- Chem Sci 402B
Associate Professor, Chemistry
Director, Biochemistry and Molecular Biology (BMB) Program
- PhD, Jawaharlal Nehru University, New Delhi, India
- MSc, Jamia Millia Islamia, New Delhi, India
- BSc, All-India Institute of Medical Sciences, New Delhi, India
Our research interest lies in the area of 'protein aggregation diseases'. The long-term goal of our laboratory is to understand the relationship between protein misfolding and aggregation, and their role in health and disease. Although, protein misfolding and aggregation have been directly linked to cellular toxicity for several protein deposition diseases, the underlying mechanism(s) by which these aggregated proteins impair cellular function(s) and cause toxicity is not clear and is a subject of intense debate. The focus of our lab is to study the consequences of protein misfolding in vitro and how it relates to misfolding in vivo.
- Protein aggregation diseases
- Consequences of protein misfolding in vitro and how it relates to misfolding in vivo
- Molecular crowding
- Tiwari A , Liba A, Sohn SH, Seetharaman SV, Bilsel O, Matthews CR, Hart PJ, Valentine JS, and Hayward LJ. Metal deficiency increases aberrant hydrophobicity of mutant superoxide dismutases that cause amyotrophic lateral sclerosis. J Biol Chem. (2009) 284(40):27746-27758.
- Molnar KS, Karabacak NM, Johnson JL, Wang Q, Tiwari A , Hayward LJ, Coales SJ, Hamuro Y and Agar JN. A common property of amyotrophic lateral sclerosis -associated variants: Destabilization of the Cu/Zn superoxide dismutase electrostatic loop. J Biol Chem. (2009) 284(45):30965-30973.
- Karabacak NM, Li L, Tiwari A, Hayward LJ, Hong P, Easterling ML, and Agar JN. Sensitive and specific identification of wild-type and variant proteins from 8 to 669 kDa using top-down mass spectrometry. Mol Cell Proteomics. (2009) 8(4):846-856.
- Cao X, Antonyuk S, Seetharaman SV, Whitson LJ, Taylor AB, Holloway SP, Strange RW, Doucette PA, Valentine JS, Tiwari A, Hayward LJ, Padua S, Cohlberg JA, Hasnain SS, and Hart PJ. Structures of the G85R variant of SOD1 in familial ALS. J Biol Chem. (2008) 283(23): 16169-77.
- Shaw BF, Lelie HL, Durazo A, Nersissian AM, Xu G, Chan PK, Gralla EB, Tiwari A, Hayward LJ, Borchelt DR, Valentine JS, and Whitelegge JP. Detergent-insoluble aggregates associated with amyotrophic lateral sclerosis in transgenic mice contain primarily full-length, unmodified superoxides dismutase-1. J Biol Chem. (2008) 283(13): 8340-8350.
- Watanabe S, Nagano S, Duce J, Kiaei M, Li Q-X, Tucker SM, Tiwari A, Brown RH, Jr., Beal MF, Hayward LJ, Culotta VC, Yoshihara S, Sakoda S, and Bush AI. Increased affinity for copper mediated by cysteine 111 in forms of mutant superoxide dismutase 1 linked to amyotrophic lateral sclerosis. Free Radic Biol Med. (2007) 42(10): 1534-1542.
- Tiwari A and Bhat R. Stabilization of yeast hexokinase A by polyol osmolytes: Correlation with physicochemical properties of aqueous solutions. Biophys Chem. (2006) 124(2):90-99.
- Invited talk “Is Hydrophobic Exposure of Misfolded Proteins a Key to Neurodegenerative Disease?” at Department of Biomedical Sciences at Iowa State University, Ames, IA.
- Invited talk “A Biochemists Quest for the Origin of Familial ALS”. General ALS research talk for patients, families, and caregivers organized by the ALS Association Massachusetts Chapter at Athol, MA (Athol Memorial Hospital).
- Invited talk “Is Hydrophobic Exposure of Misfolded Proteins a Key to Neurodegenerative Disease?” at Center for Research in Neurodegenerative Diseases, University of Toronto, Canada.
- Invited talk “Metal deficient ALS mutants of SOD1 show increased hydrophobicity”. Seventh International Consortium on Superoxide Dismutase and Amyotrophic Lateral Sclerosis; October 22-23, 2007; organized by Diane Cabelli, Ph.D., Chemistry Department, Brookhaven National Laboratory, Upton, NY.
- Invited talk “Hydrophobic ALS Mutants of Superoxide Dismutase”. Thirty-fifth Departmental Research Dinner organized by Department of Neurology, University of Massachusetts Medical School, Worcester, MA.
- Invited talk “Mutant SOD1 Enzymes That Cause Familial ALS Exhibit Aberrantly Increased Hydrophobicity”. Young Investigators Workshop 2006 (23rd -25th January, 2006) organized by the ALS Association, St. Petersburg, Florida, USA.
- Invited talk “Unfolding and Surface Abnormalities of Mutant SOD1”. Symposium 2005 “Living with ALS” organized by the ALS Association Massachusetts Chapter at Dedham, MA.