D
Donald D. Newmeyer
Researcher at La Jolla Institute for Allergy and Immunology
Publications - 51
Citations - 21271
Donald D. Newmeyer is an academic researcher from La Jolla Institute for Allergy and Immunology. The author has contributed to research in topics: Cytochrome c & Mitochondrion. The author has an hindex of 40, co-authored 50 publications receiving 20479 citations. Previous affiliations of Donald D. Newmeyer include Stanford University & Roy J. and Lucille A. Carver College of Medicine.
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Journal ArticleDOI
The Release of Cytochrome c from Mitochondria: A Primary Site for Bcl-2 Regulation of Apoptosis
TL;DR: In a cell-free apoptosis system, mitochondria spontaneously released cytochrome c, which activated DEVD-specific caspases, leading to fodrin cleavage and apoptotic nuclear morphology, and Bcl-2 acts to inhibit cy tochrome c translocation, thereby blocking caspase activation and the apoptotic process.
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Direct activation of Bax by p53 mediates mitochondrial membrane permeabilization and apoptosis.
Jerry E. Chipuk,Tomomi Kuwana,Lisa Bouchier-Hayes,Nathalie Droin,Donald D. Newmeyer,Martin Schuler,Douglas R. Green +6 more
TL;DR: It is proposed that when p53 accumulates in the cytosol, it can function analogously to the BH3-only subset of proapoptotic Bcl-2proteins to activate Bax and trigger apoptosis.
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Ordering the cytochrome c-initiated caspase cascade: hierarchical activation of caspases-2, -3, -6, -7, -8, and -10 in a caspase-9-dependent manner.
Elizabeth A. Slee,Mary T. Harte,Ruth M. Kluck,Beni B. Wolf,Carlos A. Casiano,Donald D. Newmeyer,Hong Gang Wang,John C. Reed,Donald W. Nicholson,Emad S. Alnemri,Douglas R. Green,Seamus J. Martin +11 more
TL;DR: Six additional caspases (caspases-2, -3, -6, -7, -8, and -10) are processed in cell-free extracts in response to cytochrome c, and that three others failed to be activated under the same conditions.
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Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane.
Tomomi Kuwana,Mason R. Mackey,Guy Perkins,Mark H. Ellisman,Martin Latterich,Roger Schneiter,Douglas R. Green,Donald D. Newmeyer +7 more
TL;DR: It is concluded that mitochondrial protein release in apoptosis can be mediated by supramolecular openings in the outer mitochondrial membrane, promoted by BH3/Bax/lipid interaction and directly inhibited by Bcl-x(L).
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Mitochondria - Releasing Power for Life and Unleashing the Machineries of Death
TL;DR: A review of promising mechanisms proposed for mitochondrial involvement in cell death are examined, including oxidative phosphorylation, generation of oxygen radicals, dynamic morphological rearrangements, calcium overload, and permeability transition.