Independent function of two destruction domains in hypoxia‐inducible factor‐α chains activated by prolyl hydroxylation

By N. Masson, C. Willam, P. Maxwell, C. Pugh, P. Ratcliffe. EMBO Journal, 2001

1,106 citations recorded by the source corpus.

Subfields: Cancer Research, Molecular Biology, Oncology

View Paper: https://www.semanticscholar.org/paper/eee1c3839f985851407afcb2320c008a157307cc

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In Cancer Research

1. Carlo Maria Croce
2. George A. Calin
3. G. Semenza
4. W. Kaelin
5. Chang-Gong Liu
6. M. Ferracin
7. R. Garzon
8. H. Alder

In Molecular Biology

1. Carlo Maria Croce
2. George A. Calin
3. G. Semenza
4. W. Kaelin
5. M. Ferracin
6. Chang-Gong Liu
7. R. Garzon
8. J. Espinosa

In Oncology

1. M. Eddins
2. Carlo Maria Croce
3. J. Espinosa
4. Adrian L. Harris
5. George A. Calin
6. V. L. Dengler
7. W. Kaelin
8. M. Galbraith

Citations in the corpus

• Inhibition of HIF is necessary for tumor suppression by the von Hippel-Lindau protein. (2002, background): “…in cells, although it remains possible that some residual Lager et al., 1994; Lau et al., 1988; Mydlo et al., 1989; Nicol et interaction takes place via a recently recognized second HIF al., 1997; Reifenberger et al., 1995; Richard et al., 1998; Strathydroxylation site (Masson et al., 2001).”
• ADAPTIVE AND MALADAPTIVE CARDIORESPIRATORY RESPONSES TO CONTINUOUS AND INTERMITTENT HYPOXIA MEDIATED BY HYPOXIA-INDUCIBLE FACTORS 1 AND 2 (2012, background): “HIF-1 is also hydroxylated at proline 402 (216), which requires prior hydroxylation of Pro564 (42).”
• Inhibition of HIF2α Is Sufficient to Suppress pVHL-Defective Tumor Growth (2003, background): “O cells and A498 cells produce HIF2a and not HIF1a (Maxwell et al. 1999).”
• Hypoxia — a key regulatory factor in tumour growth (2002, background): “The enzyme, which requires oxygen, ferrous iron and 2-oxoglutarate for activity, covalently modifies HIF-1&alpha”
• Fe(II)/α-Ketoglutarate-Dependent Hydroxylases and Related Enzymes (2004, background): “The VHL protein was shown to ubiquitinylate two independently-acting sites within HIFα (Masson et al., 2001).”
• Transcriptional Regulation by Hypoxia Inducible Factors (2013, background): “Notably, some HIF3A isoforms contain only a single prolyl hydroxylation site, while others are missing this region entirely and are therefore not subject to regulation in response to oxygen.”
• Ubiquitin: structures, functions, mechanisms. (2004, background): “This proposal was confirmed by structures of a hydroxylated HIF-1a peptide bound to VHL [130,131].”
• HIF‐1α induces cell cycle arrest by functionally counteracting Myc (2004, background): “The VHL binding is controlled by hydroxylation of two proline residues in HIF- 1a: Pro-402 (Masson et al, 2001) and Pro-564 (Ivan et al, 2001; Jaakkola et al, 2001).”