B. Raman

发表

Fibrillogenic and non-fibrillogenic ensembles of SDS-bound human alpha-synuclein.

Md. Faiz Ahmad, T. Ramakrishna, B. Raman, 2006, Journal of molecular biology.

Structural perturbation of α-crystallin and its chaperone-like activity

M. B. Sukhaswami, D. Ghosh, S. Datta, 1998 .

Molten-Globule State of Carbonic Anhydrase Binds to the Chaperone-like α-Crystallin*

B. Raman, C. M. Rao, K. Rajaraman, 1996, The Journal of Biological Chemistry.

Selective Cu2+ binding, redox silencing, and cytoprotective effects of the small heat shock proteins alphaA- and alphaB-crystallin.

Md. Faiz Ahmad, T. Ramakrishna, B. Raman, 2008, Journal of molecular biology.

Effect of phosphorylation on alpha B-crystallin: differences in stability, subunit exchange and chaperone activity of homo and mixed oligomers of alpha B-crystallin and its phosphorylation-mimicking mutant.

Md. Faiz Ahmad, T. Ramakrishna, B. Raman, 2008, Journal of molecular biology.

Chaperone-like activity and quaternary structure of alpha-crystallin.

B. Raman, C. M. Rao, C. Rao, 1994, The Journal of biological chemistry.

Temperature dependent chaperone‐like activity of alpha‐crystallin

T. Ramakrishna, B. Raman, C. Mohan Rao, 1995, FEBS letters.

Chaperone-like Activity and Temperature-induced Structural Changes of α-Crystallin*

B. Raman, C. M. Rao, C. Rao, 1997, The Journal of Biological Chemistry.

The IXI/V motif in the C-terminal extension of alpha-crystallins: alternative interactions and oligomeric assemblies.

T. Ramakrishna, B. Raman, C. M. Rao, 2004, Molecular vision.

Arginine hydrochloride enhances the dynamics of subunit assembly and the chaperone-like activity of alpha-crystallin.

V. Srinivas, T. Ramakrishna, B. Raman, 2005, Molecular vision.

αB-crystallin, a small heat-shock protein, prevents the amyloid fibril growth of an amyloid β-peptide and β2-microglobulin

T. Ban, H. Naiki, Y. Goto, 2005 .

Mammalian Hsp22 is a heat-inducible small heat-shock protein with chaperone-like activity.

T. K. Chowdary, T. Ramakrishna, B. Raman, 2004, The Biochemical journal.

Interaction of mammalian Hsp22 with lipid membranes.

T. K. Chowdary, T. Ramakrishna, B. Raman, 2007, The Biochemical journal.

Interaction of mammalian Hsp 22 with lipid membranes

T. K. Chowdary, T. Ramakrishna, B. Raman, 2006 .

Interaction of human recombinant αA‐ and αB‐crystallins with early and late unfolding intermediates of citrate synthase on its thermal denaturation

T. Ramakrishna, B. Raman, K. Rajaraman, 2001 .

Oligomeric Hsp33 with Enhanced Chaperone Activity

K. Maki, K. Kuwajima, T. Inobe, 2004, Journal of Biological Chemistry.

DNA-mediated assembly of weakly interacting DNA-binding protein subunits: in vitro recruitment of phage 434 repressor and yeast GCN4 DNA-binding domains.

S. Pongor, S. Zahariev, B. Raman, 2004, Nucleic acids research.

Recruitment of archaeal DTD is a key event toward the emergence of land plants

R. Sankaranarayanan, B. Raman, Pradeep Kumar, 2021, Science Advances.

Recruitment of Archaeal DTD is a Key Event in the Emergence of Land Plants

R. Sankaranarayanan, B. Raman, Pradeep Kumar, 2020, bioRxiv.

Rapid refolding studies on the chaperone-like alpha-crystallin. Effect of alpha-crystallin on refolding of beta- and gamma-crystallins.

T. Ramakrishna, B. Raman, C. Rao, 1995, The Journal of biological chemistry.

Rapid Refolding Studies on the Chaperone-like α-Crystallin

T. Ramakrishna, B. Raman, C. Rao, 1995, The Journal of Biological Chemistry.

Aggregation of lasalocid A in membranes: a fluorescence study.

A. Chattopadhyay, B. Raman, S. Komath, 1992, Biochimica et biophysica acta.

Structural Aspects and Chaperone Activity of Human HspB3: Role of the “C-Terminal Extension”

T. Ramakrishna, B. Raman, A. Asthana, 2012, Cell Biochemistry and Biophysics.

Inhibition of Cu2+-mediated generation of reactive oxygen species by the small heat shock protein αB-crystallin: the relative contributions of the N- and C-terminal domains.

V. Srinivas, T. Ramakrishna, B. Raman, 2011, Free radical biology & medicine.

Role of the C-terminal Extensions of α-Crystallins

T. Ramakrishna, B. Raman, S. Pasta, 2002, The Journal of Biological Chemistry.

Role of the C-terminal extensions of alpha-crystallins. Swapping the C-terminal extension of alpha-crystallin to alphaB-crystallin results in enhanced chaperone activity.

T. Ramakrishna, B. Raman, S. Pasta, 2002, The Journal of biological chemistry.

Interaction of human recombinant alphaA- and alphaB-crystallins with early and late unfolding intermediates of citrate synthase on its thermal denaturation.

T. Ramakrishna, B. Raman, K. Rajaraman, 2001, FEBS letters.

The Chaperone-like α-Crystallin forms a complex only with the aggregation-prone molten globule state of α-Lactalbumin

T. Ramakrishna, B. Raman, K. Rajaraman, 1998 .

The chaperone-like alpha-crystallin forms a complex only with the aggregation-prone molten globule state of alpha-lactalbumin.

T. Ramakrishna, B. Raman, K. Rajaraman, 1998, Biochemical and biophysical research communications.

AlphaB-crystallin, a small heat-shock protein, prevents the amyloid fibril growth of an amyloid beta-peptide and beta2-microglobulin.

T. Ban, H. Naiki, Y. Goto, 2005, The Biochemical journal.

Mixed oligomer formation between human alphaA-crystallin and its cataract-causing G98R mutant: structural, stability and functional differences.

T. Ramakrishna, B. Raman, Devendra Singh, 2007, Journal of molecular biology.

Hydrophobic surfaces in oligosaccharides: linear dextrins are amphiphilic chains.

C. Sundari, D. Balasubramanian, B. Raman, 1991, Biochimica et biophysica acta.

Effect of the chaperone‐like alpha‐crystallin on the refolding of lysozyme and ribonuclease A

T. Ramakrishna, B. Raman, C. Rao, 1997, FEBS letters.

Unfolding and refolding of a quinone oxidoreductase: alpha-crystallin, a molecular chaperone, assists its reactivation.

T. Ramakrishna, B. Raman, S. Goenka, 2001, The Biochemical journal.

Structural perturbation and enhancement of the chaperone‐like activity of α‐crystallin by arginine hydrochloride

V. Srinivas, T. Ramakrishna, B. Raman, 2003, Protein science : a publication of the Protein Society.

Role of the conserved SRLFDQFFG region of alpha-crystallin, a small heat shock protein. Effect on oligomeric size, subunit exchange, and chaperone-like activity.

T. Ramakrishna, B. Raman, S. Pasta, 2003, Journal of Biological Chemistry.

Role of the Conserved SRLFDQFFG Region of α-Crystallin, a Small Heat Shock Protein

T. Ramakrishna, B. Raman, S. Pasta, 2003, Journal of Biological Chemistry.

The Extracellular Chaperone Haptoglobin Prevents Serum Fatty Acid-promoted Amyloid Fibril Formation of β2-Microglobulin, Resistance to Lysosomal Degradation, and Cytotoxicity

B. Raman, R. Tangirala, C. Rao, 2013, The Journal of Biological Chemistry.

Nucleosomal association and altered interactome underlie the mechanism of cataract caused by the R54C mutation of αA-crystallin.

T. Ramakrishna, B. Raman, C. Rao, 2021, Biochimica et biophysica acta. General subjects.

Nucleosomal association and altered interactome underlie the mechanism of cataract caused by the R54C mutation of αA-crystallin

T. Ramakrishna, B. Raman, C. Rao, 2020, bioRxiv.

Artificial chaperoning of insulin, human carbonic anhydrase and hen egg lysozyme using linear dextrin chains – a sweet route to the native state of globular proteins

D. Balasubramanian, B. Raman, C. Sivakama Sundari, 1999, FEBS letters.

Critical balance of electrostatic and hydrophobic interactions is required for beta 2-microglobulin amyloid fibril growth and stability.

T. Ban, K. Hasegawa, H. Naiki, 2005, Biochemistry.

Redox‐regulated chaperone function and conformational changes of Escherichia coli Hsp33

T. Ramakrishna, B. Raman, C. Mohan Rao, 2001, FEBS letters.

HspB2/Myotonic Dystrophy Protein Kinase Binding Protein (MKBP) as a Novel Molecular Chaperone: Structural and Functional Aspects

T. Ramakrishna, B. Raman, C. Rao, 2012, PloS one.

Fibrillogenic and Non-fibrillogenic Ensembles of SDS-bound Human α-Synuclein

Md. Faiz Ahmad, T. Ramakrishna, B. Raman, 2006 .

Chaperone-like activity and temperature-induced structural changes of alpha-crystallin.

B. Raman, C. Rao, 1997, The Journal of biological chemistry.

The cataract-causing mutation G98R in human alphaA-crystallin leads to folding defects and loss of chaperone activity.

T. Ramakrishna, B. Raman, Devendra Singh, 2006, Molecular vision.

Metal Ion-dependent Effects of Clioquinol on the Fibril Growth of an Amyloid β Peptide*

T. Kawai, T. Ban, H. Naiki, 2005, Journal of Biological Chemistry.

Refolding of Denatured and Denatured/Reduced Lysozyme at High Concentrations*

T. Ramakrishna, B. Raman, C. Rao, 1996, The Journal of Biological Chemistry.

Co‐refolding denatured‐reduced hen egg white lysozyme with acidic and basic proteins

T. Ramakrishna, B. Raman, V. D. Trivedi, 1997, FEBS letters.

Amphiphilic properties of polysaccharides: dextrin chains as example.

C. Sundari, D. Balasubramanian, B. Raman, 1992, Indian Journal of Biochemistry & Biophysics.

Polysaccharides as amphiphiles

C. Sundari, D. Balasubramanian, B. Raman, 1993 .

Inhibition of Cu2+-mediated generation of reactive oxygen species by the small heat shock protein αB-crystallin: the relative contributions of the N- and C-terminal domains.

V. Srinivas, T. Ramakrishna, B. Raman, 2011, Free radical biology & medicine.

Distinct localization of chiral proofreaders resolves organellar translation conflict in plants.

R. Sankaranarayanan, I. Siddiqi, B. Raman, 2023, Proceedings of the National Academy of Sciences of the United States of America.

Structural Aspects and Chaperone Activity of Human HspB3: Role of the “C-Terminal Extension”

T. Ramakrishna, B. Raman, A. Asthana, 2012, Cell Biochemistry and Biophysics.

Contributory presentations/posters

Diederichs, Bosco K. Ho, Hironori K. Nakamura, 1999, Journal of Biosciences.