M
Mark E. Dumont
Researcher at University of Rochester
Publications - 59
Citations - 2748
Mark E. Dumont is an academic researcher from University of Rochester. The author has contributed to research in topics: G protein-coupled receptor & Receptor. The author has an hindex of 30, co-authored 58 publications receiving 2622 citations. Previous affiliations of Mark E. Dumont include City University of New York & Texas Tech University Health Sciences Center.
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Journal ArticleDOI
Biochemical and genetic analysis of the yeast proteome with a movable ORF collection
Daniel M. Gelperin,Michael A. White,Martha L. Wilkinson,Yoshiko Kon,Li A. Kung,Kevin J. Wise,Nelson Lopez-Hoyo,Lixia Jiang,Stacy Piccirillo,Haiyuan Yu,Mark Gerstein,Mark E. Dumont,Eric M. Phizicky,Michael Snyder,Elizabeth J. Grayhack +14 more
TL;DR: A MORF (moveable ORF) library of 5854 yeast expression plasmids was constructed, each expressing a sequence-verified ORF as a C-terminal ORF fusion protein, under regulated control, demonstrating that nearly all verified ORFs are expressed and suggesting the authenticity of 48 ORFs characterized as dubious.
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Identification and sequence of the gene encoding cytochrome c heme lyase in the yeast Saccharomyces cerevisiae.
TL;DR: It is demonstrated here that the nuclear gene, CYC3, in the yeast Saccharomyces cerevisiae, encodes cy tochrome c heme lyase (CCHL), the enzyme catalyzing the attachment of heme to apocytochrome c.
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Role of cytochrome c heme lyase in mitochondrial import and accumulation of cytochrome c in Saccharomyces cerevisiae.
TL;DR: Results suggest that apocytochrome c is transported across the outer mitochondrial membrane by a freely reversible process, binds to heme lyase in the intermembrane space, and is then trapped inside mitochondria by an irreversible conversion to holocy tochrome c accompanied by folding to the native conformation.
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Coupling of heme attachment to import of cytochrome c into yeast mitochondria. Studies with heme lyase-deficient mitochondria and altered apocytochromes c.
TL;DR: Results suggest that protein folding triggered by heme attachment to apocytochrome c is required for import into mitochondria, and that CYC3-encoded heme lyase activity in solubilized yeast extracts and in an Escherichia coli expression system is detected.
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Fluorescent approaches for understanding interactions of ligands with G protein coupled receptors.
TL;DR: An overview of the extensive array of fluorescent ligands that have been used in studies of G protein coupled receptors and spectroscopic approaches for assaying binding and probing the environment of receptor-bound ligands with particular attention to examples involving yeast pheromone receptors are described.