A Conserved Family of Prolyl-4-Hydroxylases That Modify HIF

By R. Bruick, S. McKnight. Science, 2001

2,620 citations recorded by the source corpus.

Subfields: Cancer Research, Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/9b66c0ed5710ca90fdaab38f0f37b5c42fb6e686

How researchers see this paper

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

In Cancer Research

1. G. Semenza
2. M. C. Simon
3. Amato J. Giaccia
4. Navdeep S. Chandel
5. J. Pouysségur
6. P. Schumacker
7. N. Denko
8. R. Guzy

In Molecular Biology

1. G. Semenza
2. M. C. Simon
3. Navdeep S. Chandel
4. J. Pouysségur
5. P. Schumacker
6. Amato J. Giaccia
7. N. Denko
8. C. V. Dang

In Physiology

1. G. Semenza
2. Amato J. Giaccia
3. M. C. Simon
4. Roland H. Wenger
5. P. Schumacker
6. R. Guzy
7. Ana Samimi
8. Robert B Rucker

Citations in the corpus

• Oxygen sensing requires mitochondrial ROS but not oxidative phosphorylation. (2005, background): “HIF-1α is targeted for degradation under normoxia by a set of enzymes known as prolyl hydroxylases (PHDs) (Bruick and McKnight, 2001; Epstein et al., 2001).”
• The impact of O2 availability on human cancer (2008, background): “A family of three HIF-specific prolyl hydroxylases was subsequently identified by characterizing candidate genes that encode 2-oxoglutarate-dependent dioxygenases and by biochemical purificatio”
• Cellular adaptation to hypoxia: O2‐sensing protein hydroxylases, hypoxia‐inducible transcription factors, and O2‐regulated gene expression (2002, methodology): “The same three HIF-prolyl hydroxylases (termed HPH 3, 2, and 1, respectively) were cloned by Bruick and McKnight based on sequence similarity to collagen-modifying prolyl hydroxylases (57).”
• ADAPTIVE AND MALADAPTIVE CARDIORESPIRATORY RESPONSES TO CONTINUOUS AND INTERMITTENT HYPOXIA MEDIATED BY HYPOXIA-INDUCIBLE FACTORS 1 AND 2 (2012, background): “Three prolyl-4-hydroxylase domain proteins (PHDs) that hydroxylate proline-564 in an O2-dependent manner were identified in mammalian cells (28, 80, 133).”
• FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor. (2002, background): “Indeed, suppression of the inhibitory effects of the HIF prolyl hydroxylase on HIF activity has been observed under hypoxic conditions (Bruick and McKnight 2001).”
• HIF-1 mediates adaptation to hypoxia by actively downregulating mitochondrial oxygen consumption. (2006, background): “VHL then recognizes the modified HIF-a proteins, acts as an E3-type of ubiquitin ligase, and along with elongins B and C is responsible for the polyubiquitination of HIF-as and their proteosomal degradation (Bruick and McKnight, 2001; Chan et al., 2002; Ivan et al., 2001; Jaakkola et al., 2001).”
• Targeting HIF-1 for cancer therapy (2003, background): “Three prolyl hydroxylases — known as prolyl hydroxylase-domain protein (PHD) 1–3, or, alternatively, as HIF-1 prolyl hydroxylase (HPH) 1–3 — modify proline(Pro)-402 and -564 of HIF-1&alpha”