PubMed:9182556
Annnotations
sentences
{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":122},"obj":"Sentence"},{"id":"T2","span":{"begin":123,"end":311},"obj":"Sentence"},{"id":"T3","span":{"begin":312,"end":513},"obj":"Sentence"},{"id":"T4","span":{"begin":514,"end":825},"obj":"Sentence"},{"id":"T5","span":{"begin":826,"end":960},"obj":"Sentence"},{"id":"T6","span":{"begin":961,"end":1221},"obj":"Sentence"},{"id":"T7","span":{"begin":1222,"end":1372},"obj":"Sentence"},{"id":"T8","span":{"begin":1373,"end":1507},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":122},"obj":"Sentence"},{"id":"T2","span":{"begin":123,"end":311},"obj":"Sentence"},{"id":"T3","span":{"begin":312,"end":513},"obj":"Sentence"},{"id":"T4","span":{"begin":514,"end":825},"obj":"Sentence"},{"id":"T5","span":{"begin":826,"end":960},"obj":"Sentence"},{"id":"T6","span":{"begin":961,"end":1221},"obj":"Sentence"},{"id":"T7","span":{"begin":1222,"end":1372},"obj":"Sentence"},{"id":"T8","span":{"begin":1373,"end":1507},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Overexpression of HSF2-beta inhibits hemin-induced heat shock gene expression and erythroid differentiation in K562 cells.\nAcquisition of heat shock factor 2 (HSF2) DNA binding activity is accompanied by induced transcription of heat shock genes in hemin-treated K562 cells undergoing erythroid differentiation. Previous studies revealed that HSF2 consists of two alternatively spliced isoforms, HSF2-alpha and HSF2-beta, whose relative abundance is developmentally regulated and varies between different tissues. To investigate whether the molar ratio of HSF2-alpha and HSF2-beta isoforms is crucial for the activation of HSF2 and whether the HSF2 isoforms play functionally distinct roles during the hemin-mediated erythroid differentiation, we generated cell clones expressing different levels of HSF2-alpha and HSF2-beta. We show that in parental K562 cells, the HSF2-alpha isoform is predominantly expressed and HSF2 can be activated upon hemin treatment. In contrast, when HSF2-beta is expressed at levels exceeding those of endogenous HSF2-alpha, the hemin-induced DNA binding activity and transcription of heat shock genes are repressed, whereas overexpression of HSF2-alpha results in an enhanced hemin response. Furthermore, the hemin-induced accumulation of globin, known as a marker of erythroid differentiation, is decreased in cells overexpressing HSF2-beta. We suggest that HSF2-beta acts as a negative regulator of HSF2 activity during hemin-mediated erythroid differentiation of K562 cells."}
jnlpba-st-training
{"project":"jnlpba-st-training","denotations":[{"id":"T1","span":{"begin":18,"end":27},"obj":"protein"},{"id":"T2","span":{"begin":37,"end":42},"obj":"protein"},{"id":"T3","span":{"begin":111,"end":121},"obj":"cell_line"},{"id":"T4","span":{"begin":229,"end":245},"obj":"DNA"},{"id":"T5","span":{"begin":263,"end":273},"obj":"cell_line"},{"id":"T6","span":{"begin":343,"end":347},"obj":"protein"},{"id":"T7","span":{"begin":396,"end":406},"obj":"protein"},{"id":"T8","span":{"begin":411,"end":420},"obj":"protein"},{"id":"T9","span":{"begin":556,"end":566},"obj":"protein"},{"id":"T10","span":{"begin":571,"end":580},"obj":"protein"},{"id":"T11","span":{"begin":623,"end":627},"obj":"protein"},{"id":"T12","span":{"begin":644,"end":648},"obj":"protein"},{"id":"T13","span":{"begin":800,"end":810},"obj":"protein"},{"id":"T14","span":{"begin":815,"end":824},"obj":"protein"},{"id":"T15","span":{"begin":851,"end":861},"obj":"cell_line"},{"id":"T16","span":{"begin":867,"end":885},"obj":"protein"},{"id":"T17","span":{"begin":917,"end":921},"obj":"protein"},{"id":"T18","span":{"begin":979,"end":988},"obj":"protein"},{"id":"T19","span":{"begin":1031,"end":1052},"obj":"protein"},{"id":"T20","span":{"begin":1114,"end":1130},"obj":"DNA"},{"id":"T21","span":{"begin":1172,"end":1182},"obj":"protein"},{"id":"T22","span":{"begin":1206,"end":1211},"obj":"protein"},{"id":"T23","span":{"begin":1239,"end":1244},"obj":"protein"},{"id":"T24","span":{"begin":1269,"end":1275},"obj":"protein"},{"id":"T25","span":{"begin":1362,"end":1371},"obj":"protein"},{"id":"T26","span":{"begin":1389,"end":1398},"obj":"protein"},{"id":"T27","span":{"begin":1431,"end":1435},"obj":"protein"},{"id":"T28","span":{"begin":1496,"end":1506},"obj":"cell_line"}],"text":"Overexpression of HSF2-beta inhibits hemin-induced heat shock gene expression and erythroid differentiation in K562 cells.\nAcquisition of heat shock factor 2 (HSF2) DNA binding activity is accompanied by induced transcription of heat shock genes in hemin-treated K562 cells undergoing erythroid differentiation. Previous studies revealed that HSF2 consists of two alternatively spliced isoforms, HSF2-alpha and HSF2-beta, whose relative abundance is developmentally regulated and varies between different tissues. To investigate whether the molar ratio of HSF2-alpha and HSF2-beta isoforms is crucial for the activation of HSF2 and whether the HSF2 isoforms play functionally distinct roles during the hemin-mediated erythroid differentiation, we generated cell clones expressing different levels of HSF2-alpha and HSF2-beta. We show that in parental K562 cells, the HSF2-alpha isoform is predominantly expressed and HSF2 can be activated upon hemin treatment. In contrast, when HSF2-beta is expressed at levels exceeding those of endogenous HSF2-alpha, the hemin-induced DNA binding activity and transcription of heat shock genes are repressed, whereas overexpression of HSF2-alpha results in an enhanced hemin response. Furthermore, the hemin-induced accumulation of globin, known as a marker of erythroid differentiation, is decreased in cells overexpressing HSF2-beta. We suggest that HSF2-beta acts as a negative regulator of HSF2 activity during hemin-mediated erythroid differentiation of K562 cells."}
genia-medco-coref
{"project":"genia-medco-coref","denotations":[{"id":"C1","span":{"begin":18,"end":27},"obj":"NP"},{"id":"C2","span":{"begin":82,"end":107},"obj":"NP"},{"id":"C3","span":{"begin":111,"end":121},"obj":"NP"},{"id":"C4","span":{"begin":138,"end":185},"obj":"NP"},{"id":"C5","span":{"begin":204,"end":245},"obj":"NP"},{"id":"C6","span":{"begin":285,"end":310},"obj":"NP"},{"id":"C7","span":{"begin":343,"end":347},"obj":"NP"},{"id":"C10","span":{"begin":396,"end":406},"obj":"NP"},{"id":"C11","span":{"begin":411,"end":420},"obj":"NP"},{"id":"C9","span":{"begin":396,"end":420},"obj":"NP"},{"id":"C8","span":{"begin":360,"end":420},"obj":"NP"},{"id":"C12","span":{"begin":422,"end":427},"obj":"NP"},{"id":"C13","span":{"begin":556,"end":589},"obj":"NP"},{"id":"C14","span":{"begin":623,"end":627},"obj":"NP"},{"id":"C15","span":{"begin":640,"end":657},"obj":"NP"},{"id":"C16","span":{"begin":698,"end":742},"obj":"NP"},{"id":"C18","span":{"begin":800,"end":810},"obj":"NP"},{"id":"C19","span":{"begin":815,"end":824},"obj":"NP"},{"id":"C17","span":{"begin":800,"end":824},"obj":"NP"},{"id":"C20","span":{"begin":863,"end":885},"obj":"NP"},{"id":"C21","span":{"begin":917,"end":921},"obj":"NP"},{"id":"C22","span":{"begin":979,"end":988},"obj":"NP"},{"id":"C23","span":{"begin":1005,"end":1011},"obj":"NP"},{"id":"C24","span":{"begin":1022,"end":1027},"obj":"NP"},{"id":"C25","span":{"begin":1054,"end":1092},"obj":"NP"},{"id":"C26","span":{"begin":1097,"end":1130},"obj":"NP"},{"id":"C27","span":{"begin":1172,"end":1182},"obj":"NP"},{"id":"C28","span":{"begin":1362,"end":1371},"obj":"NP"},{"id":"C29","span":{"begin":1389,"end":1398},"obj":"NP"},{"id":"C31","span":{"begin":1496,"end":1506},"obj":"NP"},{"id":"C30","span":{"begin":1452,"end":1506},"obj":"NP"}],"relations":[{"id":"R1","pred":"coref-ident","subj":"C6","obj":"C2"},{"id":"R2","pred":"coref-ident","subj":"C11","obj":"C1"},{"id":"R3","pred":"coref-appos","subj":"C9","obj":"C8"},{"id":"R4","pred":"coref-relat","subj":"C12","obj":"C9"},{"id":"R5","pred":"coref-ident","subj":"C13","obj":"C8"},{"id":"R6","pred":"coref-ident","subj":"C14","obj":"C7"},{"id":"R7","pred":"coref-ident","subj":"C15","obj":"C13"},{"id":"R8","pred":"coref-ident","subj":"C16","obj":"C6"},{"id":"R9","pred":"coref-ident","subj":"C18","obj":"C10"},{"id":"R10","pred":"coref-ident","subj":"C19","obj":"C11"},{"id":"R11","pred":"coref-ident","subj":"C17","obj":"C15"},{"id":"R12","pred":"coref-ident","subj":"C20","obj":"C18"},{"id":"R13","pred":"coref-ident","subj":"C21","obj":"C14"},{"id":"R14","pred":"coref-ident","subj":"C22","obj":"C19"},{"id":"R15","pred":"coref-pron","subj":"C24","obj":"C23"},{"id":"R16","pred":"coref-ident","subj":"C25","obj":"C4"},{"id":"R17","pred":"coref-ident","subj":"C26","obj":"C5"},{"id":"R18","pred":"coref-ident","subj":"C27","obj":"C20"},{"id":"R19","pred":"coref-ident","subj":"C29","obj":"C28"},{"id":"R20","pred":"coref-ident","subj":"C31","obj":"C3"},{"id":"R21","pred":"coref-ident","subj":"C30","obj":"C16"}],"text":"Overexpression of HSF2-beta inhibits hemin-induced heat shock gene expression and erythroid differentiation in K562 cells.\nAcquisition of heat shock factor 2 (HSF2) DNA binding activity is accompanied by induced transcription of heat shock genes in hemin-treated K562 cells undergoing erythroid differentiation. Previous studies revealed that HSF2 consists of two alternatively spliced isoforms, HSF2-alpha and HSF2-beta, whose relative abundance is developmentally regulated and varies between different tissues. To investigate whether the molar ratio of HSF2-alpha and HSF2-beta isoforms is crucial for the activation of HSF2 and whether the HSF2 isoforms play functionally distinct roles during the hemin-mediated erythroid differentiation, we generated cell clones expressing different levels of HSF2-alpha and HSF2-beta. We show that in parental K562 cells, the HSF2-alpha isoform is predominantly expressed and HSF2 can be activated upon hemin treatment. In contrast, when HSF2-beta is expressed at levels exceeding those of endogenous HSF2-alpha, the hemin-induced DNA binding activity and transcription of heat shock genes are repressed, whereas overexpression of HSF2-alpha results in an enhanced hemin response. Furthermore, the hemin-induced accumulation of globin, known as a marker of erythroid differentiation, is decreased in cells overexpressing HSF2-beta. We suggest that HSF2-beta acts as a negative regulator of HSF2 activity during hemin-mediated erythroid differentiation of K562 cells."}
pubmed-sentences-benchmark
{"project":"pubmed-sentences-benchmark","denotations":[{"id":"S1","span":{"begin":0,"end":122},"obj":"Sentence"},{"id":"S2","span":{"begin":123,"end":311},"obj":"Sentence"},{"id":"S3","span":{"begin":312,"end":513},"obj":"Sentence"},{"id":"S4","span":{"begin":514,"end":825},"obj":"Sentence"},{"id":"S5","span":{"begin":826,"end":960},"obj":"Sentence"},{"id":"S6","span":{"begin":961,"end":1221},"obj":"Sentence"},{"id":"S7","span":{"begin":1222,"end":1372},"obj":"Sentence"},{"id":"S8","span":{"begin":1373,"end":1507},"obj":"Sentence"}],"text":"Overexpression of HSF2-beta inhibits hemin-induced heat shock gene expression and erythroid differentiation in K562 cells.\nAcquisition of heat shock factor 2 (HSF2) DNA binding activity is accompanied by induced transcription of heat shock genes in hemin-treated K562 cells undergoing erythroid differentiation. Previous studies revealed that HSF2 consists of two alternatively spliced isoforms, HSF2-alpha and HSF2-beta, whose relative abundance is developmentally regulated and varies between different tissues. To investigate whether the molar ratio of HSF2-alpha and HSF2-beta isoforms is crucial for the activation of HSF2 and whether the HSF2 isoforms play functionally distinct roles during the hemin-mediated erythroid differentiation, we generated cell clones expressing different levels of HSF2-alpha and HSF2-beta. We show that in parental K562 cells, the HSF2-alpha isoform is predominantly expressed and HSF2 can be activated upon hemin treatment. In contrast, when HSF2-beta is expressed at levels exceeding those of endogenous HSF2-alpha, the hemin-induced DNA binding activity and transcription of heat shock genes are repressed, whereas overexpression of HSF2-alpha results in an enhanced hemin response. Furthermore, the hemin-induced accumulation of globin, known as a marker of erythroid differentiation, is decreased in cells overexpressing HSF2-beta. We suggest that HSF2-beta acts as a negative regulator of HSF2 activity during hemin-mediated erythroid differentiation of K562 cells."}
GENIAcorpus
{"project":"GENIAcorpus","denotations":[{"id":"T1","span":{"begin":18,"end":27},"obj":"protein_molecule"},{"id":"T2","span":{"begin":37,"end":42},"obj":"protein_molecule"},{"id":"T3","span":{"begin":82,"end":107},"obj":"other_name"},{"id":"T4","span":{"begin":111,"end":121},"obj":"cell_line"},{"id":"T5","span":{"begin":229,"end":245},"obj":"DNA_family_or_group"},{"id":"T6","span":{"begin":263,"end":273},"obj":"cell_line"},{"id":"T7","span":{"begin":285,"end":310},"obj":"other_name"},{"id":"T8","span":{"begin":343,"end":347},"obj":"protein_molecule"},{"id":"T9","span":{"begin":396,"end":406},"obj":"protein_molecule"},{"id":"T10","span":{"begin":411,"end":420},"obj":"protein_molecule"},{"id":"T11","span":{"begin":556,"end":566},"obj":"protein_molecule"},{"id":"T12","span":{"begin":571,"end":580},"obj":"protein_molecule"},{"id":"T13","span":{"begin":623,"end":627},"obj":"protein_molecule"},{"id":"T14","span":{"begin":644,"end":648},"obj":"protein_molecule"},{"id":"T15","span":{"begin":717,"end":742},"obj":"other_name"},{"id":"T16","span":{"begin":800,"end":810},"obj":"protein_molecule"},{"id":"T17","span":{"begin":815,"end":824},"obj":"protein_molecule"},{"id":"T18","span":{"begin":851,"end":861},"obj":"cell_line"},{"id":"T19","span":{"begin":867,"end":877},"obj":"protein_molecule"},{"id":"T20","span":{"begin":917,"end":921},"obj":"protein_molecule"},{"id":"T21","span":{"begin":979,"end":988},"obj":"protein_molecule"},{"id":"T22","span":{"begin":1031,"end":1041},"obj":"protein_molecule"},{"id":"T23","span":{"begin":1042,"end":1052},"obj":"protein_molecule"},{"id":"T24","span":{"begin":1114,"end":1130},"obj":"DNA_family_or_group"},{"id":"T25","span":{"begin":1172,"end":1182},"obj":"protein_molecule"},{"id":"T26","span":{"begin":1206,"end":1211},"obj":"protein_molecule"},{"id":"T27","span":{"begin":1239,"end":1244},"obj":"protein_molecule"},{"id":"T28","span":{"begin":1269,"end":1275},"obj":"protein_complex"},{"id":"T29","span":{"begin":1298,"end":1323},"obj":"other_name"},{"id":"T30","span":{"begin":1362,"end":1371},"obj":"protein_molecule"},{"id":"T31","span":{"begin":1389,"end":1398},"obj":"protein_molecule"},{"id":"T32","span":{"begin":1431,"end":1435},"obj":"protein_molecule"},{"id":"T33","span":{"begin":1452,"end":1466},"obj":"other_name"},{"id":"T34","span":{"begin":1467,"end":1492},"obj":"other_name"},{"id":"T35","span":{"begin":1496,"end":1506},"obj":"cell_line"}],"text":"Overexpression of HSF2-beta inhibits hemin-induced heat shock gene expression and erythroid differentiation in K562 cells.\nAcquisition of heat shock factor 2 (HSF2) DNA binding activity is accompanied by induced transcription of heat shock genes in hemin-treated K562 cells undergoing erythroid differentiation. Previous studies revealed that HSF2 consists of two alternatively spliced isoforms, HSF2-alpha and HSF2-beta, whose relative abundance is developmentally regulated and varies between different tissues. To investigate whether the molar ratio of HSF2-alpha and HSF2-beta isoforms is crucial for the activation of HSF2 and whether the HSF2 isoforms play functionally distinct roles during the hemin-mediated erythroid differentiation, we generated cell clones expressing different levels of HSF2-alpha and HSF2-beta. We show that in parental K562 cells, the HSF2-alpha isoform is predominantly expressed and HSF2 can be activated upon hemin treatment. In contrast, when HSF2-beta is expressed at levels exceeding those of endogenous HSF2-alpha, the hemin-induced DNA binding activity and transcription of heat shock genes are repressed, whereas overexpression of HSF2-alpha results in an enhanced hemin response. Furthermore, the hemin-induced accumulation of globin, known as a marker of erythroid differentiation, is decreased in cells overexpressing HSF2-beta. We suggest that HSF2-beta acts as a negative regulator of HSF2 activity during hemin-mediated erythroid differentiation of K562 cells."}
Anatomy-UBERON
{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":541,"end":546},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0003655"}],"text":"Overexpression of HSF2-beta inhibits hemin-induced heat shock gene expression and erythroid differentiation in K562 cells.\nAcquisition of heat shock factor 2 (HSF2) DNA binding activity is accompanied by induced transcription of heat shock genes in hemin-treated K562 cells undergoing erythroid differentiation. Previous studies revealed that HSF2 consists of two alternatively spliced isoforms, HSF2-alpha and HSF2-beta, whose relative abundance is developmentally regulated and varies between different tissues. To investigate whether the molar ratio of HSF2-alpha and HSF2-beta isoforms is crucial for the activation of HSF2 and whether the HSF2 isoforms play functionally distinct roles during the hemin-mediated erythroid differentiation, we generated cell clones expressing different levels of HSF2-alpha and HSF2-beta. We show that in parental K562 cells, the HSF2-alpha isoform is predominantly expressed and HSF2 can be activated upon hemin treatment. In contrast, when HSF2-beta is expressed at levels exceeding those of endogenous HSF2-alpha, the hemin-induced DNA binding activity and transcription of heat shock genes are repressed, whereas overexpression of HSF2-alpha results in an enhanced hemin response. Furthermore, the hemin-induced accumulation of globin, known as a marker of erythroid differentiation, is decreased in cells overexpressing HSF2-beta. We suggest that HSF2-beta acts as a negative regulator of HSF2 activity during hemin-mediated erythroid differentiation of K562 cells."}
HP-phenotype
{"project":"HP-phenotype","denotations":[{"id":"T1","span":{"begin":56,"end":61},"obj":"Phenotype"},{"id":"T2","span":{"begin":143,"end":148},"obj":"Phenotype"},{"id":"T3","span":{"begin":234,"end":239},"obj":"Phenotype"},{"id":"T4","span":{"begin":1119,"end":1124},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0031273"},{"id":"A2","pred":"hp_id","subj":"T2","obj":"HP:0031273"},{"id":"A3","pred":"hp_id","subj":"T3","obj":"HP:0031273"},{"id":"A4","pred":"hp_id","subj":"T4","obj":"HP:0031273"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"Overexpression of HSF2-beta inhibits hemin-induced heat shock gene expression and erythroid differentiation in K562 cells.\nAcquisition of heat shock factor 2 (HSF2) DNA binding activity is accompanied by induced transcription of heat shock genes in hemin-treated K562 cells undergoing erythroid differentiation. Previous studies revealed that HSF2 consists of two alternatively spliced isoforms, HSF2-alpha and HSF2-beta, whose relative abundance is developmentally regulated and varies between different tissues. To investigate whether the molar ratio of HSF2-alpha and HSF2-beta isoforms is crucial for the activation of HSF2 and whether the HSF2 isoforms play functionally distinct roles during the hemin-mediated erythroid differentiation, we generated cell clones expressing different levels of HSF2-alpha and HSF2-beta. We show that in parental K562 cells, the HSF2-alpha isoform is predominantly expressed and HSF2 can be activated upon hemin treatment. In contrast, when HSF2-beta is expressed at levels exceeding those of endogenous HSF2-alpha, the hemin-induced DNA binding activity and transcription of heat shock genes are repressed, whereas overexpression of HSF2-alpha results in an enhanced hemin response. Furthermore, the hemin-induced accumulation of globin, known as a marker of erythroid differentiation, is decreased in cells overexpressing HSF2-beta. We suggest that HSF2-beta acts as a negative regulator of HSF2 activity during hemin-mediated erythroid differentiation of K562 cells."}