alexa Vinayak Prasad | OMICS International
ISSN: 2161-0711

Journal of Community Medicine & Health Education
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Vinayak Prasad

Professor, Department of Microbiology & Immunology Albert Einstein College of Medicine, NY. USA

Biography

Dr. Prasad received his Ph. D. degree in Biochemistry from the Indian Institute of Science, Bangalore. He did a brief post-doctoral stint at the Fox Chase Cancer Center, Philadelphia on the Mechanism of Tumorigenesis by Moloney murine leukemia virus (Advisor: Phillip Tsichlis) followed by a second post-doctoral stint at the Columbia University P & S on the Structure-Function of HIV-1 Reverse Transcriptase (Advisor: Stephen P. Goff). He started his independent career in 1990 as Assistant Professor at the Albert Einstein College of Medicine and is currently a Professor in the Department of Microbiology and Immunology at Albert Einstein.

Dr. Prasad is the Director of the NIH Fogarty International Center-funded AIDS International Training and Research Program, an Institutional AIDS Training grant (T32) titled 'HIV, AIDS and Opportunistic Infections' and the Director of the Developmental Core of the Center for AIDS Research all at the Albert Einstein. Dr. Prasad is a Member of the Editorial Board of the journals Frontiers in Bioscience and RNA Biology.

Research Interest

Dr. Prasad’s long-standing interest in HIV lies in the early events of HIV-1 replication, and his laboratory has now expanded into other aspects of HIV replication. They are interested in the structure-function of HIV-1 reverse transcriptase (RT). Recent work from the laboratory has outlined the role of a critical residue in the polymerase domain that increases the propensity of HIV-1 RT to make errors during DNA synthesis. Furthermore, they are interested in understanding functional interactions of HIV-1 RT with other viral and cellular proteins with a view to generating a better picture of the overall intracellular setting in which reverse transcription proceeds upon infection. Their newer areas of interest also include assembly and budding of HIV-1.

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