Ronald S. Kaplan
Rosalind Franklin University of Medicine and Science
45 Papers
438 Citations
Ronald S. Kaplan is an academic researcher from Rosalind Franklin University of Medicine and Science. The author has contributed to research in topics: Mitochondrial citrate transport & Transport protein. The author has an hindex of 23, co-authored 44 publications. Previous affiliations of Ronald S. Kaplan include University of South Alabama & Johns Hopkins University School of Medicine.
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Papers
The mitochondrial tricarboxylate transport protein. cDNA cloning, primary structure, and comparison with other mitochondrial transport proteins
TL;DR: The amino acid sequence of the rat liver mitochondrial tricarboxylate transport protein has been deduced from its corresponding cDNA and this information is able, on the basis of both structural and functional considerations, to assign this metabolically important transporter to the mitochondrial carrier family.
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High Level Expression and Characterization of the Mitochondrial Citrate Transport Protein from the Yeast Saccharomyces cerevisiae
TL;DR: The identification of the yeast CTP gene, and the expression and purification of large quantities of its protein product, pave the way for investigations into the roles of specific amino acids in the CTP translocation mechanism, as well as for the initiation of crystallization trials.
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Isolation and reconstitution of the n-butylmalonate-sensitive dicarboxylate transporter from rat liver mitochondria.
TL;DR: The mitochondrial dicarboxylate carrier has been substantially purified from rat liver mitoplasts by extraction with Triton X-114 in the presence of cardiolipin followed by chromatography on hydroxylapatite and it is concluded that this highly purified fraction contains a reconstitutively active dICarboxyate transporter which, based on its substrate specificity and inhibitor sensitivity, appears to be identical to the native dicarsenate transport system found in intact
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Characterization of phosphate efflux pathways in rat liver mitochondria.
TL;DR: Results presented here rule out an atractyloside-sensitive ATP/ADP,0.5Pi transport system as a mechanism for Pi efflux in rat liver mitochondria, andPi efflux appears to occur on the classical Pi/H+ transport system and via a mersalyl-insensitive saturable process, thus suggesting carrier mediation.
The Yeast Mitochondrial Citrate Transport Protein PROBING THE SECONDARY STRUCTURE OF TRANSMEMBRANE DOMAIN IV AND IDENTIFICATION OF RESIDUES THAT LIKELY COMPRISE A PORTION OF THE CITRATE TRANSLOCATION PATHWAY
TL;DR: It is concluded that residues 177–193 exist as an α-helix and a water-accessible face of the helix comprises a portion of the substrate translocation pathway through the CTP, whereas the water-inaccessible surface faces the lipid bilayer.
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