Zobrazeno 1 - 8 of 8 pro vyhledávání: '"Debasmita Sinha"'
1
The cofactors and domains of a staphylococcal capsule-producing enzyme preserve its structure, stability, shape and dimerization ability
Autor: Tushar Chakraborty, Nilanjan Banerjee, Debasmita Sinha, Soham Seal, Subhrangsu Chatterjee, Subrata Sau
Publikováno v: The Journal of Biochemistry. 173:471-486
CapF, a staphylococcal capsule-producing enzyme, binds Zn2+ ion and NADPH using its C-terminal domain (CTD) and N-terminal domain (NTD), respectively. To elucidate the roles of cofactors and domains, we have systematically investigated the related re
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::ec68dcd486921d8e2a43a85abb1cb2fd
https://doi.org/10.1093/jb/mvad014
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3
Alternative Sigma Factor of Staphylococcus aureus Interacts with the Cognate Antisigma Factor Primarily Using Its Domain 3
Autor: Asim Poddar, Anindya Dutta, Rajkrishna Mondal, Debasmita Sinha, Tushar Chakraborty, Soham Seal, Subrata Sau, Debabrata Sinha, Subhrangsu Chatterjee
Publikováno v: Biochemistry. 60:135-151
σB, an alternative sigma factor, is usually employed to tackle the general stress response in Staphylococcus aureus and other Gram-positive bacteria. This protein, involved in S. aureus-mediated pathogenesis, is typically blocked by RsbW, an antisig
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b7c0606addcfc725c172ebaa573d2d9b
https://doi.org/10.1021/acs.biochem.0c00881
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4
Understanding the structure, stability, and anti-sigma factor-binding thermodynamics of an anti-anti-sigma factor from Staphylococcus aureus
Autor: Subrata Sau, Rajagopal Chattopadhyaya, Debabrata Sinha, Tushar Chakraborty, Asim Poddar, Debasmita Sinha
Publikováno v: Journal of Biomolecular Structure and Dynamics. 39:6539-6552
Staphylococcus aureus and many related bacteria encode both anti-sigma factor RsbW and anti-anti-sigma factor RsbV to control stress response by σB, an alternative sigma factor. Our structural and ...
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::824cecda2167ab9fb9705b1c695af4bb
https://doi.org/10.1080/07391102.2020.1801511
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5
Serine 106 preserves the tertiary structure, function, and stability of a cyclophilin from
Autor: Soham, Seal, Nilanjan, Banerjee, Rohit, Mahato, Tanmoy, Kundu, Debabrata, Sinha, Tushar, Chakraborty, Debasmita, Sinha, Keya, Sau, Subhrangsu, Chatterjee, Subrata, Sau
Publikováno v: Journal of biomolecular structuredynamics.
SaCyp, a staphylococcal cyclophilin involved in both protein folding and pathogenesis, has a Ser residue at position 106 and a Trp residue at position 136. While Ser 106 of SaCyp aligned with a cyclosporin A (CsA) binding Ala residue, its Trp 136 ali
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::36e0af7fcfbd2241e7c14bdc3e2f2861
https://pubmed.ncbi.nlm.nih.gov/34967275
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7
A conserved arginine residue in a staphylococcal anti-sigma factor is required to preserve its kinase activity, structure, and stability
Autor: Priya Rai, Debabrata Sinha, Tushar Chakraborty, Soham Seal, Subrata Sau, Nilanjan Banerjee, Debasmita Sinha, Subhrangsu Chatterjee
Publikováno v: Journal of biomolecular structuredynamics. 40(11)
RsbW, σB, and RsbV, encoded by Staphylococcus aureus and related bacteria, act as an anti-sigma factor, an sigma factor, and an anti-anti-sigma factor, respectively. The interaction between RsbW an...
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cded5bf78510e37e4c87064d278c4a39
https://pubmed.ncbi.nlm.nih.gov/33356973
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