H
H F Bunn
Researcher at Brigham and Women's Hospital
Publications - 118
Citations - 19864
H F Bunn is an academic researcher from Brigham and Women's Hospital. The author has contributed to research in topics: Hemoglobin & Erythropoietin. The author has an hindex of 59, co-authored 118 publications receiving 19438 citations. Previous affiliations of H F Bunn include Boston University & United States Department of the Army.
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Regulation of hypoxia-inducible factor 1α is mediated by an O2-dependent degradation domain via the ubiquitin-proteasome pathway
TL;DR: The identification of an oxygen-dependent degradation (ODD) domain within HIF-1alpha that controls its degradation by the ubiquitin-proteasome pathway is reported and may provide a means of controlling gene expression by changes in oxygen tension.
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Analysis of cytokine mRNA and DNA: detection and quantitation by competitive polymerase chain reaction
TL;DR: An adaptation of the polymerase chain reaction (PCR) for highly accurate quantitation of mRNA or DNA from a small number of cells for expression of two cytokines and the copy number of the human GM-CSF gene in normal human cells is described.
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Oxygen sensing and molecular adaptation to hypoxia
H F Bunn,Robert O. Poyton +1 more
TL;DR: Redox chemistry appears to play a critical role both in the trans-activation of oxygen-responsive genes in unicellular organisms as well as in the activation of HIF-1, which is required for the hypoxic induction of physiologically important genes.
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Pathogenesis and Treatment of Sickle Cell Disease
TL;DR: A wealth of information is produced on the mechanisms by which a single base substitution in the gene encoding the human β-globin subunit, with the resulting replacement of β6 glutamic acid by valine, leads to the protean and devastating clinical manifestations of sickle cell disease.
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Regulation of the erythropoietin gene: evidence that the oxygen sensor is a heme protein
M A Goldberg,Dunning Sp,H F Bunn +2 more
TL;DR: A model is proposed in which a ligand-dependent conformational change in a heme protein accounts for the mechanism by which hypoxia as well as cobalt and nickel stimulate the production of Epo.