Prasanna Venkatraman, Ph.D.
Advanced Centre for Treatment Research and Education in Cancer
Prasanna Lab
KS 137, Sector 22, Tata Memorial Centre, Kharghar
Navi Mumbai - 410 210
Maharashtra
E-mail: vprasanna@actrec.gov.in
Phone: +91-22-27405091
Fax: +91-22-27405377
URL: http://ns1.actrec.gov.in/pi-webpages/Prasanna/index.htm
Area of Specialization:
Proteomics
Oncology
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
Publications:
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
Education
::
Ph.D.
Indian Institute of Science, Bangalore, India