biblio

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2006
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.
2008
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.
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.
2013
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.
2014
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.
2015
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.
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.
2018
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.
2019
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.