| pubmed-article:9890965 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9890965 | lifeskim:mentions | umls-concept:C0014257 | lld:lifeskim |
| pubmed-article:9890965 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:9890965 | lifeskim:mentions | umls-concept:C0030125 | lld:lifeskim |
| pubmed-article:9890965 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:9890965 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:9890965 | lifeskim:mentions | umls-concept:C1707455 | lld:lifeskim |
| pubmed-article:9890965 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:9890965 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:9890965 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:9890965 | pubmed:dateCreated | 1999-2-16 | lld:pubmed |
| pubmed-article:9890965 | pubmed:abstractText | Endothelial PAS protein 1 (EPAS1) is a basic helix-loop-helix Per-AHR-ARNT-Sim transcription factor related to hypoxia-inducible factor-1alpha (HIF-1alpha). To analyze EPAS1 domains responsible for transactivation and oxygen-regulated function, we constructed chimeric fusions of EPAS1 with a GAL4 DNA binding domain, plus or minus the VP16 activation domain. Two transactivation domains were defined in EPAS1; a C-terminal domain (amino acids 828-870), and a larger internal domain (amino acids 517-682). These activation domains were interspersed by functionally repressive sequences, several of which independently conveyed oxygen-regulated activity. Two types of activity were defined. Sequences lying N-terminal to and overlapping the internal transactivation domain conferred regulated repression on the VP16 transactivator. Sequences lying C-terminal to this internal domain conveyed repression and oxygen-regulated activity on the native EPAS1 C-terminal activation domain, but not the Gal/VP16 fusion. Fusions containing internal but not C-terminal regulatory domains manifested regulation of fusion protein level. Comparison of EPAS1 with HIF-1alpha demonstrated a similar organization for both proteins, and for the C terminus defined a conserved RLL motif critical for inducibility. Overall, EPAS1 sequences were less inducible than those of HIF-1alpha, and inducibility was strikingly reduced as their expression level was increased. Despite these quantitative differences, EPAS1 regulation appeared similar to HIF-1alpha, conforming to a model involving the modulation of both protein level and activity, through distinct internal and C-terminal domains. | lld:pubmed |
| pubmed-article:9890965 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9890965 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9890965 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9890965 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9890965 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:9890965 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:9890965 | pubmed:author | pubmed-author:RatcliffeP... | lld:pubmed |
| pubmed-article:9890965 | pubmed:author | pubmed-author:O'RourkeJ FJF | lld:pubmed |
| pubmed-article:9890965 | pubmed:author | pubmed-author:PughC WCW | lld:pubmed |
| pubmed-article:9890965 | pubmed:author | pubmed-author:TianY MYM | lld:pubmed |
| pubmed-article:9890965 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9890965 | pubmed:day | 22 | lld:pubmed |
| pubmed-article:9890965 | pubmed:volume | 274 | lld:pubmed |
| pubmed-article:9890965 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9890965 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9890965 | pubmed:pagination | 2060-71 | lld:pubmed |
| pubmed-article:9890965 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:9890965 | pubmed:meshHeading | pubmed-meshheading:9890965-... | lld:pubmed |
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| pubmed-article:9890965 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:9890965 | pubmed:articleTitle | Oxygen-regulated and transactivating domains in endothelial PAS protein 1: comparison with hypoxia-inducible factor-1alpha. | lld:pubmed |
| pubmed-article:9890965 | pubmed:affiliation | Erythropoietin Group, Room 425, Institute of Molecular Medicine, John Radcliffe Hospital, Oxford, OX3 9DS, United Kingdom. | lld:pubmed |
| pubmed-article:9890965 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9890965 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:9890965 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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