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Department of Biochemistry & Molecular Biology

Virendra N. Pandey, Ph.D.


International Center for Public Health (ICPH)
225 Warren Street Room E450B

Hours: 9:30 am - 6 pm
Phone: (973) 972-0660
Fax: (973) 972-5594



Dr. Virendra Pandey received his Ph.D. (Biochemistry) in 1985 from the University of
Mumbai at Bhabha
Atomic Research Center (BARC), India. He served as Scientist-F at BARC until 1994 and
received the most
prestigious Shanti Swaroop Bhatnagar Award in 1991 for from the Prime Minister of
India for his research
contribution in Life Sciences.



Ph.D., 1985, University of Mumbai, India


Curriculum Vitae

View CV






Relevant Publications:

Dixit U, Pandey AK, Mishra P, Sengupta A, Pandey VN. Staufen1 promotes HCV replication by inhibiting protein kinase R and transporting viral RNA to the site of translation and replication in the cells. NUCLEIC ACIDS RESEARCH 2016 (PMID: 27106056
Dixit U, Pandey AK, Liu Z, Kumar S, Neiditch MB, Klein KM, Pandey, VN. FUSE Binding Protein 1 Facilitates Persistent Hepatitis C Virus Replication in Hepatoma Cells by Regulating Tumor Suppressor p53. J. VIROLOGY. 89(15):7905-7921, 2015
Dixit U, Liu Z, Manvar D, V. N Pandey. FUSE Binding Protein1 Antagonizes the Transcription Activity of Tumor Suppressor Protein p53. BMC-CANCER 14, 925, 2014
A. Upadhyay, U. Dixit, D. Manvar, N. Chaturvedi, V.N. Pandey. Affinity capture and identification of host cell factors associated with hepatitis C virus (+) strand subgenomic RNA. MOL CELL PROTEOMICS 12:1539-1552, 2013
D. Manvar, K. Singh, and V. N. Pandey. Affinity Labeling of Hepatitis C Virus Replicase with a Nucleotide Analogue: Identification of Binding Site. BIOCHEMISTRY 52: 432-444, 2012
I. Das, J. De´sire, Manvar, D., I. Baussanne, V. N. Pandey,*and Jean-Luc De´cout*. A Peptide Nucleic Acid-Aminosugar Conjugate Targeting Transactivation Response Element of HIV-1 RNA Genome Shows a High Bioavailability in Human Cells and Strongly Inhibits Tat- Mediated Transactivation of HIV-1 Transcription. J. MED. CHEM. 55, 6021-6032, 2012 (* Corresponding authors)
Manvar, D., Mishra, M., Kumar, S., Pandey, V.N. Identification and evaluation of anti Hepatitis C virus phytochemicals from Eclipta alba J. ETHNOPHARMACOLOGY 144: 545-554, 2012
N. Pandey, C.A. Mishra,C.A., D. Manvar, A. Upadhyay, T.T. Talele, T.W. Comollo, N. Kaushik-Basu, and V. N. Pandey. Glutamine side chain at position 91 on the ß5a-ß5b loop of Human Immunodeficiency Virus Type 1 Reverse Transcriptase is required for stabilizing the dNTP binding pocket. BIOCHEMISTRY 50: 8067-8077 (2011)


Courses Taught

BIOC5240Q Molec Biol of the News

Current Research

HCV-host cell interaction.
The molecular mechanisms that establish chronic HCV infection and cause its subsequent progression to LC and HCC are poorly understood. Recently, using affinity capture and LC/MS/MS approach, we identified numerous cellular factors associated with the HCV genome; many of these were shown to be essential for HCV replication. One of the proteins that we identified is FUSE binding protein (FBP) which is abundantly expressed in LC and HCC with hepatitis C background. FBP interacts with various proapoptotic and anti-apoptotic cellular factors and facilitates persistent HCV replication. Currently we are investigating the molecular mechanism of these interactions and their implication on HCV replication.

Structure-function relationship in HIV-1 reverse transcriptase.
Until recently, only the N-terminal polymerase domain of HIV-1 RT, corresponding to 1-321 amino acid residues, was considered to be the primary site of specific mutational changes leading to the emergence of drug-resistant strains. However, studies have now implicated both the connection subdomain (residues 322-440) and RNase H domain (residues 441-560) in the emergence of drug-resistant strains of HIV-1, in spite of their distal location from the polymerase active site. Several mechanisms have been proposed to explain how mutational changes in the connection subdomain (CN) and RNase H (RNH) domain may confer drug resistance on the enzyme. One potential mechanism that has not been explored thus far is that the C-terminal of RNH interacting with the CN may be structurally important in subunit dimerization or dimer stability of the enzyme. This hypothesis is supported by the fact that a hydrophobic cluster in the CN encompassing residues W398, W401, W402, Y405, W406, W410, and W414 has an important role in RT dimerization. Our current focus is to identify specific motif /amino acid residues in RNase H domain that play crucial role in in dimerization of HIV-1 RT.



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