id
stringlengths
15
19
document_id
stringlengths
15
19
passages
list
entities
list
events
list
coreferences
list
relations
list
split_0_train_28000
split_0_train_28000
[ { "id": "split_0_train_28000_passage", "type": "progene_text", "text": [ "However , the previously characterized mutation cdc4 - 1 and a new allele , cdc4 - 12 , do not alleviate the defect of cdc20 - 1 cells ." ], "offsets": [ [ 0, 136 ] ] } ]
[ { "id": "split_0_train_45333_entity", "type": "progene_text", "text": [ "cdc4" ], "offsets": [ [ 48, 52 ] ], "normalized": [] }, { "id": "split_0_train_45334_entity", "type": "progene_text", "text": [ "cdc4" ], "offsets": [ [ 76, 80 ] ], "normalized": [] }, { "id": "split_0_train_45335_entity", "type": "progene_text", "text": [ "cdc20" ], "offsets": [ [ 119, 124 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28001
split_0_train_28001
[ { "id": "split_0_train_28001_passage", "type": "progene_text", "text": [ "This genetic interaction suggests an additional role for Cdc4 in G(2) / M ." ], "offsets": [ [ 0, 75 ] ] } ]
[ { "id": "split_0_train_45336_entity", "type": "progene_text", "text": [ "Cdc4" ], "offsets": [ [ 57, 61 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28002
split_0_train_28002
[ { "id": "split_0_train_28002_passage", "type": "progene_text", "text": [ "Reexamination of the cdc4 - 1 mutant revealed that , in addition to being defective in the onset of S phase , it is also defective in G(2) / M transition when released from hydroxyurea - induced S-phase arrest ." ], "offsets": [ [ 0, 211 ] ] } ]
[ { "id": "split_0_train_45337_entity", "type": "progene_text", "text": [ "cdc4" ], "offsets": [ [ 21, 25 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28003
split_0_train_28003
[ { "id": "split_0_train_28003_passage", "type": "progene_text", "text": [ "A second function for CDC4 in late S or G(2) phase was further confirmed by the observation that cells lacking the CDC4 gene are arrested both at G(1) / S and at G(2)/M ." ], "offsets": [ [ 0, 170 ] ] } ]
[ { "id": "split_0_train_45338_entity", "type": "progene_text", "text": [ "CDC4" ], "offsets": [ [ 22, 26 ] ], "normalized": [] }, { "id": "split_0_train_45339_entity", "type": "progene_text", "text": [ "CDC4" ], "offsets": [ [ 115, 119 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28004
split_0_train_28004
[ { "id": "split_0_train_28004_passage", "type": "progene_text", "text": [ "We subsequently isolated additional temperature - sensitive mutations in the CDC4 gene ( such as cdc4 - 12 ) that render the mutant defective in both G(1) / S and G(2) / M transitions at the restrictive temperature ." ], "offsets": [ [ 0, 216 ] ] } ]
[ { "id": "split_0_train_45340_entity", "type": "progene_text", "text": [ "CDC4" ], "offsets": [ [ 77, 81 ] ], "normalized": [] }, { "id": "split_0_train_45341_entity", "type": "progene_text", "text": [ "cdc4" ], "offsets": [ [ 97, 101 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28005
split_0_train_28005
[ { "id": "split_0_train_28005_passage", "type": "progene_text", "text": [ "While the G(1) / S block in both cdc4 - 12 and cdc4Delta mutants is abolished by the deletion of the SIC1 gene ( causing the mutants to be arrested predominantly in G(2) / M ) , the preanaphase arrest in the cdc4 - 12 mutant is relieved by the deletion of PDS1 ." ], "offsets": [ [ 0, 262 ] ] } ]
[ { "id": "split_0_train_45342_entity", "type": "progene_text", "text": [ "cdc4" ], "offsets": [ [ 33, 37 ] ], "normalized": [] }, { "id": "split_0_train_45343_entity", "type": "progene_text", "text": [ "cdc4Delta" ], "offsets": [ [ 47, 56 ] ], "normalized": [] }, { "id": "split_0_train_45344_entity", "type": "progene_text", "text": [ "SIC1" ], "offsets": [ [ 101, 105 ] ], "normalized": [] }, { "id": "split_0_train_45345_entity", "type": "progene_text", "text": [ "cdc4" ], "offsets": [ [ 208, 212 ] ], "normalized": [] }, { "id": "split_0_train_45346_entity", "type": "progene_text", "text": [ "PDS1" ], "offsets": [ [ 256, 260 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28006
split_0_train_28006
[ { "id": "split_0_train_28006_passage", "type": "progene_text", "text": [ "Collectively , these observations suggest that , in addition to its involvement in the initiation of S phase , Cdc4 may also be required for the onset of anaphase ." ], "offsets": [ [ 0, 164 ] ] } ]
[ { "id": "split_0_train_45347_entity", "type": "progene_text", "text": [ "Cdc4" ], "offsets": [ [ 111, 115 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28007
split_0_train_28007
[ { "id": "split_0_train_28007_passage", "type": "progene_text", "text": [ "Required role of focal adhesion kinase ( FAK ) for integrin - stimulated cell migration ." ], "offsets": [ [ 0, 89 ] ] } ]
[ { "id": "split_0_train_45348_entity", "type": "progene_text", "text": [ "focal adhesion kinase" ], "offsets": [ [ 17, 38 ] ], "normalized": [] }, { "id": "split_0_train_45349_entity", "type": "progene_text", "text": [ "FAK" ], "offsets": [ [ 41, 44 ] ], "normalized": [] }, { "id": "split_0_train_45350_entity", "type": "progene_text", "text": [ "integrin" ], "offsets": [ [ 51, 59 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28008
split_0_train_28008
[ { "id": "split_0_train_28008_passage", "type": "progene_text", "text": [ "FAK localizes to sites of transmembrane integrin receptor clustering and facilitates intracellular signaling events ." ], "offsets": [ [ 0, 117 ] ] } ]
[ { "id": "split_0_train_45351_entity", "type": "progene_text", "text": [ "FAK" ], "offsets": [ [ 0, 3 ] ], "normalized": [] }, { "id": "split_0_train_45352_entity", "type": "progene_text", "text": [ "integrin" ], "offsets": [ [ 40, 48 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28009
split_0_train_28009
[ { "id": "split_0_train_28009_passage", "type": "progene_text", "text": [ "FAK - null ( FAK - ) fibroblasts exhibit a rounded morphology , defects in cell migration , and an elevated number of cell - substratum contact sites ." ], "offsets": [ [ 0, 151 ] ] } ]
[ { "id": "split_0_train_45353_entity", "type": "progene_text", "text": [ "FAK" ], "offsets": [ [ 0, 3 ] ], "normalized": [] }, { "id": "split_0_train_45354_entity", "type": "progene_text", "text": [ "FAK" ], "offsets": [ [ 13, 16 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28010
split_0_train_28010
[ { "id": "split_0_train_28010_passage", "type": "progene_text", "text": [ "Here we show that stable re - expression of epitope - tagged FAK reversed the morphological defects of the FAK - cells through the dynamic regulation of actin structures and focal contact sites in fibronectin ( FN ) stimulated cells ." ], "offsets": [ [ 0, 234 ] ] } ]
[ { "id": "split_0_train_45355_entity", "type": "progene_text", "text": [ "FAK" ], "offsets": [ [ 61, 64 ] ], "normalized": [] }, { "id": "split_0_train_45356_entity", "type": "progene_text", "text": [ "FAK" ], "offsets": [ [ 107, 110 ] ], "normalized": [] }, { "id": "split_0_train_45357_entity", "type": "progene_text", "text": [ "fibronectin" ], "offsets": [ [ 197, 208 ] ], "normalized": [] }, { "id": "split_0_train_45358_entity", "type": "progene_text", "text": [ "FN" ], "offsets": [ [ 211, 213 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28011
split_0_train_28011
[ { "id": "split_0_train_28011_passage", "type": "progene_text", "text": [ "FAK re - expressing fibroblasts ( clones DA2 and DP3 ) exhibit a characteristic fibrillar shape and display indistinguishable FN receptor - stimulated migration properties compared to normal fibroblasts ." ], "offsets": [ [ 0, 204 ] ] } ]
[ { "id": "split_0_train_45359_entity", "type": "progene_text", "text": [ "FAK" ], "offsets": [ [ 0, 3 ] ], "normalized": [] }, { "id": "split_0_train_45360_entity", "type": "progene_text", "text": [ "FN receptor" ], "offsets": [ [ 126, 137 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28012
split_0_train_28012
[ { "id": "split_0_train_28012_passage", "type": "progene_text", "text": [ "Expression of various FAK mutants in the FAK - cells showed that FAK kinase activity , the Tyr - 397 / SH2 domain binding site , and the first proline - rich SH3 binding region in the FAK C - terminal domain were individually needed to promote full FAK - mediated FAK - cell migration to FN whereas direct paxillin binding to FAK was not required ." ], "offsets": [ [ 0, 348 ] ] } ]
[ { "id": "split_0_train_45361_entity", "type": "progene_text", "text": [ "FAK" ], "offsets": [ [ 22, 25 ] ], "normalized": [] }, { "id": "split_0_train_45362_entity", "type": "progene_text", "text": [ "FAK" ], "offsets": [ [ 41, 44 ] ], "normalized": [] }, { "id": "split_0_train_45363_entity", "type": "progene_text", "text": [ "FAK" ], "offsets": [ [ 65, 68 ] ], "normalized": [] }, { "id": "split_0_train_45364_entity", "type": "progene_text", "text": [ "kinase" ], "offsets": [ [ 69, 75 ] ], "normalized": [] }, { "id": "split_0_train_45365_entity", "type": "progene_text", "text": [ "FAK" ], "offsets": [ [ 184, 187 ] ], "normalized": [] }, { "id": "split_0_train_45366_entity", "type": "progene_text", "text": [ "FAK" ], "offsets": [ [ 249, 252 ] ], "normalized": [] }, { "id": "split_0_train_45367_entity", "type": "progene_text", "text": [ "FAK" ], "offsets": [ [ 264, 267 ] ], "normalized": [] }, { "id": "split_0_train_45368_entity", "type": "progene_text", "text": [ "FN" ], "offsets": [ [ 288, 290 ] ], "normalized": [] }, { "id": "split_0_train_45369_entity", "type": "progene_text", "text": [ "paxillin" ], "offsets": [ [ 306, 314 ] ], "normalized": [] }, { "id": "split_0_train_45370_entity", "type": "progene_text", "text": [ "FAK" ], "offsets": [ [ 326, 329 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28013
split_0_train_28013
[ { "id": "split_0_train_28013_passage", "type": "progene_text", "text": [ "Expression of the FAK Phe-397 mutant did not promote FAK - cell migration and overexpression of p50(csk) in DA2 cells inhibited migration to FN suggesting that Src-family PTKs play important roles in FAK - mediated motility events ." ], "offsets": [ [ 0, 232 ] ] } ]
[ { "id": "split_0_train_45371_entity", "type": "progene_text", "text": [ "FAK" ], "offsets": [ [ 18, 21 ] ], "normalized": [] }, { "id": "split_0_train_45372_entity", "type": "progene_text", "text": [ "FAK" ], "offsets": [ [ 53, 56 ] ], "normalized": [] }, { "id": "split_0_train_45373_entity", "type": "progene_text", "text": [ "p50(csk)" ], "offsets": [ [ 96, 104 ] ], "normalized": [] }, { "id": "split_0_train_45374_entity", "type": "progene_text", "text": [ "FN" ], "offsets": [ [ 141, 143 ] ], "normalized": [] }, { "id": "split_0_train_45375_entity", "type": "progene_text", "text": [ "Src-family PTKs" ], "offsets": [ [ 160, 175 ] ], "normalized": [] }, { "id": "split_0_train_45376_entity", "type": "progene_text", "text": [ "FAK" ], "offsets": [ [ 200, 203 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28014
split_0_train_28014
[ { "id": "split_0_train_28014_passage", "type": "progene_text", "text": [ "Expression of the FAK C - terminal domain , FRNK , promoted FAK dephosphorylation at Tyr-397 and potently blocked FAK - mediated cell migration ." ], "offsets": [ [ 0, 145 ] ] } ]
[ { "id": "split_0_train_45377_entity", "type": "progene_text", "text": [ "FAK" ], "offsets": [ [ 18, 21 ] ], "normalized": [] }, { "id": "split_0_train_45378_entity", "type": "progene_text", "text": [ "FAK" ], "offsets": [ [ 60, 63 ] ], "normalized": [] }, { "id": "split_0_train_45379_entity", "type": "progene_text", "text": [ "FAK" ], "offsets": [ [ 114, 117 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28015
split_0_train_28015
[ { "id": "split_0_train_28015_passage", "type": "progene_text", "text": [ "This dominant - negative effect of FRNK was reversed by a point mutation ( Leu - 1034 to Ser ) which prevented FRNK localization to focal contact sites ." ], "offsets": [ [ 0, 153 ] ] } ]
[]
[]
[]
[]
split_0_train_28016
split_0_train_28016
[ { "id": "split_0_train_28016_passage", "type": "progene_text", "text": [ "Our results show that FAK functions as a key regulator of fibronectin receptor stimulated cell migration events through the recruitment of both SH2 and SH3 domain - containing signaling proteins to sites of integrin receptor clustering ." ], "offsets": [ [ 0, 237 ] ] } ]
[ { "id": "split_0_train_45380_entity", "type": "progene_text", "text": [ "FAK" ], "offsets": [ [ 22, 25 ] ], "normalized": [] }, { "id": "split_0_train_45381_entity", "type": "progene_text", "text": [ "fibronectin receptor" ], "offsets": [ [ 58, 78 ] ], "normalized": [] }, { "id": "split_0_train_45382_entity", "type": "progene_text", "text": [ "integrin" ], "offsets": [ [ 207, 215 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28017
split_0_train_28017
[ { "id": "split_0_train_28017_passage", "type": "progene_text", "text": [ "Molecular determinants of the interaction between the C - terminal domain of Alzheimer 's beta-amyloid peptide and apolipoprotein E alpha - helices ." ], "offsets": [ [ 0, 149 ] ] } ]
[ { "id": "split_0_train_45383_entity", "type": "progene_text", "text": [ "beta-amyloid peptide" ], "offsets": [ [ 90, 110 ] ], "normalized": [] }, { "id": "split_0_train_45384_entity", "type": "progene_text", "text": [ "apolipoprotein E" ], "offsets": [ [ 115, 131 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28018
split_0_train_28018
[ { "id": "split_0_train_28018_passage", "type": "progene_text", "text": [ "In a previous work , we predicted and demonstrated that the 29-42-residue fragment of beta-amyloid peptide ( Abeta peptide ) has in vitro capacities close to those of the tilted fragment of viral fusion proteins ." ], "offsets": [ [ 0, 213 ] ] } ]
[ { "id": "split_0_train_45385_entity", "type": "progene_text", "text": [ "beta-amyloid peptide" ], "offsets": [ [ 86, 106 ] ], "normalized": [] }, { "id": "split_0_train_45386_entity", "type": "progene_text", "text": [ "Abeta peptide" ], "offsets": [ [ 109, 122 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28019
split_0_train_28019
[ { "id": "split_0_train_28019_passage", "type": "progene_text", "text": [ "We further demonstrated that apolipoprotein E2 and E3 but not apolipoprotein E4 can decrease the fusogenic activity of Abeta ( 29-42 ) via a direct interaction ." ], "offsets": [ [ 0, 161 ] ] } ]
[ { "id": "split_0_train_45387_entity", "type": "progene_text", "text": [ "apolipoprotein E2" ], "offsets": [ [ 29, 46 ] ], "normalized": [] }, { "id": "split_0_train_45388_entity", "type": "progene_text", "text": [ "apolipoprotein E4" ], "offsets": [ [ 62, 79 ] ], "normalized": [] }, { "id": "split_0_train_45389_entity", "type": "progene_text", "text": [ "Abeta" ], "offsets": [ [ 119, 124 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28020
split_0_train_28020
[ { "id": "split_0_train_28020_passage", "type": "progene_text", "text": [ "Therefore , we suggested that this fragment is implicated in the neurotoxicity of Abeta and in the protective effects of apolipoprotein E in Alzheimer 's disease ." ], "offsets": [ [ 0, 163 ] ] } ]
[ { "id": "split_0_train_45390_entity", "type": "progene_text", "text": [ "Abeta" ], "offsets": [ [ 82, 87 ] ], "normalized": [] }, { "id": "split_0_train_45391_entity", "type": "progene_text", "text": [ "apolipoprotein E" ], "offsets": [ [ 121, 137 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28021
split_0_train_28021
[ { "id": "split_0_train_28021_passage", "type": "progene_text", "text": [ "Because structurally related apolipoproteins do not interact with the Abeta C - terminal domain but inhibit viral fusion , we suggested that interactions existing between fusogenic peptides and apolipoproteins are selective and responsible for the inhibition of fusion ." ], "offsets": [ [ 0, 270 ] ] } ]
[ { "id": "split_0_train_45392_entity", "type": "progene_text", "text": [ "apolipoproteins" ], "offsets": [ [ 29, 44 ] ], "normalized": [] }, { "id": "split_0_train_45393_entity", "type": "progene_text", "text": [ "Abeta" ], "offsets": [ [ 70, 75 ] ], "normalized": [] }, { "id": "split_0_train_45394_entity", "type": "progene_text", "text": [ "apolipoproteins" ], "offsets": [ [ 194, 209 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28022
split_0_train_28022
[ { "id": "split_0_train_28022_passage", "type": "progene_text", "text": [ "In this study , we simulated interactions of all amphipathic helices of apolipoproteins E and A-I with Abeta and simian immunodeficiency virus ( SIV ) fusogenic fragments by molecular modeling ." ], "offsets": [ [ 0, 194 ] ] } ]
[ { "id": "split_0_train_45395_entity", "type": "progene_text", "text": [ "apolipoproteins E and A-I" ], "offsets": [ [ 72, 97 ] ], "normalized": [] }, { "id": "split_0_train_45396_entity", "type": "progene_text", "text": [ "Abeta" ], "offsets": [ [ 103, 108 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28023
split_0_train_28023
[ { "id": "split_0_train_28023_passage", "type": "progene_text", "text": [ "We further calculated cross - interactions that do not inhibit fusion in vitro ." ], "offsets": [ [ 0, 80 ] ] } ]
[]
[]
[]
[]
split_0_train_28024
split_0_train_28024
[ { "id": "split_0_train_28024_passage", "type": "progene_text", "text": [ "The results suggest that interactions of hydrophobic residues are the major event to inhibit the fusogenic capacities of Abeta ( 29-42 ) and SIV peptides ." ], "offsets": [ [ 0, 155 ] ] } ]
[ { "id": "split_0_train_45397_entity", "type": "progene_text", "text": [ "Abeta" ], "offsets": [ [ 121, 126 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28025
split_0_train_28025
[ { "id": "split_0_train_28025_passage", "type": "progene_text", "text": [ "Selectivity of those interactions is due to the steric complementarity between bulky hydrophobic residues in the fusogenic fragments and hydrophobic residues in the apolipoprotein C - terminal amphipathic helices ." ], "offsets": [ [ 0, 214 ] ] } ]
[ { "id": "split_0_train_45398_entity", "type": "progene_text", "text": [ "apolipoprotein C" ], "offsets": [ [ 165, 181 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28026
split_0_train_28026
[ { "id": "split_0_train_28026_passage", "type": "progene_text", "text": [ "Repair of endonuclease - induced double - strand breaks in Saccharomyces cerevisiae : essential role for genes associated with nonhomologous end - joining ." ], "offsets": [ [ 0, 156 ] ] } ]
[ { "id": "split_0_train_45399_entity", "type": "progene_text", "text": [ "endonuclease" ], "offsets": [ [ 10, 22 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28027
split_0_train_28027
[ { "id": "split_0_train_28027_passage", "type": "progene_text", "text": [ "Repair of double - strand breaks ( DSBs ) in chromosomal DNA by nonhomologous end - joining ( NHEJ ) is not well characterized in the yeast Saccharomyces cerevisiae ." ], "offsets": [ [ 0, 166 ] ] } ]
[]
[]
[]
[]
split_0_train_28028
split_0_train_28028
[ { "id": "split_0_train_28028_passage", "type": "progene_text", "text": [ "Here we demonstrate that several genes associated with NHEJ perform essential functions in the repair of endonuclease - induced DSBs in vivo ." ], "offsets": [ [ 0, 142 ] ] } ]
[ { "id": "split_0_train_45400_entity", "type": "progene_text", "text": [ "endonuclease" ], "offsets": [ [ 105, 117 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28029
split_0_train_28029
[ { "id": "split_0_train_28029_passage", "type": "progene_text", "text": [ "Galactose - induced expression of EcoRI endonuclease in rad50 , mre11 , or xrs2 mutants , which are deficient in plasmid DSB end - joining and some forms of recombination , resulted in G2 arrest and rapid cell killing ." ], "offsets": [ [ 0, 219 ] ] } ]
[ { "id": "split_0_train_45401_entity", "type": "progene_text", "text": [ "EcoRI" ], "offsets": [ [ 34, 39 ] ], "normalized": [] }, { "id": "split_0_train_45402_entity", "type": "progene_text", "text": [ "endonuclease" ], "offsets": [ [ 40, 52 ] ], "normalized": [] }, { "id": "split_0_train_45403_entity", "type": "progene_text", "text": [ "rad50" ], "offsets": [ [ 56, 61 ] ], "normalized": [] }, { "id": "split_0_train_45404_entity", "type": "progene_text", "text": [ "mre11" ], "offsets": [ [ 64, 69 ] ], "normalized": [] }, { "id": "split_0_train_45405_entity", "type": "progene_text", "text": [ "xrs2" ], "offsets": [ [ 75, 79 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28030
split_0_train_28030
[ { "id": "split_0_train_28030_passage", "type": "progene_text", "text": [ "Endonuclease synthesis also produced moderate cell killing in sir4 strains ." ], "offsets": [ [ 0, 76 ] ] } ]
[ { "id": "split_0_train_45406_entity", "type": "progene_text", "text": [ "Endonuclease" ], "offsets": [ [ 0, 12 ] ], "normalized": [] }, { "id": "split_0_train_45407_entity", "type": "progene_text", "text": [ "sir4" ], "offsets": [ [ 62, 66 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28031
split_0_train_28031
[ { "id": "split_0_train_28031_passage", "type": "progene_text", "text": [ "In contrast , EcoRI caused prolonged cell - cycle arrest of recombination - defective rad51 , rad52 , rad54 , rad55 , and rad57 mutants , but cells remained viable ." ], "offsets": [ [ 0, 165 ] ] } ]
[ { "id": "split_0_train_45408_entity", "type": "progene_text", "text": [ "EcoRI" ], "offsets": [ [ 14, 19 ] ], "normalized": [] }, { "id": "split_0_train_45409_entity", "type": "progene_text", "text": [ "rad51" ], "offsets": [ [ 86, 91 ] ], "normalized": [] }, { "id": "split_0_train_45410_entity", "type": "progene_text", "text": [ "rad52" ], "offsets": [ [ 94, 99 ] ], "normalized": [] }, { "id": "split_0_train_45411_entity", "type": "progene_text", "text": [ "rad54" ], "offsets": [ [ 102, 107 ] ], "normalized": [] }, { "id": "split_0_train_45412_entity", "type": "progene_text", "text": [ "rad55" ], "offsets": [ [ 110, 115 ] ], "normalized": [] }, { "id": "split_0_train_45413_entity", "type": "progene_text", "text": [ "rad57" ], "offsets": [ [ 122, 127 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28032
split_0_train_28032
[ { "id": "split_0_train_28032_passage", "type": "progene_text", "text": [ "Cell - cycle progression was inhibited in excision repair - defective rad1 mutants , but not in rad2 cells , indicating a role for Rad1 processing of the DSB ends ." ], "offsets": [ [ 0, 164 ] ] } ]
[ { "id": "split_0_train_45414_entity", "type": "progene_text", "text": [ "rad1" ], "offsets": [ [ 70, 74 ] ], "normalized": [] }, { "id": "split_0_train_45415_entity", "type": "progene_text", "text": [ "rad2" ], "offsets": [ [ 96, 100 ] ], "normalized": [] }, { "id": "split_0_train_45416_entity", "type": "progene_text", "text": [ "Rad1" ], "offsets": [ [ 131, 135 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28033
split_0_train_28033
[ { "id": "split_0_train_28033_passage", "type": "progene_text", "text": [ "Phenotypic responses of additional mutants , including exo1 , srs2 , rad5 , and rdh54 strains , suggest roles in recombinational repair , but not in NHEJ ." ], "offsets": [ [ 0, 155 ] ] } ]
[ { "id": "split_0_train_45417_entity", "type": "progene_text", "text": [ "exo1" ], "offsets": [ [ 55, 59 ] ], "normalized": [] }, { "id": "split_0_train_45418_entity", "type": "progene_text", "text": [ "srs2" ], "offsets": [ [ 62, 66 ] ], "normalized": [] }, { "id": "split_0_train_45419_entity", "type": "progene_text", "text": [ "rad5" ], "offsets": [ [ 69, 73 ] ], "normalized": [] }, { "id": "split_0_train_45420_entity", "type": "progene_text", "text": [ "rdh54" ], "offsets": [ [ 80, 85 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28034
split_0_train_28034
[ { "id": "split_0_train_28034_passage", "type": "progene_text", "text": [ "Interestingly , the rapid cell killing in haploid rad50 and mre11 strains was largely eliminated in diploids , suggesting that the cohesive - ended DSBs could be efficiently repaired by homologous recombination throughout the cell cycle in the diploid mutants ." ], "offsets": [ [ 0, 261 ] ] } ]
[ { "id": "split_0_train_45421_entity", "type": "progene_text", "text": [ "rad50" ], "offsets": [ [ 50, 55 ] ], "normalized": [] }, { "id": "split_0_train_45422_entity", "type": "progene_text", "text": [ "mre11" ], "offsets": [ [ 60, 65 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28035
split_0_train_28035
[ { "id": "split_0_train_28035_passage", "type": "progene_text", "text": [ "These results demonstrate essential but separable roles for NHEJ pathway genes in the repair of chromosomal DSBs that are structurally similar to those occurring during cellular development ." ], "offsets": [ [ 0, 191 ] ] } ]
[]
[]
[]
[]
split_0_train_28036
split_0_train_28036
[ { "id": "split_0_train_28036_passage", "type": "progene_text", "text": [ "Expression of tumour necrosis factor receptors ( CD120a and CD120b ) on bronchoalveolar cells ." ], "offsets": [ [ 0, 95 ] ] } ]
[ { "id": "split_0_train_45423_entity", "type": "progene_text", "text": [ "tumour necrosis factor receptors" ], "offsets": [ [ 14, 46 ] ], "normalized": [] }, { "id": "split_0_train_45424_entity", "type": "progene_text", "text": [ "CD120a" ], "offsets": [ [ 49, 55 ] ], "normalized": [] }, { "id": "split_0_train_45425_entity", "type": "progene_text", "text": [ "CD120b" ], "offsets": [ [ 60, 66 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28037
split_0_train_28037
[ { "id": "split_0_train_28037_passage", "type": "progene_text", "text": [ "It is generally accepted that physiological modulators for tumour necrosis factor ( TNF ) are present in a variety of body fluids including serum ." ], "offsets": [ [ 0, 147 ] ] } ]
[ { "id": "split_0_train_45426_entity", "type": "progene_text", "text": [ "tumour necrosis factor" ], "offsets": [ [ 59, 81 ] ], "normalized": [] }, { "id": "split_0_train_45427_entity", "type": "progene_text", "text": [ "TNF" ], "offsets": [ [ 84, 87 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28038
split_0_train_28038
[ { "id": "split_0_train_28038_passage", "type": "progene_text", "text": [ "Among these modulators are soluble TNF receptors ( TNF-R ) that are cleaved from the extracellular domain of the TNF-Rs ." ], "offsets": [ [ 0, 121 ] ] } ]
[ { "id": "split_0_train_45428_entity", "type": "progene_text", "text": [ "TNF receptors" ], "offsets": [ [ 35, 48 ] ], "normalized": [] }, { "id": "split_0_train_45429_entity", "type": "progene_text", "text": [ "TNF-R" ], "offsets": [ [ 51, 56 ] ], "normalized": [] }, { "id": "split_0_train_45430_entity", "type": "progene_text", "text": [ "TNF-Rs" ], "offsets": [ [ 113, 119 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28039
split_0_train_28039
[ { "id": "split_0_train_28039_passage", "type": "progene_text", "text": [ "Two receptors of different structures with molecular weights of 55 kDa ( CD120a ) and 75 kDa ( CD120b ) are known to be expressed on monocytes , lymphocytes , granulocytes and other cells of peripheral blood ." ], "offsets": [ [ 0, 209 ] ] } ]
[ { "id": "split_0_train_45431_entity", "type": "progene_text", "text": [ "CD120a" ], "offsets": [ [ 73, 79 ] ], "normalized": [] }, { "id": "split_0_train_45432_entity", "type": "progene_text", "text": [ "CD120b" ], "offsets": [ [ 95, 101 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28040
split_0_train_28040
[ { "id": "split_0_train_28040_passage", "type": "progene_text", "text": [ "The aim of our study was to determine the expression of CD120a and CD120b on bronchoalveolar lavage cells ( BAL cells ) ." ], "offsets": [ [ 0, 121 ] ] } ]
[ { "id": "split_0_train_45433_entity", "type": "progene_text", "text": [ "CD120a" ], "offsets": [ [ 56, 62 ] ], "normalized": [] }, { "id": "split_0_train_45434_entity", "type": "progene_text", "text": [ "CD120b" ], "offsets": [ [ 67, 73 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28041
split_0_train_28041
[ { "id": "split_0_train_28041_passage", "type": "progene_text", "text": [ "BAL cells of 14 patients with different pulmonary disorders were stained with anti - CD120a and anti - CD120b monoclonal antibodies and were differentiated by FACS analysis ." ], "offsets": [ [ 0, 174 ] ] } ]
[ { "id": "split_0_train_45435_entity", "type": "progene_text", "text": [ "CD120a" ], "offsets": [ [ 85, 91 ] ], "normalized": [] }, { "id": "split_0_train_45436_entity", "type": "progene_text", "text": [ "CD120b" ], "offsets": [ [ 103, 109 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28042
split_0_train_28042
[ { "id": "split_0_train_28042_passage", "type": "progene_text", "text": [ "Both TNF-Rs are expressed on monocytes , macrophages , lymphocytes and granulocytes of the BAL ." ], "offsets": [ [ 0, 96 ] ] } ]
[ { "id": "split_0_train_45437_entity", "type": "progene_text", "text": [ "TNF-Rs" ], "offsets": [ [ 5, 11 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28043
split_0_train_28043
[ { "id": "split_0_train_28043_passage", "type": "progene_text", "text": [ "Although the relation of CD120a to CD120b is individual for a given cell type and an individual patient , strict correlations between both receptors were observed for BAL monocytes and alveolar macrophages ." ], "offsets": [ [ 0, 207 ] ] } ]
[ { "id": "split_0_train_45438_entity", "type": "progene_text", "text": [ "CD120a" ], "offsets": [ [ 25, 31 ] ], "normalized": [] }, { "id": "split_0_train_45439_entity", "type": "progene_text", "text": [ "CD120b" ], "offsets": [ [ 35, 41 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28044
split_0_train_28044
[ { "id": "split_0_train_28044_passage", "type": "progene_text", "text": [ "CD120a are expressed on 29.7 % of alveolar macrophages ; similar data were obtained for CD120b ." ], "offsets": [ [ 0, 96 ] ] } ]
[ { "id": "split_0_train_45440_entity", "type": "progene_text", "text": [ "CD120a" ], "offsets": [ [ 0, 6 ] ], "normalized": [] }, { "id": "split_0_train_45441_entity", "type": "progene_text", "text": [ "CD120b" ], "offsets": [ [ 88, 94 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28045
split_0_train_28045
[ { "id": "split_0_train_28045_passage", "type": "progene_text", "text": [ "24.3 % of the BAL monocytes were positive for CD120a and 25.5 % for CD120b ." ], "offsets": [ [ 0, 76 ] ] } ]
[ { "id": "split_0_train_45442_entity", "type": "progene_text", "text": [ "CD120a" ], "offsets": [ [ 46, 52 ] ], "normalized": [] }, { "id": "split_0_train_45443_entity", "type": "progene_text", "text": [ "CD120b" ], "offsets": [ [ 68, 74 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28046
split_0_train_28046
[ { "id": "split_0_train_28046_passage", "type": "progene_text", "text": [ "4.1 % of the BAL lymphocytes were positive for CD120a whereas the percentage of CD120b positive BAL lymphocytes was approximately six times greater ." ], "offsets": [ [ 0, 149 ] ] } ]
[ { "id": "split_0_train_45444_entity", "type": "progene_text", "text": [ "CD120a" ], "offsets": [ [ 47, 53 ] ], "normalized": [] }, { "id": "split_0_train_45445_entity", "type": "progene_text", "text": [ "CD120b" ], "offsets": [ [ 80, 86 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28047
split_0_train_28047
[ { "id": "split_0_train_28047_passage", "type": "progene_text", "text": [ "Analysis of BAL granulocytes revealed 21.2 % cells positive for CD120a and 11.6 % for CD120b ." ], "offsets": [ [ 0, 94 ] ] } ]
[ { "id": "split_0_train_45446_entity", "type": "progene_text", "text": [ "CD120a" ], "offsets": [ [ 64, 70 ] ], "normalized": [] }, { "id": "split_0_train_45447_entity", "type": "progene_text", "text": [ "CD120b" ], "offsets": [ [ 86, 92 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28048
split_0_train_28048
[ { "id": "split_0_train_28048_passage", "type": "progene_text", "text": [ "In contrast to the BAL cells named above there was no positive correlation between CD120a and CD120b expression on BAL lymphocytes and granulocytes ." ], "offsets": [ [ 0, 149 ] ] } ]
[ { "id": "split_0_train_45448_entity", "type": "progene_text", "text": [ "CD120a" ], "offsets": [ [ 83, 89 ] ], "normalized": [] }, { "id": "split_0_train_45449_entity", "type": "progene_text", "text": [ "CD120b" ], "offsets": [ [ 94, 100 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28049
split_0_train_28049
[ { "id": "split_0_train_28049_passage", "type": "progene_text", "text": [ "We were able to show that TNF-Rs of BAL cells , like those of blood cells , are shedded in vitro after incubation with or without lipopolysaccharide ( LPS ) , detected as TNFalpha - inhibitor activity in cell culture supernatant ." ], "offsets": [ [ 0, 230 ] ] } ]
[ { "id": "split_0_train_45450_entity", "type": "progene_text", "text": [ "TNF-Rs" ], "offsets": [ [ 26, 32 ] ], "normalized": [] }, { "id": "split_0_train_45451_entity", "type": "progene_text", "text": [ "TNFalpha" ], "offsets": [ [ 171, 179 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28050
split_0_train_28050
[ { "id": "split_0_train_28050_passage", "type": "progene_text", "text": [ "In conclusion , BAL cells express and shed TNF-Rs , as is known for cells of other body compartments ." ], "offsets": [ [ 0, 102 ] ] } ]
[ { "id": "split_0_train_45452_entity", "type": "progene_text", "text": [ "TNF-Rs" ], "offsets": [ [ 43, 49 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28051
split_0_train_28051
[ { "id": "split_0_train_28051_passage", "type": "progene_text", "text": [ "The B cell antigen receptor activates the Akt ( protein kinase B ) / glycogen synthase kinase-3 signaling pathway via phosphatidylinositol 3-kinase ." ], "offsets": [ [ 0, 149 ] ] } ]
[ { "id": "split_0_train_45453_entity", "type": "progene_text", "text": [ "B cell antigen receptor" ], "offsets": [ [ 4, 27 ] ], "normalized": [] }, { "id": "split_0_train_45454_entity", "type": "progene_text", "text": [ "Akt" ], "offsets": [ [ 42, 45 ] ], "normalized": [] }, { "id": "split_0_train_45455_entity", "type": "progene_text", "text": [ "protein kinase B" ], "offsets": [ [ 48, 64 ] ], "normalized": [] }, { "id": "split_0_train_45456_entity", "type": "progene_text", "text": [ "glycogen synthase kinase-3" ], "offsets": [ [ 69, 95 ] ], "normalized": [] }, { "id": "split_0_train_45457_entity", "type": "progene_text", "text": [ "phosphatidylinositol 3-kinase" ], "offsets": [ [ 118, 147 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28052
split_0_train_28052
[ { "id": "split_0_train_28052_passage", "type": "progene_text", "text": [ "We have previously shown that the B cell Ag receptor ( BCR ) activates phosphatidylinositol ( PI ) 3-kinase ." ], "offsets": [ [ 0, 109 ] ] } ]
[ { "id": "split_0_train_45458_entity", "type": "progene_text", "text": [ "B cell Ag receptor" ], "offsets": [ [ 34, 52 ] ], "normalized": [] }, { "id": "split_0_train_45459_entity", "type": "progene_text", "text": [ "BCR" ], "offsets": [ [ 55, 58 ] ], "normalized": [] }, { "id": "split_0_train_45460_entity", "type": "progene_text", "text": [ "phosphatidylinositol ( PI ) 3-kinase" ], "offsets": [ [ 71, 107 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28053
split_0_train_28053
[ { "id": "split_0_train_28053_passage", "type": "progene_text", "text": [ "We now show that a serine / threonine kinase called Akt or protein kinase B is a downstream target of PI 3-kinase in B cells ." ], "offsets": [ [ 0, 126 ] ] } ]
[ { "id": "split_0_train_45461_entity", "type": "progene_text", "text": [ "serine / threonine kinase" ], "offsets": [ [ 19, 44 ] ], "normalized": [] }, { "id": "split_0_train_45462_entity", "type": "progene_text", "text": [ "Akt" ], "offsets": [ [ 52, 55 ] ], "normalized": [] }, { "id": "split_0_train_45463_entity", "type": "progene_text", "text": [ "protein kinase B" ], "offsets": [ [ 59, 75 ] ], "normalized": [] }, { "id": "split_0_train_45464_entity", "type": "progene_text", "text": [ "PI 3-kinase" ], "offsets": [ [ 102, 113 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28054
split_0_train_28054
[ { "id": "split_0_train_28054_passage", "type": "progene_text", "text": [ "Akt has been shown to promote cell survival as well as the transcription and translation of proteins involved in cell cycle progression ." ], "offsets": [ [ 0, 137 ] ] } ]
[ { "id": "split_0_train_45465_entity", "type": "progene_text", "text": [ "Akt" ], "offsets": [ [ 0, 3 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28055
split_0_train_28055
[ { "id": "split_0_train_28055_passage", "type": "progene_text", "text": [ "Using an Ab that specifically recognizes the activated form of Akt that is phosphorylated on serine 473 , we show that BCR engagement activates Akt in a PI 3-kinase - dependent manner ." ], "offsets": [ [ 0, 185 ] ] } ]
[ { "id": "split_0_train_45466_entity", "type": "progene_text", "text": [ "Ab" ], "offsets": [ [ 9, 11 ] ], "normalized": [] }, { "id": "split_0_train_45467_entity", "type": "progene_text", "text": [ "Akt" ], "offsets": [ [ 63, 66 ] ], "normalized": [] }, { "id": "split_0_train_45468_entity", "type": "progene_text", "text": [ "BCR" ], "offsets": [ [ 119, 122 ] ], "normalized": [] }, { "id": "split_0_train_45469_entity", "type": "progene_text", "text": [ "Akt" ], "offsets": [ [ 144, 147 ] ], "normalized": [] }, { "id": "split_0_train_45470_entity", "type": "progene_text", "text": [ "PI 3-kinase" ], "offsets": [ [ 153, 164 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28056
split_0_train_28056
[ { "id": "split_0_train_28056_passage", "type": "progene_text", "text": [ "These results were confirmed using in vitro kinase assays ." ], "offsets": [ [ 0, 59 ] ] } ]
[ { "id": "split_0_train_45471_entity", "type": "progene_text", "text": [ "kinase" ], "offsets": [ [ 44, 50 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28057
split_0_train_28057
[ { "id": "split_0_train_28057_passage", "type": "progene_text", "text": [ "Moreover , BCR ligation also induced phosphorylation of Akt of threonine 308 , another modification that is required for activation of Akt ." ], "offsets": [ [ 0, 140 ] ] } ]
[ { "id": "split_0_train_45472_entity", "type": "progene_text", "text": [ "BCR" ], "offsets": [ [ 11, 14 ] ], "normalized": [] }, { "id": "split_0_train_45473_entity", "type": "progene_text", "text": [ "Akt" ], "offsets": [ [ 56, 59 ] ], "normalized": [] }, { "id": "split_0_train_45474_entity", "type": "progene_text", "text": [ "Akt" ], "offsets": [ [ 135, 138 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28058
split_0_train_28058
[ { "id": "split_0_train_28058_passage", "type": "progene_text", "text": [ "In the DT40 chicken B cell line , phosphorylation of Akt on serine 473 was completely dependent on the Lyn tyrosine kinase , while the Syk tyrosine kinase was required for sustained phosphorylation of Akt ." ], "offsets": [ [ 0, 206 ] ] } ]
[ { "id": "split_0_train_45475_entity", "type": "progene_text", "text": [ "Akt" ], "offsets": [ [ 53, 56 ] ], "normalized": [] }, { "id": "split_0_train_45476_entity", "type": "progene_text", "text": [ "Lyn" ], "offsets": [ [ 103, 106 ] ], "normalized": [] }, { "id": "split_0_train_45477_entity", "type": "progene_text", "text": [ "tyrosine kinase" ], "offsets": [ [ 107, 122 ] ], "normalized": [] }, { "id": "split_0_train_45478_entity", "type": "progene_text", "text": [ "Syk" ], "offsets": [ [ 135, 138 ] ], "normalized": [] }, { "id": "split_0_train_45479_entity", "type": "progene_text", "text": [ "tyrosine kinase" ], "offsets": [ [ 139, 154 ] ], "normalized": [] }, { "id": "split_0_train_45480_entity", "type": "progene_text", "text": [ "Akt" ], "offsets": [ [ 201, 204 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28059
split_0_train_28059
[ { "id": "split_0_train_28059_passage", "type": "progene_text", "text": [ "Complementary experiments in BCR - expressing AtT20 endocrine cells confirmed that Src kinases are sufficient for BCR - induced Akt phosphorylation , but that Syk is required for sustained phosphorylation of Akt on both serine 473 and threonine 308 ." ], "offsets": [ [ 0, 250 ] ] } ]
[ { "id": "split_0_train_45481_entity", "type": "progene_text", "text": [ "BCR" ], "offsets": [ [ 29, 32 ] ], "normalized": [] }, { "id": "split_0_train_45482_entity", "type": "progene_text", "text": [ "Src" ], "offsets": [ [ 83, 86 ] ], "normalized": [] }, { "id": "split_0_train_45483_entity", "type": "progene_text", "text": [ "kinases" ], "offsets": [ [ 87, 94 ] ], "normalized": [] }, { "id": "split_0_train_45484_entity", "type": "progene_text", "text": [ "BCR" ], "offsets": [ [ 114, 117 ] ], "normalized": [] }, { "id": "split_0_train_45485_entity", "type": "progene_text", "text": [ "Akt" ], "offsets": [ [ 128, 131 ] ], "normalized": [] }, { "id": "split_0_train_45486_entity", "type": "progene_text", "text": [ "Syk" ], "offsets": [ [ 159, 162 ] ], "normalized": [] }, { "id": "split_0_train_45487_entity", "type": "progene_text", "text": [ "Akt" ], "offsets": [ [ 208, 211 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28060
split_0_train_28060
[ { "id": "split_0_train_28060_passage", "type": "progene_text", "text": [ "In insulin - responsive cells , Akt phosphorylates and inactivates the serine / threonine kinase glycogen synthase kinase-3 ( GSK-3 ) ." ], "offsets": [ [ 0, 135 ] ] } ]
[ { "id": "split_0_train_45488_entity", "type": "progene_text", "text": [ "insulin" ], "offsets": [ [ 3, 10 ] ], "normalized": [] }, { "id": "split_0_train_45489_entity", "type": "progene_text", "text": [ "Akt" ], "offsets": [ [ 32, 35 ] ], "normalized": [] }, { "id": "split_0_train_45490_entity", "type": "progene_text", "text": [ "serine / threonine kinase" ], "offsets": [ [ 71, 96 ] ], "normalized": [] }, { "id": "split_0_train_45491_entity", "type": "progene_text", "text": [ "glycogen synthase kinase-3" ], "offsets": [ [ 97, 123 ] ], "normalized": [] }, { "id": "split_0_train_45492_entity", "type": "progene_text", "text": [ "GSK-3" ], "offsets": [ [ 126, 131 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28061
split_0_train_28061
[ { "id": "split_0_train_28061_passage", "type": "progene_text", "text": [ "Inactivation of GSK-3 may promote nuclear accumulation of several transcription factors , including NF-ATc ." ], "offsets": [ [ 0, 108 ] ] } ]
[ { "id": "split_0_train_45493_entity", "type": "progene_text", "text": [ "GSK-3" ], "offsets": [ [ 16, 21 ] ], "normalized": [] }, { "id": "split_0_train_45494_entity", "type": "progene_text", "text": [ "transcription factors" ], "offsets": [ [ 66, 87 ] ], "normalized": [] }, { "id": "split_0_train_45495_entity", "type": "progene_text", "text": [ "NF-ATc" ], "offsets": [ [ 100, 106 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28062
split_0_train_28062
[ { "id": "split_0_train_28062_passage", "type": "progene_text", "text": [ "We found that BCR engagement induced GSK-3 phosphorylation and decreased GSK-3 enzyme activity ." ], "offsets": [ [ 0, 96 ] ] } ]
[ { "id": "split_0_train_45496_entity", "type": "progene_text", "text": [ "BCR" ], "offsets": [ [ 14, 17 ] ], "normalized": [] }, { "id": "split_0_train_45497_entity", "type": "progene_text", "text": [ "GSK-3" ], "offsets": [ [ 37, 42 ] ], "normalized": [] }, { "id": "split_0_train_45498_entity", "type": "progene_text", "text": [ "GSK-3" ], "offsets": [ [ 73, 78 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28063
split_0_train_28063
[ { "id": "split_0_train_28063_passage", "type": "progene_text", "text": [ "Thus , BCR ligation initiates a PI 3-kinase / Akt / GSK-3 signaling pathway ." ], "offsets": [ [ 0, 77 ] ] } ]
[ { "id": "split_0_train_45499_entity", "type": "progene_text", "text": [ "BCR" ], "offsets": [ [ 7, 10 ] ], "normalized": [] }, { "id": "split_0_train_45500_entity", "type": "progene_text", "text": [ "PI 3-kinase" ], "offsets": [ [ 32, 43 ] ], "normalized": [] }, { "id": "split_0_train_45501_entity", "type": "progene_text", "text": [ "Akt" ], "offsets": [ [ 46, 49 ] ], "normalized": [] }, { "id": "split_0_train_45502_entity", "type": "progene_text", "text": [ "GSK-3" ], "offsets": [ [ 52, 57 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28064
split_0_train_28064
[ { "id": "split_0_train_28064_passage", "type": "progene_text", "text": [ "Binge drinking and bone metabolism in a young actively growing rat model ." ], "offsets": [ [ 0, 74 ] ] } ]
[]
[]
[]
[]
split_0_train_28065
split_0_train_28065
[ { "id": "split_0_train_28065_passage", "type": "progene_text", "text": [ "BACKGROUND :" ], "offsets": [ [ 0, 12 ] ] } ]
[]
[]
[]
[]
split_0_train_28066
split_0_train_28066
[ { "id": "split_0_train_28066_passage", "type": "progene_text", "text": [ "Chronic alcohol consumption has been demonstrated to be deleterious to bone health ." ], "offsets": [ [ 0, 84 ] ] } ]
[]
[]
[]
[]
split_0_train_28067
split_0_train_28067
[ { "id": "split_0_train_28067_passage", "type": "progene_text", "text": [ "However , binge drinking is the prevalent form of drinking in young people , which was the impetus for the present study to determine the effect of week - end and week - long binge drinking on bone health in a young actively growing animal model ." ], "offsets": [ [ 0, 247 ] ] } ]
[]
[]
[]
[]
split_0_train_28068
split_0_train_28068
[ { "id": "split_0_train_28068_passage", "type": "progene_text", "text": [ "METHODS :" ], "offsets": [ [ 0, 9 ] ] } ]
[]
[]
[]
[]
split_0_train_28069
split_0_train_28069
[ { "id": "split_0_train_28069_passage", "type": "progene_text", "text": [ "Four - week - old , female , Sprague - Dawley rats were given the amount of 5 % alcohol by gavage to be equivalent to a 63 kg woman drinking six beers a day for either 2 or 5 consecutive days per week ." ], "offsets": [ [ 0, 202 ] ] } ]
[]
[]
[]
[]
split_0_train_28070
split_0_train_28070
[ { "id": "split_0_train_28070_passage", "type": "progene_text", "text": [ "RESULTS :" ], "offsets": [ [ 0, 9 ] ] } ]
[]
[]
[]
[]
split_0_train_28071
split_0_train_28071
[ { "id": "split_0_train_28071_passage", "type": "progene_text", "text": [ "There were no changes in the 5 - day binge animals , but the 2 - day binge animals were hypocalcemic ." ], "offsets": [ [ 0, 102 ] ] } ]
[]
[]
[]
[]
split_0_train_28072
split_0_train_28072
[ { "id": "split_0_train_28072_passage", "type": "progene_text", "text": [ "Similarly , 2 - day binge animals had slightly increased bone chemistry and histomorphometric values for both tibia and femur , but only femur length , dry weight , and ash weight as well as femur density , presented either as g / ml or ash weight per unit volume , were increased by a statistically significant level ." ], "offsets": [ [ 0, 319 ] ] } ]
[]
[]
[]
[]
split_0_train_28073
split_0_train_28073
[ { "id": "split_0_train_28073_passage", "type": "progene_text", "text": [ "Cross - section periosteal Mineral Apposition Rate ( MAR ) was significantly decreased in the 2 - day alcohol fed animals ." ], "offsets": [ [ 0, 123 ] ] } ]
[]
[]
[]
[]
split_0_train_28074
split_0_train_28074
[ { "id": "split_0_train_28074_passage", "type": "progene_text", "text": [ "CONCLUSIONS :" ], "offsets": [ [ 0, 13 ] ] } ]
[]
[]
[]
[]
split_0_train_28075
split_0_train_28075
[ { "id": "split_0_train_28075_passage", "type": "progene_text", "text": [ "Actively growing rats given 5 % alcohol by gavage for 2 days per week have an increased bone length , bone weight , and bone density ." ], "offsets": [ [ 0, 134 ] ] } ]
[]
[]
[]
[]
split_0_train_28076
split_0_train_28076
[ { "id": "split_0_train_28076_passage", "type": "progene_text", "text": [ "The interpretation of these results must be viewed with great caution because studies of chronic alcohol consumption , and many studies of acute drinking , clearly indicate deleterious effects of alcohol on bone health ." ], "offsets": [ [ 0, 220 ] ] } ]
[]
[]
[]
[]
split_0_train_28077
split_0_train_28077
[ { "id": "split_0_train_28077_passage", "type": "progene_text", "text": [ "Those fed alcohol for 5 days per week showed no change ." ], "offsets": [ [ 0, 56 ] ] } ]
[]
[]
[]
[]
split_0_train_28078
split_0_train_28078
[ { "id": "split_0_train_28078_passage", "type": "progene_text", "text": [ "Activator protein-2 mediates transcriptional activation of the CYP11A1 gene by interaction with Sp1 rather than binding to DNA ." ], "offsets": [ [ 0, 128 ] ] } ]
[ { "id": "split_0_train_45503_entity", "type": "progene_text", "text": [ "Activator protein-2" ], "offsets": [ [ 0, 19 ] ], "normalized": [] }, { "id": "split_0_train_45504_entity", "type": "progene_text", "text": [ "CYP11A1" ], "offsets": [ [ 63, 70 ] ], "normalized": [] }, { "id": "split_0_train_45505_entity", "type": "progene_text", "text": [ "Sp1" ], "offsets": [ [ 96, 99 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28079
split_0_train_28079
[ { "id": "split_0_train_28079_passage", "type": "progene_text", "text": [ "The ovine P45 side chain cleavage ( CYP11A1 ) enzyme gene , which catalyzes the initial enzymatic step in steroid hormone biosynthesis is transcriptionally regulated in cultured steroidogenic human trophoblastic JEG-3 cells ." ], "offsets": [ [ 0, 225 ] ] } ]
[ { "id": "split_0_train_45506_entity", "type": "progene_text", "text": [ "P45 side chain cleavage" ], "offsets": [ [ 10, 33 ] ], "normalized": [] }, { "id": "split_0_train_45507_entity", "type": "progene_text", "text": [ "CYP11A1" ], "offsets": [ [ 36, 43 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28080
split_0_train_28080
[ { "id": "split_0_train_28080_passage", "type": "progene_text", "text": [ "The ovine CYP11A1 promoter contains two GC - rich footprinted regions referred to as ovine footprints 5 ( OF5 ) and OF3 , which are well conserved among the CYP11A1 promoters of different species ." ], "offsets": [ [ 0, 197 ] ] } ]
[ { "id": "split_0_train_45508_entity", "type": "progene_text", "text": [ "CYP11A1" ], "offsets": [ [ 10, 17 ] ], "normalized": [] }, { "id": "split_0_train_45509_entity", "type": "progene_text", "text": [ "CYP11A1" ], "offsets": [ [ 157, 164 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28081
split_0_train_28081
[ { "id": "split_0_train_28081_passage", "type": "progene_text", "text": [ "These GC - rich sequences resemble activator protein-2 ( AP-2 ) / Sp1 binding sites and were previously implicated in basal and cAMP - regulated activity of the bovine and ovine CYP11A1 promoters ." ], "offsets": [ [ 0, 197 ] ] } ]
[ { "id": "split_0_train_45510_entity", "type": "progene_text", "text": [ "activator protein-2" ], "offsets": [ [ 35, 54 ] ], "normalized": [] }, { "id": "split_0_train_45511_entity", "type": "progene_text", "text": [ "AP-2" ], "offsets": [ [ 57, 61 ] ], "normalized": [] }, { "id": "split_0_train_45512_entity", "type": "progene_text", "text": [ "Sp1" ], "offsets": [ [ 66, 69 ] ], "normalized": [] }, { "id": "split_0_train_45513_entity", "type": "progene_text", "text": [ "CYP11A1" ], "offsets": [ [ 178, 185 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28082
split_0_train_28082
[ { "id": "split_0_train_28082_passage", "type": "progene_text", "text": [ "In the current studies , AP-2 induced the ovine CYP11A1 promoter 4.5 - fold in JEG-3 cells with full induction requiring the previously defined cAMP - responsive elements ." ], "offsets": [ [ 0, 172 ] ] } ]
[ { "id": "split_0_train_45514_entity", "type": "progene_text", "text": [ "AP-2" ], "offsets": [ [ 25, 29 ] ], "normalized": [] }, { "id": "split_0_train_45515_entity", "type": "progene_text", "text": [ "CYP11A1" ], "offsets": [ [ 48, 55 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28083
split_0_train_28083
[ { "id": "split_0_train_28083_passage", "type": "progene_text", "text": [ "Point mutation of OF3 abolished induction by AP-2 , and OF3 was sufficient for induction by AP-2 when linked to a heterologous promoter ." ], "offsets": [ [ 0, 137 ] ] } ]
[ { "id": "split_0_train_45516_entity", "type": "progene_text", "text": [ "AP-2" ], "offsets": [ [ 45, 49 ] ], "normalized": [] }, { "id": "split_0_train_45517_entity", "type": "progene_text", "text": [ "AP-2" ], "offsets": [ [ 92, 96 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28084
split_0_train_28084
[ { "id": "split_0_train_28084_passage", "type": "progene_text", "text": [ "AP-2 induction of the CYP11A1 promoter required the basic region ( N165 - N278 ) and the carboxy terminus of AP-2 ( N413-N437 ) ." ], "offsets": [ [ 0, 129 ] ] } ]
[ { "id": "split_0_train_45518_entity", "type": "progene_text", "text": [ "AP-2" ], "offsets": [ [ 0, 4 ] ], "normalized": [] }, { "id": "split_0_train_45519_entity", "type": "progene_text", "text": [ "CYP11A1" ], "offsets": [ [ 22, 29 ] ], "normalized": [] }, { "id": "split_0_train_45520_entity", "type": "progene_text", "text": [ "AP-2" ], "offsets": [ [ 109, 113 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28085
split_0_train_28085
[ { "id": "split_0_train_28085_passage", "type": "progene_text", "text": [ "In the course of investigating the mechanisms by which OF5 and OF3 regulated CYP11A1 transcription , we found that OF5 and OF3 bound Sp1 and Sp3 in JEG-3 cells ." ], "offsets": [ [ 0, 161 ] ] } ]
[ { "id": "split_0_train_45521_entity", "type": "progene_text", "text": [ "CYP11A1" ], "offsets": [ [ 77, 84 ] ], "normalized": [] }, { "id": "split_0_train_45522_entity", "type": "progene_text", "text": [ "Sp1" ], "offsets": [ [ 133, 136 ] ], "normalized": [] }, { "id": "split_0_train_45523_entity", "type": "progene_text", "text": [ "Sp3" ], "offsets": [ [ 141, 144 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28086
split_0_train_28086
[ { "id": "split_0_train_28086_passage", "type": "progene_text", "text": [ "AP-2 did not bind OF5 or OF3 directly but rather formed a multiprotein complex with Sp1 in JEG-3 cells ." ], "offsets": [ [ 0, 104 ] ] } ]
[ { "id": "split_0_train_45524_entity", "type": "progene_text", "text": [ "AP-2" ], "offsets": [ [ 0, 4 ] ], "normalized": [] }, { "id": "split_0_train_45525_entity", "type": "progene_text", "text": [ "Sp1" ], "offsets": [ [ 84, 87 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28087
split_0_train_28087
[ { "id": "split_0_train_28087_passage", "type": "progene_text", "text": [ "AP-2 associated directly with Sp1 in vitro requiring the AP-2 basic region and the Sp1 carboxy terminus ." ], "offsets": [ [ 0, 105 ] ] } ]
[ { "id": "split_0_train_45526_entity", "type": "progene_text", "text": [ "AP-2" ], "offsets": [ [ 0, 4 ] ], "normalized": [] }, { "id": "split_0_train_45527_entity", "type": "progene_text", "text": [ "Sp1" ], "offsets": [ [ 30, 33 ] ], "normalized": [] }, { "id": "split_0_train_45528_entity", "type": "progene_text", "text": [ "AP-2" ], "offsets": [ [ 57, 61 ] ], "normalized": [] }, { "id": "split_0_train_45529_entity", "type": "progene_text", "text": [ "Sp1" ], "offsets": [ [ 83, 86 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28088
split_0_train_28088
[ { "id": "split_0_train_28088_passage", "type": "progene_text", "text": [ "AP-2 induced Sp1 / Sp3 activity independently of AP-2 binding to DNA using a GAL4 paradigm ." ], "offsets": [ [ 0, 92 ] ] } ]
[ { "id": "split_0_train_45530_entity", "type": "progene_text", "text": [ "AP-2" ], "offsets": [ [ 0, 4 ] ], "normalized": [] }, { "id": "split_0_train_45531_entity", "type": "progene_text", "text": [ "Sp1" ], "offsets": [ [ 13, 16 ] ], "normalized": [] }, { "id": "split_0_train_45532_entity", "type": "progene_text", "text": [ "Sp3" ], "offsets": [ [ 19, 22 ] ], "normalized": [] }, { "id": "split_0_train_45533_entity", "type": "progene_text", "text": [ "AP-2" ], "offsets": [ [ 49, 53 ] ], "normalized": [] }, { "id": "split_0_train_45534_entity", "type": "progene_text", "text": [ "GAL4" ], "offsets": [ [ 77, 81 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28089
split_0_train_28089
[ { "id": "split_0_train_28089_passage", "type": "progene_text", "text": [ "The Sp1 and Sp3 transactivation domains were linked to the DNA - binding domain of GAL4 , and their activity was assessed using a luciferase reporter gene containing only the GAL4 DNA - binding sites linked to the minimal TATA site ." ], "offsets": [ [ 0, 233 ] ] } ]
[ { "id": "split_0_train_45535_entity", "type": "progene_text", "text": [ "Sp1" ], "offsets": [ [ 4, 7 ] ], "normalized": [] }, { "id": "split_0_train_45536_entity", "type": "progene_text", "text": [ "Sp3" ], "offsets": [ [ 12, 15 ] ], "normalized": [] }, { "id": "split_0_train_45537_entity", "type": "progene_text", "text": [ "GAL4" ], "offsets": [ [ 83, 87 ] ], "normalized": [] }, { "id": "split_0_train_45538_entity", "type": "progene_text", "text": [ "luciferase" ], "offsets": [ [ 130, 140 ] ], "normalized": [] }, { "id": "split_0_train_45539_entity", "type": "progene_text", "text": [ "GAL4" ], "offsets": [ [ 175, 179 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28090
split_0_train_28090
[ { "id": "split_0_train_28090_passage", "type": "progene_text", "text": [ "AP-2 induced Sp1 / Sp3 - GAL4 activity 3 - to 4 - fold , requiring both the amino and extreme carboxy terminus of AP-2 ." ], "offsets": [ [ 0, 120 ] ] } ]
[ { "id": "split_0_train_45540_entity", "type": "progene_text", "text": [ "AP-2" ], "offsets": [ [ 0, 4 ] ], "normalized": [] }, { "id": "split_0_train_45541_entity", "type": "progene_text", "text": [ "Sp1" ], "offsets": [ [ 13, 16 ] ], "normalized": [] }, { "id": "split_0_train_45542_entity", "type": "progene_text", "text": [ "Sp3" ], "offsets": [ [ 19, 22 ] ], "normalized": [] }, { "id": "split_0_train_45543_entity", "type": "progene_text", "text": [ "GAL4" ], "offsets": [ [ 25, 29 ] ], "normalized": [] }, { "id": "split_0_train_45544_entity", "type": "progene_text", "text": [ "AP-2" ], "offsets": [ [ 114, 118 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28091
split_0_train_28091
[ { "id": "split_0_train_28091_passage", "type": "progene_text", "text": [ "We conclude that AP-2 can bind to and stimulate Sp1 activity and induces the ovine CYP11A1 promoter through conserved Sp1 / Sp3 - binding sites in JEG-3 cells ." ], "offsets": [ [ 0, 160 ] ] } ]
[ { "id": "split_0_train_45545_entity", "type": "progene_text", "text": [ "AP-2" ], "offsets": [ [ 17, 21 ] ], "normalized": [] }, { "id": "split_0_train_45546_entity", "type": "progene_text", "text": [ "Sp1" ], "offsets": [ [ 48, 51 ] ], "normalized": [] }, { "id": "split_0_train_45547_entity", "type": "progene_text", "text": [ "CYP11A1" ], "offsets": [ [ 83, 90 ] ], "normalized": [] }, { "id": "split_0_train_45548_entity", "type": "progene_text", "text": [ "Sp1" ], "offsets": [ [ 118, 121 ] ], "normalized": [] }, { "id": "split_0_train_45549_entity", "type": "progene_text", "text": [ "Sp3" ], "offsets": [ [ 124, 127 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28092
split_0_train_28092
[ { "id": "split_0_train_28092_passage", "type": "progene_text", "text": [ "The induction of Sp1 activity by AP-2 may contribute to the induction of other genes that bind Sp1 ." ], "offsets": [ [ 0, 100 ] ] } ]
[ { "id": "split_0_train_45550_entity", "type": "progene_text", "text": [ "Sp1" ], "offsets": [ [ 17, 20 ] ], "normalized": [] }, { "id": "split_0_train_45551_entity", "type": "progene_text", "text": [ "AP-2" ], "offsets": [ [ 33, 37 ] ], "normalized": [] }, { "id": "split_0_train_45552_entity", "type": "progene_text", "text": [ "Sp1" ], "offsets": [ [ 95, 98 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_28093
split_0_train_28093
[ { "id": "split_0_train_28093_passage", "type": "progene_text", "text": [ "Tobacco smoking and supragingival dental calculus ." ], "offsets": [ [ 0, 51 ] ] } ]
[]
[]
[]
[]
split_0_train_28094
split_0_train_28094
[ { "id": "split_0_train_28094_passage", "type": "progene_text", "text": [ "Supragingival calculus is frequent in all ages from adolescence to old age ." ], "offsets": [ [ 0, 76 ] ] } ]
[]
[]
[]
[]
split_0_train_28095
split_0_train_28095
[ { "id": "split_0_train_28095_passage", "type": "progene_text", "text": [ "The influence of tobacco smoking on the occurrence and severity of supragingival calculus has received surprisingly little attention ." ], "offsets": [ [ 0, 134 ] ] } ]
[]
[]
[]
[]
split_0_train_28096
split_0_train_28096
[ { "id": "split_0_train_28096_passage", "type": "progene_text", "text": [ "The present investigation conducted in a population of 258 dentally aware individuals in the age range 20 - 69 years , was initiated to elucidate the relationship between tobacco smoking and supragingival calculus , taking into account possible confounding factors such as age , gender , oral hygiene and gingival inflammation ." ], "offsets": [ [ 0, 328 ] ] } ]
[]
[]
[]
[]
split_0_train_28097
split_0_train_28097
[ { "id": "split_0_train_28097_passage", "type": "progene_text", "text": [ "The calculus deposition was bilaterally assessed on the lingual surfaces of the mandibular anteriors and the vestibular surfaces of the maxillary premolars and molars ." ], "offsets": [ [ 0, 168 ] ] } ]
[]
[]
[]
[]
split_0_train_28098
split_0_train_28098
[ { "id": "split_0_train_28098_passage", "type": "progene_text", "text": [ "The overall prevalence of supragingival calculus was 69 % ranging from 59 % in age group 20 - 34 years to 84 % in age group 50 - 69 years ." ], "offsets": [ [ 0, 139 ] ] } ]
[]
[]
[]
[]
split_0_train_28099
split_0_train_28099
[ { "id": "split_0_train_28099_passage", "type": "progene_text", "text": [ "The prevalence rates for current smokers , former smokers , and nonsmokers were 86 % , 66 % , and 65 % ." ], "offsets": [ [ 0, 104 ] ] } ]
[]
[]
[]
[]