M
M A Goldberg
Researcher at Harvard University
Publications - 43
Citations - 4945
M A Goldberg is an academic researcher from Harvard University. The author has contributed to research in topics: Erythropoietin & Magnetic resonance imaging. The author has an hindex of 28, co-authored 43 publications receiving 4812 citations. Previous affiliations of M A Goldberg include Howard Hughes Medical Institute & Johns Hopkins University School of Medicine.
Papers
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Journal ArticleDOI
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.
Journal ArticleDOI
An essential role for p300/CBP in the cellular response to hypoxia
Zoltan Arany,L. Eric Huang,Richard Eckner,Shoumo Bhattacharya,C. H. Jiang,M A Goldberg,H. Franklin Bunn,David M. Livingston +7 more
TL;DR: In this article, the intact cDNA for HIF-1α and p300/CBP were cloned and shown to participate in the induction of hypoxia-responsive genes, including vascular endothelial growth factor.
Journal ArticleDOI
Regulation of the erythropoietin gene.
TL;DR: Erythropoietin (Epo), the hormone that stimulates red blood cell production, is induced by hypoxia and the human hepatoma cell line, Hep3B, is utilized to investigate the regulation of the Epo gene.
Book ChapterDOI
Regulation of the Erythropoietin Gene
S Imagawa,M A Goldberg,H F Bunn +2 more
TL;DR: Evidence that the oxygen sensor in Hep3B cells is a heme protein is presented, and enhancer and promoter elements appear to cooperate in enabling the Epo gene to respond to hypoxia in a physiologically appropriate manner.
Journal ArticleDOI
Inhibition of hypoxia-inducible factor 1 activation by carbon monoxide and nitric oxide. Implications for oxygen sensing and signaling.
TL;DR: The mechanism by which two heme-binding ligands, carbon monoxide and nitric oxide, affect oxygen sensing and signaling is investigated, presumably as heme ligands binding to the oxygen sensor, whereas desferrioxamine and perhaps cobalt appear to act at a site downstream.