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Dimerization, DNA binding, and transactivation properties of hypoxia-inducible factor 1

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Dimerization, DNA binding, and transactivation properties of hypoxia-inducible factor 1 (English)

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5

G L Semenza

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author name string

B H Jiang

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1

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E Rue

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2

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G L Wang

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3

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R Roe

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4

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language of work or name

English

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publication date

26 July 1996

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published in

Journal of Biological Chemistry

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volume

271

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issue

30

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page(s)

17771-8

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cites work

Identification of transactivation and repression functions of the dioxin receptor and its basic helix-loop-helix/PAS partner factor Arnt: inducible versus constitutive modes of regulation

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Hypoxic Regulation of Lactate Dehydrogenase A

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Inducible operation of the erythropoietin 3' enhancer in multiple cell lines: evidence for a widespread oxygen-sensing mechanism

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The orphan receptor hepatic nuclear factor 4 functions as a transcriptional activator for tissue-specific and hypoxia-specific erythropoietin gene expression and is antagonized by EAR3/COUP-TF1.

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Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension

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Possible function of Ah receptor nuclear translocator (Arnt) homodimer in transcriptional regulation

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A nuclear factor induced by hypoxia via de novo protein synthesis binds to the human erythropoietin gene enhancer at a site required for transcriptional activation

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(Q28282227)

Dimerization, DNA binding, and transactivation properties of hypoxia-inducible factor 1

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