Abraham M. Brown
Cornell University
22 Papers
381 Citations
Abraham M. Brown is an academic researcher from Cornell University. The author has contributed to research in topics: Mitochondrial permeability transition pore & Mitochondrion. The author has an hindex of 16, co-authored 22 publications.
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Papers
Zinc Irreversibly Damages Major Enzymes of Energy Production and Antioxidant Defense Prior to Mitochondrial Permeability Transition
TL;DR: Evidence is presented that, unlike Ca2+, exogenous Zn2+ interferes with mitochondrial NADH production and directly alters redox protection in the matrix, contributing to mitochondrial dysfunction.
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Zinc Is a Potent Inhibitor of Thiol Oxidoreductase Activity and Stimulates Reactive Oxygen Species Production by Lipoamide Dehydrogenase
Irina G. Gazaryan,Boris F. Krasnikov,Gillian A. Ashby,Roger N. F. Thorneley,Bruce S. Kristal,Abraham M. Brown +5 more
TL;DR: The results suggest that Zn2+ can interfere with mitochondrial antioxidant production and may also stimulate production of reactive oxygen species by a novel mechanism.
171
Zn2+ Inhibits α-Ketoglutarate-stimulated Mitochondrial Respiration and the Isolated α-Ketoglutarate Dehydrogenase Complex *
Abraham M. Brown,Bruce S. Kristal,Michelle S. Effron,Alexander I. Shestopalov,Paul A. Ullucci,K.-F. Rex Sheu,John P. Blass,Arthur J.L. Cooper +7 more
TL;DR: Physiological free Zn2+ may modulate hepatic mitochondrial respiration by reversible inhibition of the α-ketoglutarate dehydrogenase complex upstream from bc 1 complex.
159
Clinically Approved Heterocyclics Act on a Mitochondrial Target and Reduce Stroke-induced Pathology
Irina G. Stavrovskaya,Malini V. Narayanan,Wenhua Zhang,Boris F. Krasnikov,Jill Heemskerk,S. Stanley Young,John P. Blass,Abraham M. Brown,M. Flint Beal,Robert M. Friedlander,Bruce S. Kristal +10 more
TL;DR: Clinically achievable doses of one drug in this general structural class that inhibits mPT, promethazine, were protective in both in vitro and mouse models of stroke and provide discovery-based evidence that mPT is an essential, causative event in stroke-related injury.
104
pH-dependent substrate preference of pig heart lipoamide dehydrogenase varies with oligomeric state: response to mitochondrial matrix acidification.
Natalia L. Klyachko,Valentina A. Shchedrina,Alexander V. Efimov,Sergey Kazakov,Irina G. Gazaryan,Bruce S. Kristal,Abraham M. Brown +6 more
TL;DR: P pH-dependent equilibria between monomeric, dimeric, and a previously undescribed tetrameric form of pig heart lipoamide dehydrogenase (LADH), a mitochondrial matrix enzyme are observed, indicating a correlation between pH- dependent changes in the LADH reaction specificity and its oligomeric state.
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