Faculty Opinions recommendation of Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation.

By P. O’Farrell. 2001

1,008 citations recorded by the source corpus.

Subfields: Cancer Research, Molecular Biology, Surgery

View Paper: https://www.semanticscholar.org/paper/7a06410b9371e5652f62f0e718fdaa040b629a2b

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Citations in the corpus

Heme oxygenase-1/carbon monoxide: from basic science to therapeutic applications. (2006, background): “Recently, it has been discovered that the prolyl hydroxylase activity responsible for basal degradation of HIF-1 requires iron for activity (275, 276).”
Hypoxia-Inducible Factor 1 and Dysregulated c-Myc Cooperatively Induce Vascular Endothelial Growth Factor and Metabolic Switches Hexokinase 2 and Pyruvate Dehydrogenase Kinase 1 (2007, background): “Oxygen regulation of HIF-1 levels depends on the HIF-1 oxygen-dependent domain, which contains two prolyl residues (402 and 564), which are hydroxylated by prolyl hydroxylase in the presence of oxygen (4, 33, 34, 52, 70, 73).”
RING domain E3 ubiquitin ligases. (2009, background): “Indeed, the vast majority of CRL substrates are targeted to their respective ligase by a covalent modification, including glycosylation (117) and proline hydroxylation (118, 119).”
The role of hypoxia-inducible factors in tumorigenesis (2008, background): “Hydroxylation of conserved proline residues within the HIF-a ODD by prolyl-4hydroxylase domain (PHD)-containing proteins mediates pVHL binding and degradation.(20,21) Under hypoxia, HIF-a subunits are stabilized and translocate to the nucleus, where they heterodimerize with ARNT and bind to HREs loc”
Regulation of Hypoxia-Inducible Factor 1α Expression and Function by the Mammalian Target of Rapamycin (2002, background): “The first pathway is triggered by hypoxia or CoCl2 and involves the inhibition of a family of PHDs that modify Pro-564 and Pro-402 of HIF-1 (5, 21, 22, 27, 41).”
Hypoxia-Inducible Factor-1 (HIF-1) (2006, positive): “2-OG analogs can increase the half-life of HIF-1 (Jaakkola et al., 2001; Ivan et al., 2002).”
The Distinct Metabolic Profile of Hematopoietic Stem Cells Reflects Their Location in a Hypoxic Niche (2010, background): “Hif-1a undergoes hydroxylation, followed by ubiquitination and degradation during normoxia in most cells (Ivan et al., 2001; Jaakkola et al., 2001; Kamura et al., 2000; Maxwell et al., 1999; Salceda and Caro, 1997).”
Mitochondrial complex III is required for hypoxia-induced ROS production and cellular oxygen sensing. (2005, positive): “HIF-α is degraded under normoxia following proline hydroxylation by prolyl hydroxylases (PHDs; Jaakkola et al., 2001; Ivan et al., 2001).”
Redox Regulation of Cell Survival (2008, positive): “The hydroxylated HIF is then recognized by the von Hippel–Lindau (VHL) ubiquitin E3 ligase complex, which promotes the degradation of HIF-1 by the 26S proteosome (134).”
Vitamins C and E: Beneficial effects from a mechanistic perspective (2011, background): “Under normoxic conditions, the HIF-1α subunit is targeted for degradation by HIFspecific prolyl hydroxylases that hydroxylate HIF-1α at proline residues 402 and564 [22].”
Hypoxia inducible mir-210 regulates normoxic gene expression involved in tumor initiation (2009, positive): “Under normoxic conditions, the a subunit of HIF1 is hydroxylated at prolines 402 and 564 by prolyl-4-hydroxylases (PHDs), targeting HIF1a for proteasome destruction mediated by the von Hippel-Lindau (VHL) protein, an E3 ubiquitin ligase (Chan et al., 2005; Ivan et al., 2001; Jaakkola et al., 2001).”
Therapeutic targeting of hypoxia and hypoxia-inducible factors in cancer. (2016, background): “In the presence of oxygen, conserved proline residues on the α-subunit are hydroxylated, promoting its degradation (Ivan et al., 2001; Jaakkola et al., 2001).”