DR. JIMUT KANTI GHOSH
 
Divison of Molecular & Structural Biology
Central Drug Reserch Institute
Lucknow-226 001
 
E-Mail jighosh@]yahoo.com
Educational qualifications M.Sc., Ph.D
 
Group Member (PhD student)
 
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 Ms. Neeta Asthana (SRF)
•
 Aqeel Ahmad (SRF)
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 Richa Verma (SRF)
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 Brijesh Kumar Pandey (SRF)
•
 Sarfuddin (JRF)
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 Dr. Sharada Prasad Yadav, postdoctoral fellow, National Eye Research Inst., NIH, USA- already obtained Ph.D. degree
 
CURRENT AREAS OF INTEREST
 
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 The broad area of research in my lab is “Structure-function studies of membrane-associated proteins and peptides”. At present we are working on pore-forming toxin, naturally occurring antimicrobial peptides, design of novel cell-selective antimicrobial peptides and K+ channel proteins. By synthesizing conserved segments from these proteins and peptides, we are trying to identify and characterize their important structural and functional elements. Our long-term goal is to design peptides/peptidomimetics of pharmacological importance.
 
SELECTED PUBLICATIONS
 
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 Inhibition of lytic activity of E. coli toxin hemolysin E against human red blood cells by a leucine zipper peptide and understanding the underlying mechanism. Sharada Prasad Yadav, Aqeel Ahmad and Jimut Kanti Ghosh Biochemistry (ACS, in Press Dec. 2007).
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 Addition of a small hydrophobic segment from the head region region to an amphipathic leucine zipper like motif of E. coli toxin hemolysin E enhances the peptide-induced permeability of zwitterionic lipid vesicles. S. P. Yadav, A. Ahmad and J. K. Ghosh Biochim. Biophys. Acta 1768 (Biomembrane) 1574-1582 (2007).
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 Utilization of an amphipathic leucine zipper sequence to design antibacterial peptides with simultaneous modulation of toxic activity against human red blood cells. A. Ahmad, S. P. Yadav, N. Asthana, K. Mitra, S. P. Srivastava and J. K. Ghosh J. Biol. Chem. 281, 22029-22038 (2006).
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 Dissection of antibacterial and toxic activity of melittin: A leucine zipper motif plays crucial role in determining its hemolytic activity but not antibacterial activity. N. Asthana, S. P. Yadav and J. K. Ghosh J. Biol. Chem 279, 55042-55050 (2004).
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 Identification and characterization of an amphipathic leucine zipper like motif in E. coli toxin hemolysin E: Plausible role in the assembly and membrane-destabilization. S. P. Yadav, B. Kundu and J. K. Ghosh J. Biol. Chem. 278, 51023-34 (2003).
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 Sendai virus internal fusion peptide: structural and functional charaterization and a plausible mode of viral entry inhibition. J. K. Ghosh, S. G. Peisajovich, and Y Shai- Biochemistry 39, 11581-11592 (2000).
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 Direct evidence that a heptad repeat assists the fusion peptide derived from the sendai virus fusion protein in membrane fusion. J. K. Ghosh,., and Y. Shai, - J. Mol. Biol. 292, 531-546 (1999).
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 A peptide derived from a conserved domain of sendai virus fusion protein inhibits virus-cell fusion: Implication to the mechanism of viral fusion. J. K. Ghosh and Y. Shai- J. Biol. Chem. 273, 7252-7259 (1998).
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 Structure-function study of a heptad repeat positioned near the transmembrane domain of sendai virus fusion protein which blocks virus-cell fusion. J. K. Ghosh, S. G. Peisajovich, M. Ovadia and Y Shai- J. Biol. Chem. 273, 27182-27190 (1998).
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 Selective cytotoxicity of dermaceptin S3 towards intraerythrocytic Plasmodium Falciparum and the underlying molecular basis. J. K. Ghosh, D. Shaool, P. Guillaud, L. Ciceron, D. Mazier, I. Kustanovich, Y. Shai and A Mor- J. Biol. Chem. 272, 31609-30616 (1997)