FIH-1: a novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity.

By P. Mahon, K. Hirota, G. Semenza. Genes & Development, 2001

1,231 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/8f68866afc121c8bdfbedae95da13d058b3cd68f

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

1. G. Semenza
2. Erinn B. Rankin
3. Amato J. Giaccia
4. Robert P. Hausinger
5. Richard J. Johnson
6. V. L. Dengler
7. D. Lando
8. J. Richards

Citations in the corpus

• FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor. (2002, background): “Although the two modes of regulation can be apparently uncoupled from each other through the construction of chimeras containing either the ODD or the CAD, the machinery regulating the two appears to be linked (Mahon et al. 2001).”
• Fe(II)/α-Ketoglutarate-Dependent Hydroxylases and Related Enzymes (2004, methodology): “A yeast two-hybrid approach was used to identify the HIFα-specific asparaginyl hydroxylase that was shown to be identical to the “factor-inhibiting HIF” (FIH), a protein known to interact with HIFα and VHL and to repress HIF transcriptional activity (Hewitson et al., 2002; Mahon et al., 2001).”
• Hypoxia-induced angiogenesis: good and evil. (2011, background): “For instance, factor-inhibiting HIF-1α (FIH-1), another Fe(II) and 2-oxoglutarate-dependent dioxygenase, hydroxylates a conserved asparaginyl residue in the C-TAD of HIF-α, which inhibits binding to p300 and CBP.(20) HIF-α is also modified by acetylation,(21) phosphorylation,(22,23) sumoylation,(24-”
• The role of hypoxia-inducible factors in tumorigenesis (2008, background): “FIH hydroxylates asparagine residues located within the HIF-a C-terminal transactivation domain (CTAD) and prevents p300/CBP binding.(23) Thus, full activation of HIF transcriptional activity requires both HIFa stabilization and CTAD activation (Figure 2).”
• Hypoxia-Inducible Factor-1 (HIF-1) (2006, unknown): “Unraveling such questions should provide new insights into cellular adaptation to hypoxia and aid to discover new therapeutic approaches to diverse human diseases.”
• Chapter 10 Metabolic and Molecular Responses of Fish to Hypoxia (2009, methodology): “The O2-dependent control of HIF a is provided by the actions of two proteins, prolyl hydroxylase (PHDs) and factor inhibiting HIF (FIH; Mahon et al., 2001), both of which are members of the 2- oxoglutarate-dependent dioxygenase superfamily of hydroxylases.”
• Oncometabolite 2-Hydroxyglutarate Is a Competitive Inhibitor of α-Ketoglutarate-Dependent Dioxygenases (2011, unknown): “In addition to PHDs, the stability and steady-state levels of HIF-1a protein are also regulated by FIH-1 (factor inhibiting HIF-1a) (Lando et al., 2002; Mahon et al., 2001), an asparaginyl hydrogenase whose activity is dependent on a-KG and could therefore also be affected by reduced function of IDH”
• Hypoxia-Inducible Factors in Physiology and Medicine (2012, unknown): “Factor-inhibiting HIF-1 (FIH-1) represses HIF-1a transactivation function (Mahon et al., 2001).”