Area of Specialization

• X-ray Crystallography
• Computational Biology
• Computational methods to analyse large-scale biological data

Research Projects executed

Ph. D. students successfully guided

>15, degrees awarded by Jawaharlal Nehru University, New Delhi; Manipal University, Manipal; University of Hyderabad, Hyderabad and Savitribai Phule Pune University, Pune

Publications in peer reviewed journals

• 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 Å 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.  Prot. Sci. (1999) 8, 2791- 2805.
• 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.
• 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. Biomolec. Str. 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. (2000) ed. H. S. Subramanya. 23, 6- 11.
• 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.
• 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 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.
• Structure of Mycobacterium tuberculosis chaperonin-10 at 3.5 Å 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) 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) 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) 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.
• Identification of conserved residue patterns in small b- barrel proteins.  R. Qamra, B. Taneja and S. C. Mande.  Prot. Eng. (2002) 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. 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.
• 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
• 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
• 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
• 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
• 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.
• 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.
• The unusual chaperonins of Mycobacterium tuberculosis.  R. Qamra, S. C. Mande, A. R. M. Coates and B. Henderson.  Tuberculosis (2005) 85, 385- 394.
• 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.
• 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.
• The 2.15Å 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.
• 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.
• 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.
• Inferring genome-wide functional linkages in prokaryotes by combining improved genome context methods. S. Yellaboina, K. Goyal and S. C. Mande.  Genome Res. (2007) 17, 527-535.
• BioSuite: A comprehensive bioinformatics software package (A unique industry- academia collaboration).  M. Vidyasagar and 111 other authors.  Curr. Sci. (2007) 92, 29- 38.
• 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.
• 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.
• 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.
• 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.
• 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.
• Dynamic changes in protein functional linkage networks revealed by integration with gene expression data.  S. Hegde, P. Manimaran and S. C. Mande.  PLoS Comput. Biol. (2008) 4(11): e1000237
• 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.  Nucleic Acids Res. (2009) 37, 4944- 4954.
• 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.
• Prediction of conditional gene essentiality through graph theoretical analysis of genome-wide functional linkages.  P. Manimaran, S. R. Hegde, S. C. Mande.  Mol Biosyst. (2009) 5, 1936-1942.
• 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.
• Mapping conformational transitions in the cyclic-AMP receptor protein: Crystal structure and Normal Mode Analysis of M. 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.
• Book review: Annual Reviews of Biophysics.  S. C. Mande.  Curr Sci (2010) 99, 242-243.
• Structural Biology of Mycobacterium tuberculosis proteins: the Indian Efforts.  A. Arora, N. R. Chandra, A. Das, B. Gopal, S. C. Mande^*, B. Prakash, R. Ramachandran, R. Sankaranarayanan, K. Sekar, K. Suguna, A. K. Tyagi and M. Vijayan.  Tuberculosis (2011) 91, 456-458.
• Protein chaperones and non-protein substrates: on substrate promiscuity of GroEL.  C. M. S. Kumar and S. C. Mande.  Curr Sci (2011) 100, 1646- 1653.
• Delineation of key regulatory elements identifies points of vulnerability in the mitogen-activated signaling network.  N. Jailkhani, S. Ravichandran, S. R. Hegde, Z. Siddiqui, S. C. Mande and K. V. Rao.  Genome Res (2011) 21, 2067- 2081.
• Understanding communication signals during mycobacterial latency through predicted genome-wide protein interactions and Boolean modeling.  S. R. Hegde, H. Rajasingh, C. Das, S. S. Mande and S. C. Mande.  PLoS One (2012) 7, e33893.
• Identification of self-consistent modulons from bacterial microarray expression data with help of structured regulon gene set.  E. A. Permina, Y. A. Medvedeva, P. M. Baeck, S. R. Hegde, S. C. Mande and V. J. Makeev.  J Biomol Struct Dyn (2013) 31, 115- 124.
• Probing gene regulatory networks to decipher host-pathogen interactions.  K. V. S. Rao, D. Kumar and S. C. Mande.  in Systems Biology of Tuberculosis Ed.s McFadden, Beste and Kierzek. (2012) Pp. 37-54.
• Analysis of dihedral angle variability in related protein structures.  S. C. Mande, A. Kumar and P. Ghosh.  in Biomolecular forms and functions, A celebration of 50 years of Ramachandran map. Eds. M. Bansal and N. Srinivasan. (2013) World Scientific Publishing, Singapore, pp. 107-115.
• Evolution of bacterial chaperonin 60 paralogs and moonlighting activity.  S. C. Mande, C. M. Santosh Kumar and A. Sharma.  In Moonlighting cell stress proteins in microbial infections.  Heat Shock Proteins book series Vol. 7.  Ed. B. Henderson, Springer Netherlands, pp. 101-121.
• Crystal structure of M. tuberculosis NrdH at 0.87 Å resolution suggests a possible mode of its activity.  S. Phulera and S. C. Mande.  Biochemistry (2013) 52, 4056- 4065.
• Differential enrichment of regulatory motifs in the composite network of protein-protein and gene regulatory interactions.  SR Hegde, K Pal and S. C.  Mande.  BMC Syst Biol. (2014) 8, 26.
• Early developments in Crystallography.  S. C. Mande.  Resonance, December (2014) 1077- 86.
• Redox proteins of Mycobacterium tuberculosis.  S Phulera, Mohd Akif, A. Sardesai and S. C. Mande.  J IISc (2014) 94, 127- 137.
• Status of the crystallography beamlines at Elettra .  A. Lausi, M. Polentarutti, S. Onesti, J. R. Plaisier,  E. Busetto, G. Bais, L. Barba, A. Cassetta, G. Campi, D. Lamba, A. Pifferi, S. C. Mande, D. D. Sarma, S. M. Sharma, G. Paolucci.  The European Physical Journal Plus (2015) 130, 43.
• Multiple chaperonins in bacteria- novel functions and non-canonical behaviours.  C. M. Kumar, S. C. Mande and G. Mahajan.  Cell Stress Chaperones (2015) 20, 555-574.
• From system-wide differential gene expression to perturbed regulatory factors: a combinatorial approach.  G. Mahajan and S. C. Mande.  PLoS One (2015) 10, e0142147
• Towards understanding the biological function of the unusual chaperonin Cpn601. (GroEL1) of Mycobacterium tuberculosis.  A. Sharma, T. Rustad, G. Mahajan, A. Kumar, K. V. Rao, S. Banerjee, D. R. Sherman and S. C. Mande.  Tuberculosis (2016) 97, 137-46.
• GroEL2 of M. tuberculosis reveals the importance of structural pliability in chaperonin function.  N. Chilukoti, C. M. Kumar and S. C. Mande.  J. Bacteriol. (2016) 198, 486-97.
• Book review: The most wanted man in China, my journey from scientist to enemy of the state by Fang Lizhi.  S. C. Mande.  Curr Sci (2016) 110, 2183- 2184.
• Biology across scales: historical perspective on some Indian contributions.  S. C. Mande.  Curr Sci (2016) 110, 529-532.
• Nobel prize in Physiology or Medicine 2016.  S. C. Mande.  Curr Sci (2016) 111, 1294-1295.
• Editorial in Current Science: Indian human microbiome initiative, Indian-ness through the magnifying glass.  Y. S. Shouche and S. C. Mande.  Curr Sci (2017) 112, 207- 208.
• Using structural knowledge in the protein data bank to inform the search for potential host-microbe protein interactions in sequence space: application to Mycobacterium tuberculosis.  G. Mahajan and S. C. Mande.  BMC Bioinform (2017) 18, 201
• Book: Prokaryotic chaperonins.  Eds. C. M. S. Kumar and S. C. Mande.  (2017) Springer series on Heat Shock Proteins
• Ser/Thr protein kinase PrkC-mediated regulation of GroEL is critical for biofilm formation in Bacillus anthracis.  G. Arora, A. Sajid, R. Viramani, A. Singhal, C. M. S. Kumar, N. Dhasmana, T. Khanna, A. Maji, R. Misra, V. Molle, D. Becher, U. Gerth, S. C. Mande and Y. Singh.  NPJ Biofilms Microbiom (2017) 3:7.
• A glimpse into the structure and function of atypical type I chaperonins.  M. Y. Ansari and S. C. Mande.  Front. Mol. Biosci (2018) 5: 31Structural basis of hypoxic gene regulation by the Rv0081
• Structural basis of hypoxic gene regulation by the Rv0081 transcription factor of Mycobacterium tuberculosis.  A. Kumar, S. Phulera, A. Rizvi, P. J. Sonawane, H. S. Panwar, S. Banerjee, A. Sahu and S. C. Mande.  FEBS Letts (2019) 593, 982-9
• Genome analysis identifies a spontaneous nonsense mutation in ppsD leading to attenuation of virulence in laboratory-manipulated Mycobacterium tuberculosis.  S. De Majumdar, K. Sikri, P. Ghosh, N. Jaisinghani, M. Nandi, S. Gandotra, S. Mande and J. S. Tyagi.  BMC Genomics (2019) 20: 129
• Multiple transcription factors co-regulate the Mycobacterium tuberculosis adaptation response to vitamin C.  M. Nandi, K. Sikri, N. Chaudhary, S. C. Mande, R. D. Sharma and J. S. Tyagi.  BMC Genomics (2019) 20: 887
• 16S rDNA based skin microbiome data of healthy individuals and leprosy patients from India.  N. Bayal, S. Nagpal, M. M. Haque, M. S. Patole, V. Valluri, R. Suryavanshi, S. S. Mande and S. C. Mande.  Scientific Data (2019) 6: 225
• Spatially conserved motifs in complement control protein domains determine functionality in regulators of complement activation- family proteins.  H. Ojha, P. Ghosh, H. S. Panwar, R. Shende, A. Gondane, S. C. Mande and A. Sahu.  Comm Biol (2019) 2: 290
• Rewiring of metabolic network in Mycobacterium tuberculosis during adaptation to different stresses.  A. Rizvi, A. Shankar, A. Chatterjee, T. H. More, T. Bose, A. Dutta, K. Balakrishnan, L. Madugulla, S. Rapole, S. S. Mande, S. Banerjee and S. C. Mande.  Front Microbiol (2019) 10: 2417
• Metabolomics studies to decipher stress responses in Mycobacterium smegmatis point to a putative pathway of methylated amine biosynthesis.  A. Rizvi, S. Yousf, K. Balakrishnan, H. K. Dubey, S. C. Mande, J. Chugh and S. Banerjee.  J. Bacteriol. (2019) 201: e00707-18.
• A novel function of Mycobacterium tuberculosis chaperonin paralog GroEL1 in copper homeostasis.  M. Y. Ansari, S. D. Batra, H. Ojha, K. Dhiman, A. Ganguly, J. S. Tyagi and S. C. Mande.  FEBS Letts (2020) 594, 3305- 3323.
• Active and prospective latent tuberculosis are associated with different metabolomics profiles: clinical potential for the identification of rapid and non-invasive biomarkers.  A. Albors-Vaquer, A. Rizvi, M. Matzapetakis, P. Lamosa, A. V. Coelho, A. B. Patel, S. C. Mande, S. Gaddam, A. Pineda-Lucena, S. Banerjee and L. Puchades-Carrasco.  Emerg. Microbes & Infect. (2020) 9:1, 1131-1139.
• CoRNeA: A pipeline to decrypt the inter-protein interfaces from amino acid sequence information.  K. Chopra, B. Burdak, K. Sharma, A. Kembhavi, S. C. Mande and R. Chauhan.  Biomol. (2020) 10, 938
• Role of S&T organisations in mitigation of Covid-19: CSIR as a case study.  G. V. Rayasam and S. C. Mande.  Ind. Chem. Eng. (2020) 62, 333-342
• Structural aspects of lesional and non-lesional skin microbiota reveal key community changes in leprosy patients from India.  N. Bayal, S. Nagpal, M. M. Haque, M. S. Patole, Y. S. Shouche, S. C. Mande and S. S. Mande.  Sci. Reports (2021) 11: 3294
• Mortality due to Covid-19 in different countries is associated with their demographic character and prevalence of autoimmunity.  B. Chatterjee, R. L. Karandikar and S. C. Mande.  Curr. Sci. (2021) 120, 501- 508.
• Discovery of serum biomarkers for diagnosis of tuberculosis by NMR metabolomics including cross-validation with a second cohort.  R. Conde, R. Laires, L. G. Gonsalves, A. Rizvi, C. Barroso, M. Villar, R. Macedo, M. J. Simoes, S. Gaddam, P. Lamosa, L. Puchades-Carrasco, A. Pineda-Lucena, A. B. Patel, S. C. Mande, S. Banerjee, M. Matzapetakis and A. C. Coelho.  Biomed J (2021) S2319-4170(21)00094-9
• Chaperonin abundance enhances bacterial fitness.  C. M. S. Kumar, K. Chugh, A. Dutta, V. Mahamkali, T. Bose, S. S. Mande, S. C. Mande and P. A. Lund.  Front. Mol. Biosci. (2021) 8: 669996
• Structure-sequence features based prediction of phosphosites of serine/ threonine protein kinases of Mycobacterium tuberculosis.  V. V. Nilkanth and S. C. Mande.  Proteins (2022) 90, 131- 141.

Awards/Honour/Memberships 

Fellowships and Memberships of professional bodies:

• Fellow, Indian National Science Academy, Delhi, Elected 2010
• Fellow, National Academy of Sciences, Allahabad, India, Elected 2003
• Fellow, Indian Academy of Sciences, Bangalore, Elected 2003

Awards:

• B M Birla Young Scientist Award, 1999
• Shanti Swarup Bhatnagar Prize for Biological Sciences, 2005
• B K Bachhawat Memorial Lecture award of the National Academy of Sciences, Allahabad, 2017
• B C Guha Memorial Lecture award of the Indian National Science Academy, Delhi, 2017
• Aryabhata Medal of the Indian National Science Academy, 2020

Other recognitions:

• Wellcome Trust International Senior Research Fellow, 2003-08
• Fellow, Andhra Pradesh Akademi of Sciences, Elected 2010
• Fellow, Maharashtra Academy of Sciences, Elected, 2015
• Bharat Asmita Award of MIT World Peace University, Pune, 2019
• H K Firodia Vijnan Bhushan Award, 2020

Memberships of Professional Bodies:

• Life member, Indian Crystallographic Association
• Life member, Indian Science Congress Association
• Life member, Indian Biophysical Society
• Member, Indian Cancer Genome Atlas (ICGA)

Some key role in Institutional, National and International bodies:

• Nominee of the Hon’ble President of India in the pan- Indian Institute of Technology council, May 2022-
• Chairman, Governing Body, National Council of Science Museums (an autonomous body under the Ministry of Culture, Govt of India).
• Chairman of Indian delegation to the General Assembly of International Union of Crystallography (IUCr), 2017
• Dean (Academic affairs), CDFD, Hyderabad 2003- 11
• Vice President, Indian Crystallographic Association, 2012-14.
• National President of Vijnana Bharati
• Currently Consultant, Commission on Crystallography in Arts and Cultural Heritage of the International Union of Crystallography (IUCr)
• Former Member of the Management Council of the Tata Institute of Fundamental Research, Mumbai
• Served on selection committees of Directors of CSIR Laboratories; Selection committees of Vice Chancellors of Universities and Directors of National Laboratories; Committees to select candidates for high level bodies; Committees constituted by the learned Academies in India.