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Prasanna Venkatraman, Ph.D.
Principal Investigator 
Advanced Centre for Treatment Research and Education in Cancer
Prasanna Lab
KS 137, Sector 22, Tata Memorial Centre, Kharghar
Navi Mumbai - 410 210   
Phone: +91-22-27405091
Fax: +91-22-27405377
Area of Specialization:
Research Summary:
Molecular characterization of medulloblastoma by global analysis of the cerebrospinal fluid
Neural stem cell model: understanding the role of ubiquitin proteasome pathway in neural stem cell differentiation and tumorogenesis of medulloblastoma
Elucidating the structural basis of substrate recognition by the proteasomes - a global approach
A sequence and structure based method to predict putative substrates, functions and regulatory networks of endoproteases
A computational method for short listing the vast amount of data deposited in various phosphorylation databases
Molecular dynamic simulation studies on a model substrate of the proteasome
Identification of a novel ATP binding site in 14-3-3 zeta and elucidation of its ATP dependent functions
Biochemical and biophysical analysis of substrate recognition, global unfolding and protein degradation by eukaryotic proteasome
Chemopreventive and potential anti-carcinogenic effect of curcumin encapsulated nanoparticles
Validation of novel putative substrates of matriptase identified through bioinformatics approach and their importance in cell adhesion and invasion
1. Venkatraman P.  Specificity in the interaction of natural products with their target proteins--a biochemical and structural insight. Mini Reviews in Medicinal Chemistry. 2010.  10, 540-549. [PubMed]
2. Venkatraman, P., Balakrishnan, S., Rao, S., Hooda, Y. and Pol, S.  A sequence and structure based method to predict putative substrates, functions and regulatory networks of endo proteases. PloS One. 2009.  4, e5700. [PubMed]
3. Telles, E., Hosing, A. S., Kundu, S. T., Venkatraman, P. and Dalal, S. N.  A novel pocket in 14-3-3epsilon is required to mediate specific complex formation with cdc25C and to inhibit cell cycle progression upon activation of checkpoint pathways. Experimental Cell Research. 2009.  315, 1448-1457. [PubMed]
4. Venkatraman, P., Nguyen, T. T., Sainlos, M., Bilsel, O., Chitta, S., Imperiali, B. and Stern, L. J.  Fluorogenic probes for monitoring peptide binding to class II MHC proteins in living cells. Nature Chemical Biology. 2007.  3, 222-228. [PubMed]
5. Bhutani, N., Venkatraman, P. and Goldberg, A. L.  Puromycin-sensitive aminopeptidase is the major peptidase responsible for digesting polyglutamine sequences released by proteasomes during protein degradation. The EMBO Journal. 2007.  26, 1385-1396. [PubMed]
6. Venkatraman, P., Wetzel, R., Tanaka, M., Nukina, N. and Goldberg, A. L.  Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins. Molecular Cell. 2004.  14, 95-104. [PubMed]
7. Variath, P., Liu, Y., Lee, T. T., Stroud, R. M. and Santi, D. V.  Effects of subunit occupancy on partitioning of an intermediate in thymidylate synthase mutants. Biochemistry. 2000.  39, 2429-2435. [PubMed]
8. Prasanna, V., Gopal, B., Murthy, M. R., Santi, D. V. and Balaram, P.  Effect of amino acid substitutions at the subunit interface on the stability and aggregation properties of a dimeric protein: role of Arg 178 and Arg 218 at the Dimer interface of thymidylate synthase. Proteins. 1999.  34, 356-368. [PubMed]
9. Prasanna, V., Bhattacharjya, S. and Balaram, P.  Synthetic interface peptides as inactivators of multimeric enzymes: inhibitory and conformational properties of three fragments from Lactobacillus casei thymidylate synthase. Biochemistry. 1998.  37, 6883-6893. [PubMed]


Book Chapters:
Annual Review of Pharmacology and Toxicology. Vol-46, 2006 edited by Cho AK Current Science, 2007. 92(3). 388-389
Ph.D. Indian Institute of Science, Bangalore, India
  Last modified on : Mar 4, 2011
India Cancer Research Database has been developed by the Institute of Bioinformatics with funding from the Department of Biotechnology, Government of India.