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split_0_train_29800
split_0_train_29800
[ { "id": "split_0_train_29800_passage", "type": "progene_text", "text": [ "Since patients with MAD frequently have partial lipodystrophy and insulin resistance , we hypothesized that the disease may be caused by mutations in the LMNA gene ." ], "offsets": [ [ 0, 165 ] ] } ]
[ { "id": "split_0_train_47961_entity", "type": "progene_text", "text": [ "insulin" ], "offsets": [ [ 66, 73 ] ], "normalized": [] }, { "id": "split_0_train_47962_entity", "type": "progene_text", "text": [ "LMNA" ], "offsets": [ [ 154, 158 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29801
split_0_train_29801
[ { "id": "split_0_train_29801_passage", "type": "progene_text", "text": [ "We analyzed five consanguineous Italian families and demonstrated linkage of MAD to chromosome 1q21 , by use of homozygosity mapping ." ], "offsets": [ [ 0, 134 ] ] } ]
[]
[]
[]
[]
split_0_train_29802
split_0_train_29802
[ { "id": "split_0_train_29802_passage", "type": "progene_text", "text": [ "We then sequenced the LMNA gene and identified a homozygous missense mutation ( R527H ) that was shared by all affected patients ." ], "offsets": [ [ 0, 130 ] ] } ]
[ { "id": "split_0_train_47963_entity", "type": "progene_text", "text": [ "LMNA" ], "offsets": [ [ 22, 26 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29803
split_0_train_29803
[ { "id": "split_0_train_29803_passage", "type": "progene_text", "text": [ "Patient skin fibroblasts showed nuclei that presented abnormal lamin A / C distribution and a dysmorphic envelope , thus demonstrating the pathogenic effect of the R527H LMNA mutation ." ], "offsets": [ [ 0, 185 ] ] } ]
[ { "id": "split_0_train_47964_entity", "type": "progene_text", "text": [ "lamin A / C" ], "offsets": [ [ 63, 74 ] ], "normalized": [] }, { "id": "split_0_train_47965_entity", "type": "progene_text", "text": [ "LMNA" ], "offsets": [ [ 170, 174 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29804
split_0_train_29804
[ { "id": "split_0_train_29804_passage", "type": "progene_text", "text": [ "Interaction of p58 ( PITSLRE ) , a G2 / M - specific protein kinase , with cyclin D3 ." ], "offsets": [ [ 0, 86 ] ] } ]
[ { "id": "split_0_train_47966_entity", "type": "progene_text", "text": [ "p58 ( PITSLRE )" ], "offsets": [ [ 15, 30 ] ], "normalized": [] }, { "id": "split_0_train_47967_entity", "type": "progene_text", "text": [ "protein kinase" ], "offsets": [ [ 53, 67 ] ], "normalized": [] }, { "id": "split_0_train_47968_entity", "type": "progene_text", "text": [ "cyclin D3" ], "offsets": [ [ 75, 84 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29805
split_0_train_29805
[ { "id": "split_0_train_29805_passage", "type": "progene_text", "text": [ "The p58 ( PITSLRE ) is a p34 ( cdc2 ) - related protein kinase that plays an important role in normal cell cycle progression ." ], "offsets": [ [ 0, 126 ] ] } ]
[ { "id": "split_0_train_47969_entity", "type": "progene_text", "text": [ "p58 ( PITSLRE )" ], "offsets": [ [ 4, 19 ] ], "normalized": [] }, { "id": "split_0_train_47970_entity", "type": "progene_text", "text": [ "p34 ( cdc2 )" ], "offsets": [ [ 25, 37 ] ], "normalized": [] }, { "id": "split_0_train_47971_entity", "type": "progene_text", "text": [ "protein kinase" ], "offsets": [ [ 48, 62 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29806
split_0_train_29806
[ { "id": "split_0_train_29806_passage", "type": "progene_text", "text": [ "Elevated expression of p58 ( PITSLRE ) in eukaryotic cells prevents them from undergoing normal cytokinesis and appears to delay them in late telophase ." ], "offsets": [ [ 0, 153 ] ] } ]
[ { "id": "split_0_train_47972_entity", "type": "progene_text", "text": [ "p58 ( PITSLRE )" ], "offsets": [ [ 23, 38 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29807
split_0_train_29807
[ { "id": "split_0_train_29807_passage", "type": "progene_text", "text": [ "To investigate the molecular mechanism of p58 ( PITSLRE ) action , we used the yeast two - hybrid system , screened a human fetal liver cDNA library , and identified cyclin D3 as an interacting partner of p58 ( PITSLRE ) ." ], "offsets": [ [ 0, 222 ] ] } ]
[ { "id": "split_0_train_47973_entity", "type": "progene_text", "text": [ "p58 ( PITSLRE )" ], "offsets": [ [ 42, 57 ] ], "normalized": [] }, { "id": "split_0_train_47974_entity", "type": "progene_text", "text": [ "cyclin D3" ], "offsets": [ [ 166, 175 ] ], "normalized": [] }, { "id": "split_0_train_47975_entity", "type": "progene_text", "text": [ "p58 ( PITSLRE )" ], "offsets": [ [ 205, 220 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29808
split_0_train_29808
[ { "id": "split_0_train_29808_passage", "type": "progene_text", "text": [ "In vitro binding assay , in vivo coimmunoprecipitation , and immunofluorescence cell staining further confirmed the association of p58 ( PITSLRE ) with cyclin D3 ." ], "offsets": [ [ 0, 163 ] ] } ]
[ { "id": "split_0_train_47976_entity", "type": "progene_text", "text": [ "p58 ( PITSLRE )" ], "offsets": [ [ 131, 146 ] ], "normalized": [] }, { "id": "split_0_train_47977_entity", "type": "progene_text", "text": [ "cyclin D3" ], "offsets": [ [ 152, 161 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29809
split_0_train_29809
[ { "id": "split_0_train_29809_passage", "type": "progene_text", "text": [ "This binding was observed only in the G(2) / M phase but not in the G(1) / S phase of the cell cycle ; meanwhile , no interaction between p110 ( PITSLRE ) and cyclin D3 was observed in all the cell cycle ." ], "offsets": [ [ 0, 205 ] ] } ]
[ { "id": "split_0_train_47978_entity", "type": "progene_text", "text": [ "PITSLRE" ], "offsets": [ [ 145, 152 ] ], "normalized": [] }, { "id": "split_0_train_47979_entity", "type": "progene_text", "text": [ "cyclin D3" ], "offsets": [ [ 159, 168 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29810
split_0_train_29810
[ { "id": "split_0_train_29810_passage", "type": "progene_text", "text": [ "The overexpression of cyclin D3 in 7721 cells leads to an exclusively accumulation of p58 ( PITSLRE ) in the nuclear region , affecting its cellular distribution ." ], "offsets": [ [ 0, 163 ] ] } ]
[ { "id": "split_0_train_47980_entity", "type": "progene_text", "text": [ "cyclin D3" ], "offsets": [ [ 22, 31 ] ], "normalized": [] }, { "id": "split_0_train_47981_entity", "type": "progene_text", "text": [ "p58 ( PITSLRE )" ], "offsets": [ [ 86, 101 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29811
split_0_train_29811
[ { "id": "split_0_train_29811_passage", "type": "progene_text", "text": [ "Histone H1 kinase activity of p58 ( PITSLRE ) was greatly enhanced upon interaction with cyclin D3 ." ], "offsets": [ [ 0, 100 ] ] } ]
[ { "id": "split_0_train_47982_entity", "type": "progene_text", "text": [ "kinase" ], "offsets": [ [ 11, 17 ] ], "normalized": [] }, { "id": "split_0_train_47983_entity", "type": "progene_text", "text": [ "p58 ( PITSLRE )" ], "offsets": [ [ 30, 45 ] ], "normalized": [] }, { "id": "split_0_train_47984_entity", "type": "progene_text", "text": [ "cyclin D3" ], "offsets": [ [ 89, 98 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29812
split_0_train_29812
[ { "id": "split_0_train_29812_passage", "type": "progene_text", "text": [ "Furthermore , kinase activity of p58 ( PITSLRE ) was found to increase greatly in the presence of cyclin D3 using a specific substrate , beta-1,4-galactosyltransferase 1 ." ], "offsets": [ [ 0, 171 ] ] } ]
[ { "id": "split_0_train_47985_entity", "type": "progene_text", "text": [ "kinase" ], "offsets": [ [ 14, 20 ] ], "normalized": [] }, { "id": "split_0_train_47986_entity", "type": "progene_text", "text": [ "p58 ( PITSLRE )" ], "offsets": [ [ 33, 48 ] ], "normalized": [] }, { "id": "split_0_train_47987_entity", "type": "progene_text", "text": [ "cyclin D3" ], "offsets": [ [ 98, 107 ] ], "normalized": [] }, { "id": "split_0_train_47988_entity", "type": "progene_text", "text": [ "beta-1,4-galactosyltransferase 1" ], "offsets": [ [ 137, 169 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29813
split_0_train_29813
[ { "id": "split_0_train_29813_passage", "type": "progene_text", "text": [ "These data provide a new clue to our understanding of the cellular function of p58 ( PITSLRE ) and cyclin D3 ." ], "offsets": [ [ 0, 110 ] ] } ]
[ { "id": "split_0_train_47989_entity", "type": "progene_text", "text": [ "p58 ( PITSLRE )" ], "offsets": [ [ 79, 94 ] ], "normalized": [] }, { "id": "split_0_train_47990_entity", "type": "progene_text", "text": [ "cyclin D3" ], "offsets": [ [ 99, 108 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29814
split_0_train_29814
[ { "id": "split_0_train_29814_passage", "type": "progene_text", "text": [ "Expression of the leucocyte common antigen - related ( LAR ) tyrosine phosphatase is regulated by cell density through functional E-cadherin complexes ." ], "offsets": [ [ 0, 152 ] ] } ]
[ { "id": "split_0_train_47991_entity", "type": "progene_text", "text": [ "leucocyte common antigen - related ( LAR ) tyrosine phosphatase" ], "offsets": [ [ 18, 81 ] ], "normalized": [] }, { "id": "split_0_train_47992_entity", "type": "progene_text", "text": [ "E-cadherin" ], "offsets": [ [ 130, 140 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29815
split_0_train_29815
[ { "id": "split_0_train_29815_passage", "type": "progene_text", "text": [ "The leucocyte common antigen - related phosphatase ( LAR ) has been implicated in receptor tyrosine kinase signalling pathways while also displaying cell - density - dependency and localization to adherens junctions ." ], "offsets": [ [ 0, 217 ] ] } ]
[ { "id": "split_0_train_47993_entity", "type": "progene_text", "text": [ "leucocyte common antigen - related phosphatase" ], "offsets": [ [ 4, 50 ] ], "normalized": [] }, { "id": "split_0_train_47994_entity", "type": "progene_text", "text": [ "LAR" ], "offsets": [ [ 53, 56 ] ], "normalized": [] }, { "id": "split_0_train_47995_entity", "type": "progene_text", "text": [ "receptor tyrosine kinase" ], "offsets": [ [ 82, 106 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29816
split_0_train_29816
[ { "id": "split_0_train_29816_passage", "type": "progene_text", "text": [ "Whereas physiological substrates for LAR have not been identified unequivocally , beta-catenin associates with LAR and is a substrate in vitro ." ], "offsets": [ [ 0, 144 ] ] } ]
[ { "id": "split_0_train_47996_entity", "type": "progene_text", "text": [ "LAR" ], "offsets": [ [ 37, 40 ] ], "normalized": [] }, { "id": "split_0_train_47997_entity", "type": "progene_text", "text": [ "beta-catenin" ], "offsets": [ [ 82, 94 ] ], "normalized": [] }, { "id": "split_0_train_47998_entity", "type": "progene_text", "text": [ "LAR" ], "offsets": [ [ 111, 114 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29817
split_0_train_29817
[ { "id": "split_0_train_29817_passage", "type": "progene_text", "text": [ "With the implication that LAR may play a role in regulating E-cadherin - dependent cell - cell communication and contact inhibition , the relationship of LAR with E-cadherin was investigated ." ], "offsets": [ [ 0, 192 ] ] } ]
[ { "id": "split_0_train_47999_entity", "type": "progene_text", "text": [ "LAR" ], "offsets": [ [ 26, 29 ] ], "normalized": [] }, { "id": "split_0_train_48000_entity", "type": "progene_text", "text": [ "E-cadherin" ], "offsets": [ [ 60, 70 ] ], "normalized": [] }, { "id": "split_0_train_48001_entity", "type": "progene_text", "text": [ "LAR" ], "offsets": [ [ 154, 157 ] ], "normalized": [] }, { "id": "split_0_train_48002_entity", "type": "progene_text", "text": [ "E-cadherin" ], "offsets": [ [ 163, 173 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29818
split_0_train_29818
[ { "id": "split_0_train_29818_passage", "type": "progene_text", "text": [ "LAR expression increased with cell density in the human breast cancer cell line MCF-7 and in Ln 3 cells derived from the 13762NF rat mammary adenocarcinoma ." ], "offsets": [ [ 0, 157 ] ] } ]
[ { "id": "split_0_train_48003_entity", "type": "progene_text", "text": [ "LAR" ], "offsets": [ [ 0, 3 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29819
split_0_train_29819
[ { "id": "split_0_train_29819_passage", "type": "progene_text", "text": [ "LAR protein levels decreased rapidly when cells were replated at a low density after attaining high expression of LAR at high cell density ." ], "offsets": [ [ 0, 140 ] ] } ]
[ { "id": "split_0_train_48004_entity", "type": "progene_text", "text": [ "LAR" ], "offsets": [ [ 0, 3 ] ], "normalized": [] }, { "id": "split_0_train_48005_entity", "type": "progene_text", "text": [ "LAR" ], "offsets": [ [ 114, 117 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29820
split_0_train_29820
[ { "id": "split_0_train_29820_passage", "type": "progene_text", "text": [ "COS-7 cells displayed comparable density - dependent regulation of LAR expression when transiently expressing exogenous LAR under the control of a constitutively active promoter , indicating that the regulation of expression is not at the level of gene regulation ." ], "offsets": [ [ 0, 265 ] ] } ]
[ { "id": "split_0_train_48006_entity", "type": "progene_text", "text": [ "LAR" ], "offsets": [ [ 67, 70 ] ], "normalized": [] }, { "id": "split_0_train_48007_entity", "type": "progene_text", "text": [ "LAR" ], "offsets": [ [ 120, 123 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29821
split_0_train_29821
[ { "id": "split_0_train_29821_passage", "type": "progene_text", "text": [ "Disrupting homophilic E-cadherin complexes by chelating extracellular calcium caused a marked decrease in LAR protein levels ." ], "offsets": [ [ 0, 126 ] ] } ]
[ { "id": "split_0_train_48008_entity", "type": "progene_text", "text": [ "E-cadherin" ], "offsets": [ [ 22, 32 ] ], "normalized": [] }, { "id": "split_0_train_48009_entity", "type": "progene_text", "text": [ "LAR" ], "offsets": [ [ 106, 109 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29822
split_0_train_29822
[ { "id": "split_0_train_29822_passage", "type": "progene_text", "text": [ "Similarly , blocking E-cadherin interactions with saturating amounts of E-cadherin antibody ( HECD-1 ) also led to a rapid and pronounced loss of cellular LAR ." ], "offsets": [ [ 0, 160 ] ] } ]
[ { "id": "split_0_train_48010_entity", "type": "progene_text", "text": [ "E-cadherin" ], "offsets": [ [ 21, 31 ] ], "normalized": [] }, { "id": "split_0_train_48011_entity", "type": "progene_text", "text": [ "E-cadherin" ], "offsets": [ [ 72, 82 ] ], "normalized": [] }, { "id": "split_0_train_48012_entity", "type": "progene_text", "text": [ "LAR" ], "offsets": [ [ 155, 158 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29823
split_0_train_29823
[ { "id": "split_0_train_29823_passage", "type": "progene_text", "text": [ "In contrast , mimicking cell - surface E-cadherin engagement by plating cells at low density on to dishes coated with HECD-1 resulted in a 2 - fold increase in LAR expression compared with controls ." ], "offsets": [ [ 0, 199 ] ] } ]
[ { "id": "split_0_train_48013_entity", "type": "progene_text", "text": [ "E-cadherin" ], "offsets": [ [ 39, 49 ] ], "normalized": [] }, { "id": "split_0_train_48014_entity", "type": "progene_text", "text": [ "LAR" ], "offsets": [ [ 160, 163 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29824
split_0_train_29824
[ { "id": "split_0_train_29824_passage", "type": "progene_text", "text": [ "These results suggest that density - dependent regulation of LAR expression is mediated by functional E-cadherin and may play a role in density - dependent contact inhibition by regulating tyrosine phosphorylation in E-cadherin complexes ." ], "offsets": [ [ 0, 239 ] ] } ]
[ { "id": "split_0_train_48015_entity", "type": "progene_text", "text": [ "LAR" ], "offsets": [ [ 61, 64 ] ], "normalized": [] }, { "id": "split_0_train_48016_entity", "type": "progene_text", "text": [ "E-cadherin" ], "offsets": [ [ 102, 112 ] ], "normalized": [] }, { "id": "split_0_train_48017_entity", "type": "progene_text", "text": [ "E-cadherin" ], "offsets": [ [ 217, 227 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29825
split_0_train_29825
[ { "id": "split_0_train_29825_passage", "type": "progene_text", "text": [ "The transcriptional regulating protein of 132 kDa ( TReP-132 ) enhances P450scc gene transcription through interaction with steroidogenic factor-1 in human adrenal cells ." ], "offsets": [ [ 0, 171 ] ] } ]
[ { "id": "split_0_train_48018_entity", "type": "progene_text", "text": [ "transcriptional regulating protein of 132 kDa" ], "offsets": [ [ 4, 49 ] ], "normalized": [] }, { "id": "split_0_train_48019_entity", "type": "progene_text", "text": [ "TReP-132" ], "offsets": [ [ 52, 60 ] ], "normalized": [] }, { "id": "split_0_train_48020_entity", "type": "progene_text", "text": [ "P450scc" ], "offsets": [ [ 72, 79 ] ], "normalized": [] }, { "id": "split_0_train_48021_entity", "type": "progene_text", "text": [ "steroidogenic factor-1" ], "offsets": [ [ 124, 146 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29826
split_0_train_29826
[ { "id": "split_0_train_29826_passage", "type": "progene_text", "text": [ "The human P450scc gene is regulated by the tissue - specific orphan nuclear receptor , steroidogenic factor-1 ( SF-1 ) , which plays a key role in several physiologic processes including steroid synthesis , adrenal and gonadal development , and sexual differentiation ." ], "offsets": [ [ 0, 269 ] ] } ]
[ { "id": "split_0_train_48022_entity", "type": "progene_text", "text": [ "P450scc" ], "offsets": [ [ 10, 17 ] ], "normalized": [] }, { "id": "split_0_train_48023_entity", "type": "progene_text", "text": [ "steroidogenic factor-1" ], "offsets": [ [ 87, 109 ] ], "normalized": [] }, { "id": "split_0_train_48024_entity", "type": "progene_text", "text": [ "SF-1" ], "offsets": [ [ 112, 116 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29827
split_0_train_29827
[ { "id": "split_0_train_29827_passage", "type": "progene_text", "text": [ "Several studies have demonstrated the interaction of SF-1 with different proteins ." ], "offsets": [ [ 0, 83 ] ] } ]
[ { "id": "split_0_train_48025_entity", "type": "progene_text", "text": [ "SF-1" ], "offsets": [ [ 53, 57 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29828
split_0_train_29828
[ { "id": "split_0_train_29828_passage", "type": "progene_text", "text": [ "However , it is clear that additional factors not yet identified are involved with SF-1 to regulate different target genes ." ], "offsets": [ [ 0, 124 ] ] } ]
[ { "id": "split_0_train_48026_entity", "type": "progene_text", "text": [ "SF-1" ], "offsets": [ [ 83, 87 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29829
split_0_train_29829
[ { "id": "split_0_train_29829_passage", "type": "progene_text", "text": [ "Recently , it was demonstrated that a novel transcriptional regulating protein of 132 kDa ( TReP-132 ) regulates expression of the human P450scc gene ." ], "offsets": [ [ 0, 151 ] ] } ]
[ { "id": "split_0_train_48027_entity", "type": "progene_text", "text": [ "transcriptional regulating protein of 132 kDa" ], "offsets": [ [ 44, 89 ] ], "normalized": [] }, { "id": "split_0_train_48028_entity", "type": "progene_text", "text": [ "TReP-132" ], "offsets": [ [ 92, 100 ] ], "normalized": [] }, { "id": "split_0_train_48029_entity", "type": "progene_text", "text": [ "P450scc" ], "offsets": [ [ 137, 144 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29830
split_0_train_29830
[ { "id": "split_0_train_29830_passage", "type": "progene_text", "text": [ "The overexpression of TReP-132 in adrenal cells increases the production of pregnenolone , which is associated with the activation of P450scc gene expression ." ], "offsets": [ [ 0, 159 ] ] } ]
[ { "id": "split_0_train_48030_entity", "type": "progene_text", "text": [ "TReP-132" ], "offsets": [ [ 22, 30 ] ], "normalized": [] }, { "id": "split_0_train_48031_entity", "type": "progene_text", "text": [ "P450scc" ], "offsets": [ [ 134, 141 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29831
split_0_train_29831
[ { "id": "split_0_train_29831_passage", "type": "progene_text", "text": [ "Considering the colocalization of TReP-132 and SF-1 in steroidogenic tissues such as the adrenal and testis , and the presence of two putative LXXLL motifs in TReP-132 that can potentially interact with SF-1 , the relationship between these two factors on the P450scc gene promoter was determined ." ], "offsets": [ [ 0, 298 ] ] } ]
[ { "id": "split_0_train_48032_entity", "type": "progene_text", "text": [ "TReP-132" ], "offsets": [ [ 34, 42 ] ], "normalized": [] }, { "id": "split_0_train_48033_entity", "type": "progene_text", "text": [ "SF-1" ], "offsets": [ [ 47, 51 ] ], "normalized": [] }, { "id": "split_0_train_48034_entity", "type": "progene_text", "text": [ "TReP-132" ], "offsets": [ [ 159, 167 ] ], "normalized": [] }, { "id": "split_0_train_48035_entity", "type": "progene_text", "text": [ "SF-1" ], "offsets": [ [ 203, 207 ] ], "normalized": [] }, { "id": "split_0_train_48036_entity", "type": "progene_text", "text": [ "P450scc" ], "offsets": [ [ 260, 267 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29832
split_0_train_29832
[ { "id": "split_0_train_29832_passage", "type": "progene_text", "text": [ "The coexpression of SF-1 and TReP-132 in adrenal NCI-H295 cells cooperates to increase promoter activity ." ], "offsets": [ [ 0, 106 ] ] } ]
[ { "id": "split_0_train_48037_entity", "type": "progene_text", "text": [ "SF-1" ], "offsets": [ [ 20, 24 ] ], "normalized": [] }, { "id": "split_0_train_48038_entity", "type": "progene_text", "text": [ "TReP-132" ], "offsets": [ [ 29, 37 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29833
split_0_train_29833
[ { "id": "split_0_train_29833_passage", "type": "progene_text", "text": [ "Pull - down experiments demonstrated the interaction between TReP-132 and SF-1 , and this was further confirmed in intact cells by coimmunoprecipitation / Western blot and two - hybrid analyses ." ], "offsets": [ [ 0, 195 ] ] } ]
[ { "id": "split_0_train_48039_entity", "type": "progene_text", "text": [ "TReP-132" ], "offsets": [ [ 61, 69 ] ], "normalized": [] }, { "id": "split_0_train_48040_entity", "type": "progene_text", "text": [ "SF-1" ], "offsets": [ [ 74, 78 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29834
split_0_train_29834
[ { "id": "split_0_train_29834_passage", "type": "progene_text", "text": [ "Deletions and mutations of the TReP-132 cDNA sequence demonstrate that SF-1 interaction requires the LXXLL motif found at the amino - terminal region of the protein ." ], "offsets": [ [ 0, 166 ] ] } ]
[ { "id": "split_0_train_48041_entity", "type": "progene_text", "text": [ "TReP-132" ], "offsets": [ [ 31, 39 ] ], "normalized": [] }, { "id": "split_0_train_48042_entity", "type": "progene_text", "text": [ "SF-1" ], "offsets": [ [ 71, 75 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29835
split_0_train_29835
[ { "id": "split_0_train_29835_passage", "type": "progene_text", "text": [ "Also , the \" proximal activation domain \" and the \" AF-2 hexamer \" motif of SF-1 are involved in interaction with TReP-132 ." ], "offsets": [ [ 0, 124 ] ] } ]
[ { "id": "split_0_train_48043_entity", "type": "progene_text", "text": [ "SF-1" ], "offsets": [ [ 76, 80 ] ], "normalized": [] }, { "id": "split_0_train_48044_entity", "type": "progene_text", "text": [ "TReP-132" ], "offsets": [ [ 114, 122 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29836
split_0_train_29836
[ { "id": "split_0_train_29836_passage", "type": "progene_text", "text": [ "Consistent with previous studies showing interaction between CBP / p300 and SF-1 or TReP-132 , the coexpression of these three proteins results in a synergistic effect on P450scc gene promoter activity ." ], "offsets": [ [ 0, 203 ] ] } ]
[ { "id": "split_0_train_48045_entity", "type": "progene_text", "text": [ "CBP" ], "offsets": [ [ 61, 64 ] ], "normalized": [] }, { "id": "split_0_train_48046_entity", "type": "progene_text", "text": [ "p300" ], "offsets": [ [ 67, 71 ] ], "normalized": [] }, { "id": "split_0_train_48047_entity", "type": "progene_text", "text": [ "SF-1" ], "offsets": [ [ 76, 80 ] ], "normalized": [] }, { "id": "split_0_train_48048_entity", "type": "progene_text", "text": [ "TReP-132" ], "offsets": [ [ 84, 92 ] ], "normalized": [] }, { "id": "split_0_train_48049_entity", "type": "progene_text", "text": [ "P450scc" ], "offsets": [ [ 171, 178 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29837
split_0_train_29837
[ { "id": "split_0_train_29837_passage", "type": "progene_text", "text": [ "Taken together the results in this study identify a novel function of TReP-132 as a partner in a complex with SF-1 and CBP / p300 to regulate gene transcription involved in steroidogenesis ." ], "offsets": [ [ 0, 190 ] ] } ]
[ { "id": "split_0_train_48050_entity", "type": "progene_text", "text": [ "TReP-132" ], "offsets": [ [ 70, 78 ] ], "normalized": [] }, { "id": "split_0_train_48051_entity", "type": "progene_text", "text": [ "SF-1" ], "offsets": [ [ 110, 114 ] ], "normalized": [] }, { "id": "split_0_train_48052_entity", "type": "progene_text", "text": [ "CBP" ], "offsets": [ [ 119, 122 ] ], "normalized": [] }, { "id": "split_0_train_48053_entity", "type": "progene_text", "text": [ "p300" ], "offsets": [ [ 125, 129 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29838
split_0_train_29838
[ { "id": "split_0_train_29838_passage", "type": "progene_text", "text": [ "HIV-1 Tat interaction with RNA polymerase II C - terminal domain ( CTD ) and a dynamic association with CDK2 induce CTD phosphorylation and transcription from HIV-1 promoter ." ], "offsets": [ [ 0, 175 ] ] } ]
[ { "id": "split_0_train_48054_entity", "type": "progene_text", "text": [ "Tat" ], "offsets": [ [ 6, 9 ] ], "normalized": [] }, { "id": "split_0_train_48055_entity", "type": "progene_text", "text": [ "RNA polymerase II" ], "offsets": [ [ 27, 44 ] ], "normalized": [] }, { "id": "split_0_train_48056_entity", "type": "progene_text", "text": [ "CDK2" ], "offsets": [ [ 104, 108 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29839
split_0_train_29839
[ { "id": "split_0_train_29839_passage", "type": "progene_text", "text": [ "Human immunodeficiency virus , type 1 ( HIV-1 ) , Tat protein activates viral gene expression through promoting transcriptional elongation by RNA polymerase II ( RNAPII ) ." ], "offsets": [ [ 0, 172 ] ] } ]
[ { "id": "split_0_train_48057_entity", "type": "progene_text", "text": [ "Tat" ], "offsets": [ [ 50, 53 ] ], "normalized": [] }, { "id": "split_0_train_48058_entity", "type": "progene_text", "text": [ "RNA polymerase II" ], "offsets": [ [ 142, 159 ] ], "normalized": [] }, { "id": "split_0_train_48059_entity", "type": "progene_text", "text": [ "RNAPII" ], "offsets": [ [ 162, 168 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29840
split_0_train_29840
[ { "id": "split_0_train_29840_passage", "type": "progene_text", "text": [ "In this process Tat enhances phosphorylation of the C - terminal domain ( CTD ) of RNAPII by activating cell cycle - dependent kinases ( CDKs ) associated with general transcription factors of the promoter complex , specifically CDK7 and CDK9 ." ], "offsets": [ [ 0, 244 ] ] } ]
[ { "id": "split_0_train_48060_entity", "type": "progene_text", "text": [ "Tat" ], "offsets": [ [ 16, 19 ] ], "normalized": [] }, { "id": "split_0_train_48061_entity", "type": "progene_text", "text": [ "RNAPII" ], "offsets": [ [ 83, 89 ] ], "normalized": [] }, { "id": "split_0_train_48062_entity", "type": "progene_text", "text": [ "cell cycle - dependent kinases" ], "offsets": [ [ 104, 134 ] ], "normalized": [] }, { "id": "split_0_train_48063_entity", "type": "progene_text", "text": [ "CDKs" ], "offsets": [ [ 137, 141 ] ], "normalized": [] }, { "id": "split_0_train_48064_entity", "type": "progene_text", "text": [ "transcription factors" ], "offsets": [ [ 168, 189 ] ], "normalized": [] }, { "id": "split_0_train_48065_entity", "type": "progene_text", "text": [ "CDK7" ], "offsets": [ [ 229, 233 ] ], "normalized": [] }, { "id": "split_0_train_48066_entity", "type": "progene_text", "text": [ "CDK9" ], "offsets": [ [ 238, 242 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29841
split_0_train_29841
[ { "id": "split_0_train_29841_passage", "type": "progene_text", "text": [ "We reported a Tat - associated T-cell - derived kinase , which contained CDK2 ." ], "offsets": [ [ 0, 79 ] ] } ]
[ { "id": "split_0_train_48067_entity", "type": "progene_text", "text": [ "Tat" ], "offsets": [ [ 14, 17 ] ], "normalized": [] }, { "id": "split_0_train_48068_entity", "type": "progene_text", "text": [ "kinase" ], "offsets": [ [ 48, 54 ] ], "normalized": [] }, { "id": "split_0_train_48069_entity", "type": "progene_text", "text": [ "CDK2" ], "offsets": [ [ 73, 77 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29842
split_0_train_29842
[ { "id": "split_0_train_29842_passage", "type": "progene_text", "text": [ "Here , we provide further evidence that CDK2 is involved in Tat - mediated CTD phosphorylation and in HIV-1 transcription in vitro ." ], "offsets": [ [ 0, 132 ] ] } ]
[ { "id": "split_0_train_48070_entity", "type": "progene_text", "text": [ "CDK2" ], "offsets": [ [ 40, 44 ] ], "normalized": [] }, { "id": "split_0_train_48071_entity", "type": "progene_text", "text": [ "Tat" ], "offsets": [ [ 60, 63 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29843
split_0_train_29843
[ { "id": "split_0_train_29843_passage", "type": "progene_text", "text": [ "Tat - mediated CTD phosphorylation by CDK2 required cysteine 22 in the activation domain of Tat and amino acids 42 - 72 of Tat ." ], "offsets": [ [ 0, 128 ] ] } ]
[ { "id": "split_0_train_48072_entity", "type": "progene_text", "text": [ "Tat" ], "offsets": [ [ 0, 3 ] ], "normalized": [] }, { "id": "split_0_train_48073_entity", "type": "progene_text", "text": [ "CDK2" ], "offsets": [ [ 38, 42 ] ], "normalized": [] }, { "id": "split_0_train_48074_entity", "type": "progene_text", "text": [ "Tat" ], "offsets": [ [ 92, 95 ] ], "normalized": [] }, { "id": "split_0_train_48075_entity", "type": "progene_text", "text": [ "Tat" ], "offsets": [ [ 123, 126 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29844
split_0_train_29844
[ { "id": "split_0_train_29844_passage", "type": "progene_text", "text": [ "CDK2 phosphorylated Tat itself , apparently by forming dynamic contacts with amino acids 15 - 24 and 36 - 49 of Tat ." ], "offsets": [ [ 0, 117 ] ] } ]
[ { "id": "split_0_train_48076_entity", "type": "progene_text", "text": [ "CDK2" ], "offsets": [ [ 0, 4 ] ], "normalized": [] }, { "id": "split_0_train_48077_entity", "type": "progene_text", "text": [ "Tat" ], "offsets": [ [ 20, 23 ] ], "normalized": [] }, { "id": "split_0_train_48078_entity", "type": "progene_text", "text": [ "Tat" ], "offsets": [ [ 112, 115 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29845
split_0_train_29845
[ { "id": "split_0_train_29845_passage", "type": "progene_text", "text": [ "Also , amino acids 24 - 36 and 45 - 72 of Tat interacted with CTD ." ], "offsets": [ [ 0, 67 ] ] } ]
[ { "id": "split_0_train_48079_entity", "type": "progene_text", "text": [ "Tat" ], "offsets": [ [ 42, 45 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29846
split_0_train_29846
[ { "id": "split_0_train_29846_passage", "type": "progene_text", "text": [ "CDK2 associated with RNAPII and was found in elongation complexes assembled on HIV-1 long - terminal repeat template ." ], "offsets": [ [ 0, 118 ] ] } ]
[ { "id": "split_0_train_48080_entity", "type": "progene_text", "text": [ "CDK2" ], "offsets": [ [ 0, 4 ] ], "normalized": [] }, { "id": "split_0_train_48081_entity", "type": "progene_text", "text": [ "RNAPII" ], "offsets": [ [ 21, 27 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29847
split_0_train_29847
[ { "id": "split_0_train_29847_passage", "type": "progene_text", "text": [ "Recombinant CDK2 / cyclin E stimulated Tat - dependent HIV-1 transcription in reconstituted transcription assay ." ], "offsets": [ [ 0, 113 ] ] } ]
[ { "id": "split_0_train_48082_entity", "type": "progene_text", "text": [ "CDK2" ], "offsets": [ [ 12, 16 ] ], "normalized": [] }, { "id": "split_0_train_48083_entity", "type": "progene_text", "text": [ "cyclin E" ], "offsets": [ [ 19, 27 ] ], "normalized": [] }, { "id": "split_0_train_48084_entity", "type": "progene_text", "text": [ "Tat" ], "offsets": [ [ 39, 42 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29848
split_0_train_29848
[ { "id": "split_0_train_29848_passage", "type": "progene_text", "text": [ "Immunodepletion of CDK2 / cyclin E in HeLa nuclear extract blocked Tat - dependent transcription ." ], "offsets": [ [ 0, 98 ] ] } ]
[ { "id": "split_0_train_48085_entity", "type": "progene_text", "text": [ "CDK2" ], "offsets": [ [ 19, 23 ] ], "normalized": [] }, { "id": "split_0_train_48086_entity", "type": "progene_text", "text": [ "cyclin E" ], "offsets": [ [ 26, 34 ] ], "normalized": [] }, { "id": "split_0_train_48087_entity", "type": "progene_text", "text": [ "Tat" ], "offsets": [ [ 67, 70 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29849
split_0_train_29849
[ { "id": "split_0_train_29849_passage", "type": "progene_text", "text": [ "We suggest that CDK2 is part of a transcription complex that is required for Tat - dependent transcription and that interaction of Tat with CTD and a dynamic association of Tat with CDK2 / cyclin E stimulated CTD phosphorylation by CDK2 ." ], "offsets": [ [ 0, 238 ] ] } ]
[ { "id": "split_0_train_48088_entity", "type": "progene_text", "text": [ "CDK2" ], "offsets": [ [ 16, 20 ] ], "normalized": [] }, { "id": "split_0_train_48089_entity", "type": "progene_text", "text": [ "Tat" ], "offsets": [ [ 77, 80 ] ], "normalized": [] }, { "id": "split_0_train_48090_entity", "type": "progene_text", "text": [ "Tat" ], "offsets": [ [ 131, 134 ] ], "normalized": [] }, { "id": "split_0_train_48091_entity", "type": "progene_text", "text": [ "Tat" ], "offsets": [ [ 173, 176 ] ], "normalized": [] }, { "id": "split_0_train_48092_entity", "type": "progene_text", "text": [ "CDK2" ], "offsets": [ [ 182, 186 ] ], "normalized": [] }, { "id": "split_0_train_48093_entity", "type": "progene_text", "text": [ "cyclin E" ], "offsets": [ [ 189, 197 ] ], "normalized": [] }, { "id": "split_0_train_48094_entity", "type": "progene_text", "text": [ "CDK2" ], "offsets": [ [ 232, 236 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29850
split_0_train_29850
[ { "id": "split_0_train_29850_passage", "type": "progene_text", "text": [ "A bimolecular mechanism of HIV-1 Tat protein interaction with RNA polymerase II transcription elongation complexes ." ], "offsets": [ [ 0, 116 ] ] } ]
[ { "id": "split_0_train_48095_entity", "type": "progene_text", "text": [ "Tat" ], "offsets": [ [ 33, 36 ] ], "normalized": [] }, { "id": "split_0_train_48096_entity", "type": "progene_text", "text": [ "RNA polymerase II" ], "offsets": [ [ 62, 79 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29851
split_0_train_29851
[ { "id": "split_0_train_29851_passage", "type": "progene_text", "text": [ "Transcriptional activation of the human immunodeficiency virus type 1 ( HIV-1 ) long terminal repeat ( LTR ) promoter element is regulated by the essential viral Tat protein that binds to the viral TAR RNA target and recruits a positive transcription elongation complex ( P - TEFb ) ." ], "offsets": [ [ 0, 284 ] ] } ]
[ { "id": "split_0_train_48097_entity", "type": "progene_text", "text": [ "Tat" ], "offsets": [ [ 162, 165 ] ], "normalized": [] }, { "id": "split_0_train_48098_entity", "type": "progene_text", "text": [ "positive transcription elongation complex" ], "offsets": [ [ 228, 269 ] ], "normalized": [] }, { "id": "split_0_train_48099_entity", "type": "progene_text", "text": [ "P - TEFb" ], "offsets": [ [ 272, 280 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29852
split_0_train_29852
[ { "id": "split_0_train_29852_passage", "type": "progene_text", "text": [ "We have used a stepwise transcription approach and a highly sensitive assay to determine the dynamics of interactions between HIV-1 Tat and the transcription complexes actively engaged in elongation ." ], "offsets": [ [ 0, 200 ] ] } ]
[ { "id": "split_0_train_48100_entity", "type": "progene_text", "text": [ "Tat" ], "offsets": [ [ 132, 135 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29853
split_0_train_29853
[ { "id": "split_0_train_29853_passage", "type": "progene_text", "text": [ "Our results demonstrate that Tat protein associates with RNA polymerase II complexes during early transcription elongation after the promoter clearance and before the synthesis of full - length TAR RNA transcript ." ], "offsets": [ [ 0, 214 ] ] } ]
[ { "id": "split_0_train_48101_entity", "type": "progene_text", "text": [ "Tat" ], "offsets": [ [ 29, 32 ] ], "normalized": [] }, { "id": "split_0_train_48102_entity", "type": "progene_text", "text": [ "RNA polymerase II" ], "offsets": [ [ 57, 74 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29854
split_0_train_29854
[ { "id": "split_0_train_29854_passage", "type": "progene_text", "text": [ "This interaction of Tat with RNA polymerase II elongation complexes is P-TEFb - independent ." ], "offsets": [ [ 0, 93 ] ] } ]
[ { "id": "split_0_train_48103_entity", "type": "progene_text", "text": [ "Tat" ], "offsets": [ [ 20, 23 ] ], "normalized": [] }, { "id": "split_0_train_48104_entity", "type": "progene_text", "text": [ "RNA polymerase II" ], "offsets": [ [ 29, 46 ] ], "normalized": [] }, { "id": "split_0_train_48105_entity", "type": "progene_text", "text": [ "P-TEFb" ], "offsets": [ [ 71, 77 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29855
split_0_train_29855
[ { "id": "split_0_train_29855_passage", "type": "progene_text", "text": [ "Our results also show that there are two Tat binding sites on each transcription elongation complex ; one is located on TAR RNA and the other one on RNA polymerase II near the exit site for nascent mRNA transcripts ." ], "offsets": [ [ 0, 216 ] ] } ]
[ { "id": "split_0_train_48106_entity", "type": "progene_text", "text": [ "Tat" ], "offsets": [ [ 41, 44 ] ], "normalized": [] }, { "id": "split_0_train_48107_entity", "type": "progene_text", "text": [ "RNA polymerase II" ], "offsets": [ [ 149, 166 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29856
split_0_train_29856
[ { "id": "split_0_train_29856_passage", "type": "progene_text", "text": [ "These findings suggest that two Tat molecules are involved in performing various functions during a single round of HIV-1 mRNA synthesis ." ], "offsets": [ [ 0, 138 ] ] } ]
[ { "id": "split_0_train_48108_entity", "type": "progene_text", "text": [ "Tat" ], "offsets": [ [ 32, 35 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29857
split_0_train_29857
[ { "id": "split_0_train_29857_passage", "type": "progene_text", "text": [ "QM , a putative tumor suppressor , regulates proto - oncogene c-yes ." ], "offsets": [ [ 0, 69 ] ] } ]
[ { "id": "split_0_train_48109_entity", "type": "progene_text", "text": [ "QM" ], "offsets": [ [ 0, 2 ] ], "normalized": [] }, { "id": "split_0_train_48110_entity", "type": "progene_text", "text": [ "c-yes" ], "offsets": [ [ 62, 67 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29858
split_0_train_29858
[ { "id": "split_0_train_29858_passage", "type": "progene_text", "text": [ "The QM gene encodes a 24.5 kDa ribosomal protein L10 known to be highly homologous to a Jun - binding protein ( Jif-1 ) , which inhibits the formation of Jun - Jun dimers ." ], "offsets": [ [ 0, 172 ] ] } ]
[ { "id": "split_0_train_48111_entity", "type": "progene_text", "text": [ "QM" ], "offsets": [ [ 4, 6 ] ], "normalized": [] }, { "id": "split_0_train_48112_entity", "type": "progene_text", "text": [ "ribosomal protein L10" ], "offsets": [ [ 31, 52 ] ], "normalized": [] }, { "id": "split_0_train_48113_entity", "type": "progene_text", "text": [ "Jun" ], "offsets": [ [ 88, 91 ] ], "normalized": [] }, { "id": "split_0_train_48114_entity", "type": "progene_text", "text": [ "Jif-1" ], "offsets": [ [ 112, 117 ] ], "normalized": [] }, { "id": "split_0_train_48115_entity", "type": "progene_text", "text": [ "Jun" ], "offsets": [ [ 154, 157 ] ], "normalized": [] }, { "id": "split_0_train_48116_entity", "type": "progene_text", "text": [ "Jun" ], "offsets": [ [ 160, 163 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29859
split_0_train_29859
[ { "id": "split_0_train_29859_passage", "type": "progene_text", "text": [ "Here we have carried out screening with the c-Yes protein and found that a QM homologous protein showed interactions with c-Yes and other Src family members ." ], "offsets": [ [ 0, 158 ] ] } ]
[ { "id": "split_0_train_48117_entity", "type": "progene_text", "text": [ "c-Yes" ], "offsets": [ [ 44, 49 ] ], "normalized": [] }, { "id": "split_0_train_48118_entity", "type": "progene_text", "text": [ "QM" ], "offsets": [ [ 75, 77 ] ], "normalized": [] }, { "id": "split_0_train_48119_entity", "type": "progene_text", "text": [ "c-Yes" ], "offsets": [ [ 122, 127 ] ], "normalized": [] }, { "id": "split_0_train_48120_entity", "type": "progene_text", "text": [ "Src family" ], "offsets": [ [ 138, 148 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29860
split_0_train_29860
[ { "id": "split_0_train_29860_passage", "type": "progene_text", "text": [ "We have found that two different regions of QM protein were associated with the SH3 domain of c-Yes ." ], "offsets": [ [ 0, 101 ] ] } ]
[ { "id": "split_0_train_48121_entity", "type": "progene_text", "text": [ "QM" ], "offsets": [ [ 44, 46 ] ], "normalized": [] }, { "id": "split_0_train_48122_entity", "type": "progene_text", "text": [ "c-Yes" ], "offsets": [ [ 94, 99 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29861
split_0_train_29861
[ { "id": "split_0_train_29861_passage", "type": "progene_text", "text": [ "The QM protein does not contain canonical SH3 binding motifs or previously reported amino acid fragments showing interaction with SH3 domains ." ], "offsets": [ [ 0, 143 ] ] } ]
[ { "id": "split_0_train_48123_entity", "type": "progene_text", "text": [ "QM" ], "offsets": [ [ 4, 6 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29862
split_0_train_29862
[ { "id": "split_0_train_29862_passage", "type": "progene_text", "text": [ "Several c-Yes kinase activity assays indicated that the QM protein reduced c-Yes kinase activity by 70 % and that this suppression is related not only to the two SH3 binding regions but also to the C - terminal region of QM ." ], "offsets": [ [ 0, 225 ] ] } ]
[ { "id": "split_0_train_48124_entity", "type": "progene_text", "text": [ "c-Yes" ], "offsets": [ [ 8, 13 ] ], "normalized": [] }, { "id": "split_0_train_48125_entity", "type": "progene_text", "text": [ "kinase" ], "offsets": [ [ 14, 20 ] ], "normalized": [] }, { "id": "split_0_train_48126_entity", "type": "progene_text", "text": [ "QM" ], "offsets": [ [ 56, 58 ] ], "normalized": [] }, { "id": "split_0_train_48127_entity", "type": "progene_text", "text": [ "c-Yes" ], "offsets": [ [ 75, 80 ] ], "normalized": [] }, { "id": "split_0_train_48128_entity", "type": "progene_text", "text": [ "kinase" ], "offsets": [ [ 81, 87 ] ], "normalized": [] }, { "id": "split_0_train_48129_entity", "type": "progene_text", "text": [ "QM" ], "offsets": [ [ 221, 223 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29863
split_0_train_29863
[ { "id": "split_0_train_29863_passage", "type": "progene_text", "text": [ "Moreover , our autophosphorylation assays clarified that this regulation resulted from the inhibition of c-Yes autophosphorylation ." ], "offsets": [ [ 0, 132 ] ] } ]
[ { "id": "split_0_train_48130_entity", "type": "progene_text", "text": [ "c-Yes" ], "offsets": [ [ 105, 110 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29864
split_0_train_29864
[ { "id": "split_0_train_29864_passage", "type": "progene_text", "text": [ "Immunofluorescence studies showed that the QM proteins and c-Yes are able to interact in various tumor cell lines in vivo ." ], "offsets": [ [ 0, 123 ] ] } ]
[ { "id": "split_0_train_48131_entity", "type": "progene_text", "text": [ "QM" ], "offsets": [ [ 43, 45 ] ], "normalized": [] }, { "id": "split_0_train_48132_entity", "type": "progene_text", "text": [ "c-Yes" ], "offsets": [ [ 59, 64 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29865
split_0_train_29865
[ { "id": "split_0_train_29865_passage", "type": "progene_text", "text": [ "The increases of the c-Yes protein and mRNA levels were detected when the QM was transfected ." ], "offsets": [ [ 0, 94 ] ] } ]
[ { "id": "split_0_train_48133_entity", "type": "progene_text", "text": [ "c-Yes" ], "offsets": [ [ 21, 26 ] ], "normalized": [] }, { "id": "split_0_train_48134_entity", "type": "progene_text", "text": [ "QM" ], "offsets": [ [ 74, 76 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29866
split_0_train_29866
[ { "id": "split_0_train_29866_passage", "type": "progene_text", "text": [ "These results suggest that the QM protein might be a regulator for various signal transduction pathways involving SH3 domain - containing membrane proteins ." ], "offsets": [ [ 0, 157 ] ] } ]
[ { "id": "split_0_train_48135_entity", "type": "progene_text", "text": [ "QM" ], "offsets": [ [ 31, 33 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29867
split_0_train_29867
[ { "id": "split_0_train_29867_passage", "type": "progene_text", "text": [ "Induction of homologue of Slimb ubiquitin ligase receptor by mitogen signaling ." ], "offsets": [ [ 0, 80 ] ] } ]
[ { "id": "split_0_train_48136_entity", "type": "progene_text", "text": [ "Slimb" ], "offsets": [ [ 26, 31 ] ], "normalized": [] }, { "id": "split_0_train_48137_entity", "type": "progene_text", "text": [ "ubiquitin ligase" ], "offsets": [ [ 32, 48 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29868
split_0_train_29868
[ { "id": "split_0_train_29868_passage", "type": "progene_text", "text": [ "Homologue of Slimb ( HOS ) is the substrate - recognizing component of the SCF(HOS)-Roc1 E3 ubiquitin protein ligase ." ], "offsets": [ [ 0, 118 ] ] } ]
[ { "id": "split_0_train_48138_entity", "type": "progene_text", "text": [ "Homologue of Slimb" ], "offsets": [ [ 0, 18 ] ], "normalized": [] }, { "id": "split_0_train_48139_entity", "type": "progene_text", "text": [ "HOS" ], "offsets": [ [ 21, 24 ] ], "normalized": [] }, { "id": "split_0_train_48140_entity", "type": "progene_text", "text": [ "SCF(HOS)-Roc1 E3 ubiquitin protein ligase" ], "offsets": [ [ 75, 116 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29869
split_0_train_29869
[ { "id": "split_0_train_29869_passage", "type": "progene_text", "text": [ "This ligase mediates ubiquitination of the inhibitor of NF-kappaB transcription factor ( IkappaB ) ." ], "offsets": [ [ 0, 100 ] ] } ]
[ { "id": "split_0_train_48141_entity", "type": "progene_text", "text": [ "ligase" ], "offsets": [ [ 5, 11 ] ], "normalized": [] }, { "id": "split_0_train_48142_entity", "type": "progene_text", "text": [ "inhibitor of NF-kappaB" ], "offsets": [ [ 43, 65 ] ], "normalized": [] }, { "id": "split_0_train_48143_entity", "type": "progene_text", "text": [ "transcription factor" ], "offsets": [ [ 66, 86 ] ], "normalized": [] }, { "id": "split_0_train_48144_entity", "type": "progene_text", "text": [ "IkappaB" ], "offsets": [ [ 89, 96 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29870
split_0_train_29870
[ { "id": "split_0_train_29870_passage", "type": "progene_text", "text": [ "We have found that HOS is highly expressed in a number of human cancer cell lines ." ], "offsets": [ [ 0, 83 ] ] } ]
[ { "id": "split_0_train_48145_entity", "type": "progene_text", "text": [ "HOS" ], "offsets": [ [ 19, 22 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29871
split_0_train_29871
[ { "id": "split_0_train_29871_passage", "type": "progene_text", "text": [ "The rates of the HOS gene transcription as well as HOS mRNA and protein levels were up - regulated in cells treated with mitogens or transfected with the inducers of mitogen - activated protein kinase pathway ." ], "offsets": [ [ 0, 210 ] ] } ]
[ { "id": "split_0_train_48146_entity", "type": "progene_text", "text": [ "HOS" ], "offsets": [ [ 17, 20 ] ], "normalized": [] }, { "id": "split_0_train_48147_entity", "type": "progene_text", "text": [ "HOS" ], "offsets": [ [ 51, 54 ] ], "normalized": [] }, { "id": "split_0_train_48148_entity", "type": "progene_text", "text": [ "mitogen - activated protein kinase" ], "offsets": [ [ 166, 200 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29872
split_0_train_29872
[ { "id": "split_0_train_29872_passage", "type": "progene_text", "text": [ "Conversely , mitogen withdrawal strikingly reduced HOS levels during differentiation of mouse myoblasts ." ], "offsets": [ [ 0, 105 ] ] } ]
[ { "id": "split_0_train_48149_entity", "type": "progene_text", "text": [ "HOS" ], "offsets": [ [ 51, 54 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29873
split_0_train_29873
[ { "id": "split_0_train_29873_passage", "type": "progene_text", "text": [ "Activators of mitogen - activated protein kinase accelerated IkappaBalpha degradation and increased NF-kappaB transcriptional activity ." ], "offsets": [ [ 0, 136 ] ] } ]
[ { "id": "split_0_train_48150_entity", "type": "progene_text", "text": [ "mitogen - activated protein kinase" ], "offsets": [ [ 14, 48 ] ], "normalized": [] }, { "id": "split_0_train_48151_entity", "type": "progene_text", "text": [ "IkappaBalpha" ], "offsets": [ [ 61, 73 ] ], "normalized": [] }, { "id": "split_0_train_48152_entity", "type": "progene_text", "text": [ "NF-kappaB" ], "offsets": [ [ 100, 109 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29874
split_0_train_29874
[ { "id": "split_0_train_29874_passage", "type": "progene_text", "text": [ "Inhibition of HOS function via expression of dominant negative HOS ( HOS ( DeltaF ) ) initiated mouse myoblast differentiation and prevented Ras - mediated acceleration of IkappaBalpha degradation as well as NF-kappaB trans-activation and transformation of NIH3T3 cells ." ], "offsets": [ [ 0, 271 ] ] } ]
[ { "id": "split_0_train_48153_entity", "type": "progene_text", "text": [ "HOS" ], "offsets": [ [ 14, 17 ] ], "normalized": [] }, { "id": "split_0_train_48154_entity", "type": "progene_text", "text": [ "HOS" ], "offsets": [ [ 63, 66 ] ], "normalized": [] }, { "id": "split_0_train_48155_entity", "type": "progene_text", "text": [ "HOS" ], "offsets": [ [ 69, 72 ] ], "normalized": [] }, { "id": "split_0_train_48156_entity", "type": "progene_text", "text": [ "Ras" ], "offsets": [ [ 141, 144 ] ], "normalized": [] }, { "id": "split_0_train_48157_entity", "type": "progene_text", "text": [ "IkappaBalpha" ], "offsets": [ [ 172, 184 ] ], "normalized": [] }, { "id": "split_0_train_48158_entity", "type": "progene_text", "text": [ "NF-kappaB" ], "offsets": [ [ 208, 217 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29875
split_0_train_29875
[ { "id": "split_0_train_29875_passage", "type": "progene_text", "text": [ "These data link the induction of HOS in proliferating cells with mitogen - signaling - dependent inhibition of cell differentiation and promotion of cell transformation ." ], "offsets": [ [ 0, 170 ] ] } ]
[ { "id": "split_0_train_48159_entity", "type": "progene_text", "text": [ "HOS" ], "offsets": [ [ 33, 36 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29876
split_0_train_29876
[ { "id": "split_0_train_29876_passage", "type": "progene_text", "text": [ "Basic fibroblast growth factor : effects on matrix remodeling , receptor expression , and transduction pathway in human periosteal fibroblasts with FGFR2 gene mutation ." ], "offsets": [ [ 0, 169 ] ] } ]
[ { "id": "split_0_train_48160_entity", "type": "progene_text", "text": [ "Basic fibroblast growth factor" ], "offsets": [ [ 0, 30 ] ], "normalized": [] }, { "id": "split_0_train_48161_entity", "type": "progene_text", "text": [ "FGFR2" ], "offsets": [ [ 148, 153 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29877
split_0_train_29877
[ { "id": "split_0_train_29877_passage", "type": "progene_text", "text": [ "The Crouzon syndrome , which is associated with fibroblast growth factor receptor ( FGFR2 ) mutations , is characterized by premature fusion of cranial sutures ." ], "offsets": [ [ 0, 161 ] ] } ]
[ { "id": "split_0_train_48162_entity", "type": "progene_text", "text": [ "fibroblast growth factor receptor" ], "offsets": [ [ 48, 81 ] ], "normalized": [] }, { "id": "split_0_train_48163_entity", "type": "progene_text", "text": [ "FGFR2" ], "offsets": [ [ 84, 89 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29878
split_0_train_29878
[ { "id": "split_0_train_29878_passage", "type": "progene_text", "text": [ "We used an in vitro model of cultured periosteal fibroblasts from normal subjects and from Crouzon patients with FGFR2 mutation ." ], "offsets": [ [ 0, 129 ] ] } ]
[ { "id": "split_0_train_48164_entity", "type": "progene_text", "text": [ "FGFR2" ], "offsets": [ [ 113, 118 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29879
split_0_train_29879
[ { "id": "split_0_train_29879_passage", "type": "progene_text", "text": [ "We analyzed the matrix turnover rate and the effects of adding FGF2 by evaluating fibronectin synthesis and the activity of some proteolytic enzymes ." ], "offsets": [ [ 0, 150 ] ] } ]
[ { "id": "split_0_train_48165_entity", "type": "progene_text", "text": [ "FGF2" ], "offsets": [ [ 63, 67 ] ], "normalized": [] }, { "id": "split_0_train_48166_entity", "type": "progene_text", "text": [ "fibronectin" ], "offsets": [ [ 82, 93 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29880
split_0_train_29880
[ { "id": "split_0_train_29880_passage", "type": "progene_text", "text": [ "To assess the role of some FGF signaling molecules involved in FGFR2 regulation , we studied Grb2 tyrosine phosphorylation and the phosphotyrosine proteins associated with Grb2 ." ], "offsets": [ [ 0, 178 ] ] } ]
[ { "id": "split_0_train_48167_entity", "type": "progene_text", "text": [ "FGF" ], "offsets": [ [ 27, 30 ] ], "normalized": [] }, { "id": "split_0_train_48168_entity", "type": "progene_text", "text": [ "FGFR2" ], "offsets": [ [ 63, 68 ] ], "normalized": [] }, { "id": "split_0_train_48169_entity", "type": "progene_text", "text": [ "Grb2" ], "offsets": [ [ 93, 97 ] ], "normalized": [] }, { "id": "split_0_train_48170_entity", "type": "progene_text", "text": [ "Grb2" ], "offsets": [ [ 172, 176 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29881
split_0_train_29881
[ { "id": "split_0_train_29881_passage", "type": "progene_text", "text": [ "The iodinate FGF binding assay was performed to quantify FGFR expression ." ], "offsets": [ [ 0, 74 ] ] } ]
[ { "id": "split_0_train_48171_entity", "type": "progene_text", "text": [ "FGF" ], "offsets": [ [ 13, 16 ] ], "normalized": [] }, { "id": "split_0_train_48172_entity", "type": "progene_text", "text": [ "FGFR" ], "offsets": [ [ 57, 61 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29882
split_0_train_29882
[ { "id": "split_0_train_29882_passage", "type": "progene_text", "text": [ "Compared with normal fibroblasts , fibronectin synthesis was decreased in Crouzon fibroblasts , and protease activities in cells and medium were enhanced , suggesting that excess fibronectin catabolism is present ." ], "offsets": [ [ 0, 214 ] ] } ]
[ { "id": "split_0_train_48173_entity", "type": "progene_text", "text": [ "fibronectin" ], "offsets": [ [ 35, 46 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29883
split_0_train_29883
[ { "id": "split_0_train_29883_passage", "type": "progene_text", "text": [ "Differences were more marked when FGF2 was added ." ], "offsets": [ [ 0, 50 ] ] } ]
[ { "id": "split_0_train_48174_entity", "type": "progene_text", "text": [ "FGF2" ], "offsets": [ [ 34, 38 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29884
split_0_train_29884
[ { "id": "split_0_train_29884_passage", "type": "progene_text", "text": [ "Very few phosphoproteins were visible in anti - Grb2 immunoprecipitations from Crouzon fibroblasts , which showed a significant increase in the number of high - affinity and low - affinity FGF2 receptors ." ], "offsets": [ [ 0, 205 ] ] } ]
[ { "id": "split_0_train_48175_entity", "type": "progene_text", "text": [ "Grb2" ], "offsets": [ [ 48, 52 ] ], "normalized": [] }, { "id": "split_0_train_48176_entity", "type": "progene_text", "text": [ "FGF2 receptors" ], "offsets": [ [ 189, 203 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29885
split_0_train_29885
[ { "id": "split_0_train_29885_passage", "type": "progene_text", "text": [ "These results suggest that the abnormal genotype and the Crouzon cellular phenotype are related ." ], "offsets": [ [ 0, 97 ] ] } ]
[]
[]
[]
[]
split_0_train_29886
split_0_train_29886
[ { "id": "split_0_train_29886_passage", "type": "progene_text", "text": [ "To compensate the low levels of tyrosine phosphorylation , Crouzon cells might increase the numbers of FGFR2 , thus increasing the cell surface binding sites for FGF2 ." ], "offsets": [ [ 0, 168 ] ] } ]
[ { "id": "split_0_train_48177_entity", "type": "progene_text", "text": [ "FGFR2" ], "offsets": [ [ 103, 108 ] ], "normalized": [] }, { "id": "split_0_train_48178_entity", "type": "progene_text", "text": [ "FGF2" ], "offsets": [ [ 162, 166 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29887
split_0_train_29887
[ { "id": "split_0_train_29887_passage", "type": "progene_text", "text": [ "Transcription factor NF-IL6 ( C / EBPbeta ) activates the expression of the mouse MHC class I H2-Kb gene in response to TNF-alpha via the intragenic downstream regulatory element ." ], "offsets": [ [ 0, 180 ] ] } ]
[ { "id": "split_0_train_48179_entity", "type": "progene_text", "text": [ "Transcription factor" ], "offsets": [ [ 0, 20 ] ], "normalized": [] }, { "id": "split_0_train_48180_entity", "type": "progene_text", "text": [ "NF-IL6" ], "offsets": [ [ 21, 27 ] ], "normalized": [] }, { "id": "split_0_train_48181_entity", "type": "progene_text", "text": [ "C / EBPbeta" ], "offsets": [ [ 30, 41 ] ], "normalized": [] }, { "id": "split_0_train_48182_entity", "type": "progene_text", "text": [ "MHC class I" ], "offsets": [ [ 82, 93 ] ], "normalized": [] }, { "id": "split_0_train_48183_entity", "type": "progene_text", "text": [ "H2-Kb" ], "offsets": [ [ 94, 99 ] ], "normalized": [] }, { "id": "split_0_train_48184_entity", "type": "progene_text", "text": [ "TNF-alpha" ], "offsets": [ [ 120, 129 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29888
split_0_train_29888
[ { "id": "split_0_train_29888_passage", "type": "progene_text", "text": [ "The 5'-enhancer - deleted genomic construct of the H2-K(b) gene , stably integrated into the genome of L(tk-) fibroblasts , retains full competence to be induced by tumor necrosis factor - alpha ( TNF-alpha ) treatment ." ], "offsets": [ [ 0, 220 ] ] } ]
[ { "id": "split_0_train_48185_entity", "type": "progene_text", "text": [ "H2-K(b)" ], "offsets": [ [ 51, 58 ] ], "normalized": [] }, { "id": "split_0_train_48186_entity", "type": "progene_text", "text": [ "tumor necrosis factor - alpha" ], "offsets": [ [ 165, 194 ] ], "normalized": [] }, { "id": "split_0_train_48187_entity", "type": "progene_text", "text": [ "TNF-alpha" ], "offsets": [ [ 197, 206 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29889
split_0_train_29889
[ { "id": "split_0_train_29889_passage", "type": "progene_text", "text": [ "The only defined regulatory region in this construct is the intragenic downstream regulatory element ( H2DRE ) ." ], "offsets": [ [ 0, 112 ] ] } ]
[]
[]
[]
[]
split_0_train_29890
split_0_train_29890
[ { "id": "split_0_train_29890_passage", "type": "progene_text", "text": [ "Computational inspection uncovered two potential NF-IL6 ( C / EBPbeta ) binding motifs within the H2DRE ." ], "offsets": [ [ 0, 105 ] ] } ]
[ { "id": "split_0_train_48188_entity", "type": "progene_text", "text": [ "NF-IL6" ], "offsets": [ [ 49, 55 ] ], "normalized": [] }, { "id": "split_0_train_48189_entity", "type": "progene_text", "text": [ "C / EBPbeta" ], "offsets": [ [ 58, 69 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29891
split_0_train_29891
[ { "id": "split_0_train_29891_passage", "type": "progene_text", "text": [ "Chloramphenicol acetyltransferase ( CAT ) reporter gene assay revealed that NF-IL6 is able to elevate transcription from H2DRE ." ], "offsets": [ [ 0, 128 ] ] } ]
[ { "id": "split_0_train_48190_entity", "type": "progene_text", "text": [ "Chloramphenicol acetyltransferase" ], "offsets": [ [ 0, 33 ] ], "normalized": [] }, { "id": "split_0_train_48191_entity", "type": "progene_text", "text": [ "CAT" ], "offsets": [ [ 36, 39 ] ], "normalized": [] }, { "id": "split_0_train_48192_entity", "type": "progene_text", "text": [ "NF-IL6" ], "offsets": [ [ 76, 82 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29892
split_0_train_29892
[ { "id": "split_0_train_29892_passage", "type": "progene_text", "text": [ "Moreover , transient transfection of an NF-IL6 expression vector increased both constitutive and TNF-alpha - induced mRNA levels of endogenous H2 class I genes , and transfection of an NF-IL6 dominant negative construct decreased the expression of endogenous H2 class I genes in a dose - dependent manner ." ], "offsets": [ [ 0, 306 ] ] } ]
[ { "id": "split_0_train_48193_entity", "type": "progene_text", "text": [ "NF-IL6" ], "offsets": [ [ 40, 46 ] ], "normalized": [] }, { "id": "split_0_train_48194_entity", "type": "progene_text", "text": [ "TNF-alpha" ], "offsets": [ [ 97, 106 ] ], "normalized": [] }, { "id": "split_0_train_48195_entity", "type": "progene_text", "text": [ "H2 class I" ], "offsets": [ [ 143, 153 ] ], "normalized": [] }, { "id": "split_0_train_48196_entity", "type": "progene_text", "text": [ "NF-IL6" ], "offsets": [ [ 185, 191 ] ], "normalized": [] }, { "id": "split_0_train_48197_entity", "type": "progene_text", "text": [ "H2 class I" ], "offsets": [ [ 259, 269 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29893
split_0_train_29893
[ { "id": "split_0_train_29893_passage", "type": "progene_text", "text": [ "Using the electrophoretic mobility shift assay ( EMSA ) and antibody supershift assay , we were able to qualify the two computationally identified NF-IL6 binding motifs as one high - affinity and one low - affinity binding site ." ], "offsets": [ [ 0, 229 ] ] } ]
[ { "id": "split_0_train_48198_entity", "type": "progene_text", "text": [ "NF-IL6" ], "offsets": [ [ 147, 153 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29894
split_0_train_29894
[ { "id": "split_0_train_29894_passage", "type": "progene_text", "text": [ "We conclude that the H2-K(b) gene belongs to target genes of the NF-IL6 ( C / EBPbeta ) in the course of the cellular response to TNF-alpha , and we discuss some consequences of this conclusion in a general framework of inducible expression of the H2-K(b) gene ." ], "offsets": [ [ 0, 262 ] ] } ]
[ { "id": "split_0_train_48199_entity", "type": "progene_text", "text": [ "H2-K(b)" ], "offsets": [ [ 21, 28 ] ], "normalized": [] }, { "id": "split_0_train_48200_entity", "type": "progene_text", "text": [ "NF-IL6" ], "offsets": [ [ 65, 71 ] ], "normalized": [] }, { "id": "split_0_train_48201_entity", "type": "progene_text", "text": [ "C / EBPbeta" ], "offsets": [ [ 74, 85 ] ], "normalized": [] }, { "id": "split_0_train_48202_entity", "type": "progene_text", "text": [ "TNF-alpha" ], "offsets": [ [ 130, 139 ] ], "normalized": [] }, { "id": "split_0_train_48203_entity", "type": "progene_text", "text": [ "H2-K(b)" ], "offsets": [ [ 248, 255 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29895
split_0_train_29895
[ { "id": "split_0_train_29895_passage", "type": "progene_text", "text": [ "Hypoxia activates beta(1)-integrin via ERK 1 / 2 and p38 MAP kinase in human vascular smooth muscle cells ." ], "offsets": [ [ 0, 107 ] ] } ]
[ { "id": "split_0_train_48204_entity", "type": "progene_text", "text": [ "beta(1)-integrin" ], "offsets": [ [ 18, 34 ] ], "normalized": [] }, { "id": "split_0_train_48205_entity", "type": "progene_text", "text": [ "ERK 1 / 2" ], "offsets": [ [ 39, 48 ] ], "normalized": [] }, { "id": "split_0_train_48206_entity", "type": "progene_text", "text": [ "p38 MAP kinase" ], "offsets": [ [ 53, 67 ] ], "normalized": [] } ]
[]
[]
[]
split_0_train_29896
split_0_train_29896
[ { "id": "split_0_train_29896_passage", "type": "progene_text", "text": [ "Hypoxia plays an important role in vascular remodeling and directly affects vascular smooth muscle cell ( VSMC ) functions ." ], "offsets": [ [ 0, 124 ] ] } ]
[]
[]
[]
[]
split_0_train_29897
split_0_train_29897
[ { "id": "split_0_train_29897_passage", "type": "progene_text", "text": [ "VSMC adhesion participates in changes of vascular structure ; however , little is known about VSMC adhesion under hypoxic conditions ." ], "offsets": [ [ 0, 134 ] ] } ]
[]
[]
[]
[]
split_0_train_29898
split_0_train_29898
[ { "id": "split_0_train_29898_passage", "type": "progene_text", "text": [ "It was the aim of the present study to investigate the effects of hypoxia on adhesion mechanisms in human VSMCs ." ], "offsets": [ [ 0, 113 ] ] } ]
[]
[]
[]
[]
split_0_train_29899
split_0_train_29899
[ { "id": "split_0_train_29899_passage", "type": "progene_text", "text": [ "Compared to normoxic cells , hypoxia ( 1 % O(2) , 24h ) significantly increased adhesion of VSMCs to collagen I by 30.2 % and fibronectin by 58.0 % ." ], "offsets": [ [ 0, 149 ] ] } ]
[ { "id": "split_0_train_48207_entity", "type": "progene_text", "text": [ "collagen I" ], "offsets": [ [ 101, 111 ] ], "normalized": [] }, { "id": "split_0_train_48208_entity", "type": "progene_text", "text": [ "fibronectin" ], "offsets": [ [ 126, 137 ] ], "normalized": [] } ]
[]
[]
[]