ], "offsets": [ [ 150, 153 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6006
split_0_train_6006
[ { "id": "split_0_train_6006_passage", "type": "progene_text", "text": [ "These genes are tandemly clustered on the mitochondrial genome of Trichoderma pseudokoningii S38 ." ], "offsets": [ [ 0, 98 ] ] } ]
[]
[]
[]
[]
split_0_train_6007
split_0_train_6007
[ { "id": "split_0_train_6007_passage", "type": "progene_text", "text": [ "Phylogenetic analysis showed that cytochrome C oxidase subunits III exhibited high degree of similarity to sequences from Hypocrea jecorina , Verticillium lecanii , Podospora anserine , Neurospora crassa and Magnaporthe grisea ( 99 , 90 , 84 , 82 and 79 % identity , respectively ) ." ], "offsets": [ [ 0, 283 ] ] } ]
[ { "id": "split_0_train_9331_entity", "type": "progene_text", "text": [ "cytochrome C oxidase subunits III" ], "offsets": [ [ 34, 67 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6008
split_0_train_6008
[ { "id": "split_0_train_6008_passage", "type": "progene_text", "text": [ "Prediction of transmembrane helices revealed that COX3 was a transmembrane protein ." ], "offsets": [ [ 0, 84 ] ] } ]
[ { "id": "split_0_train_9332_entity", "type": "progene_text", "text": [ "COX3" ], "offsets": [ [ 50, 54 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6009
split_0_train_6009
[ { "id": "split_0_train_6009_passage", "type": "progene_text", "text": [ "Northern dot blot analysis showed that the cytochrome c oxidase subunits III gene we had cloned is actively transcribed in the T. pseudokoningii mitochondria ." ], "offsets": [ [ 0, 159 ] ] } ]
[ { "id": "split_0_train_9333_entity", "type": "progene_text", "text": [ "cytochrome c oxidase subunits III" ], "offsets": [ [ 43, 76 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6010
split_0_train_6010
[ { "id": "split_0_train_6010_passage", "type": "progene_text", "text": [ "The L1 major capsid protein of human papillomavirus type 11 interacts with Kap beta2 and Kap beta3 nuclear import receptors ." ], "offsets": [ [ 0, 125 ] ] } ]
[ { "id": "split_0_train_9334_entity", "type": "progene_text", "text": [ "L1 major capsid protein" ], "offsets": [ [ 4, 27 ] ], "normalized": [] }, { "id": "split_0_train_9335_entity", "type": "progene_text", "text": [ "Kap beta2" ], "offsets": [ [ 75, 84 ] ], "normalized": [] }, { "id": "split_0_train_9336_entity", "type": "progene_text", "text": [ "Kap beta3" ], "offsets": [ [ 89, 98 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6011
split_0_train_6011
[ { "id": "split_0_train_6011_passage", "type": "progene_text", "text": [ "We have previously shown that the L1 major capsid protein of low - risk HPV11 binds to the Kap alpha2 adapter and enters the nucleus via a Kap alpha2beta1 - mediated pathway ." ], "offsets": [ [ 0, 175 ] ] } ]
[ { "id": "split_0_train_9337_entity", "type": "progene_text", "text": [ "L1 major capsid protein" ], "offsets": [ [ 34, 57 ] ], "normalized": [] }, { "id": "split_0_train_9338_entity", "type": "progene_text", "text": [ "Kap alpha2" ], "offsets": [ [ 91, 101 ] ], "normalized": [] }, { "id": "split_0_train_9339_entity", "type": "progene_text", "text": [ "Kap alpha2beta1" ], "offsets": [ [ 139, 154 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6012
split_0_train_6012
[ { "id": "split_0_train_6012_passage", "type": "progene_text", "text": [ "In this study , we discovered that HPV11 L1 capsomeres bind to Kap beta2 import receptor , known to mediate nuclear import of hnRNP A1 via interaction with its nuclear localization signal termed M9 ." ], "offsets": [ [ 0, 199 ] ] } ]
[ { "id": "split_0_train_9340_entity", "type": "progene_text", "text": [ "L1" ], "offsets": [ [ 41, 43 ] ], "normalized": [] }, { "id": "split_0_train_9341_entity", "type": "progene_text", "text": [ "Kap beta2" ], "offsets": [ [ 63, 72 ] ], "normalized": [] }, { "id": "split_0_train_9342_entity", "type": "progene_text", "text": [ "hnRNP A1" ], "offsets": [ [ 126, 134 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6013
split_0_train_6013
[ { "id": "split_0_train_6013_passage", "type": "progene_text", "text": [ "Significantly , binding of HPV11 L1 capsomeres to Kap beta2 inhibited the nuclear import of Kap beta2 , and its specific M9 - containing cargo ." ], "offsets": [ [ 0, 144 ] ] } ]
[ { "id": "split_0_train_9343_entity", "type": "progene_text", "text": [ "L1" ], "offsets": [ [ 33, 35 ] ], "normalized": [] }, { "id": "split_0_train_9344_entity", "type": "progene_text", "text": [ "Kap beta2" ], "offsets": [ [ 50, 59 ] ], "normalized": [] }, { "id": "split_0_train_9345_entity", "type": "progene_text", "text": [ "Kap beta2" ], "offsets": [ [ 92, 101 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6014
split_0_train_6014
[ { "id": "split_0_train_6014_passage", "type": "progene_text", "text": [ "Interestingly , HPV11 L1 capsomeres also interacted with Kap beta3 import receptor and inhibited Kap beta3 nuclear import ." ], "offsets": [ [ 0, 123 ] ] } ]
[ { "id": "split_0_train_9346_entity", "type": "progene_text", "text": [ "L1" ], "offsets": [ [ 22, 24 ] ], "normalized": [] }, { "id": "split_0_train_9347_entity", "type": "progene_text", "text": [ "Kap beta3" ], "offsets": [ [ 57, 66 ] ], "normalized": [] }, { "id": "split_0_train_9348_entity", "type": "progene_text", "text": [ "Kap beta3" ], "offsets": [ [ 97, 106 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6015
split_0_train_6015
[ { "id": "split_0_train_6015_passage", "type": "progene_text", "text": [ "Moreover , the L1 capsomeres of high - risk HPV-16 shared these activities ." ], "offsets": [ [ 0, 76 ] ] } ]
[ { "id": "split_0_train_9349_entity", "type": "progene_text", "text": [ "L1" ], "offsets": [ [ 15, 17 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6016
split_0_train_6016
[ { "id": "split_0_train_6016_passage", "type": "progene_text", "text": [ "These data suggest that HPV L1 major capsid proteins interact with Kap beta2 and Kap beta3 , and they may inhibit the Kap beta2 - and Kap beta3 - mediated nuclear import pathways during the productive phase of the viral life cycle when the virions are assembled and released ." ], "offsets": [ [ 0, 276 ] ] } ]
[ { "id": "split_0_train_9350_entity", "type": "progene_text", "text": [ "L1 major capsid proteins" ], "offsets": [ [ 28, 52 ] ], "normalized": [] }, { "id": "split_0_train_9351_entity", "type": "progene_text", "text": [ "Kap beta2" ], "offsets": [ [ 67, 76 ] ], "normalized": [] }, { "id": "split_0_train_9352_entity", "type": "progene_text", "text": [ "Kap beta3" ], "offsets": [ [ 81, 90 ] ], "normalized": [] }, { "id": "split_0_train_9353_entity", "type": "progene_text", "text": [ "Kap beta2" ], "offsets": [ [ 118, 127 ] ], "normalized": [] }, { "id": "split_0_train_9354_entity", "type": "progene_text", "text": [ "Kap beta3" ], "offsets": [ [ 134, 143 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6017
split_0_train_6017
[ { "id": "split_0_train_6017_passage", "type": "progene_text", "text": [ "Crystal structure of the human natural killer cell activating receptor KIR2DS2 ( CD158j ) ." ], "offsets": [ [ 0, 91 ] ] } ]
[ { "id": "split_0_train_9355_entity", "type": "progene_text", "text": [ "KIR2DS2" ], "offsets": [ [ 71, 78 ] ], "normalized": [] }, { "id": "split_0_train_9356_entity", "type": "progene_text", "text": [ "CD158j" ], "offsets": [ [ 81, 87 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6018
split_0_train_6018
[ { "id": "split_0_train_6018_passage", "type": "progene_text", "text": [ "Killer cell Ig - like receptors ( KIRs ) regulate the function of human natural killer and T cell subsets ." ], "offsets": [ [ 0, 107 ] ] } ]
[ { "id": "split_0_train_9357_entity", "type": "progene_text", "text": [ "Killer cell Ig - like receptors" ], "offsets": [ [ 0, 31 ] ], "normalized": [] }, { "id": "split_0_train_9358_entity", "type": "progene_text", "text": [ "KIRs" ], "offsets": [ [ 34, 38 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6019
split_0_train_6019
[ { "id": "split_0_train_6019_passage", "type": "progene_text", "text": [ "A feature of the KIR locus is the clustering of homologous genes encoding for inhibitory and activating KIR ." ], "offsets": [ [ 0, 109 ] ] } ]
[ { "id": "split_0_train_9359_entity", "type": "progene_text", "text": [ "KIR" ], "offsets": [ [ 17, 20 ] ], "normalized": [] }, { "id": "split_0_train_9360_entity", "type": "progene_text", "text": [ "KIR" ], "offsets": [ [ 104, 107 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6020
split_0_train_6020
[ { "id": "split_0_train_6020_passage", "type": "progene_text", "text": [ "Inhibitory and activating KIR differ for ligand specificities and/or affinities ." ], "offsets": [ [ 0, 81 ] ] } ]
[ { "id": "split_0_train_9361_entity", "type": "progene_text", "text": [ "KIR" ], "offsets": [ [ 26, 29 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6021
split_0_train_6021
[ { "id": "split_0_train_6021_passage", "type": "progene_text", "text": [ "In particular , we show here with KIR tetramers that activating KIR2DS2 does not bind HLA-Cw3 molecules recognized by inhibitory KIR2DL2 , despite 99 % extracellular amino acid identity ." ], "offsets": [ [ 0, 187 ] ] } ]
[ { "id": "split_0_train_9362_entity", "type": "progene_text", "text": [ "KIR" ], "offsets": [ [ 34, 37 ] ], "normalized": [] }, { "id": "split_0_train_9363_entity", "type": "progene_text", "text": [ "KIR2DS2" ], "offsets": [ [ 64, 71 ] ], "normalized": [] }, { "id": "split_0_train_9364_entity", "type": "progene_text", "text": [ "HLA-Cw3" ], "offsets": [ [ 86, 93 ] ], "normalized": [] }, { "id": "split_0_train_9365_entity", "type": "progene_text", "text": [ "KIR2DL2" ], "offsets": [ [ 129, 136 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6022
split_0_train_6022
[ { "id": "split_0_train_6022_passage", "type": "progene_text", "text": [ "We also report the 2.3 - A structure of KIR2DS2 , which reveals subtle displacements of two residues ( Tyr45 and Gln71 ) involved in the interaction of KIR2DL2 with HLA-Cw3 ." ], "offsets": [ [ 0, 174 ] ] } ]
[ { "id": "split_0_train_9366_entity", "type": "progene_text", "text": [ "KIR2DS2" ], "offsets": [ [ 40, 47 ] ], "normalized": [] }, { "id": "split_0_train_9367_entity", "type": "progene_text", "text": [ "KIR2DL2" ], "offsets": [ [ 152, 159 ] ], "normalized": [] }, { "id": "split_0_train_9368_entity", "type": "progene_text", "text": [ "HLA-Cw3" ], "offsets": [ [ 165, 172 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6023
split_0_train_6023
[ { "id": "split_0_train_6023_passage", "type": "progene_text", "text": [ "These results show that KIR molecules cannot tolerate any variability in their three - dimensional structure without altering their MHC class I recognition capacities ." ], "offsets": [ [ 0, 168 ] ] } ]
[ { "id": "split_0_train_9369_entity", "type": "progene_text", "text": [ "KIR" ], "offsets": [ [ 24, 27 ] ], "normalized": [] }, { "id": "split_0_train_9370_entity", "type": "progene_text", "text": [ "MHC class I" ], "offsets": [ [ 132, 143 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6024
split_0_train_6024
[ { "id": "split_0_train_6024_passage", "type": "progene_text", "text": [ "Therefore , the mode of recognition used by KIR largely differs from the conformational changes that characterize T cell receptor or NKG2D interaction with their respective ligands ." ], "offsets": [ [ 0, 182 ] ] } ]
[ { "id": "split_0_train_9371_entity", "type": "progene_text", "text": [ "KIR" ], "offsets": [ [ 44, 47 ] ], "normalized": [] }, { "id": "split_0_train_9372_entity", "type": "progene_text", "text": [ "NKG2D" ], "offsets": [ [ 133, 138 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6025
split_0_train_6025
[ { "id": "split_0_train_6025_passage", "type": "progene_text", "text": [ "The sensor protein KdpD inserts into the Escherichia coli membrane independent of the Sec translocase and YidC ." ], "offsets": [ [ 0, 112 ] ] } ]
[ { "id": "split_0_train_9373_entity", "type": "progene_text", "text": [ "KdpD" ], "offsets": [ [ 19, 23 ] ], "normalized": [] }, { "id": "split_0_train_9374_entity", "type": "progene_text", "text": [ "Sec translocase" ], "offsets": [ [ 86, 101 ] ], "normalized": [] }, { "id": "split_0_train_9375_entity", "type": "progene_text", "text": [ "YidC" ], "offsets": [ [ 106, 110 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6026
split_0_train_6026
[ { "id": "split_0_train_6026_passage", "type": "progene_text", "text": [ "KdpD is a sensor kinase protein in the inner membrane of Escherichia coli containing four transmembrane regions ." ], "offsets": [ [ 0, 113 ] ] } ]
[ { "id": "split_0_train_9376_entity", "type": "progene_text", "text": [ "KdpD" ], "offsets": [ [ 0, 4 ] ], "normalized": [] }, { "id": "split_0_train_9377_entity", "type": "progene_text", "text": [ "sensor kinase" ], "offsets": [ [ 10, 23 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6027
split_0_train_6027
[ { "id": "split_0_train_6027_passage", "type": "progene_text", "text": [ "The periplasmic loops connecting the transmembrane regions are intriguingly short and protease mapping allowed us to only follow the translocation of the second periplasmic loop ." ], "offsets": [ [ 0, 179 ] ] } ]
[ { "id": "split_0_train_9378_entity", "type": "progene_text", "text": [ "protease" ], "offsets": [ [ 86, 94 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6028
split_0_train_6028
[ { "id": "split_0_train_6028_passage", "type": "progene_text", "text": [ "The results show that neither the Sec translocase nor the YidC protein are required for membrane insertion of the second loop of KdpD ." ], "offsets": [ [ 0, 135 ] ] } ]
[ { "id": "split_0_train_9379_entity", "type": "progene_text", "text": [ "Sec translocase" ], "offsets": [ [ 34, 49 ] ], "normalized": [] }, { "id": "split_0_train_9380_entity", "type": "progene_text", "text": [ "YidC" ], "offsets": [ [ 58, 62 ] ], "normalized": [] }, { "id": "split_0_train_9381_entity", "type": "progene_text", "text": [ "KdpD" ], "offsets": [ [ 129, 133 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6029
split_0_train_6029
[ { "id": "split_0_train_6029_passage", "type": "progene_text", "text": [ "To study the translocation of the first periplasmic loop a short HA epitope tag was genetically introduced into this region ." ], "offsets": [ [ 0, 125 ] ] } ]
[]
[]
[]
[]
split_0_train_6030
split_0_train_6030
[ { "id": "split_0_train_6030_passage", "type": "progene_text", "text": [ "The results show that also the first loop was translocated independently of YidC and the Sec translocase ." ], "offsets": [ [ 0, 106 ] ] } ]
[ { "id": "split_0_train_9382_entity", "type": "progene_text", "text": [ "YidC" ], "offsets": [ [ 76, 80 ] ], "normalized": [] }, { "id": "split_0_train_9383_entity", "type": "progene_text", "text": [ "Sec translocase" ], "offsets": [ [ 89, 104 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6031
split_0_train_6031
[ { "id": "split_0_train_6031_passage", "type": "progene_text", "text": [ "We conclude that KdpD resembles a new class of membrane proteins that insert into the membrane without enzymatic assistance by the known translocases ." ], "offsets": [ [ 0, 151 ] ] } ]
[ { "id": "split_0_train_9384_entity", "type": "progene_text", "text": [ "KdpD" ], "offsets": [ [ 17, 21 ] ], "normalized": [] }, { "id": "split_0_train_9385_entity", "type": "progene_text", "text": [ "translocases" ], "offsets": [ [ 137, 149 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6032
split_0_train_6032
[ { "id": "split_0_train_6032_passage", "type": "progene_text", "text": [ "When the second periplasmic loop was extended by an epitope tag to 27 amino acid residues , the membrane insertion of this loop of KdpD depended on SecE and YidC ." ], "offsets": [ [ 0, 163 ] ] } ]
[ { "id": "split_0_train_9386_entity", "type": "progene_text", "text": [ "KdpD" ], "offsets": [ [ 131, 135 ] ], "normalized": [] }, { "id": "split_0_train_9387_entity", "type": "progene_text", "text": [ "SecE" ], "offsets": [ [ 148, 152 ] ], "normalized": [] }, { "id": "split_0_train_9388_entity", "type": "progene_text", "text": [ "YidC" ], "offsets": [ [ 157, 161 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6033
split_0_train_6033
[ { "id": "split_0_train_6033_passage", "type": "progene_text", "text": [ "To test whether the two periplasmic regions are translocated independently of each other , the KdpD protein was split between helix 2 and 3 into two approximately equal - sized fragments ." ], "offsets": [ [ 0, 188 ] ] } ]
[ { "id": "split_0_train_9389_entity", "type": "progene_text", "text": [ "KdpD" ], "offsets": [ [ 95, 99 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6034
split_0_train_6034
[ { "id": "split_0_train_6034_passage", "type": "progene_text", "text": [ "Both constructed fragments , which contained KdpD - N ( residues 1 - 448 of KdpD ) and the KdpD - C ( residues 444-894 of KdpD ) , readily inserted into the membrane ." ], "offsets": [ [ 0, 167 ] ] } ]
[ { "id": "split_0_train_9390_entity", "type": "progene_text", "text": [ "KdpD" ], "offsets": [ [ 45, 49 ] ], "normalized": [] }, { "id": "split_0_train_9391_entity", "type": "progene_text", "text": [ "KdpD" ], "offsets": [ [ 91, 95 ] ], "normalized": [] }, { "id": "split_0_train_9392_entity", "type": "progene_text", "text": [ "KdpD" ], "offsets": [ [ 122, 126 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6035
split_0_train_6035
[ { "id": "split_0_train_6035_passage", "type": "progene_text", "text": [ "Similar to the epitope - tagged KdpD protein , only KdpD - C depended on the presence of the Sec translocase and YidC ." ], "offsets": [ [ 0, 119 ] ] } ]
[ { "id": "split_0_train_9393_entity", "type": "progene_text", "text": [ "KdpD" ], "offsets": [ [ 32, 36 ] ], "normalized": [] }, { "id": "split_0_train_9394_entity", "type": "progene_text", "text": [ "KdpD" ], "offsets": [ [ 52, 56 ] ], "normalized": [] }, { "id": "split_0_train_9395_entity", "type": "progene_text", "text": [ "Sec translocase" ], "offsets": [ [ 93, 108 ] ], "normalized": [] }, { "id": "split_0_train_9396_entity", "type": "progene_text", "text": [ "YidC" ], "offsets": [ [ 113, 117 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6036
split_0_train_6036
[ { "id": "split_0_train_6036_passage", "type": "progene_text", "text": [ "This confirms that the four transmembrane helices of KdpD are inserted pairwise , each translocation event involving two transmembrane helices and a periplasmic loop ." ], "offsets": [ [ 0, 167 ] ] } ]
[ { "id": "split_0_train_9397_entity", "type": "progene_text", "text": [ "KdpD" ], "offsets": [ [ 53, 57 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6037
split_0_train_6037
[ { "id": "split_0_train_6037_passage", "type": "progene_text", "text": [ "2-Amino-3-benzoylthiophene allosteric enhancers of A1 adenosine agonist binding : new 3 , 4 - , and 5 - modifications ." ], "offsets": [ [ 0, 119 ] ] } ]
[]
[]
[]
[]
split_0_train_6038
split_0_train_6038
[ { "id": "split_0_train_6038_passage", "type": "progene_text", "text": [ "2-Amino-3-aroylthiophenes are agonist allosteric enhancers ( AE ) at the A(1) adenosine receptor ( A(1) AR ) ." ], "offsets": [ [ 0, 110 ] ] } ]
[ { "id": "split_0_train_9398_entity", "type": "progene_text", "text": [ "A(1) adenosine receptor" ], "offsets": [ [ 73, 96 ] ], "normalized": [] }, { "id": "split_0_train_9399_entity", "type": "progene_text", "text": [ "A(1) AR" ], "offsets": [ [ 99, 106 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6039
split_0_train_6039
[ { "id": "split_0_train_6039_passage", "type": "progene_text", "text": [ "Here we report the syntheses of three kinds of novel 2-aminothiophenes and assays of their AE activity at the human A(1) AR ( hA(1)AR ) , namely , (1) 2-amino-4,5-diphenylthiophene-3-carboxylates , 3a-h , (2) 2-amino-3-benzoyl-4,5-diphenylthiophenes , 7a-p , and ( 3 ) 2-amino-5-bromo-3-benzoyl-4-phenylthiophenes , 10a-h ." ], "offsets": [ [ 0, 323 ] ] } ]
[ { "id": "split_0_train_9400_entity", "type": "progene_text", "text": [ "A(1) AR" ], "offsets": [ [ 116, 123 ] ], "normalized": [] }, { "id": "split_0_train_9401_entity", "type": "progene_text", "text": [ "hA(1)AR" ], "offsets": [ [ 126, 133 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6040
split_0_train_6040
[ { "id": "split_0_train_6040_passage", "type": "progene_text", "text": [ "An in vitro assay employing the A(1) AR agonist [(125)I]ABA and membranes from CHO-K1 cells stably expressing the hA(1) AR measured an index of AE activity , the ability of a candidate AE to stabilize the agonist - A(1)AR - G protein ternary complex , scored as the percentage of ternary complex remaining after 10 min of dissociation initiated by CPX and GTPgammaS ." ], "offsets": [ [ 0, 367 ] ] } ]
[ { "id": "split_0_train_9402_entity", "type": "progene_text", "text": [ "A(1) AR" ], "offsets": [ [ 32, 39 ] ], "normalized": [] }, { "id": "split_0_train_9403_entity", "type": "progene_text", "text": [ "hA(1) AR" ], "offsets": [ [ 114, 122 ] ], "normalized": [] }, { "id": "split_0_train_9404_entity", "type": "progene_text", "text": [ "A(1)AR" ], "offsets": [ [ 215, 221 ] ], "normalized": [] }, { "id": "split_0_train_9405_entity", "type": "progene_text", "text": [ "G protein" ], "offsets": [ [ 224, 233 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6041
split_0_train_6041
[ { "id": "split_0_train_6041_passage", "type": "progene_text", "text": [ "The AE activity score of 2-amino-4,5-dimethyl-3-(3-trifluoromethylbenzoyl ) thiophene ( PD 81 , 723 ) , which was 19 % , served as a standard for comparison ." ], "offsets": [ [ 0, 158 ] ] } ]
[]
[]
[]
[]
split_0_train_6042
split_0_train_6042
[ { "id": "split_0_train_6042_passage", "type": "progene_text", "text": [ "Two 3-carboxythiophene 3-trifluoromethylbenzyl esters , 3d ( 49 % ) and 3f ( 63 % ) , had substantial AE activity ." ], "offsets": [ [ 0, 115 ] ] } ]
[]
[]
[]
[]
split_0_train_6043
split_0_train_6043
[ { "id": "split_0_train_6043_passage", "type": "progene_text", "text": [ "The 3-(1-naphthoyl ) substituent of 7e ( 52 % ) also supported AE activity ." ], "offsets": [ [ 0, 76 ] ] } ]
[]
[]
[]
[]
split_0_train_6044
split_0_train_6044
[ { "id": "split_0_train_6044_passage", "type": "progene_text", "text": [ "Compounds in series 3 tended to be more potent , 10a and 10c having scores of 91 and 80 % , respectively ." ], "offsets": [ [ 0, 106 ] ] } ]
[]
[]
[]
[]
split_0_train_6045
split_0_train_6045
[ { "id": "split_0_train_6045_passage", "type": "progene_text", "text": [ "The activity of 2-amino-5-bromo-3-ethoxycarbonyl-4-(3-nitrophenyl ) thiophene , 10h ( 26 % ) , is an exception to the rule that a 3-ethoxycarbonyl substituent cannot support AE activity ." ], "offsets": [ [ 0, 187 ] ] } ]
[]
[]
[]
[]
split_0_train_6046
split_0_train_6046
[ { "id": "split_0_train_6046_passage", "type": "progene_text", "text": [ "Methylation of histone H3 by Set2 in Saccharomyces cerevisiae is linked to transcriptional elongation by RNA polymerase II ." ], "offsets": [ [ 0, 124 ] ] } ]
[ { "id": "split_0_train_9406_entity", "type": "progene_text", "text": [ "histone H3" ], "offsets": [ [ 15, 25 ] ], "normalized": [] }, { "id": "split_0_train_9407_entity", "type": "progene_text", "text": [ "Set2" ], "offsets": [ [ 29, 33 ] ], "normalized": [] }, { "id": "split_0_train_9408_entity", "type": "progene_text", "text": [ "RNA polymerase II" ], "offsets": [ [ 105, 122 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6047
split_0_train_6047
[ { "id": "split_0_train_6047_passage", "type": "progene_text", "text": [ "Set2 methylates Lys36 of histone H3 ." ], "offsets": [ [ 0, 37 ] ] } ]
[ { "id": "split_0_train_9409_entity", "type": "progene_text", "text": [ "Set2" ], "offsets": [ [ 0, 4 ] ], "normalized": [] }, { "id": "split_0_train_9410_entity", "type": "progene_text", "text": [ "histone H3" ], "offsets": [ [ 25, 35 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6048
split_0_train_6048
[ { "id": "split_0_train_6048_passage", "type": "progene_text", "text": [ "We show here that yeast Set2 copurifies with RNA polymerase II ( RNAPII ) ." ], "offsets": [ [ 0, 75 ] ] } ]
[ { "id": "split_0_train_9411_entity", "type": "progene_text", "text": [ "Set2" ], "offsets": [ [ 24, 28 ] ], "normalized": [] }, { "id": "split_0_train_9412_entity", "type": "progene_text", "text": [ "RNA polymerase II" ], "offsets": [ [ 45, 62 ] ], "normalized": [] }, { "id": "split_0_train_9413_entity", "type": "progene_text", "text": [ "RNAPII" ], "offsets": [ [ 65, 71 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6049
split_0_train_6049
[ { "id": "split_0_train_6049_passage", "type": "progene_text", "text": [ "Chromatin immunoprecipitation analyses demonstrated that Set2 and histone H3 Lys36 methylation are associated with the coding regions of several genes that were tested and correlate with active transcription ." ], "offsets": [ [ 0, 209 ] ] } ]
[ { "id": "split_0_train_9414_entity", "type": "progene_text", "text": [ "Set2" ], "offsets": [ [ 57, 61 ] ], "normalized": [] }, { "id": "split_0_train_9415_entity", "type": "progene_text", "text": [ "histone H3" ], "offsets": [ [ 66, 76 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6050
split_0_train_6050
[ { "id": "split_0_train_6050_passage", "type": "progene_text", "text": [ "Both depend , as well , on the Paf1 elongation factor complex ." ], "offsets": [ [ 0, 63 ] ] } ]
[ { "id": "split_0_train_9416_entity", "type": "progene_text", "text": [ "Paf1 elongation factor complex" ], "offsets": [ [ 31, 61 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6051
split_0_train_6051
[ { "id": "split_0_train_6051_passage", "type": "progene_text", "text": [ "The C terminus of Set2 , which contains a WW domain , is also required for effective Lys36 methylation ." ], "offsets": [ [ 0, 104 ] ] } ]
[ { "id": "split_0_train_9417_entity", "type": "progene_text", "text": [ "Set2" ], "offsets": [ [ 18, 22 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6052
split_0_train_6052
[ { "id": "split_0_train_6052_passage", "type": "progene_text", "text": [ "Deletion of CTK1 , encoding an RNAPII CTD kinase , prevents Lys36 methylation and Set2 recruitment , suggesting that methylation may be triggered by contact of the WW domain or C terminus of Set2 with Ser2 - phosphorylated CTD ." ], "offsets": [ [ 0, 228 ] ] } ]
[ { "id": "split_0_train_9418_entity", "type": "progene_text", "text": [ "CTK1" ], "offsets": [ [ 12, 16 ] ], "normalized": [] }, { "id": "split_0_train_9419_entity", "type": "progene_text", "text": [ "RNAPII" ], "offsets": [ [ 31, 37 ] ], "normalized": [] }, { "id": "split_0_train_9420_entity", "type": "progene_text", "text": [ "CTD kinase" ], "offsets": [ [ 38, 48 ] ], "normalized": [] }, { "id": "split_0_train_9421_entity", "type": "progene_text", "text": [ "Set2" ], "offsets": [ [ 82, 86 ] ], "normalized": [] }, { "id": "split_0_train_9422_entity", "type": "progene_text", "text": [ "Set2" ], "offsets": [ [ 191, 195 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6053
split_0_train_6053
[ { "id": "split_0_train_6053_passage", "type": "progene_text", "text": [ "A set2 deletion results in slight sensitivity to 6-azauracil and much less beta-galactosidase produced by a reporter plasmid , resulting from a defect in transcription ." ], "offsets": [ [ 0, 169 ] ] } ]
[ { "id": "split_0_train_9423_entity", "type": "progene_text", "text": [ "set2" ], "offsets": [ [ 2, 6 ] ], "normalized": [] }, { "id": "split_0_train_9424_entity", "type": "progene_text", "text": [ "beta-galactosidase" ], "offsets": [ [ 75, 93 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6054
split_0_train_6054
[ { "id": "split_0_train_6054_passage", "type": "progene_text", "text": [ "In synthetic genetic array ( SGA ) analysis , synthetic growth defects were obtained when a set2 deletion was combined with deletions of all five components of the Paf1 complex , the chromodomain elongation factor Chd1 , the putative elongation factor Soh1 , the Bre1 or Lge1 components of the histone H2B ubiquitination complex , or the histone H2A variant Htz1 ." ], "offsets": [ [ 0, 364 ] ] } ]
[ { "id": "split_0_train_9425_entity", "type": "progene_text", "text": [ "set2" ], "offsets": [ [ 92, 96 ] ], "normalized": [] }, { "id": "split_0_train_9426_entity", "type": "progene_text", "text": [ "Paf1 complex" ], "offsets": [ [ 164, 176 ] ], "normalized": [] }, { "id": "split_0_train_9427_entity", "type": "progene_text", "text": [ "elongation factor" ], "offsets": [ [ 196, 213 ] ], "normalized": [] }, { "id": "split_0_train_9428_entity", "type": "progene_text", "text": [ "Chd1" ], "offsets": [ [ 214, 218 ] ], "normalized": [] }, { "id": "split_0_train_9429_entity", "type": "progene_text", "text": [ "elongation factor" ], "offsets": [ [ 234, 251 ] ], "normalized": [] }, { "id": "split_0_train_9430_entity", "type": "progene_text", "text": [ "Soh1" ], "offsets": [ [ 252, 256 ] ], "normalized": [] }, { "id": "split_0_train_9431_entity", "type": "progene_text", "text": [ "Bre1" ], "offsets": [ [ 263, 267 ] ], "normalized": [] }, { "id": "split_0_train_9432_entity", "type": "progene_text", "text": [ "Lge1" ], "offsets": [ [ 271, 275 ] ], "normalized": [] }, { "id": "split_0_train_9433_entity", "type": "progene_text", "text": [ "histone H2B" ], "offsets": [ [ 294, 305 ] ], "normalized": [] }, { "id": "split_0_train_9434_entity", "type": "progene_text", "text": [ "histone H2A" ], "offsets": [ [ 338, 349 ] ], "normalized": [] }, { "id": "split_0_train_9435_entity", "type": "progene_text", "text": [ "Htz1" ], "offsets": [ [ 358, 362 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6055
split_0_train_6055
[ { "id": "split_0_train_6055_passage", "type": "progene_text", "text": [ "SET2 also interacts genetically with components of the Set1 and Set3 complexes , suggesting that Set1 , Set2 , and Set3 similarly affect transcription by RNAPII ." ], "offsets": [ [ 0, 162 ] ] } ]
[ { "id": "split_0_train_9436_entity", "type": "progene_text", "text": [ "SET2" ], "offsets": [ [ 0, 4 ] ], "normalized": [] }, { "id": "split_0_train_9437_entity", "type": "progene_text", "text": [ "Set1" ], "offsets": [ [ 55, 59 ] ], "normalized": [] }, { "id": "split_0_train_9438_entity", "type": "progene_text", "text": [ "Set3" ], "offsets": [ [ 64, 68 ] ], "normalized": [] }, { "id": "split_0_train_9439_entity", "type": "progene_text", "text": [ "Set1" ], "offsets": [ [ 97, 101 ] ], "normalized": [] }, { "id": "split_0_train_9440_entity", "type": "progene_text", "text": [ "Set2" ], "offsets": [ [ 104, 108 ] ], "normalized": [] }, { "id": "split_0_train_9441_entity", "type": "progene_text", "text": [ "Set3" ], "offsets": [ [ 115, 119 ] ], "normalized": [] }, { "id": "split_0_train_9442_entity", "type": "progene_text", "text": [ "RNAPII" ], "offsets": [ [ 154, 160 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6056
split_0_train_6056
[ { "id": "split_0_train_6056_passage", "type": "progene_text", "text": [ "Intramembrane proteolysis by presenilin and presenilin - like proteases ." ], "offsets": [ [ 0, 73 ] ] } ]
[ { "id": "split_0_train_9443_entity", "type": "progene_text", "text": [ "presenilin" ], "offsets": [ [ 29, 39 ] ], "normalized": [] }, { "id": "split_0_train_9444_entity", "type": "progene_text", "text": [ "presenilin" ], "offsets": [ [ 44, 54 ] ], "normalized": [] }, { "id": "split_0_train_9445_entity", "type": "progene_text", "text": [ "proteases" ], "offsets": [ [ 62, 71 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6057
split_0_train_6057
[ { "id": "split_0_train_6057_passage", "type": "progene_text", "text": [ "Regulated intramembrane proteolysis is a novel mechanism involving proteases that hydrolyze their substrates in a hydrophobic environment ." ], "offsets": [ [ 0, 139 ] ] } ]
[ { "id": "split_0_train_9446_entity", "type": "progene_text", "text": [ "proteases" ], "offsets": [ [ 67, 76 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6058
split_0_train_6058
[ { "id": "split_0_train_6058_passage", "type": "progene_text", "text": [ "Presenilin ( PS ) 1 and PS 2 are required for intramembrane cleavage of an increasing number of type I membrane proteins , including the amyloid precursor protein of Alzheimer ' s disease and the Notch receptor , which signals during differentiation and development ." ], "offsets": [ [ 0, 267 ] ] } ]
[ { "id": "split_0_train_9447_entity", "type": "progene_text", "text": [ "Presenilin ( PS ) 1" ], "offsets": [ [ 0, 19 ] ], "normalized": [] }, { "id": "split_0_train_9448_entity", "type": "progene_text", "text": [ "PS 2" ], "offsets": [ [ 24, 28 ] ], "normalized": [] }, { "id": "split_0_train_9449_entity", "type": "progene_text", "text": [ "amyloid precursor protein" ], "offsets": [ [ 137, 162 ] ], "normalized": [] }, { "id": "split_0_train_9450_entity", "type": "progene_text", "text": [ "Notch" ], "offsets": [ [ 196, 201 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6059
split_0_train_6059
[ { "id": "split_0_train_6059_passage", "type": "progene_text", "text": [ "Mutagenesis , affinity labeling , biochemical isolation , and reconstitution in cells reveal that PS , in complex with co - factors nicastrin , APH - 1 and PEN - 2 , apparently contains the active site of gamma - secretase , a novel membrane aspartyl protease ." ], "offsets": [ [ 0, 261 ] ] } ]
[ { "id": "split_0_train_9451_entity", "type": "progene_text", "text": [ "PS" ], "offsets": [ [ 98, 100 ] ], "normalized": [] }, { "id": "split_0_train_9452_entity", "type": "progene_text", "text": [ "nicastrin" ], "offsets": [ [ 132, 141 ] ], "normalized": [] }, { "id": "split_0_train_9453_entity", "type": "progene_text", "text": [ "APH - 1" ], "offsets": [ [ 144, 151 ] ], "normalized": [] }, { "id": "split_0_train_9454_entity", "type": "progene_text", "text": [ "PEN - 2" ], "offsets": [ [ 156, 163 ] ], "normalized": [] }, { "id": "split_0_train_9455_entity", "type": "progene_text", "text": [ "gamma - secretase" ], "offsets": [ [ 205, 222 ] ], "normalized": [] }, { "id": "split_0_train_9456_entity", "type": "progene_text", "text": [ "aspartyl protease" ], "offsets": [ [ 242, 259 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6060
split_0_train_6060
[ { "id": "split_0_train_6060_passage", "type": "progene_text", "text": [ "In addition , other related aspartyl proteases have been identified ." ], "offsets": [ [ 0, 69 ] ] } ]
[ { "id": "split_0_train_9457_entity", "type": "progene_text", "text": [ "aspartyl proteases" ], "offsets": [ [ 28, 46 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6061
split_0_train_6061
[ { "id": "split_0_train_6061_passage", "type": "progene_text", "text": [ "These include members of the type-4 prepilin peptidase family in bacteria , which are known proteases and carry a GD motif conserved in PS ." ], "offsets": [ [ 0, 140 ] ] } ]
[ { "id": "split_0_train_9458_entity", "type": "progene_text", "text": [ "type-4 prepilin peptidase family" ], "offsets": [ [ 29, 61 ] ], "normalized": [] }, { "id": "split_0_train_9459_entity", "type": "progene_text", "text": [ "proteases" ], "offsets": [ [ 92, 101 ] ], "normalized": [] }, { "id": "split_0_train_9460_entity", "type": "progene_text", "text": [ "PS" ], "offsets": [ [ 136, 138 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6062
split_0_train_6062
[ { "id": "split_0_train_6062_passage", "type": "progene_text", "text": [ "A group of multi - pass membrane proteins found in eukaryotes also contain YD and LGXGD motifs in two transmembrane domains that are conserved in PS and postulated to constitute an aspartyl protease active site ." ], "offsets": [ [ 0, 212 ] ] } ]
[ { "id": "split_0_train_9461_entity", "type": "progene_text", "text": [ "PS" ], "offsets": [ [ 146, 148 ] ], "normalized": [] }, { "id": "split_0_train_9462_entity", "type": "progene_text", "text": [ "aspartyl protease" ], "offsets": [ [ 181, 198 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6063
split_0_train_6063
[ { "id": "split_0_train_6063_passage", "type": "progene_text", "text": [ "Among these is signal peptide peptidase ( SPP ) , which cleaves remnant signal peptides derived from signal - peptidase - mediated ectodomain shedding ." ], "offsets": [ [ 0, 152 ] ] } ]
[ { "id": "split_0_train_9463_entity", "type": "progene_text", "text": [ "signal peptide peptidase" ], "offsets": [ [ 15, 39 ] ], "normalized": [] }, { "id": "split_0_train_9464_entity", "type": "progene_text", "text": [ "SPP" ], "offsets": [ [ 42, 45 ] ], "normalized": [] }, { "id": "split_0_train_9465_entity", "type": "progene_text", "text": [ "signal - peptidase" ], "offsets": [ [ 101, 119 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6064
split_0_train_6064
[ { "id": "split_0_train_6064_passage", "type": "progene_text", "text": [ "SPP cuts type II membrane proteins , illustrating that PS - like proteases play a key role in intramembrane proteolysis of single - pass membrane proteins oriented in either direction ." ], "offsets": [ [ 0, 185 ] ] } ]
[ { "id": "split_0_train_9466_entity", "type": "progene_text", "text": [ "SPP" ], "offsets": [ [ 0, 3 ] ], "normalized": [] }, { "id": "split_0_train_9467_entity", "type": "progene_text", "text": [ "PS" ], "offsets": [ [ 55, 57 ] ], "normalized": [] }, { "id": "split_0_train_9468_entity", "type": "progene_text", "text": [ "proteases" ], "offsets": [ [ 65, 74 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6065
split_0_train_6065
[ { "id": "split_0_train_6065_passage", "type": "progene_text", "text": [ "Structural and biochemical dissection of photorespiration in hybrids differing in genome constitution between Diplotaxis tenuifolia ( C3-C4 ) and radish ( C3 ) ." ], "offsets": [ [ 0, 161 ] ] } ]
[]
[]
[]
[]
split_0_train_6066
split_0_train_6066
[ { "id": "split_0_train_6066_passage", "type": "progene_text", "text": [ "We compared the structural , biochemical , and physiological characteristics involved in photorespiration of intergeneric hybrids differing in genome constitution ( DtDtR , DtDtRR , and DtRR ) between the C(3)-C(4) intermediate species Diplotaxis tenuifolia ( DtDt ) and the C(3) species radish ( Raphanus sativus ; RR ) ." ], "offsets": [ [ 0, 322 ] ] } ]
[]
[]
[]
[]
split_0_train_6067
split_0_train_6067
[ { "id": "split_0_train_6067_passage", "type": "progene_text", "text": [ "The bundle sheath ( BS ) cells in D. tenuifolia included many centripetally located chloroplasts and mitochondria , but those of radish had only a few chloroplasts and mitochondria ." ], "offsets": [ [ 0, 182 ] ] } ]
[]
[]
[]
[]
split_0_train_6068
split_0_train_6068
[ { "id": "split_0_train_6068_passage", "type": "progene_text", "text": [ "In the hybrids , the numbers of chloroplasts and mitochondria , the ratio of centripetally located organelles to total organelles , and the mitochondrial size in the BS cells increased with an increase in the constitution ratio of the Dt : R genome ." ], "offsets": [ [ 0, 250 ] ] } ]
[]
[]
[]
[]
split_0_train_6069
split_0_train_6069
[ { "id": "split_0_train_6069_passage", "type": "progene_text", "text": [ "The P-protein of glycine decarboxylase ( GDC ) was confined to the BS mitochondria in D. tenuifolia , whereas in radish , it accumulated more densely in the mesophyll than in the BS mitochondria ." ], "offsets": [ [ 0, 196 ] ] } ]
[ { "id": "split_0_train_9469_entity", "type": "progene_text", "text": [ "P-protein of glycine decarboxylase" ], "offsets": [ [ 4, 38 ] ], "normalized": [] }, { "id": "split_0_train_9470_entity", "type": "progene_text", "text": [ "GDC" ], "offsets": [ [ 41, 44 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6070
split_0_train_6070
[ { "id": "split_0_train_6070_passage", "type": "progene_text", "text": [ "In the hybrids , more intense accumulation of GDC in the BS relative to the mesophyll mitochondria occurred with an increase in the Dt : R ratio ." ], "offsets": [ [ 0, 146 ] ] } ]
[ { "id": "split_0_train_9471_entity", "type": "progene_text", "text": [ "GDC" ], "offsets": [ [ 46, 49 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6071
split_0_train_6071
[ { "id": "split_0_train_6071_passage", "type": "progene_text", "text": [ "These structural and biochemical features in the hybrids were reflected in the gas exchange characteristics of leaves , such as the CO ( 2 ) compensation point ." ], "offsets": [ [ 0, 161 ] ] } ]
[]
[]
[]
[]
split_0_train_6072
split_0_train_6072
[ { "id": "split_0_train_6072_passage", "type": "progene_text", "text": [ "Our data indicate that the leaf structure , the intercellular pattern of GDC expression , and the gas exchange characteristics of C ( 3 ) - C ( 4 ) intermediate photosynthesis are inherited in the hybrids depending on the constitution ratio of the parent genomes ." ], "offsets": [ [ 0, 264 ] ] } ]
[ { "id": "split_0_train_9472_entity", "type": "progene_text", "text": [ "GDC" ], "offsets": [ [ 73, 76 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6073
split_0_train_6073
[ { "id": "split_0_train_6073_passage", "type": "progene_text", "text": [ "Our findings also demonstrate that the apparent reduced photorespiration in C(3)-C(4) intermediate plants is mainly due to the structural differentiation of mitochondria and chloroplasts in the BS cells combined with the BS - dominant expression of GDC ." ], "offsets": [ [ 0, 254 ] ] } ]
[ { "id": "split_0_train_9473_entity", "type": "progene_text", "text": [ "GDC" ], "offsets": [ [ 249, 252 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6074
split_0_train_6074
[ { "id": "split_0_train_6074_passage", "type": "progene_text", "text": [ "Apolipoprotein D levels are elevated in prefrontal cortex of subjects with Alzheimer 's disease : no relation to apolipoprotein E expression or genotype ." ], "offsets": [ [ 0, 154 ] ] } ]
[ { "id": "split_0_train_9474_entity", "type": "progene_text", "text": [ "Apolipoprotein D" ], "offsets": [ [ 0, 16 ] ], "normalized": [] }, { "id": "split_0_train_9475_entity", "type": "progene_text", "text": [ "apolipoprotein E" ], "offsets": [ [ 113, 129 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6075
split_0_train_6075
[ { "id": "split_0_train_6075_passage", "type": "progene_text", "text": [ "BACKGROUND :" ], "offsets": [ [ 0, 12 ] ] } ]
[]
[]
[]
[]
split_0_train_6076
split_0_train_6076
[ { "id": "split_0_train_6076_passage", "type": "progene_text", "text": [ "Apolipoprotein E ( apoE ) has been implicated in the pathology of AD ever since inheritance of the epsilon4 allele was shown to be an important risk factor for the development of AD ." ], "offsets": [ [ 0, 183 ] ] } ]
[ { "id": "split_0_train_9476_entity", "type": "progene_text", "text": [ "Apolipoprotein E" ], "offsets": [ [ 0, 16 ] ], "normalized": [] }, { "id": "split_0_train_9477_entity", "type": "progene_text", "text": [ "apoE" ], "offsets": [ [ 19, 23 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6077
split_0_train_6077
[ { "id": "split_0_train_6077_passage", "type": "progene_text", "text": [ "Apolipoprotein D ( apoD ) is elevated in association with several central nervous system disorders , including Alzheimer 's disease ( AD ) , and has been proposed to be an especially robust marker for brain regions specifically affected by particular neuropathologies ." ], "offsets": [ [ 0, 269 ] ] } ]
[ { "id": "split_0_train_9478_entity", "type": "progene_text", "text": [ "Apolipoprotein D" ], "offsets": [ [ 0, 16 ] ], "normalized": [] }, { "id": "split_0_train_9479_entity", "type": "progene_text", "text": [ "apoD" ], "offsets": [ [ 19, 23 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6078
split_0_train_6078
[ { "id": "split_0_train_6078_passage", "type": "progene_text", "text": [ "Progressive cognitive decline is the core clinical feature of AD and is associated with disturbances in the prefrontal cortex ." ], "offsets": [ [ 0, 127 ] ] } ]
[]
[]
[]
[]
split_0_train_6079
split_0_train_6079
[ { "id": "split_0_train_6079_passage", "type": "progene_text", "text": [ "METHODS :" ], "offsets": [ [ 0, 9 ] ] } ]
[]
[]
[]
[]
split_0_train_6080
split_0_train_6080
[ { "id": "split_0_train_6080_passage", "type": "progene_text", "text": [ "We measured apoD levels in prefrontal cortex samples obtained postmortem from 20 autopsy - confirmed AD subjects and 40 control subjects ." ], "offsets": [ [ 0, 138 ] ] } ]
[ { "id": "split_0_train_9480_entity", "type": "progene_text", "text": [ "apoD" ], "offsets": [ [ 12, 16 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6081
split_0_train_6081
[ { "id": "split_0_train_6081_passage", "type": "progene_text", "text": [ "RESULTS :" ], "offsets": [ [ 0, 9 ] ] } ]
[]
[]
[]
[]
split_0_train_6082
split_0_train_6082
[ { "id": "split_0_train_6082_passage", "type": "progene_text", "text": [ "Enzyme - linked immunosorbent assay analysis revealed a significant increase in apoD expression in AD subjects compared with control subjects ( .218 +/- .029 microg / mg protein vs.117 +/- .011 microg / mg protein ; p = 0003 ) ." ], "offsets": [ [ 0, 228 ] ] } ]
[ { "id": "split_0_train_9481_entity", "type": "progene_text", "text": [ "apoD" ], "offsets": [ [ 80, 84 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6083
split_0_train_6083
[ { "id": "split_0_train_6083_passage", "type": "progene_text", "text": [ "There was no significant difference in apoD expression between early - onset and late - onset Alzheimer 's subjects ." ], "offsets": [ [ 0, 117 ] ] } ]
[ { "id": "split_0_train_9482_entity", "type": "progene_text", "text": [ "apoD" ], "offsets": [ [ 39, 43 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6084
split_0_train_6084
[ { "id": "split_0_train_6084_passage", "type": "progene_text", "text": [ "Apolipoprotein D expression levels were not correlated with apoE levels , nor were they correlated with inheritance of the APOE epsilon4 allele ." ], "offsets": [ [ 0, 145 ] ] } ]
[ { "id": "split_0_train_9483_entity", "type": "progene_text", "text": [ "Apolipoprotein D" ], "offsets": [ [ 0, 16 ] ], "normalized": [] }, { "id": "split_0_train_9484_entity", "type": "progene_text", "text": [ "apoE" ], "offsets": [ [ 60, 64 ] ], "normalized": [] }, { "id": "split_0_train_9485_entity", "type": "progene_text", "text": [ "APOE" ], "offsets": [ [ 123, 127 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6085
split_0_train_6085
[ { "id": "split_0_train_6085_passage", "type": "progene_text", "text": [ "CONCLUSIONS :" ], "offsets": [ [ 0, 13 ] ] } ]
[]
[]
[]
[]
split_0_train_6086
split_0_train_6086
[ { "id": "split_0_train_6086_passage", "type": "progene_text", "text": [ "These findings suggest that apoD may be related to the cognitive decline observed in AD patients and that apoD and apoE likely play different roles in the pathogenesis of AD ." ], "offsets": [ [ 0, 175 ] ] } ]
[ { "id": "split_0_train_9486_entity", "type": "progene_text", "text": [ "apoD" ], "offsets": [ [ 28, 32 ] ], "normalized": [] }, { "id": "split_0_train_9487_entity", "type": "progene_text", "text": [ "apoD" ], "offsets": [ [ 106, 110 ] ], "normalized": [] }, { "id": "split_0_train_9488_entity", "type": "progene_text", "text": [ "apoE" ], "offsets": [ [ 115, 119 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6087
split_0_train_6087
[ { "id": "split_0_train_6087_passage", "type": "progene_text", "text": [ "New members of the Escherichia coli sigmaE regulon identified by a two - plasmid system ." ], "offsets": [ [ 0, 89 ] ] } ]
[ { "id": "split_0_train_9489_entity", "type": "progene_text", "text": [ "sigmaE" ], "offsets": [ [ 36, 42 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6088
split_0_train_6088
[ { "id": "split_0_train_6088_passage", "type": "progene_text", "text": [ "A previously established method , based on a two - plasmid system , was used to identify promoters recognized by RNA polymerase containing the extracytoplasmic stress response sigma factor sigmaE in Escherichia coli ." ], "offsets": [ [ 0, 217 ] ] } ]
[ { "id": "split_0_train_9490_entity", "type": "progene_text", "text": [ "RNA polymerase" ], "offsets": [ [ 113, 127 ] ], "normalized": [] }, { "id": "split_0_train_9491_entity", "type": "progene_text", "text": [ "sigma factor" ], "offsets": [ [ 176, 188 ] ], "normalized": [] }, { "id": "split_0_train_9492_entity", "type": "progene_text", "text": [ "sigmaE" ], "offsets": [ [ 189, 195 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6089
split_0_train_6089
[ { "id": "split_0_train_6089_passage", "type": "progene_text", "text": [ "In addition to previously identified rpoE - dependent promoters , 11 new promoters potentially directing the expression of 15 genes were identified that were active only after over - expression of rpoE ." ], "offsets": [ [ 0, 203 ] ] } ]
[ { "id": "split_0_train_9493_entity", "type": "progene_text", "text": [ "rpoE" ], "offsets": [ [ 37, 41 ] ], "normalized": [] }, { "id": "split_0_train_9494_entity", "type": "progene_text", "text": [ "rpoE" ], "offsets": [ [ 197, 201 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6090
split_0_train_6090
[ { "id": "split_0_train_6090_passage", "type": "progene_text", "text": [ "The promoters were confirmed and transcriptional start points of the promoters were determined by primer extension analysis and S1 - nuclease mapping ." ], "offsets": [ [ 0, 151 ] ] } ]
[ { "id": "split_0_train_9495_entity", "type": "progene_text", "text": [ "S1 - nuclease" ], "offsets": [ [ 128, 141 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6091
split_0_train_6091
[ { "id": "split_0_train_6091_passage", "type": "progene_text", "text": [ "All the promoters contained sequences similar to the consensus sequence of rpoE - dependent promoters ." ], "offsets": [ [ 0, 103 ] ] } ]
[ { "id": "split_0_train_9496_entity", "type": "progene_text", "text": [ "rpoE" ], "offsets": [ [ 75, 79 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6092
split_0_train_6092
[ { "id": "split_0_train_6092_passage", "type": "progene_text", "text": [ "The new rpoE - dependent promoters governed expression of genes encoding proteins involved in primary metabolism ( fusA , tufA , recR ) , phospholipid and lipopolysaccharide biosynthesis ( psd , lpxP ) , signal transduction ( sixA ) , proposed inner or outer membrane proteins ( bacA , sbmA , smpA , yeaY ) , and proteins with unknown function ( ybaB , yaiW , yiiS , yiiT , yfeY ) ." ], "offsets": [ [ 0, 382 ] ] } ]
[ { "id": "split_0_train_9497_entity", "type": "progene_text", "text": [ "rpoE" ], "offsets": [ [ 8, 12 ] ], "normalized": [] }, { "id": "split_0_train_9498_entity", "type": "progene_text", "text": [ "fusA" ], "offsets": [ [ 115, 119 ] ], "normalized": [] }, { "id": "split_0_train_9499_entity", "type": "progene_text", "text": [ "tufA" ], "offsets": [ [ 122, 126 ] ], "normalized": [] }, { "id": "split_0_train_9500_entity", "type": "progene_text", "text": [ "recR" ], "offsets": [ [ 129, 133 ] ], "normalized": [] }, { "id": "split_0_train_9501_entity", "type": "progene_text", "text": [ "psd" ], "offsets": [ [ 189, 192 ] ], "normalized": [] }, { "id": "split_0_train_9502_entity", "type": "progene_text", "text": [ "lpxP" ], "offsets": [ [ 195, 199 ] ], "normalized": [] }, { "id": "split_0_train_9503_entity", "type": "progene_text", "text": [ "sixA" ], "offsets": [ [ 226, 230 ] ], "normalized": [] }, { "id": "split_0_train_9504_entity", "type": "progene_text", "text": [ "bacA" ], "offsets": [ [ 279, 283 ] ], "normalized": [] }, { "id": "split_0_train_9505_entity", "type": "progene_text", "text": [ "sbmA" ], "offsets": [ [ 286, 290 ] ], "normalized": [] }, { "id": "split_0_train_9506_entity", "type": "progene_text", "text": [ "smpA" ], "offsets": [ [ 293, 297 ] ], "normalized": [] }, { "id": "split_0_train_9507_entity", "type": "progene_text", "text": [ "yeaY" ], "offsets": [ [ 300, 304 ] ], "normalized": [] }, { "id": "split_0_train_9508_entity", "type": "progene_text", "text": [ "ybaB" ], "offsets": [ [ 346, 350 ] ], "normalized": [] }, { "id": "split_0_train_9509_entity", "type": "progene_text", "text": [ "yaiW" ], "offsets": [ [ 353, 357 ] ], "normalized": [] }, { "id": "split_0_train_9510_entity", "type": "progene_text", "text": [ "yiiS" ], "offsets": [ [ 360, 364 ] ], "normalized": [] }, { "id": "split_0_train_9511_entity", "type": "progene_text", "text": [ "yiiT" ], "offsets": [ [ 367, 371 ] ], "normalized": [] }, { "id": "split_0_train_9512_entity", "type": "progene_text", "text": [ "yfeY" ], "offsets": [ [ 374, 378 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6093
split_0_train_6093
[ { "id": "split_0_train_6093_passage", "type": "progene_text", "text": [ "A synthetic peptide from transforming growth factor beta type III receptor inhibits liver fibrogenesis in rats with carbon tetrachloride liver injury ." ], "offsets": [ [ 0, 151 ] ] } ]
[ { "id": "split_0_train_9513_entity", "type": "progene_text", "text": [ "transforming growth factor beta type III receptor" ], "offsets": [ [ 25, 74 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6094
split_0_train_6094
[ { "id": "split_0_train_6094_passage", "type": "progene_text", "text": [ "Transforming growth factor beta1 ( TGF-beta1 ) is a pleiotropic cytokine , which displays potent profibrogenic effects and is highly expressed in fibrotic livers ." ], "offsets": [ [ 0, 163 ] ] } ]
[ { "id": "split_0_train_9514_entity", "type": "progene_text", "text": [ "Transforming growth factor beta1" ], "offsets": [ [ 0, 32 ] ], "normalized": [] }, { "id": "split_0_train_9515_entity", "type": "progene_text", "text": [ "TGF-beta1" ], "offsets": [ [ 35, 44 ] ], "normalized": [] }, { "id": "split_0_train_9516_entity", "type": "progene_text", "text": [ "cytokine" ], "offsets": [ [ 64, 72 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6095
split_0_train_6095
[ { "id": "split_0_train_6095_passage", "type": "progene_text", "text": [ "For this reason , development of TGF-B1 inhibitors might be of great importance to control liver fibrogenesis as well as other undesired side effects due to this cytokine ." ], "offsets": [ [ 0, 172 ] ] } ]
[ { "id": "split_0_train_9517_entity", "type": "progene_text", "text": [ "TGF-B1" ], "offsets": [ [ 33, 39 ] ], "normalized": [] }, { "id": "split_0_train_9518_entity", "type": "progene_text", "text": [ "cytokine" ], "offsets": [ [ 162, 170 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6096
split_0_train_6096
[ { "id": "split_0_train_6096_passage", "type": "progene_text", "text": [ "Potential peptide inhibitors of TGF-beta1 ( derived from TGF-beta1 and from its type III receptor ) were tested in vitro and in vivo using different assays ." ], "offsets": [ [ 0, 157 ] ] } ]
[ { "id": "split_0_train_9519_entity", "type": "progene_text", "text": [ "TGF-beta1" ], "offsets": [ [ 32, 41 ] ], "normalized": [] }, { "id": "split_0_train_9520_entity", "type": "progene_text", "text": [ "TGF-beta1" ], "offsets": [ [ 57, 66 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6097
split_0_train_6097
[ { "id": "split_0_train_6097_passage", "type": "progene_text", "text": [ "Peptides P11 and P12 , derived from TGF-beta1 , and P54 and P144 , derived from its type III receptor , prevented TGF-beta1 - dependent inhibition of MV1Lu proliferation in vitro and markedly reduced binding of TGF-beta1 to its receptors ." ], "offsets": [ [ 0, 239 ] ] } ]
[ { "id": "split_0_train_9521_entity", "type": "progene_text", "text": [ "TGF-beta1" ], "offsets": [ [ 36, 45 ] ], "normalized": [] }, { "id": "split_0_train_9522_entity", "type": "progene_text", "text": [ "TGF-beta1" ], "offsets": [ [ 114, 123 ] ], "normalized": [] }, { "id": "split_0_train_9523_entity", "type": "progene_text", "text": [ "TGF-beta1" ], "offsets": [ [ 211, 220 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6098
split_0_train_6098
[ { "id": "split_0_train_6098_passage", "type": "progene_text", "text": [ "P144 blocked TGF-beta1 - dependent stimulation of a reporter gene under the control of human alpha2(I) collagen promoter ." ], "offsets": [ [ 0, 122 ] ] } ]
[ { "id": "split_0_train_9524_entity", "type": "progene_text", "text": [ "TGF-beta1" ], "offsets": [ [ 13, 22 ] ], "normalized": [] }, { "id": "split_0_train_9525_entity", "type": "progene_text", "text": [ "alpha2(I) collagen" ], "offsets": [ [ 93, 111 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_6099
split_0_train_6099
[ { "id": "split_0_train_6099_passage", "type": "progene_text", "text": [ "Intraperitoneal administration of P144 also showed potent antifibrogenic activity in vivo in the liver of rats receiving CCl4 ." ], "offsets": [ [ 0, 127 ] ] } ]
[]
[]
[]
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