Daniel J. Peet
University of Adelaide
82 Papers
364 Citations
Daniel J. Peet is an academic researcher from University of Adelaide. The author has contributed to research in topics: Hydroxylation & Transcription factor. The author has an hindex of 31, co-authored 76 publications. Previous affiliations of Daniel J. Peet include University of Texas Southwestern Medical Center & University of Melbourne.
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Papers
Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch.
TL;DR: Full induction of HIF-1α and -2α relies on the abrogation of both Pro and Asn hydroxylation, which during normoxia occur at the degradation and COOH-terminal transactivation domains, respectively.
1.6K
FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor
David Lando,Daniel J. Peet,Jeffrey J. Gorman,Dean A. Whelan,Murray L. Whitelaw,Richard K. Bruick +5 more
TL;DR: It is shown that the protein FIH-1, previously shown to interact with HIF, is an asparaginyl hydroxylase, an Fe(II)-dependent enzyme that uses molecular O(2) to modify its substrate.
Cholesterol and Bile Acid Metabolism Are Impaired in Mice Lacking the Nuclear Oxysterol Receptor LXRα
Daniel J. Peet,Stephen D. Turley,Wenzhen Ma,Bethany A. Janowski,Jean-Marc A. Lobaccaro,Robert E. Hammer,David J. Mangelsdorf +6 more
TL;DR: The existence of a physiologically significant feed-forward regulatory pathway for sterol metabolism and the role of LXR alpha as the major sensor of dietary cholesterol are established.
1.4K
The hypoxia-inducible factors: key transcriptional regulators of hypoxic responses.
TL;DR: The current understanding of these processes is summarized, and the important role of the HIFs in the pathophysiology of many human diseases is discussed.
286
Turn me on: regulating HIF transcriptional activity.
Karolina Lisy,Daniel J. Peet +1 more
TL;DR: The hypoxia-inducible factors (HIFs) are critical for cellular adaptation to limiting oxygen and regulate a wide array of genes when cued by cellular oxygen-sensing mechanisms and there are phosphorylation and nitrosylation events reported to modulate HIF transcriptional activity.