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Suresh V. Ambudkar

Senior Investigator
Laboratory of Cell Biology
National Cancer Institute
United States of America

Biography

Dr. Ambudkar obtained his Ph.D. from Madurai Kamaraj University, Madurai, India, and received his postdoctoral training in membrane bioenergetics at the University of Maryland. He continued his postdoctoral work on biochemistry of membrane transport proteins at the Johns Hopkins University School of Medicine. In July 1995, after 5 years as an assistant professor in the departments of medicine and physiology at Johns Hopkins, he joined the Laboratory of Cell Biology at the CCR, NCI. He serves as Deputy Chief of the Laboratory of Cell Biology and Chief of the Transport Biochemistry Section.

Research Interest

Biochemistry of Multidrug Transporters 1. Elucidation of the Catalytic Cycle of ATP Hydrolysis, Transport Pathway and the Molecular Basis of Polyspecificity of P-gp Biochemistry of Multidrug Transporters 2. Development of Potent Non-Toxic Small Molecule Modulators/Inhibitors of ABC Transporters 3. Resolution of the Three-Dimensional Structure of Human P-gp 4. Role of Intracellular Loops in Protein Folding and the Mechanism of Rescue to the Cell Surface by Pharmacological Chaperones of Mutant P-gp. 5) ABC transporters; 6) Catalytic cycle; 7) Multidrug resistance; 8) Transport mechanism; 9) Tyrosine kinase inhibitors

Publications

  • Sauna ZE, Ambudkar SV. Evidence for a requirement for ATP hydrolysis at two distinct steps during a single turnover of the catalytic cycle of human P-glycoprotein. Proceedings of the National Academy of Sciences. 2000 Mar 14;97(6):2515-20.

  • Ambudkar SV, Cardarelli CO, Pashinsky I, Stein WD. Relation between the turnover number for vinblastine transport and for vinblastine-stimulated ATP hydrolysis by human P-glycoprotein. Journal of Biological Chemistry. 1997 Aug 22;272(34):21160-6.

  • Ambudkar SV, Lelong IH, Zhang J, Cardarelli CO, Gottesman MM, Pastan I. Partial purification and reconstitution of the human multidrug-resistance pump: characterization of the drug-stimulatable ATP hydrolysis. Proceedings of the National Academy of Sciences. 1992 Sep 15;89(18):8472-6.

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