Activation of HIF1alpha ubiquitination by a reconstituted von Hippel-Lindau (VHL) tumor suppressor complex.

By T. Kamura, S. Sato, K. Iwai, M. Czyzyk-Krzeska, R. Conaway, J. Conaway. Proceedings of the National Academy of Sciences of the United States of America, 2000

701 citations recorded by the source corpus.

Subfields: Cancer Research, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/206bacea3fb047a38f06b2a00fed987ac6c5022e

How researchers see this paper

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In Cancer Research

1. G. Semenza
2. W. Kaelin
3. Ralph J. Deberardinis
4. Richard J. Johnson
5. Amato J. Giaccia
6. N. Prabhakar
7. Mirna Lechpammer
8. K. Kondo

In Molecular Biology

1. G. Semenza
2. W. Kaelin
3. Ralph J. Deberardinis
4. Aaron Ciechanover
5. Richard J. Johnson
6. Amato J. Giaccia
7. N. Prabhakar
8. Mirna Lechpammer

Citations in the corpus

• Molecular basis of the VHL hereditary cancer syndrome (2002, background): “On the basis of this lead, several groups went on to show that the pVHL β-domain binds directly to the HIF-α subunits and that pVHL is indeed capable of directing the polyubiquitylation, and hence destruction, of the HIF-α subunit”
• The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. (2002, background): “It has been recently shown that pVHL is a ubiquitin ligase (196, 276) that is involved in targeting of HIF1- for ubiquitin- and proteasome-mediated degradation (219, 220, 299) after specific recognition of oxygeninduced hydroxylated Pro residue (195, 197) (see also sect.”
• 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).”
• Hypoxia-Inducible Factor-1 (HIF-1) (2006, background): “this multiprotein E3 complex causes polyubiquitination of HIF-1α, ultimately leading to its degradation by the proteasome (Kamura et al., 2000).”
• Ubiquitin and proteasomes: Themes and variations on ubiquitylation (2001, background): “cgi?l=7422">VEGF ), providing an explanation for the highly vascular nature of the clear cell renal carcinomas seen in VHL diseas”
• HIF-1 as a target for drug development (2003, background): “By contrast, the β-domain of VHL directly interacts with HIF-1&alpha”
• Targeting HIF-1 for cancer therapy (2003, background): “VHL is the recognition component of an E3 ubiquitin-protein ligase that targets HIF-1α for proteasomal degradatio”
• ADAPTIVE AND MALADAPTIVE CARDIORESPIRATORY RESPONSES TO CONTINUOUS AND INTERMITTENT HYPOXIA MEDIATED BY HYPOXIA-INDUCIBLE FACTORS 1 AND 2 (2012, background): “, HIF-1 and HIF-2 ) are bound by the von Hippel-Lindau protein (VHL), which recruits an E3-ubiquitin protein ligase consisting of Elongin 2, Elongin 3, Cullin 2, and RBX1 that is capable of functioning with E1-ubiquitin-activating and E2-ubiquitin-conjugating enzymes to mediate the ubiquitination of”