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Journal Article
S. K. Berwal, Bhatia, V., Bendre, A., Suresh, C. G., Chatterjee, S., and Pal, J. K., “Activation of HRI is mediated by Hsp90 during stress through modulation of the HRI-Hsp90 complex”, International Journal of Biological Macromolecules, vol. 118, pp. 1604-1613, 2018.
A. D. Bendre, Ramasamy, S., and Suresh, C. G., “Analysis of Kunitz inhibitors from plants for comprehensive structural and functional insights”, International Journal of Biological Macromolecules, vol. 113, pp. 933-943, 2018.
A. A. Wani, Ahanger, S. H., Bapat, S. A., Rangrez, A. Y., Hingankar, N., Suresh, C. G., Barnabas, S., Patole, M. S., and Shouche, Y. S., “Analysis of mitochondrial DNA sequences in childhood encephalomyopathies reveals new disease-associated variants”, Plos One, vol. 2, no. 9, p. e942, 2007.
A. A. Wani, Rangrez, A. Y., Kumar, H., Bapat, S. A., Suresh, C. G., Barnabas, S., Patole, M. S., and Shouche, Y., “Analysis of reactive oxygen species and antioxidant defenses in complex I deficient patients revealed a specific increase in superoxide dismutase activity”, Free Radical Research, vol. 42, no. 5, pp. 415-427, 2008.
S. R. Kumar, Suresh, C. G., Brannigan, J. A., Dodson, G. G., and Gaikwad, S. M., “Bile salt hydrolase, the member of Ntn-hydrolase family: differential modes of structural and functional transitions during denaturation”, IUBMB Life, vol. 59, no. 2, pp. 118-125, 2007.
K. N. Rao and Suresh, C. G., “Bowman-birk protease inhibitor from the seeds of vigna unguiculata forms a highly stable dimeric structure”, Biochimica et Biophysica Acta-Proteins and Proteomics, vol. 1774, no. 10, pp. 1264-1273, 2007.
A. Kumar, Prabhune, A., Suresh, C. G., and Pundle, A., “Characterization of smallest active monomeric penicillin V acylase from new source: a yeast, rhodotorula aurantiaca (NCIM 3425)”, Process Biochemistry, vol. 43, no. 9, pp. 961-967, 2008.
A. Dipak Bendre, Ramasamy, S., and Suresh, C. G., “Chickpea Kunitz Inhibitor: a mechanistic basis for trypsin inhibition”, Acta Crystallographica A‐Foundation and Advances, vol. 70, p. C271, 2014.
N. Kumar Varshney, Ramasamy, S., Brannigan, J. A., Wilkinson, A. J., and Suresh, C. G., “Cloning, overexpression, crystallization and preliminary X-ray crystallographic analysis of a slow-processing mutant of penicillin G acylase from Kluyvera citrophila”, Acta Crystallographica Section F-Structural Biology and Crystallization Communications, vol. 69, no. 8, pp. 925-929, 2013.
P. M. Chandra, Brannigan, J. A., Prabhune, A., Pundle, A., Turkenburg, J. P., Dodson, G. G., and Suresh, C. G., “Cloning, preparation and preliminary crystallographic studies of penicillin V acylase autoproteolytic processing mutants”, Acta Crystallographica Section F-Structural Biology and Crystallization Communications, vol. 61, no. Part 1, pp. 124-127, 2005.
P. Rathinaswamy, Pundle, A. V., Prabhune, A., SivaRaman, H., Brannigan, J. A., Dodson, G. G., and Suresh, C. G., “Cloning, purification, crystallization and preliminary structural studies of penicillin V acylase from Bacillus subtilis”, Acta Crystallographica Section F-Structural Biology Communications, vol. 61, no. Part 7, pp. 680-683, 2005.
P. N. Dharker, Gaikwad, S. M., Suresh, C. G., Dhuna, V., Khan, M. Islam, Singh, J., and Kamboj, S. Singh, “Comparative studies of two araceous lectins by steady state and time-resolved fluorescence and CD spectroscopy”, Journal of Fluorescence, vol. 19, no. 2, pp. 239-248, 2009.
R. S. Joshi, Mishra, M., Suresh, C. G., Gupta, V. S., and Giri, A. P., “Complementation of intramolecular interactions for structural-functional stability of plant serine proteinase inhibitors”, Biochimica Et Biophysica Acta-General Subjects, vol. 1830, no. 11, pp. 5087-5094, 2013.
R. K. Sreejith, Yadav, V. Nand, Varshney, N. K., Berwal, S. K., Suresh, C. G., Gaikwad, S. M., and Pal, J. K., “Conformational characterization of human eukaryotic initiation factor 2 alpha: a single tryptophan protein”, Biochemical and Biophysical Research Communications, vol. 390, no. 2, pp. 273-279, 2009.
U. Sharma, Gaikwad, S. M., Suresh, C. G., Dhuna, V., Singh, J., and Kamboj, S. Singh, “Conformational transitions in ariesaema curvatum lectin: characterization of an acid induced active molten globule”, Journal of Fluorescence, vol. 21, no. 2, pp. 753-763, 2011.
R. K. Sreejith, Suresh, C. G., Bhosale, S. H., Bhavnani, V., Kumar, A., Gaikwad, S. M., and Pal, J. K., “Conformational transitions of the catalytic domain of heme-regulated eukaryotic initiation factor 2 alpha kinase, a key translational regulatory molecule”, Journal of Fluorescence, vol. 22, no. 1, pp. 431-441, 2012.
L. Satyanarayana, Gaikwad, S. M., Balkrishnan, H., and Suresh, C. G., “Crystal structure and fluorescence analysis of alkaline thermostable xylanase from bacillus sp (NCL 87-6-10)”, Protein and Peptide Letters, vol. 20, no. 2, pp. 125-132, 2013.
U. Sharma, Katre, U. V., and Suresh, C. G., “Crystal structure of a plant albumin from cicer arietinum (chickpea) possessing hemopexin fold and hemagglutination activity”, Planta, vol. 241, no. 5, pp. 1061-1073, 2015.
U. V. Katre, Gaikwad, S. M., Bhagyawant, S. S., Deshpande, U. D., Khan, M. Islam, and Suresh, C. G., “Crystallization and preliminary x-ray characterization of a lectin from Cicer arietinum (chickpea)”, Acta Crystallographica Section F-Structural Biology and Crystallization Communications, vol. 61, pp. 141-143, 2005.
N. Kumar Varshney, R. Kumar, S., Ignatova, Z., Prabhune, A., Pundle, A., Dodson, E. J., and Suresh, C. G., “Crystallization and X-ray structure analysis of a thermostable penicillin G acylase from alcaligenes faecalis”, Acta Crystallographica Section F-Structural Biology and Crystallization Communications, vol. 68, pp. 273-277, 2012.
I. Das, Pathak, T., and Suresh, C. G., “Diastereoselective and general route to 5-amino-5-deoxysugars: influence of C-3 substitution on the addition of amines to C-5 of vinyl sulfone-modified Hex-5-enofuranosyl carbohydrates”, Journal of Organic Chemistry, vol. 70, no. 20, pp. 8047-8054, 2005.
P. Panigrahi, Sule, M., Ghanate, A., Ramasamy, S., and Suresh, C. G., “Engineering proteins for thermostability with iRDP web server”, Plos One, vol. 10, no. 10, p. e0139486, 2015.
U. V. Katre and Suresh, C. G., “Features of homotetrameric molecular association in protein crystals”, Acta Crystallographica Section D-Biological Crystallography, vol. 65, pp. 1-10, 2009.
R. Sharma and Suresh, C. G., “Genome-wide identification and structure-function studies of proteases and protease inhibitors in cicer arietinum (chickpea)”, Computers in Biology and Medicine, vol. 56, pp. 67-81, 2015.
R. Sharma, Rawat, V., and Suresh, C. G., “Genome-wide identification and tissue-specific expression analysis of UDP-glycosyltransferases genes confirm their abundance in cicer arietinum (chickpea) genome”, Plos One, vol. 9, no. 10, p. e109715, 2014.
D. Chand, Ramasamy, S., and Suresh, C. G., “Highly active bile salt hydrolase from enterococcus faecalis shows positive cooperative kinetics”, Process Biochemistry, vol. 51, no. 2, pp. 263-269, 2016.
T. M. Jaokar, Patil, D. P., Shouche, Y. S., Gaikwad, S. M., and Suresh, C. G., “Human mitochondrial NDUFS3 protein bearing leigh syndrome mutation is more prone to aggregation than its wild-type”, Biochimie, vol. 95, no. 12, pp. 2392-2403, 2013.
P. Panigrahi, Sule, M., Sharma, R., Ramasamy, S., and Suresh, C. G., “Improved method for specificity annotation shows a distinct evolutionary divergence among the microbial enzymes of the cholylglycine hydrolase family”, Microbiology-SGM, vol. 160, pp. 1162-1174, 2014.
R. Sharma, Panigrahi, P., and Suresh, C. G., “In-Silico analysis of binding site features and substrate selectivity in plant flavonoid-3-o glycosyltransferases (F3GT) through molecular modeling, docking and dynamics simulation studies”, Plos One, vol. 9, no. 3, p. e92636, 2014.
D. Chand, Avinash, V. S., Yadav, Y., Pundle, A. V., Suresh, C. G., and Ramasamy, S., “Molecular features of bile salt hydrolases and relevance in human health”, Biochimica et Biophysica Acta - General Subjects, vol. 1861, no. 1, pp. 2981-2991, 2017.
R. Mukherji, Varshney, N. Kumar, Panigrahi, P., Suresh, C. G., and Prabhune, A., “New role for penicillin acylases: degradation of acyl homoserine lactone quorum sensing signals by Kluyvera citrophila penicillin G acylase”, Enzyme and Microbial Technology , vol. 56, pp. 1-7, 2014.
V. Sunder Avinash, Ramasamy, S., Suresh, C. G., and Pundle, A., “Penicillin V acylase from pectobacterium atrosepticum exhibits high specific activity and unique kinetics”, International Journal of Biological Macromolecules, vol. 79, pp. 1-7, 2015.
P. Rathinaswamy, Gaikwad, S. M., Suresh, C. G., Prabhune, A., Brannigan, J. A., Dodson, G. G., and Pundle, A. V., “Purification and characterization of YxeI, a penicillin acylase from Bacillus subtilis”, International Journal of Biological Macromolecules, vol. 50, no. 1, pp. 25-30, 2012.
D. N. Nair, Suresh, C. G., and Singh, D. Deepak, “Purification, crystallization and preliminary X-ray characterization of a haemagglutinin from the seeds of Jatropha curcas”, Acta Crystallographica Section F-Structural Biology and Crystallization Communications, vol. 67, pp. 1534-1536, 2011.
U. Sharma and Suresh, C. G., “Purification, crystallization and X-ray characterization of a Kunitz-type trypsin inhibitor protein from the seeds of chickpea (Cicer arietinum)”, Acta Crystallographica Section F-Structural Biology and Crystallization Communications, vol. 67, pp. 714-717, 2011.
R. S. Joshi, Mishra, M., Tamhane, V. A., Ghosh, A., Sonavane, U., Suresh, C. G., Joshi, R., Gupta, V. S., and Giri, A. P., “Remarkable efficiency of a pin-II proteinase inhibitor sans two conserved disulfide bonds is due to enhanced flexibility and hydrogen bond density in the reactive site loop”, Journal of Biomolecular Structure & Dynamics, vol. 32, no. 1, pp. 13-26, 2014.
P. Panigrahi, Chand, D., Mukherji, R., Ramasamy, S., and Suresh, C. G., “Sequence and structure-based comparative analysis to assess, identify and improve the thermostability of penicillin G acylases”, Journal of Industrial Microbiology & Biotechnology, vol. 42, no. 11, pp. 1493-1506, 2015.
U. V. Katre, Suresh, C. G., Khan, M. Islam, and Gaikwad, S. M., “Steady state and time-resolved fluorescence studies of a hemagglutinin from Moringa oleifera”, Journal of Fluorescence, vol. 18, no. 2, pp. 479-485, 2008.
H. Balakrishnan, Satyanarayana, L., Gaikwad, S. M., and Suresh, C. G., “Structural and active site modification studies implicate Glu, Trp and Arg in the activity of xylanase from alkalophilic Bacillus sp (NCL 87-6-10)”, Enzyme and Microbial Technology, vol. 39, no. 1, pp. 67-73, 2006.
S. R. Kumar, Brannigan, J. A., Prabhune, A., Pundle, A. V., Dodson, G. G., Dodson, E. J., and Suresh, C. G., “Structural and functional analysis of a conjugated bile salt hydrolase from Bifidobacterium longum reveals an evolutionary relationship with penicillin V acylase”, Journal of Biological Chemistry, vol. 281, pp. 32516-32525, 2006.
A. D. Bendre, Suresh, C. G., Shanmugam, D., and Ramasamy, S., “Structural insights into the unique inhibitory mechanism of Kunitz type trypsin inhibitor from Cicer arietinum L. Vol. 37”, Journal of Biomolecular Structure & Dynamics, vol. 37, no. 10, pp. 2669-2677, 2019.
V. Sunder Avinash, Panigrahi, P., Suresh, C. G., Pundle, A. V., and Ramasamy, S., “Structural modelling of substrate binding and inhibition in penicillin V acylase from pectobacterium atrosepticum”, Biochemical and Biophysical Research Communications, vol. 437, no. 4, pp. 538-543, 2013.
D. Chand, “Structure and function of a highly active Bile Salt Hydrolase (BSH) from Enterococcus faecalis and post-translational processing of BSH enzymes”, Biochim Biophys Acta., vol. 1866, no. 4, pp. 507-518, 2018.
D. Chand, Varshney, N. K., Ramasamy, S., Panigrahi, P., Brannigan, J. A., Wilkinson, A. J., and Suresh, C. G., “Structure mediation in substrate binding and post-translational processing of penicillin acylases: Information from mutant structures of Kluyvera citrophila penicillin G acylase”, Protein Science, vol. 24, no. 10, pp. 1660-1670, 2015.
D. Chand, Panigrahi, P., Ramasamy, S., and Suresh, C. G., “Structure of highly active BSH enzyme with subordinated post-translational excision”, Acta Crystallographica A‐Foundation and Advances, vol. 70, p. C272, 2014.
U. V. Katre, Suresh, C. G., Khan, M. Islam, and Gaikwad, S. M., “Structure-activity relationship of a hemagglutinin from Moringa oleifera seeds”, International Journal of Biological Macromolecules, vol. 42, no. 2, pp. 203-207, 2008.
S. R. Kumar, Prabhune, A., Pundle, A. V., Karthikeyan, M., and Suresh, C. G., “Tryptophan residue is identified in the substrate binding of penicillin G acylase from Kluyvera citrophila”, Enzyme and Microbial Technology, vol. 40, no. 5, pp. 1389-1397, 2007.
R. Singh, Nawale, L., Sarkar, D., and Suresh, C. G., “Two chitotriose-specific lectins show anti-angiogenesis, induces caspase-9-mediated apoptosis and early arrest of pancreatic tumor cell cycle”, Plos One, vol. 11, no. 1, p. Article Number: e0146110, 2016.
L. Satyanarayana, Suresh, C. G., Patel, A., Mishra, S., and Ghosh, P. K., “X-ray crystallographic studies on C-phycocyanins from cyanobacteria from different habitats: marine and freshwater”, Acta Crystallographica Section F-Structural Biology and Crystallization Communications, vol. 61, no. Part 9, pp. 844-847, 2005.