Expertise:

Yeast Biology and Protein Biophysics.

Profile:

Every cell has a network of proteins known as chaperones that are evolved to refold misfolded proteins back to their native state, and if repairing fails target them for degradation. However under various conditions, protein misfolding exceeds the preservative capacity of cells leading to protein aggregation affecting cellular viability. Thus approaches to further modulate action of chaperone machinery could provide common therapeutic targets for various protein misfolding diseases. Our lab employs both yeast genetics and single molecule approaches to understand why cellular machinery that is optimally evolved to maintain protein homeostasis fails to avert accumulation of misfolded proteins as well as proteinaceous masses known as amyloid. Other aspect of our future research would be to understand the dependency of many of the viral pathogens on host chaperones. Many of viral strains require cellular chaperones for replication suggesting these proteins as potential targets against associated viral diseases. Thus one of the future focus of lab is to investigate interplay among various viral proteins and host chaperones.
Significant Recognition: Awards, fellowships, international funding etc.: (1) Indo-Japan cooperative Science Programme-2016 (2) Ramalingaswami Fellowship-2011, DBT, India (3) The fellows Award for research Excellence-2009, NIH, USA. (4) Nancy Nossal Fellowship award-2007, NIH, USA

Major Publications

• Gaur, D., et al., The yeast Hsp70 co-chaperone Ydj1 regulates functional distinction of Ssa Hsp70s in the Hsp90 chaperoning pathway. Genetics, 2020, 215 (2), 2020.
• Singh ,P., et al., HSPMdb: A Computational Repository of Heat Shock Protein Modulators.Database, 2020. Volume 2020, baaa003.
• Gupta,A., et al., The yeast stress inducible Ssa Hsp70 reduces α-synuclein toxicity by promoting its degradation through autophagy. PLoS Genet, 2018. 14(10): p. e1007751.
• Muddassir,M., et al., Single-molecule force-unfolding of titin I27 reveals correlation between size of surrounding anions and its mechanical stability. Chem. Commun, 2018. 54:p.9635-9638.
• Kumar, N., et al., Hsp90-Associated Immunophilin Homolog Cpr7 Is Required for the Mitotic Stability of [URE3] Prion in Saccharomyces cerevisiae. PLoS Genet, 2015. 11(10): p. e1005567.
• Kumar, N., et al., The BAG homology domain of Snl1 cures yeast prion [URE3] through regulation of Hsp70 chaperones. G3 (Bethesda), 2014. 4(3): p. 461-470.

Lab Members