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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Journal ArticleDOI
Glycosylated minor components of human adult hemoglobin. Purification, identification, and partial structural analysis.
TL;DR: Hemoglobin incubated with D-[14C]glucose-6-P co-chromatographs precisely with Hb A1a2, strongly suggesting that Hb Onea2 is glucose- 6-P hemoglobin, suggesting that hemoglobin can serve as a model system for nonenzymatic glycosylation of protein.
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Effects of Transition Metals on the Expression of the Erythropoietin Gene: Further Evidence That the Oxygen Sensor Is a Heme Protein
Vincent T. Ho,H F Bunn +1 more
TL;DR: Observations support the proposal that the oxygen sensor is a heme protein in which cobalt and nickel can substitute for iron in the porphyrin ring.
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Cotranslational amino-terminal processing of cytosolic proteins. Cell-free expression of site-directed mutants of human hemoglobin.
J P Boissel,T J Kasper,H F Bunn +2 more
TL;DR: Site-directed mutants of the human beta-globin gene encoding for all 19 amino acid replacements of Val-beta 1 were expressed in a cell-free transcription and translation system and faithfully mimic what occurs in nature as judged by the structures of normal and variant human hemoglobins as well as a broad spectrum of other cytosolic proteins.
Journal Article
Erythropoietin structure-function relationships
J P Boissel,H F Bunn +1 more
TL;DR: In conclusion, mutagenesis experiments have identified functionally important domains on the surface of the Epo molecule, at sites comparable with those established for other cytokines.
Journal ArticleDOI
Erythropoietin structure-function relationships. Identification of functionally important domains.
TL;DR: In conclusion, mutagenesis experiments have identified functionally important domains on the surface of the Epo molecule, at sites comparable with those established for other cytokines.