J
James I. Salach
Researcher at United States Department of Veterans Affairs
Publications - 34
Citations - 2211
James I. Salach is an academic researcher from United States Department of Veterans Affairs. The author has contributed to research in topics: Monoamine oxidase & Flavin group. The author has an hindex of 23, co-authored 34 publications receiving 2168 citations. Previous affiliations of James I. Salach include Semmelweis University & University of California, San Francisco.
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Journal ArticleDOI
Uptake of the neurotoxin 1-methyl-4-phenylpyridine (MPP+) by mitochondria and its relation to the inhibition of the mitochondrial oxidation of NAD+-linked substrates by MPP+.
Rona R. Ramsay,Rona R. Ramsay,James I. Salach,James I. Salach,Thomas P. Singer,Thomas P. Singer +5 more
TL;DR: The discovery of an uptake system for MPP+ in mitochondria which is greatly potentiated by the presence of malate plus glutamate and inhibited by respiratory inhibitors, suggesting an energy-dependent carrier is reported here.
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Inhibition of mitochondrial NADH dehydrogenase by pyridine derivatives and its possible relation to experimental and idiopathic parkinsonism
Rona R. Ramsay,Rona R. Ramsay,James I. Salach,Jahan Dadgar,Jahan Dadgar,Thomas P. Singer,Thomas P. Singer +6 more
TL;DR: 4-Phenyl-N-methylpyridinium (MPP+), the oxidation product of the neurotoxic amine MPTP, is considerably more inhibitory to the oxidation of NAD+-linked substrates in intact mitochondria in State 3 than is 4-phenylpyridine, which causes efflux of MPP+ from the mitochondria and a reversal of its inhibitory action.
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The Covalently‐Bound Flavin of Hepatic Monoamine Oxidase
Edna B. Kearney,James I. Salach,W.H. Walker,R. Seng,William C. Kenney,Eileen Zeszotek,Thomas P. Singer +6 more
TL;DR: In regard to optical and electron spin resonance spectra, chemical stability, and fluorescence characteristics the flavin peptide isolated from the enzyme agrees excellently with the properties of synthetic cysteinyl 8α-riboflavin.
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Oxidation of the neurotoxic amine 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) by monoamine oxidases A and B and suicide inactivation of the enzymes by MPTP
James I. Salach,James I. Salach,Thomas P. Singer,Thomas P. Singer,Neal Castagnoli,Anthony J. Trevor +5 more
TL;DR: MPTP appears to be a suicide inactivator of MAO, which is oxidized by brain mitochondrial preparations in a process which is blocked by deprenyl and pargyline, implying catalysis by monoamine oxidase B.
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Monoamine oxidase from beef liver mitochondria: Simplified isolation procedure, properties, and determination of its cysteinyl flavin content☆
TL;DR: It appears that the native enzyme contains two subunits not separable on polyacrylamide gels, only one of which possesses covalently linked flavin.