Shekhar C. Mande
Ph. D.,FNA, FASc, FNASc
Staff Scientist - VI, CDFD, Hyderabad
Adjunct, University of Hyderabad
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Mapping conformational transitions in cyclin AMP receptor protein: crystal structure and normal mode analysis of Mycobacterium tuberculosis apo-cAMP receptor protein. P. Kumar, D. C. Joshi, Mohd Akif, Y. Akhter, S. E. Hasnain and S. C. Mande Biophys J. (2010) 98, 305- 314[PDF]
Facilitated oligomerization of mycobacterial GroEL: evidence for phosphorylation-mediated oligomerization. C. M. Kumar, G. Khare, C. V. Srikanth, A. K. Tyagi, A. A. Sardesai and S. C. Mande J. Bacteriol. (2009) 191, 6525- 6538[PDF]
Prediction of conditional gene essentiality through graph theoretical analysis of genome-wide functional linkages. P. Manimaran, S. R. Hegde and S. C. Mande Mol Biosyst. (2009) 5, 1936- 1942[PDF]
The PPE18 of Mycobacterium tuberculosis interacts with TLR2 and activates IL-10 induction in macrophage. S. Nair, P. A. Ramaswamy, S. Ghosh, D. C. Joshi, N. Pathak, I. Siddiqui, P. Sharma, S. E. Hasnain, S. C. Mande and S. Mukhopadhyay J Immunol. (2009) 183, 6269-6281[PDF]
A novel nucleoid associated protein of M. tuberculosis is a sequence homolog of GroEL D. Basu, G. Khare, S. Singh, A. Tyagi, S. Khosla and S. C. Mande Nucl. Acid. Res. (2009) 37, 4944- 4954.[PDF]
Functional studies on multiple thioredoxins from Mycobacterium tuberculosis Mohd Akif, G. Khare, A. K. Tyagi, S. C. Mande and A. A. Sardesai J. Bacteriol. (2008) 190, 7087- 7095[PDF]
Crystal structure of Mycobacterium tuberculosis YefM antitoxin reveals that it is not an intrinsically unstructured protein P. Kumar, B. Issac, E. J. Dodson, J. P. Turkenburg and S. C. Mande J. Mol. Biol. (2008) 383, 482- 493.[PDF]
Dynamic changes in protein functional linkage networks revealed by integration with gene expression data S. Hegde, P. Manimaran and S. C. Mande PLoS Compt Biol. (2008) 4(11): e1000237[PDF]
Mycobacterium tuberculosis heat shock protein 60 modulates immune response to PPD by manipulating the surface expression of TLR2 on macrophages N. Khan, K. Alam, S. C. Mande, V. L. Valluri, S. E. Hasnain and S. Mukhopadhyay Cell Microbiol. (2008) 10, 1711- 1722[PDF]
Exploiting 3D structural templates for detection of metal binding-sites in protein structures K. Goyal and S. C. Mande
Proteins, Struct, Funct, Bioinform. (2008) 70, 1206-1218[PDF]
PAR-3D: a server to predict protein active site residues K. Goyal, D. Mohanty and S. C. Mande Nucl. Acid. Res. (2007) 35, W503-505.[PDF]
BioSuite: A comprehensive bioinformatics software package (A unique industry- academia collaboration) M. Vidyasagar and 111 other authors
Curr. Sci. (2007) 92, 29- 38[PDF]
Inferring genome-wide functional linkages in Escherichia coli by combining improved genome context methods: comparison with high throughput experimental data S. Yellaboina, K. Goyal and S. C. Mande
Genome Res. (2007) 17, 527- 535.[PDF]
Multiple gene duplication and rapid evolution in the groEL gene: functional implications K. Goyal, R. Qamra and S. C. Mande
J. Mol. Evol. (2006) 63, 781-787.[PDF]
Crystallization and preliminary X-ray crystallographic studies of Mycobacterium tuberculosis CRP/FNR family transcription regulator Mohd. Akif, Y. Akhter, S. E. Hasnain and S. C. Mande Acta crystallogr. (2006) F62, 873-875.[PDF]
The 2.15 crystal structure of M. tuberculosis chorismate mutase reveals unexpected gene duplication, and suggests a role in host-pathogen interactions R. Qamra, P. Prakash, B. Aruna, S. E. Hasnain and S. C. Mande Biochemistry (2006) 45, 6997- 7005.[PDF]
Cation mediated interplay of loops in Mycobacterium tuberculosis Chaperonin-10 S. Vijaykrishnan, R. Qamra, C. Verma, R. Sen and S. C. Mande J. Biomolec. Struct. Dyn. (2006) 23, 365- 376.[PDF]
Conformational flexibility of M. tuberculosis Thioredoxin reductase: Crystal Structure and Normal Mode Analysis Mohd. Akif, K. Suhre, C. Verma and S. C. Mande Acta crystallogr. (2005) D61, 1603- 1611.[PDF]
The unusual chaperonins of Mycobacterium tuberculosis R. Qamra, S. C. Mande, A. R. M. Coates and B. Henderson Tuberculosis (2005) 85, 385- 394.[PDF]
Effect of alcohols on protein hydration: Crystallographic analysis of hen egg white lysozyme in presence of alcohols A. Deshpande, S. Nimsadkar and S. C. Mande Acta crytallogr. (2005) D61, 1005-1008.[PDF]
Crystallization and preliminary X-ray crystallographic studies of Mycobacterium tuberculosis chorismate mutase R. Qamra, P. Prakash, B. Aruna, S. E. Hasnain and S. C. Mande Acta crystallogr. (2005) F61, 473-475[PDF]
Crystal Structure of the 65 kDa Heat Shock Protein, Chaperonin 60.2 of Mycobacterium tuberculosis R. Qamra and S. C. Mande J. Bacteriol. (2004) 186, 8105-8113[PDF]
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) 342, 605-617[PDF]
Expression, purification, crystallization and preliminary X-ray crystallographic studies of Mycobacterium tuberculosis thioredoxin reductase
Mohd. Akif, R. Chauhan and S. C. Mande Acta Crystallogr D (2004) 60, 777-779[PDF}
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.[PDF]
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. C. 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. Jacobs Jr.,T. Alber, B. Rupp Tuberculosis (2003) 83, 223- 249.[PDF]
Identification of conserved residue patterns in small - barrel proteins. R. Qamra, B. Taneja and S. C. Mande
Prot. Eng. (2002) 15, 967- 77.[PDF]
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.[PDF]
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) 365, 379-389.[PDF]
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) 2, 121- 141.[PDF]
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) 277, 13257- 13267.[PDF]
Structure of Mycobacterium tuberculosis chaperonin-10 at 3.5 resolution. B. Taneja and S. C. Mande Acta Crystallogr (2002) D58, 260-266.[PDF]
Chimeric Vitreoscilla Hemoglobin (VHb) Carrying a Flavoreductase Domain Relieves Nitrosative Stress in Escherichia coli: New Insight into the Functional Role of VHb. R. Kaur, R. Pathania, V. Sharma, S. C. Mande and K. L. Dikshit. Appl. Environ. Microbiol. (2002) 68, 152-160.[PDF]
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.[PDF]
Metal ions modulate the plastic nature of Mycobacterium tuberculosis chaperonin-10. B. Taneja and S. C. Mande Prot. Eng. (2001) 14, 391- 395.[PDF]
Characterization of the 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.[PDF]
Genomics and novel drug targets. B. Taneja, R. Chauhan and S. C. Mande In Current R & D Highlights, CDRI, Lucknow. (2000) ed. H. S. Subramanya. 23, 6- 11[PDF]
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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. Biomolec. Str. Dyn. (2000) 18, 137- 144.[PDF]
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.[PDF]
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. Sophia. Prot Eng. (2000) 13, 133- 141.[PDF]
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. Prot. Sci. (1999) 8, 2791- 2805.[PDF]
Conserved structural features and sequence patterns in the GroES fold family. B. Taneja and S. C. Mande. Prot. Eng. (1999) 12, 815- 818.[PDF]
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.[PDF]
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.[PDF]
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.[PDF]
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.[PDF]
Stabilization of human triosephosphate isomerase by improvement of the stability of individual -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.[PDF]
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.[PDF]
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.[PDF]
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.[PDF]
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.[PDF]
Crystal structure of recombinant human triosephosphate isomerase at 2.8 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.[PDF]
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.[PDF]
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.
A fast algorithm for macromolecular packing calculations. S. C. Mande and K. Suguna. J. Appl. Cryst. (1989) 22, 627-629.
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
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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.
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| Last updated on : January 27 2010. |
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