Dr. Swati Tiwari

Dr. Swati Tiwari
Assistant Professor
Ph: +91 11 26738755
Email: swati_tiwari@mail.jnu.ac.in


Ph. D. (Life Sciences),    Jawaharlal Nehru University, New Delhi.     
M. Sc. (Biochemistry),    Lucknow University, Lucknow


Assistant Professor, School of Biotechnology, JNU,  New Delhi
Assistant Professor, School of Biotechnology, GGSIP University, Delhi
Research Scientist, School of Environmental Sciences, JNU, New Delhi (Department of Science and Technology supported)
2001- 2002
Research Associate, Regulation of Protein Function Laboratory, National Cancer Institute, National Institutes of Health, Bethesda, USA
Visiting Fellow, Laboratory of Immune Cell Biology, National Cancer Institute, National Institutes of Health, Bethesda. USA

Area of Interest:

  • Molecular Cell Biology, ubiquitin-proteasome mediated regulation of protein turnover

Summary of research:

My current research interest lies in understanding the importance of the ubiquitin-proteasome pathway in the pathogenesis of various human parasitic diseases. The components of this pathway are encoded in the genome of various parasites. Therefore, it can be assumed that this pathway may be involved in various cellular functions of the parasites which may include growth and development of parasites, host-parasite interactions, evasion of host’s immune surveillance, and cell signaling. An understanding of these questions is important not only for furthering our knowledge about the pathogenesis of these diseases but also for identification of targets for developing parasite specific drugs/ inhibitors. I am currently addressing some of these questions using Entamoeba histolytica and Leishmania donovani as model systems


  • Fogarty International Visiting Fellowship (1996-2000)

Selected Publications:

  1. J. M. Webster, S. Tiwari, A. M. Weissman and R. J. H. Wojcikiewicz (2003).  Inositol 1,4,5-trisphosphate receptor ubiquitination is mediated by mamalian Ubc7, a component of the  Endoplasmic Reticulum-Associated Degradatoin pathway, and is inhibited by chelation of intracellular Zn2+. J. Biol. Chem., 278: 38238-38246.
  2. A. Magnifico, S. Ettenberg, C. Yang, J. Mariano, S. Tiwari, F. Fang, S. Lipkowitz and A. M. Weissman (2003). HECT E3s target Cbl proteins for proteasomal degradation: implications for tyrosine kinase-mediated regulation. J. Biol. Chem., 278: 43169-43177.
  3. Fang, S., Ferrone, M., Yang, C., S. Tiwari and A. M. Weissman (2001). The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA, 98: 14422-14427.
  4. S. Tiwari and A. M. Weissman (2001). Endoplasmic Reticulum Associated Degradation (ERAD) of T-cell receptor subunits: Involvement of ER-associated Ubiquitin Conjugating Enzymes (E2s). J. Biol. Chem., 19: 16193-16200.