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| pubmed-article:9840812 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:9840812 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:9840812 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:9840812 | pubmed:dateCreated | 1999-2-9 | lld:pubmed |
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| pubmed-article:9840812 | pubmed:abstractText | Hypoxia inducible factors (HIFs) are heterodimeric transcription factors that regulate a number of adaptive responses to low oxygen tension. They are composed of alpha- and beta-subunits that belong to the basic helix-loop-helix-PAS (bHLH-PAS) superfamily. In our efforts to identify new bHLH-PAS proteins, we cloned a cDNA encoding a novel alpha-class hypoxia inducible factor, HIF3alpha. The HIF3alpha open reading frame encodes a 662-amino acid protein with a predicted molecular weight of 73 kDa and is expressed in adult thymus, lung, brain, heart, and kidney. The N-terminal bHLH-PAS domain of this protein shares amino acid sequence identity with that of HIF1alpha and HIF2alpha (57% and 53% identity, respectively). The C-terminus of HIF3alpha contains a 36-amino acid sequence that shares 61% identity with the hypoxia responsive domain-1 (HRD1) of HIF1alpha. In transient transfections, this domain confers hypoxia responsiveness when linked to a heterologous transactivation domain. In vitro studies reveal that HIF3alpha dimerizes with a prototype beta-class subunit, ARNT, and that the resultant heterodimer recognizes the hypoxia responsive element (HRE) core sequence, TACGTG. Transient transfection experiments demonstrate that the HIF3alpha-ARNT interaction can occur in vivo, and that the activity of HIF3alpha is upregulated in response to cobalt chloride or low oxygen tension. | lld:pubmed |
| pubmed-article:9840812 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9840812 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9840812 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9840812 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9840812 | pubmed:issn | 1052-2166 | lld:pubmed |
| pubmed-article:9840812 | pubmed:author | pubmed-author:BradfieldC... | lld:pubmed |
| pubmed-article:9840812 | pubmed:author | pubmed-author:GuY ZYZ | lld:pubmed |
| pubmed-article:9840812 | pubmed:author | pubmed-author:MoranS MSM | lld:pubmed |
| pubmed-article:9840812 | pubmed:author | pubmed-author:HogeneschJ... | lld:pubmed |
| pubmed-article:9840812 | pubmed:author | pubmed-author:WartmanLL | lld:pubmed |
| pubmed-article:9840812 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9840812 | pubmed:volume | 7 | lld:pubmed |
| pubmed-article:9840812 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9840812 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9840812 | pubmed:pagination | 205-13 | lld:pubmed |
| pubmed-article:9840812 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:9840812 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9840812 | pubmed:articleTitle | Molecular characterization and chromosomal localization of a third alpha-class hypoxia inducible factor subunit, HIF3alpha. | lld:pubmed |
| pubmed-article:9840812 | pubmed:affiliation | McArdle Laboratory for Cancer Research, University of Wisconsin Medical School, Madison 53706, USA. | lld:pubmed |
| pubmed-article:9840812 | pubmed:publicationType | Journal Article | lld:pubmed |
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