PubMed:9119228 JSONTXT

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    relna

    {"project":"relna","denotations":[{"id":"T1","span":{"begin":0,"end":3},"obj":"Protein"},{"id":"T2","span":{"begin":40,"end":45},"obj":"DNA"},{"id":"T3","span":{"begin":50,"end":55},"obj":"DNA"},{"id":"T4","span":{"begin":73,"end":81},"obj":"Protein"},{"id":"T5","span":{"begin":101,"end":106},"obj":"DNA"},{"id":"T6","span":{"begin":199,"end":208},"obj":"Protein"},{"id":"T7","span":{"begin":328,"end":333},"obj":"DNA"},{"id":"T8","span":{"begin":641,"end":644},"obj":"Protein"},{"id":"T9","span":{"begin":654,"end":659},"obj":"DNA"},{"id":"T10","span":{"begin":681,"end":684},"obj":"Protein"},{"id":"T11","span":{"begin":790,"end":795},"obj":"DNA"},{"id":"T12","span":{"begin":800,"end":805},"obj":"DNA"},{"id":"T13","span":{"begin":807,"end":817},"obj":"DNA"},{"id":"T14","span":{"begin":819,"end":833},"obj":"DNA"},{"id":"T15","span":{"begin":918,"end":921},"obj":"Protein"},{"id":"T16","span":{"begin":955,"end":960},"obj":"DNA"},{"id":"T17","span":{"begin":997,"end":1000},"obj":"Protein"},{"id":"T18","span":{"begin":1139,"end":1142},"obj":"Protein"},{"id":"T19","span":{"begin":1246,"end":1251},"obj":"DNA"},{"id":"T20","span":{"begin":1253,"end":1256},"obj":"Protein"},{"id":"T21","span":{"begin":1426,"end":1429},"obj":"Protein"}],"relations":[{"id":"R0","pred":"linked","subj":"T1","obj":"T2"},{"id":"R1","pred":"linked","subj":"T1","obj":"T3"},{"id":"R2","pred":"linked","subj":"T5","obj":"T6"},{"id":"R3","pred":"linked","subj":"T8","obj":"T9"}],"text":"ALY, a context-dependent coactivator of LEF-1 and AML-1, is required for TCRalpha enhancer function.\nLEF-1 is a transcription factor that participates in the regulation of the T-cell receptor alpha (TCR alpha) enhancer by facilitating the assembly of multiple proteins into a higher order nucleoprotein complex. The function of LEF-1 is dependent, in part, on the HMG domain that induces a sharp bend in the DNA helix, and on an activation domain that stimulates transcription only in a specific context of other enhancer-binding proteins. With the aim of gaining insight into the function of context-dependent activation domains, we cloned ALY, a novel LEF-1-interacting protein. ALY is a ubiquitously expressed, nuclear protein that specifically associates with the activation domains of LEF-1 and AML-1 (CBF alpha2, PEBP2 alpha(B), which is another protein component of the TCR alpha enhancer complex. In addition, ALY can increase DNA binding by both LEF-1 and AML proteins. Overexpression of ALY stimulates the activity of the TCR alpha enhancer complex reconstituted in transfected nonlymphoid HeLa cells, whereas down-regulation of ALY by anti-sense oligonucleotides virtually eliminates TCR alpha enhancer activity in T cells. Similar to LEF-1, ALY can stimulate transcription in the context of the TCR alpha enhancer but apparently not when tethered to DNA through an heterologous DNA-binding domain. We propose that ALY mediates context-dependent transcriptional activation by facilitating the functional collaboration of multiple proteins in the TCR alpha enhancer complex."}

    jnlpba-st-training

    {"project":"jnlpba-st-training","denotations":[{"id":"T1","span":{"begin":0,"end":3},"obj":"protein"},{"id":"T2","span":{"begin":7,"end":36},"obj":"protein"},{"id":"T3","span":{"begin":40,"end":45},"obj":"protein"},{"id":"T4","span":{"begin":50,"end":55},"obj":"protein"},{"id":"T5","span":{"begin":73,"end":90},"obj":"DNA"},{"id":"T6","span":{"begin":101,"end":106},"obj":"protein"},{"id":"T7","span":{"begin":176,"end":218},"obj":"DNA"},{"id":"T8","span":{"begin":251,"end":268},"obj":"protein"},{"id":"T9","span":{"begin":289,"end":310},"obj":"protein"},{"id":"T10","span":{"begin":328,"end":333},"obj":"protein"},{"id":"T11","span":{"begin":364,"end":374},"obj":"protein"},{"id":"T12","span":{"begin":429,"end":446},"obj":"protein"},{"id":"T13","span":{"begin":513,"end":538},"obj":"protein"},{"id":"T14","span":{"begin":593,"end":629},"obj":"protein"},{"id":"T15","span":{"begin":641,"end":644},"obj":"protein"},{"id":"T16","span":{"begin":654,"end":679},"obj":"protein"},{"id":"T17","span":{"begin":681,"end":684},"obj":"protein"},{"id":"T18","span":{"begin":768,"end":786},"obj":"protein"},{"id":"T19","span":{"begin":790,"end":795},"obj":"protein"},{"id":"T20","span":{"begin":800,"end":805},"obj":"protein"},{"id":"T21","span":{"begin":807,"end":817},"obj":"protein"},{"id":"T22","span":{"begin":819,"end":830},"obj":"protein"},{"id":"T23","span":{"begin":877,"end":903},"obj":"protein"},{"id":"T24","span":{"begin":918,"end":921},"obj":"protein"},{"id":"T25","span":{"begin":955,"end":960},"obj":"protein"},{"id":"T26","span":{"begin":965,"end":977},"obj":"protein"},{"id":"T27","span":{"begin":997,"end":1000},"obj":"protein"},{"id":"T28","span":{"begin":1032,"end":1058},"obj":"protein"},{"id":"T29","span":{"begin":1076,"end":1110},"obj":"cell_line"},{"id":"T30","span":{"begin":1139,"end":1142},"obj":"protein"},{"id":"T31","span":{"begin":1195,"end":1213},"obj":"DNA"},{"id":"T32","span":{"begin":1226,"end":1233},"obj":"cell_type"},{"id":"T33","span":{"begin":1246,"end":1251},"obj":"protein"},{"id":"T34","span":{"begin":1253,"end":1256},"obj":"protein"},{"id":"T35","span":{"begin":1307,"end":1325},"obj":"DNA"},{"id":"T36","span":{"begin":1377,"end":1408},"obj":"protein"},{"id":"T37","span":{"begin":1426,"end":1429},"obj":"protein"},{"id":"T38","span":{"begin":1532,"end":1549},"obj":"protein"},{"id":"T39","span":{"begin":1557,"end":1583},"obj":"protein"}],"text":"ALY, a context-dependent coactivator of LEF-1 and AML-1, is required for TCRalpha enhancer function.\nLEF-1 is a transcription factor that participates in the regulation of the T-cell receptor alpha (TCR alpha) enhancer by facilitating the assembly of multiple proteins into a higher order nucleoprotein complex. The function of LEF-1 is dependent, in part, on the HMG domain that induces a sharp bend in the DNA helix, and on an activation domain that stimulates transcription only in a specific context of other enhancer-binding proteins. With the aim of gaining insight into the function of context-dependent activation domains, we cloned ALY, a novel LEF-1-interacting protein. ALY is a ubiquitously expressed, nuclear protein that specifically associates with the activation domains of LEF-1 and AML-1 (CBF alpha2, PEBP2 alpha(B), which is another protein component of the TCR alpha enhancer complex. In addition, ALY can increase DNA binding by both LEF-1 and AML proteins. Overexpression of ALY stimulates the activity of the TCR alpha enhancer complex reconstituted in transfected nonlymphoid HeLa cells, whereas down-regulation of ALY by anti-sense oligonucleotides virtually eliminates TCR alpha enhancer activity in T cells. Similar to LEF-1, ALY can stimulate transcription in the context of the TCR alpha enhancer but apparently not when tethered to DNA through an heterologous DNA-binding domain. We propose that ALY mediates context-dependent transcriptional activation by facilitating the functional collaboration of multiple proteins in the TCR alpha enhancer complex."}

    genia-medco-coref

    {"project":"genia-medco-coref","denotations":[{"id":"C1","span":{"begin":0,"end":3},"obj":"NP"},{"id":"C3","span":{"begin":40,"end":45},"obj":"NP"},{"id":"C4","span":{"begin":50,"end":55},"obj":"NP"},{"id":"C2","span":{"begin":5,"end":55},"obj":"NP"},{"id":"C5","span":{"begin":101,"end":106},"obj":"NP"},{"id":"C6","span":{"begin":110,"end":132},"obj":"NP"},{"id":"C7","span":{"begin":133,"end":137},"obj":"NP"},{"id":"C8","span":{"begin":172,"end":218},"obj":"NP"},{"id":"C9","span":{"begin":328,"end":333},"obj":"NP"},{"id":"C10","span":{"begin":360,"end":374},"obj":"NP"},{"id":"C11","span":{"begin":375,"end":379},"obj":"NP"},{"id":"C12","span":{"begin":426,"end":446},"obj":"NP"},{"id":"C13","span":{"begin":447,"end":451},"obj":"NP"},{"id":"C14","span":{"begin":641,"end":644},"obj":"NP"},{"id":"C15","span":{"begin":646,"end":679},"obj":"NP"},{"id":"C16","span":{"begin":681,"end":684},"obj":"NP"},{"id":"C17","span":{"begin":688,"end":729},"obj":"NP"},{"id":"C18","span":{"begin":730,"end":734},"obj":"NP"},{"id":"C19","span":{"begin":790,"end":795},"obj":"NP"},{"id":"C20","span":{"begin":800,"end":805},"obj":"NP"},{"id":"C21","span":{"begin":835,"end":840},"obj":"NP"},{"id":"C22","span":{"begin":873,"end":903},"obj":"NP"},{"id":"C23","span":{"begin":918,"end":921},"obj":"NP"},{"id":"C24","span":{"begin":997,"end":1000},"obj":"NP"},{"id":"C25","span":{"begin":1028,"end":1058},"obj":"NP"},{"id":"C26","span":{"begin":1139,"end":1142},"obj":"NP"},{"id":"C27","span":{"begin":1246,"end":1251},"obj":"NP"},{"id":"C28","span":{"begin":1253,"end":1256},"obj":"NP"},{"id":"C29","span":{"begin":1303,"end":1325},"obj":"NP"},{"id":"C30","span":{"begin":1426,"end":1429},"obj":"NP"},{"id":"C31","span":{"begin":1553,"end":1583},"obj":"NP"}],"relations":[{"id":"R1","pred":"coref-appos","subj":"C2","obj":"C1"},{"id":"R2","pred":"coref-ident","subj":"C5","obj":"C3"},{"id":"R3","pred":"coref-relat","subj":"C7","obj":"C6"},{"id":"R4","pred":"coref-ident","subj":"C9","obj":"C5"},{"id":"R5","pred":"coref-relat","subj":"C11","obj":"C10"},{"id":"R6","pred":"coref-relat","subj":"C13","obj":"C12"},{"id":"R7","pred":"coref-ident","subj":"C14","obj":"C1"},{"id":"R8","pred":"coref-appos","subj":"C15","obj":"C14"},{"id":"R9","pred":"coref-ident","subj":"C16","obj":"C14"},{"id":"R10","pred":"coref-relat","subj":"C18","obj":"C17"},{"id":"R11","pred":"coref-ident","subj":"C19","obj":"C9"},{"id":"R12","pred":"coref-ident","subj":"C20","obj":"C4"},{"id":"R13","pred":"coref-relat","subj":"C21","obj":"C20"},{"id":"R14","pred":"coref-ident","subj":"C23","obj":"C16"},{"id":"R15","pred":"coref-ident","subj":"C24","obj":"C23"},{"id":"R16","pred":"coref-ident","subj":"C25","obj":"C22"},{"id":"R17","pred":"coref-ident","subj":"C26","obj":"C24"},{"id":"R18","pred":"coref-ident","subj":"C27","obj":"C19"},{"id":"R19","pred":"coref-ident","subj":"C28","obj":"C26"},{"id":"R20","pred":"coref-ident","subj":"C29","obj":"C8"},{"id":"R21","pred":"coref-ident","subj":"C30","obj":"C28"},{"id":"R22","pred":"coref-ident","subj":"C31","obj":"C25"}],"text":"ALY, a context-dependent coactivator of LEF-1 and AML-1, is required for TCRalpha enhancer function.\nLEF-1 is a transcription factor that participates in the regulation of the T-cell receptor alpha (TCR alpha) enhancer by facilitating the assembly of multiple proteins into a higher order nucleoprotein complex. The function of LEF-1 is dependent, in part, on the HMG domain that induces a sharp bend in the DNA helix, and on an activation domain that stimulates transcription only in a specific context of other enhancer-binding proteins. With the aim of gaining insight into the function of context-dependent activation domains, we cloned ALY, a novel LEF-1-interacting protein. ALY is a ubiquitously expressed, nuclear protein that specifically associates with the activation domains of LEF-1 and AML-1 (CBF alpha2, PEBP2 alpha(B), which is another protein component of the TCR alpha enhancer complex. In addition, ALY can increase DNA binding by both LEF-1 and AML proteins. Overexpression of ALY stimulates the activity of the TCR alpha enhancer complex reconstituted in transfected nonlymphoid HeLa cells, whereas down-regulation of ALY by anti-sense oligonucleotides virtually eliminates TCR alpha enhancer activity in T cells. Similar to LEF-1, ALY can stimulate transcription in the context of the TCR alpha enhancer but apparently not when tethered to DNA through an heterologous DNA-binding domain. We propose that ALY mediates context-dependent transcriptional activation by facilitating the functional collaboration of multiple proteins in the TCR alpha enhancer complex."}

    pubmed-sentences-benchmark

    {"project":"pubmed-sentences-benchmark","denotations":[{"id":"S1","span":{"begin":0,"end":100},"obj":"Sentence"},{"id":"S2","span":{"begin":101,"end":311},"obj":"Sentence"},{"id":"S3","span":{"begin":312,"end":539},"obj":"Sentence"},{"id":"S4","span":{"begin":540,"end":680},"obj":"Sentence"},{"id":"S5","span":{"begin":681,"end":904},"obj":"Sentence"},{"id":"S6","span":{"begin":905,"end":978},"obj":"Sentence"},{"id":"S7","span":{"begin":979,"end":1234},"obj":"Sentence"},{"id":"S8","span":{"begin":1235,"end":1409},"obj":"Sentence"},{"id":"S9","span":{"begin":1410,"end":1584},"obj":"Sentence"}],"text":"ALY, a context-dependent coactivator of LEF-1 and AML-1, is required for TCRalpha enhancer function.\nLEF-1 is a transcription factor that participates in the regulation of the T-cell receptor alpha (TCR alpha) enhancer by facilitating the assembly of multiple proteins into a higher order nucleoprotein complex. The function of LEF-1 is dependent, in part, on the HMG domain that induces a sharp bend in the DNA helix, and on an activation domain that stimulates transcription only in a specific context of other enhancer-binding proteins. With the aim of gaining insight into the function of context-dependent activation domains, we cloned ALY, a novel LEF-1-interacting protein. ALY is a ubiquitously expressed, nuclear protein that specifically associates with the activation domains of LEF-1 and AML-1 (CBF alpha2, PEBP2 alpha(B), which is another protein component of the TCR alpha enhancer complex. In addition, ALY can increase DNA binding by both LEF-1 and AML proteins. Overexpression of ALY stimulates the activity of the TCR alpha enhancer complex reconstituted in transfected nonlymphoid HeLa cells, whereas down-regulation of ALY by anti-sense oligonucleotides virtually eliminates TCR alpha enhancer activity in T cells. Similar to LEF-1, ALY can stimulate transcription in the context of the TCR alpha enhancer but apparently not when tethered to DNA through an heterologous DNA-binding domain. We propose that ALY mediates context-dependent transcriptional activation by facilitating the functional collaboration of multiple proteins in the TCR alpha enhancer complex."}

    GENIAcorpus

    {"project":"GENIAcorpus","denotations":[{"id":"T1","span":{"begin":0,"end":3},"obj":"protein_molecule"},{"id":"T2","span":{"begin":7,"end":36},"obj":"protein_family_or_group"},{"id":"T3","span":{"begin":40,"end":45},"obj":"protein_molecule"},{"id":"T4","span":{"begin":50,"end":55},"obj":"protein_molecule"},{"id":"T5","span":{"begin":73,"end":90},"obj":"DNA_domain_or_region"},{"id":"T6","span":{"begin":101,"end":106},"obj":"protein_molecule"},{"id":"T7","span":{"begin":176,"end":218},"obj":"DNA_domain_or_region"},{"id":"T8","span":{"begin":251,"end":268},"obj":"protein_family_or_group"},{"id":"T9","span":{"begin":289,"end":310},"obj":"protein_complex"},{"id":"T10","span":{"begin":328,"end":333},"obj":"protein_molecule"},{"id":"T11","span":{"begin":364,"end":374},"obj":"protein_domain_or_region"},{"id":"T12","span":{"begin":429,"end":446},"obj":"protein_domain_or_region"},{"id":"T13","span":{"begin":513,"end":538},"obj":"protein_family_or_group"},{"id":"T14","span":{"begin":593,"end":629},"obj":"protein_domain_or_region"},{"id":"T15","span":{"begin":641,"end":644},"obj":"protein_molecule"},{"id":"T16","span":{"begin":654,"end":659},"obj":"protein_family_or_group"},{"id":"T17","span":{"begin":681,"end":684},"obj":"protein_molecule"},{"id":"T18","span":{"begin":768,"end":786},"obj":"protein_domain_or_region"},{"id":"T19","span":{"begin":790,"end":795},"obj":"protein_molecule"},{"id":"T20","span":{"begin":800,"end":805},"obj":"protein_molecule"},{"id":"T21","span":{"begin":807,"end":817},"obj":"protein_molecule"},{"id":"T22","span":{"begin":819,"end":830},"obj":"protein_molecule"},{"id":"T23","span":{"begin":877,"end":903},"obj":"protein_complex"},{"id":"T24","span":{"begin":918,"end":921},"obj":"protein_molecule"},{"id":"T25","span":{"begin":955,"end":960},"obj":"protein_molecule"},{"id":"T26","span":{"begin":965,"end":977},"obj":"protein_family_or_group"},{"id":"T27","span":{"begin":997,"end":1000},"obj":"protein_molecule"},{"id":"T28","span":{"begin":1032,"end":1058},"obj":"protein_complex"},{"id":"T29","span":{"begin":1076,"end":1110},"obj":"cell_line"},{"id":"T30","span":{"begin":1139,"end":1142},"obj":"protein_molecule"},{"id":"T31","span":{"begin":1195,"end":1213},"obj":"DNA_domain_or_region"},{"id":"T32","span":{"begin":1226,"end":1233},"obj":"cell_type"},{"id":"T33","span":{"begin":1246,"end":1251},"obj":"protein_molecule"},{"id":"T34","span":{"begin":1253,"end":1256},"obj":"protein_molecule"},{"id":"T35","span":{"begin":1307,"end":1325},"obj":"DNA_domain_or_region"},{"id":"T36","span":{"begin":1377,"end":1408},"obj":"protein_domain_or_region"},{"id":"T37","span":{"begin":1426,"end":1429},"obj":"protein_molecule"},{"id":"T38","span":{"begin":1439,"end":1483},"obj":"other_name"},{"id":"T39","span":{"begin":1532,"end":1549},"obj":"protein_family_or_group"},{"id":"T40","span":{"begin":1557,"end":1575},"obj":"DNA_domain_or_region"}],"text":"ALY, a context-dependent coactivator of LEF-1 and AML-1, is required for TCRalpha enhancer function.\nLEF-1 is a transcription factor that participates in the regulation of the T-cell receptor alpha (TCR alpha) enhancer by facilitating the assembly of multiple proteins into a higher order nucleoprotein complex. The function of LEF-1 is dependent, in part, on the HMG domain that induces a sharp bend in the DNA helix, and on an activation domain that stimulates transcription only in a specific context of other enhancer-binding proteins. With the aim of gaining insight into the function of context-dependent activation domains, we cloned ALY, a novel LEF-1-interacting protein. ALY is a ubiquitously expressed, nuclear protein that specifically associates with the activation domains of LEF-1 and AML-1 (CBF alpha2, PEBP2 alpha(B), which is another protein component of the TCR alpha enhancer complex. In addition, ALY can increase DNA binding by both LEF-1 and AML proteins. Overexpression of ALY stimulates the activity of the TCR alpha enhancer complex reconstituted in transfected nonlymphoid HeLa cells, whereas down-regulation of ALY by anti-sense oligonucleotides virtually eliminates TCR alpha enhancer activity in T cells. Similar to LEF-1, ALY can stimulate transcription in the context of the TCR alpha enhancer but apparently not when tethered to DNA through an heterologous DNA-binding domain. We propose that ALY mediates context-dependent transcriptional activation by facilitating the functional collaboration of multiple proteins in the TCR alpha enhancer complex."}