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Biochemical and Biophysical Research Communications|September 10, 1998
The chaperone-like alpha-crystallin forms a complex only with the aggregation-prone molten globule state of alpha-lactalbuminK Rajaraman, B Raman, T Ramakrishna, et al.FEBS Letters|January 15, 1998
Co-refolding denatured-reduced hen egg white lysozyme with acidic and basic proteinsV D Trivedi, B Raman, C M Rao, et al.Journal of Biochemical and Biophysical Methods|September 11, 1999
Detection and assay of proteases using calf lens beta-crystallin aggregate as substrateV D Trivedi, B Raman, T Ramakrishna, et al.International Journal of Biological Macromolecules|July 3, 1998
Structural perturbation of alpha-crystallin and its chaperone-like activityC M Rao, B Raman, T Ramakrishna, et al.Biochemical and Biophysical Research Communications|May 15, 1991
Synchronous scan fluorescence spectroscopy of proteins and human eye lensesC M RaoTalanta|April 1, 1989
Extraction and determination of zinc in pharmaceutical samplesB Raman, V M ShindeIndian Journal of Experimental Biology|November 1, 1995
Wound healing profiles of ketorolac, metronidazole and tinidazole administered post-surgicallyD Prasad, C M RaoMolecular Vision|November 10, 2000
Inability of chaperones to fold mutant zeta crystallin, an aggregation-prone eye lens proteinS Goenka, C M RaoProtein Expression and Purification|March 10, 2001
Expression of recombinant zeta-crystallin in Escherichia coli with the help of GroEL/ES and its purificationS Goenka, C M RaoBiochemistry International|August 1, 1990
Time profile of hemin aggregation: an analysisV Srinivas, C M RaoPageof 10