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
Mitochondrial Release of Pro-apoptotic Proteins ELECTROSTATIC INTERACTIONS CAN HOLD CYTOCHROME c BUT NOT Smac/DIABLO TO MITOCHONDRIAL MEMBRANES
TL;DR: The results suggest that failure to observe cytochrome c release may be due to the use of different buffers because after permeabilization by caspase-8 cleaved human Bid, cy tochrome c dissociation from mitochondria was highly dependent on ionic strength and required 50-80 mm KCl, NaCl, or LiCl.
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A Distinct Pathway of Cell-Mediated Apoptosis Initiated by Granulysin
Allan A. Kaspar,Satoshi Okada,Jayant Kumar,Francis R Poulain,Katerina A. Drouvalakis,Ameeta Kelekar,Dennis A. Hanson,Ruth M. Kluck,Yasumichi Hitoshi,Daniel Johnson,Christopher J. Froelich,Craig B. Thompson,Donald D. Newmeyer,Alberto Anel,Carol Clayberger,Alan M. Krensky +15 more
TL;DR: It is shown that granulysin damages cell membranes based upon negative charge, disrupts the transmembrane potential in mitochondria, and causes release of cytochrome c, which activates a novel pathway of CTL- and NK cell-mediated death distinct from granzyme- and death receptor-induced apoptosis.
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Caspase-2–induced Apoptosis Requires Bid Cleavage: A Physiological Role for Bid in Heat Shock–induced Death
TL;DR: It is shown that cleavage of the Bcl-2-family protein Bid is required for the induction of apoptosis by Caspase-2, and Bid-null MEFs were substantially more resistant to apoptosis induced by heat shock.
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The 'harmless' release of cytochrome c.
TL;DR: The evidence that cytochrome c release is mediated by Bcl-2 family proteins in a process that involves only outer membrane permeability but leaves inner membrane energization, protein import function and the ultrastructure of mitochondria intact is discussed.
Journal ArticleDOI
Determinants of Cytochrome c Pro-apoptotic Activity: THE ROLE OF LYSINE 72 TRIMETHYLATION *
Ruth M. Kluck,Lisa M. Ellerby,H. Michael Ellerby,Shahrouz Naiem,Michael P. Yaffe,Emanuel Margoliash,Dale E. Bredesen,A. Grant Mauk,Fred Sherman,Donald D. Newmeyer +9 more
TL;DR: Whether the inactivity of the yeast isoforms is related to a post-translational modification of lysine 72,N-ε-trimethylation is examined, which was found to abrogate pro-apoptotic activity of metazoan cytochrome cexpressed in yeast.