C
Christos Chinopoulos
Researcher at Semmelweis University
Publications - 99
Citations - 6014
Christos Chinopoulos is an academic researcher from Semmelweis University. The author has contributed to research in topics: Mitochondrion & ATP synthase. The author has an hindex of 37, co-authored 92 publications receiving 5167 citations. Previous affiliations of Christos Chinopoulos include University of New Mexico & Cornell University.
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Journal ArticleDOI
Mitochondrial α-Ketoglutarate Dehydrogenase Complex Generates Reactive Oxygen Species
Anatoly A. Starkov,Gary Fiskum,Christos Chinopoulos,Beverly J. Lorenzo,Susan E. Browne,Mulchand S. Patel,M. Flint Beal +6 more
TL;DR: The data strongly indicate that KGDHC is a primary site of ROS production in normally functioning mitochondria, and NAD+ inhibited ROS production by the isolated enzymes and by permeabilized mitochondria.
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Bioenergetics and the formation of mitochondrial reactive oxygen species.
TL;DR: Bioenergetic factors that promote ROS generation at physiologically relevant sites in mitochondria are focused on and emphasis is given to ROS generation by complex I--the first component of the respiratory chain--and to how the NADH:NAD+ ratio regulates ROS formation.
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Succinate, an intermediate in metabolism, signal transduction, ROS, hypoxia, and tumorigenesis
TL;DR: The pathways encompassing succinate as a metabolite or a signal and how these may interact in normal and pathological conditions are reviewed.
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Mitochondrial calcium and oxidative stress as mediators of ischemic brain injury.
TL;DR: Within minutes to an hour following the initialCa2+ transient, most neurons undergo delayed Ca2+ deregulation characterized by a dramatic rise in cytosolic Ca2+.
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Molecular mechanisms of cell death: central implication of ATP synthase in mitochondrial permeability transition
Massimo Bonora,Mariusz R. Wieckowski,Christos Chinopoulos,Oliver Kepp,Guido Kroemer,Lorenzo Galluzzi,Paolo Pinton +6 more
TL;DR: Recent findings suggest that another of its core components is represented by the c subunit of mitochondrial ATP synthase, the supramolecular entity that is believed to mediate MPT.