Prof. Dr. Suvroma  Gupta
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Prof. Dr. Suvroma Gupta

Professor
Haldia Institute of Technology, India


Highest Degree
Ph.D. in Biochemistry from Bose Institute, India

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Area of Interest:

Biomedical Sciences
100%
Cellular Biochemistry
62%
Inorganic Chemistry
90%
Chemical Biology
75%
Biotechnology
55%

Research Publications in Numbers

Books
0
Chapters
0
Articles
0
Abstracts
0

Selected Publications

  1. Sahu, N., S. Mondal, N. Sepay, S. Gupta and E. Torres-Lopez et al., 2017. Antibacterial activities of sulfamethoxazolyl-azo-phenols and their Cu(II) complexes along with molecular docking properties. J. Biol. Inorg. Chem., 22: 833-850.
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  2. Das, D., I. Dea, N. Sahua, S. Roya and N. Sepaya et al., 2017. Spectroscopic characterization, biological activities and theoretical computation of manganese(II) and copper(II) complexes of sulfamethoxazolyl-azoacetylacetonate. J. Indian Chem. Soc., 94: 1-13.
  3. Sahu, N., D. Das, S. Mondal, S. Roy and P. Dutta et al., 2016. The structural characterization and biological activity of sulfamethoxazolyl-azo-p-cresol, its copper(II) complex and their theoretical studies. New J. Chem., 40: 5019-5031.
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  4. Maity, S., K. Mukherjee, A. Banerjee, S. Mukherjee, D. Dasgupta and S. Gupta, 2016. Inhibition of porcine pancreatic amylase activity by sulfamethoxazole: Structural and functional aspect. Protein J., 35: 237-246.
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  5. Gupta, S. and D. Pramanik, 2016. Phytochemicals and cancer stem cells: A pancreatic cancer overview. Curr. Chem. Biol., 10: 98-108.
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  6. Mitra, G., S. Gupta, A. Poddar and B. Bhattacharyya, 2015. MAP2c prevents arachidonic acid-induced fibril formation of tau: Role of chaperone activity and phosphorylation. Biophys. Chem., 205: 16-23.
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  7. Maity, S., S. Mallik, R. Basuthakur and S. Gupta, 2015. Optimization of solid state fermentation conditions and characterization of thermostable alpha amylase from Bacillus subtilis (ATCC 6633). J. Bioprocess. Biotech., Vol. 5. 10.4172/2155-9821.1000218.
    CrossRef  |  
  8. Das, D., N. Sahu, S. Mondal, S. Roy and P. Dutta et al., 2015. Structures, antimicrobial activity, DNA interaction and molecular docking studies of sulfamethoxazolyl-azo-acetylacetone and its nickel (II) complex. Polyhedron, 99: 77-86.
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  9. Chatterjee, J., S. Giri, S. Maity, A. Sinha, A. Ranjan and S. Gupta, 2015. Production and characterization of thermostable alkaline protease of Bacillus subtilis (ATCC 6633) from optimized solid‐state fermentation. Biotechnol. Applied Biochem., 62: 709-718.
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  10. Saha, K., S. Maity, S. Roy, K. Pahan, R. Pathak, S. Majumdar and S. Gupta, 2014. Optimization of amylase production from B. amyloliquefaciens (MTCC 1270) using solid state fermentation. Int. J. Microbiol., Vol. 2014. 10.1155/2014/764046.
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  11. Raul, D., T. Biswas, S. Mukhopadhyay, S.K. Das and S. Gupta, 2014. Production and partial purification of alpha amylase from Bacillus subtilis (MTCC 121) using solid state fermentation. Biochem. Res. Int., Vol. 2014. 10.1155/2014/568141.
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  12. Gupta, S., 2014. Delineation of current development of antimitotic compounds targeting cytoskeletal protein tubulin and microtubule in the cancer therapy. Curr. Chem. Biol., 8: 165-183.
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  13. Chatterjee, S., S. Gupta, S. Mukherjee and J. Mukherjee, 2014. Nanomaterial mediated drug delivery, image-guided therapy and multifaceted theranostic systems in cancer. J. Nanotechnol. Adv. Mater., 2: 77-88.
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  14. Chakraborti, S., D. Chakravarty, S. Gupta, B.P. Chatterji and G. Dhar et al., 2012. Discrimination of ligands with different flexibilities resulting from the plasticity of the binding site in tubulin. Biochemistry, 51: 7138-7148.
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  15. Das, L., S. Gupta, A. Poddar, M.E. Janik and B. Bhattacharyya, 2009. Binding of indanocine to the colchicine site on tubulin promotes fluorescence, and its binding parameters resemble those of the colchicine analogue AC. Biochemistry, 48: 1628-1635.
  16. Bhattacharyya, B., D. Panda, S. Gupta and M. Banerjee, 2008. Anti‐mitotic activity of colchicine and the structural basis for its interaction with tubulin. Med. Res. Rev., 28: 155-183.
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  17. Gupta, S., L. Das, A. Poddar, M.E. Janik and B. Bhattacharyya, 2006. Oxalone and lactone moieties of podophyllotoxin exhibit properties of both the B and C rings of colchicine in its binding with tubulin. Biochemistry, 45: 6467-6475.
  18. Gupta, S., M. Banerjee, A. Poddar, A. Banerjee, G. Basu, D. Roy and B. Bhattacharyya, 2005. Biphasic kinetics of the colchicines-tubulin interaction: Role of amino acids surrounding the A ring of bound colchicine molecule. Biochemistry, 44: 10181-10188.
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  19. Das, L., A.B. Datta, S. Gupta, A. Poddar, S. Sengupta, M.E. Janik and B. Bhattacharyya, 2005. -NH-dansyl isocolchicine exhibits a significantly improved tubulin-binding affinity and microtubule inhibition in comparison to isocolchicine by binding tubulin through its A and B rings. Biochemistry, 44: 3249-3258.
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  20. Sarkar, T., G. Mitra, S. Gupta, T. Manna and A. Poddar et al., 2004. MAP2 prevents protein aggregation and facilitates reactivation of unfolded enzymes: Implications for the chaperone-like activity of MAP2. FEBS J., 271: 1488-1496.
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  21. Chakraborty, S., S. Gupta, T. Sarkar, A. Poddar and J. Pena et al., 2004. The B‐ring substituent at C‐7 of colchicine and the α‐C‐terminus of tubulin communicate through the “tail–body” interaction. Proteins: Struct. Funct. Bioinform., 57: 602-609.
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  22. Gupta, S., S. Chakraborty, A. Poddar, N. Sarkar, K.P. Das and B. Bhattacharyya, 2003. BisANS binding to tubulin: Isothermal titration calorimetry and the site‐specific proteolysis reveal the GTP‐induced structural stability of tubulin. Proteins: Struct. Funct. Bioinform., 50: 283-289.
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  23. Gupta, S. and B. Bhattacharyya, 2003. Antimitotic drugs binding to vinca domain of tubulin. Mol. Cell. Biochem., 253: 41-47.