The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
A Gain-of-Function Mutation in the HIF2A Gene in Familial Erythrocytosis
Open accessAbstract
Hypoxia-inducible factor (HIF) alpha, which has three isoforms, is central to the continuous balancing of the supply and demand of oxygen throughout the body. HIF-alpha is a transcription factor that modulates a wide range of processes, including erythropoiesis, angiogenesis, and cellular metabolism. We describe a family with erythrocytosis and a mutation in the HIF2A gene, which encodes the HIF-2alpha protein. Our functional studies indicate that this mutation leads to stabilization of the HIF-2alpha protein and suggest that wild-type HIF-2alpha regulates erythropoietin production in adults.
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“Most gain-of-function mutations in HIF-2α are in direct proximity to proline residue 531, which is one of the two main hydroxylation sites (the other major hydroxylation site is proline 405). 147–154”
From Regulation of erythropoiesis by hypoxia-inducible factors (2013) · cites this paper as [147]
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Cites
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Semenza, G. L. (2003) · Nature Reviews Cancer · doi:10.1038/nrc1187 · Cited by 6,717
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Schofield, C. J., & Ratcliffe, P. J. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1366 · Cited by 2,068
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Hypoxia-inducible factor-2 (HIF-2) regulates hepatic erythropoietin in vivo
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Disruption of oxygen homeostasis underlies congenital Chuvash polycythemia
Ang, S. O., Chen, H., Hirota, K., Gordeuk, V. R., Jelinek, J., Guan, Y., Liu, E., Sergueeva, A. I., Miasnikova, G. Y., Mole, D., et al. (2002) · Nature Genetics · doi:10.1038/ng1019 · Cited by 510
Proline hydroxylation and gene expression
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Self-citationHuang, J., Zhao, Q., Mooney, S. M., & Lee, F. S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206955200 · Cited by 307
Self-citationFailure to prolyl hydroxylate hypoxia‐inducible factor α phenocopies VHL inactivation in vivo
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Sequencing of 50 Human Exomes Reveals Adaptation to High Altitude
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Bertout, J. A., Patel, S. A., & Simon, M. C. (2008) · Nature Reviews Cancer · doi:10.1038/nrc2540 · Cited by 1,365
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Semenza, G. L. (2011) · New England Journal of Medicine · doi:10.1056/nejmra1011165 · Cited by 1,014
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Metadata
- Authors
- Percy, M. J., Furlow, P. W., Lucas, G. S., Li, X., Lappin, T. R. J., McMullin, M. F., & Lee, F. S.
- Affiliations
- Belfast City Hospital (GB)
- University of Pennsylvania (US)
- Manchester Royal Infirmary (GB)
- Queen's University (CA)
- Venue
- New England Journal of Medicine
- Publisher
- Massachusetts Medical Society
- Published
- 2008-01-10
- Volume
- 358
- Issue
- 2
- Pages
- 162-168
- ISSN
- 0028-4793 (ISSN-L)
- 1533-4406
- PMC
- PMC2295209
- OpenAlex
- W2086913408
- Cited by
- 314
- References
- 0
- Citations by year
- 2026: 6 · 2025: 3 · 2024: 8 · 2023: 14 · 2022: 8 · 2021: 16 · 2020: 24 · 2019: 23 · 2018: 16 · 2017: 14 · 2016: 14 · 2015: 13 · 2014: 22 · 2013: 25 · 2012: 19
- FWCI
- 19.37
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- New England Journal of Medicine (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Research Portal (Queen's University Belfast) (submittedVersion)
- Funders
- University of Pennsylvania
- U.S. Public Health Service (R01 C090261)
- National Cancer Institute (R01CA090261)
- Topics
- Health Sciences › Medicine › Hematology › Erythropoietin and Anemia Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
- Health Sciences › Medicine › Genetics (clinical) › Hemoglobinopathies and Related Disorders
- Keywords
- HIF-2α, familial erythrocytosis, gain-of-function mutations, hypoxia-inducible factor alpha, protein stabilization, erythropoietin regulation, erythropoiesis, hereditary erythrocytosis
- MeSH terms
- Endothelial PAS Domain-Containing Protein 1, Adult, DNA Mutational Analysis, Erythropoiesis, Erythropoietin, Female, Genotype, Hematocrit, Hemoglobins, Humans, Male, Pedigree, Polycythemia, Polymerase Chain Reaction, Point Mutation, Basic Helix-Loop-Helix Transcription Factors, Basic Helix-Loop-Helix Proteins
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