Dr. Ch. Mohan Rao combines biophysical, molecular biological and cell biological approaches to address problems of biomedical importance. His research interests include protein folding, molecular chaperones and heat shock proteins, molecular basis for lens transparency, cataract and keratitis; DNA based diagnostics, Nanobiology, Photoacoustic spectroscopy and its application to biomedical problems. His recent research addresses role of small heat shock proteins in gene expression, cell division, differentiation and apoptosis.
Ch. Mohan Rao and Balasubramanian, D. Study of a solid state reaction by photoacoustic spectroscopy. J. Physical Chemistry, 86, 939-943, 1982.
Balasubramanian, D., Ch. Mohan Rao, and Panijpan, B.: The malaria parasite monitored by photoacoustic spectroscopy. Science, 223, 828-830, 1984.
B.Raman and Ch. Mohan Rao: Chaperone like activity and quaternary structure of alpha-crystallin J.Biol. Chem., 269, 27264-27268, 1994.
Singh BN, Rao KS, Ramakrishna T, Rangaraj N, Ch. Mohan Rao, Association of alphaB-Crystallin, a Small Heat Shock Protein, with Actin: Role in Modulating Actin Filament Dynamics in vivo. J. Mol. Biol., 366, 756-767, 2007.
Aftab Taiyab, AS Sreedhar and Ch. Mohan Rao: Hsp90 inhibitors, GA and 17 AAG, lead to ER-Stress induced apoptosis in rat histiocytoma. Biochemical Pharmacology, 78, 142-152, 2009
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|Interaction of mammalian hsp22 with lipid membranes||Biochemical Journal., 401: 437-445||2007|
|Association of aB-crystallin, a small heat shock protein, with actin: role in modulating actin filament dynamics in vivo||Journal of Molecular Biology., 366: 756-767||2007|
|The cataract-causing mutation G98R in human aA-crystallin leads to folding defects and loss of chaperone activity Molecular Vision, 12, 1372-9 2006 PDF||Molecular Vision., 12: 1372-1379||2006|
|Critical balance of electrostatic and hydrophobic interactions is required for beta2-microglobulin amyloid fibril growth and stability||Biochemical Journal., 44: 1288-1299||2005|
|Arginine hydrochloride enhances the dynamics of subunit assembly and the chaperone-like activity of a-crystallin||Molecular Vision., 11: 249-255||2005|
|The IXI/V motif in the c-terminal extension of a-crystallins: alternative interactions and oligomeric assemblies||Molecular Vision ., 10: 655-662||2004|
|Oligomeric hsp33 with enhanced chaperone activity||Journal of Molecular Biology., 279: 55760-55769||2004|
|Oxidative refolding of lysozyme in trifluoroethanol (TFE) and ethylene glycol: interfering role of preexisting alpha-helical structure and intermolecular hydrophobic interactions||FEBS Letters., 557: 69-72||2004|
|Mammalian hsp22 is a heat-inducible small heat-shock protein with chaperone-like activity, Biochemical Journal||Biochemical Journal., 15(381): 379-387||2004|
|Structural perturbation and enhancement of the chaperone-like activity of alpha-crystallin by arginine hydrochloride.||Protein Science., 12: 1262-1270||2003|
|Role of the conserved SRLFDQFFG region of alpha-crystallin, a small heat shock protein||Journal of Molecular Biology ., 278: 51159-51166||2003|
|Role of the c-terminal extensions of alpha-crystallins.||Journal of Molecular Biology., 277: 45821-45828||2002|
|Chaperone-like activity and surface hydrophobicity of 70s ribosome,||FEBS Letters., 527: 234-238||2002|
|Redox-regulated chaperone function and conformational changes of Escherichia coli hsp33.||FEBS Letters., 489: 19-24||2001|
|Interaction of human recombinant alphaA- and alphaB-crystallins with early and late unfolding intermediates of citrate synthase on its thermal denaturation||FEBS Letters., 497: 118-123||2001|
|Enzymatic, clinical and histologic evaluation of corneal tissues in experimental fungal keratitis in rabbits||Experimental Eye Research., 72: 433-442||2001|
|Unfolding and refolding of a quinone oxidoreductase : alpha-crystallin, a molecular chaperone, assists its reactivation||Biochem. Journal., 359: 547-556||2001|
|Expression of recombinant -crystallin in escherichia coli with the help of groel/es and its purification.||Protein Expression and Purification., 21: 260-267||2001|
|Packing-induced conformational and functional changes in the subunits of alpha-crystallin.||Journal of Molecular Biology., 275: 41004-41010||2000|
|Preparation, characterization, esr and pas studies of Cu0.5 NbAlP3O12 and HNbAl P3O12||Materials Letters., 45: 58-62||2000|
|Inability of chaperones to fold mutant zeta crystallin, an aggregation-prone eye lens protein||Molecular Vision., 275: 22009-22013||2000|
|Carotenoids of an antarctic psychrotolerant bacterium, Sphingobacterium antarcticus, and a mesophilic bacterium, Sphingobacterium multivorum||Archives of Microbiology., 173: 418-424||2000|
|Domain swapping in human alphaA and alphaB crystallins affects oligomerization and enhances chaperone-like activity||Journal of Molecular Biology., 275: 22009-22013||2000|