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Publications of Dr. Shekhar C. Mande

  

  • Mycobacterium tuberculosis GroEL homologues unusually exist as lower oligomers and retain the ability to suppress aggregation of substrate proteins. R. Qamra, V. Srinivas and S. C. Mande. J. Mol. Biol. (2004) v.342, 605-617.

  • Crystal structure of the 65kDa heat shock protein, Chaperonin 60.2 of Mycobacterium tuberculosis. R. Qamra and S. C. Mande. J. Bacteriol. (2004) v. 186, 8105-8113.

  • Arrangement of subunits in peanut lectin. D. M. Salunkhe, M. J. Swamy, M. I. Khan, S. C. Mande, A. Surolia and M. Vijayan. J. Biol. Chem. (1985) 260, 13576-13579.

  • Structural studies on peanut lectin. S. C. Mande, S. Raghunathan, D. M. Salunkhe, M. I. Khan, M. J. Swamy, A. Surolia and M. Vijayan. Ind. J. Biochem. Biophys. (1988) 25, 166-171.

  • A fast algorithm for macromolecular packing calculations. S. C. Mande and K. Suguna. J. Appl. Cryst. (1989) 22, 627-629.

  • Cloning and overexpression of the triosephosphate isomerase genes from psychrophilic and thermophilic bacteria. F. Rentier-Delrue, S. C. Mande, S. Moyens, V. Mainfroid, K. Goraj, M. Lion, W. G. J. Hol and J. A. Martial. J. Mol. Biol. (1992) 229, 85-93.

  • Crystal structure of peanut lectin, a protein with unusual quaternary structure. R. Banerjee, S. C. Mande, V. Ganesh, K. Das, V. Dhanaraj, S. K. Mahanta, K. Suguna, A. Surolia and M. Vijayan. Proc. Natl. Acad. Sci., USA (1994) 91, 227-231.

  • Crystal structure of recombinant human triosephosphate isomerase at 2.8 A resolution. Triosephosphate isomerase related human genetic disorders and comparison with the trypanosomal enzyme. S. C. Mande, V. Mainfroid, K. H. Kalk, K. Goraj, J. A. Martial and W. G. J. Hol. Prot. Sci. (1994) 3, 810-821.

  • Protein crystallography and infectious diseases. C. L. M. J. Verlinde, E. A. Merritt, F. van den Akker, H. Kim, I. Feil, L. F. Delboni, S. C. Mande, S. Sarfaty, P. H. Petra and W. G. J. Hol. Prot Sci. (1994) 3, 1670-1686.

  • Crystal structure of recombinant triosephosphate isomerase from Bacillus stearothermophilus. An analysis of potential thermostability factors in six isomerases with known three dimensional structures points to the importance of hydrophobic interactions. F. Delboni, S. C. Mande, F. Rentier-Delrue, V. Mainfroid, S. Turley, F. M. D. Velliux, J. A. Martial and W. G. J. Hol. Prot. Sci. (1995) 4, 2594-2604.

  • Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae. S. C. Mande, V. Mehra, B. R. Bloom and W. G. J. Hol. Science (1996) 271, 203-206.

  • Three hTIM mutants that provide new insights on why TIM is a dimer. V. Mainfroid, P. Terpstra, M. Beauregard, J. M. Frere, S. C. Mande, W. G. J. Hol, J. A. Martial and Goraj K. J. Mol. Biol. (1996) 257, 441-456.

  • Stabilization of human triosephosphate isomerase by improvement of the stability of individual a -helices in dimeric as well as monomeric forms of the protein. V. Mainfroid, S. C. Mande, W. G. J. Hol, J. A. Martial and Goraj K. Biochemistry (1996) 35, 4110-4117.

  • Antitrypanosomiasis drug development based on structures of glycolytic enzymes. C. L. M. J. Verlinde, H. Kim, B. E. Bernstein, S. C. Mande and W. G. J. Hol in Structure Based Drug Design, (1997) P. Veerapandian ed. Marcel Dekker Inc., New York. pp. 365-394.*

  • Identification of an ABC transporter gene that exhibits mRNA level overexpression in fluoroquinolone resistant Mycobacterium smegmatis. S. Banerjee, P. Mishra, K. Bhat, S. C. Mande and P. Chakraborti. FEBS Letts. (1998) 425, 151-156.

  • Hemoglobin biosynthesis in Vitreoscilla stercoraria DW: Cloning, expression and characterization of a new homolog of a bacterial globin gene. M. Joshi, S. C. Mande and K. L. Dikshit. Appl. Environ. Microbiol. (1998) 64, 2220- 2228.

  • Identification of the INO1 gene of Mycobacterium tuberculosis H37Rv reveals a novel class of inositol-1-phosphate synthase enzyme. N. Bachhawat and S. C. Mande. J. Mol. Biol. (1999) 291, 531- 536.

  • Conserved structural features and sequence patterns in the GroES fold family. B. Taneja and S. C. Mande. Prot. Eng. (1999) 12, 815-818.

  • Function of the central domain of streptokinase in substrate plasminogen docking and processing revealed by site-directed mutagenesis. A. Chaudhary, S. Vasudha, K. Rajagopal, S. S. Komath, N. Garg, M. Yadav, S. C. Mande and G. Sahni. Protein Sci (1999) 8, 2791-805.

  • Structural characterization of protein denaturant interactions: crystal structures of hen egg white lysozyme in complex with guanidinium chloride and DMSO. S. C. Mande and M. E. Sobhia. Prot. Eng (2000) 13, 133- 141.

  • Complex evolution of the inositol-1-phosphate synthase gene among archaea and eubacteria. N. Bachhawat and S. C. Mande. Trends Genet. (2000) 16, 111-113.

  • Homology modelling of a novel xylanase: molecular basis of high thermostability and alkaline stability. S. S. Mande, N. Gupta, A. Ghosh and S. C. Mande. J. Biomol. Struct. Dyn. (2000) 18, 137-144.

  • Genomics and novel drug targets. B. Taneja, R. Chauhan and S. C. Mande. In Current R & D Highlights, CDRI, Lucknow. ed. H. S. Subramanya. (2000). 23, 6-11.**

  • Characterization of Mycobacterium tuberculosis H37Rv alkyl hydroperoxidase AhpC points to the importance of ionic interactions in oligomerization and activity. R. Chauhan and S. C. Mande Biochem. J. (2001) 354, 209- 215.

  • Metal ions modulate the plastic nature of Mycobacterium tuberculosis chaperonin-10. B. Taneja and S. C. Mande Prot. Eng. (2001) 14, 391- 395

  • Three- dimensional structure of Mycobacterium tuberculosis chaperonin-10 reveals a partially stable conformation of its mobile loop. B. Taneja and S. C. Mande Curr Sci. (2001) 81, 87- 91.

  • Chimeric Vitreoscilla hemoglobin (VHb) carrying flavoreductase domain relieves nitrosative stress in Escherichia coli: new insights into the functional role of VHb. Ramandeep, R. Pathania, V. Sharma, S. C. Mande and K. L. Dikshit Appl. Env. Microbiol. (2002) 68, 152-160.

  • Structure of Mycobacterium tuberculosis chaperonin-10 at 3.5 A resolution. B. Taneja and S. C. Mande Acta Crystallogr (2002) D58, 260-266.

  • Involvement of a nine-residue loop in the generation of the macromolecular substrate specificity by the activator complex through interaction with substrate kringle domains. J.Dhar, A.H.Pande, V.Sundram, J.S.Nanda, S.C.Mande and G.Sahni. J. Biol. Chem. (2002) v.277, 13257- 13267.

  • The TB Structural genomics consortium: providing a structural foundation for drug discovery C. W. Goulding, M. Apostol, D. H. Anderson, H. S. Gill, C. V. Smith, M. R. Kuo,J. K. Yang, G. S. Waldo, S. W. Suh, R. Chauhan, A. Kale, N. Bachhawat, S. C. Mande, J. M. Johnston, J. S. Lott, E. N. Baker, V. L. Arcus, D. Leys, K. J. McLean, A. W. Munro, J. Berendzen, V. Sharma, M. S. Park, D. Eisenberg, J. Sacchettini, T. Alber, B. Rupp, W. Jacobs, Jr. and T. C. Terwilliger Curr. Drug Targets- Infect. Dis. (2002) v.2, 121- 141.

  • Function of 90-loop (Thr90-Glu100) region of staphylokinase in plasminogen activation probed through site-directed mutagenesis and loop deletion G. Rajamohan, M. Dahiya, S. C. Mande, K. L. Dikshit Biochem J. (2002) v.365, 379- 389.

  • Site directed mutagenesis reveals a novel catalytic mechanism of Mycobacterium tuberculosis Alkylhydroperoxidase C. R. Chauhan and S. C. Mande Biochem J. (2002) 367, 255- 261.

  • Conserved sequence features in small b- barrels. R. Qamra, B. Taneja and S. C. Mande, Prot. Eng. (2003) 15, 967- 77.

  • The TB Structural Genomics Consortium: A Resource for TB Biology T. C. Terwilliger, M. S. Park, G. S. Waldo, J. Berendzen, L.-W. Hung, C.-Y. Kim, C. V. Smith, J. C. Sacchettini, M. Bellinzoni, R. Bossi, E. De Rossi, A. Mattevi, A. Milano, G. Riccardi, M. Rizzi, M. M. Roberts, A. R. Coker, P. Tormay, G. Fossati, P. Mascagni, A. R.M. Coates, S. P. Wood, C. W. Goulding, M. Apostol, D. H. Anderson, H. S. Gill, D. S. Eisenberg, B. Taneja, S. Mande, E. Pohl, V,. Lamzin, P. Tucker, M. Wilmanns, C. Colovos, W. Meyer-Klaucke, A. W. Munro, K. J. McLean, K. R. Marshall, D. Leys, J. K. Yang, H.-J. Yoon, B. I. Lee, M. G. Lee, J. E. Kwak, B. W. Han, J. Y. Lee, S.-H. Baek, S. W. Suh, M. M. Komen, V. ML. Arcus, E. N. Baker, J. S. Lott, W. JacobsU Jr.,UT. Alber,U B. Rupp Tuberculosis (2003) 83, 223- 249.

  • Human recombinant resistin protein displays a tendency to aggregate by forming intermolecular disulfide linkages B. Aruna, S. Ghosh, A. K. Singh, S. C. Mande, V. Srinivas, R. Chauhan, and N. Z. Ehtesham Biochemistry (2003) 42, 10554- 10559.




    *   Book Chapters
    ** Non peer-reviewed journals / supplements / proceedings

  • Dr. Shekhar C. Mande
    Structural Biology
    Research


    CONTACT INFORMATION

    Email :
    shekhar@cdfd.org.in

    Phone: 
    Fax     :

    +91-40-27171442, 27151344-46-47-48 extn.1400
    +91-40-27155610

    Last updated on :21 June, 2006.