Ubiquitination of hypoxia-inducible factor requires direct binding to the β-domain of the von Hippel–Lindau protein

By M. Ohh, C. Park, M. Ivan, M. Hoffman, Tae-You Kim, L. E. Huang, N. Pavletich, V. Chau, William G. Kaelin. Nature Cell Biology, 2000

1,644 citations recorded by the source corpus.

Subfields: Biochemistry, Cancer Research, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/dc4be19612c2b569b95eccc994c4cb35722f14be

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In Biochemistry

1. W. Kaelin

In Cancer Research

1. G. Semenza
2. W. Kaelin
3. P. Ratcliffe
4. Roland H. Wenger
5. M. C. Simon
6. J. Espinosa
7. V. L. Dengler
8. M. Galbraith

In Molecular Biology

1. G. Semenza
2. W. Kaelin
3. P. Ratcliffe
4. Roland H. Wenger
5. J. Espinosa
6. V. L. Dengler
7. M. Galbraith
8. W. Marston Linehan

Citations in the corpus

• Transcriptional Regulation by Hypoxia Inducible Factors (2013, background): “Proline hydroxylation allows binding of the von Hippel Lindau (VHL) E3 ubiquitin ligase complex, which polyubiquitinates the alpha subunits triggering their degradation by the proteasome (Foxler et al., 2012; Huang et al., 1998; Ohh et al., 2000; Tanimoto et al., 2000).”
• FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor. (2002, background): “…of a protein–ubiquitin ligase complex that targets the alpha subunit for degradation by the proteasome (Maxwell et al. 1999; Cockman et al. 2000; Ohh et al. 2000; Tanimoto et al. 2000). pVHL recognition of HIF- is dependent on hydroxylation of proline residues within the ODD (Ivan et al. 2001;…”
• Sequence and structural analysis of BTB domain proteins (2005, background): “This protein serves as an adaptor between ElonginB and the VHL tumor suppressor protein, which interacts with hypoxia inducible factor (HIF)-1α and targets it for degradation [89-92].”
• The General Transcription Machinery and General Cofactors (2006, background): “, 2005) and K63-linked polyubiquitin chains on the yeast plasma membrane protein uracil permease (Galan and Haguenauer-Tsapis, 1997); the pVHL complex promotes K48-linked polyubiquitination leading to HIF-1α degradation (Ohh et al., 2000); BRCA1/BARD1 enhances K6-linked polyubiquitination on nucleop”
• HIF‐1α induces cell cycle arrest by functionally counteracting Myc (2004, background): “Polyubiquitination of HIF-1a is mediated by the von Hippel-Lindau tumor suppressor (Maxwell et al, 1999; Cockman et al, 2000; Kamura et al, 2000; Ohh et al, 2000; Tanimoto et al, 2000), a part of an E3 ubiquitin ligase, that binds to the oxygen-dependent degrada- tion domain (ODD) (Huang et al,…”