Oxygen sensing by HIF hydroxylases

By Christopher J. Schofield, P. Ratcliffe. Nature reviews. Molecular cell biology, 2004

2,112 citations recorded by the source corpus.

Subfields: Cancer Research, Cell Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/17237b87d7ea79ae6e18c24d4de83bfeffbd7c2e

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Citations in the corpus

Binding of Natively Unfolded HIF-1α ODD Domain to p53 (2005, background): “bicity H and the mean net charge R were calcu- Conformation can also be induced by changes in the environment such as pH, temperature, ionic strength, lated as in Uversky et al. (2000). The values are 0.”
Tumour hypoxia induces a metabolic shift causing acidosis: a common feature in cancer (2009, background): “Three isoforms of the -subunit (HIF-1 , HIF-2 , HIF-3 ) and two isoforms of the -subunit have been described to contribute to the in vivo response to hypoxia [91, 92].”
Vascular endothelial growth factor in eye disease. (2008, background): “Under normoxic conditions, HIF-1α is inactivated and targeted for proteasomal degradation by hydroxylation, whereas under hypoxic conditions the specific hydroxylases are inhibited, resulting in the rescue of HIF-1α from degradation (Schofield and Ratcliffe, 2004).”
The unfolded protein response protects human tumor cells during hypoxia through regulation of the autophagy genes MAP1LC3B and ATG5. (2010, background): “This includes activation of the HIF transcription factors (HIF1, HIF2, HIF3), which induce a large number of genes involved in glycolysis, angiogenesis, pH regulation, and cell motility (6, 9).”
Hypoxia and cancer (2007, background): “A broad range of genes that are implicated in events such as angiogenesis, cell survival/death, metabolism, pH regulation, adhesion, extracellular matrix remodeling, migration and metastasis are targeted [12, 15, 17, 18].”
HIF-1-mediated expression of pyruvate dehydrogenase kinase: a metabolic switch required for cellular adaptation to hypoxia. (2006, background): “HIF-1 is a heterodimeric transcription factor, consisting of HIF1a and HIF-1b subunits, which functions as a master regulator of oxygen homeostasis in all metazoan species (Schofield and Ratcliffe, 2004; Semenza, 2004).”
Metalloproteins and metal sensing (2009, background): “Cobalt mimics hypoxia in humans possibly because cobalt replaces iron in prolyl 4-hydroxylase, which in iron-form hydroxylates the hypoxia-responsive transcription factor HIF1 (also known as HIF1A”
hsa-miR-210 Is Induced by Hypoxia and Is an Independent Prognostic Factor in Breast Cancer (2008, neutral): “org Clin Cancer Res 2008;14(5) March1, 2008 1343”
Oxygen sensing requires mitochondrial ROS but not oxidative phosphorylation. (2005, background): “The recent discovery that hydroxylation of proline residues by prolyl hydroxylases regulate the stabilization of HIF-1α protein has raised the possibility that the hydroxylases themselves serve as oxygen sensors regulating HIF-dependent gene expression (Kaelin, 2002; Schofield and Ratcliffe, 2004).”
Hypoxic microenvironment in cancer: molecular mechanisms and therapeutic interventions (2023, background): “The accumulated HIF-1α binds to HIF-1β and enters the nucleus to bind the hypoxia response element (HRE) in the promoter region of the target gene to reduce cellular oxygen consumption.(92,93) HIF-3α exerts the opposite effects in cancer cells by impairing angiogenesis, proliferation, and metabolism”
Vitamins C and E: Beneficial effects from a mechanistic perspective (2011, background): “Vitamin C as a regulator of hypoxia-inducible factor (HIF)-1 Vitamin C-dependent proline hydroxylation also plays a role in gene transcriptionmediated by HIF-1 [20,21].”