Zobrazeno 1 - 10 of 10 pro vyhledávání: '"Soham, Seal"'
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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2
Akademický článek
A staphylococcal cyclophilin carries a single domain and unfolds via the formation of an intermediate that preserves cyclosporin A binding activity.
Autor: Soham Seal, Soumitra Polley, Subrata Sau
Publikováno v: PLoS ONE, Vol 14, Iss 3, p e0210771 (2019)
Cyclophilin (Cyp), a peptidyl-prolyl cis-trans isomerase (PPIase), acts as a virulence factor in many bacteria including Staphylococcus aureus. The enzymatic activity of Cyp is inhibited by cyclosporin A (CsA), an immunosuppressive drug. To precisely
Externí odkaz: https://doaj.org/article/815eb56150db42e6a98b074a107a13cc
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4
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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5
Dimerization ability, denaturation mechanism, and the stability of a staphylococcal phage repressor and its two domains
Autor: Anindya Biswas, Semanti Ghosh, Anindya Dutta, Soham Seal, Debabrata Sinha, Angshuman Bagchi, Subrata Sau
Publikováno v: International Journal of Biological Macromolecules. 124:903-914
The lysogenic growth of phage ф11 in Staphylococcus aureus is controlled by a repressor (CI) that harbors an N-terminal domain (NTD), and a C-terminal domain (CTD). Previously, NTD, like CI, showed DNA binding activity and dimerized in the aqueous s
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14c2180a7301268b6041af2019631fc7
https://doi.org/10.1016/j.ijbiomac.2018.11.263
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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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8
Alanine substitution mutations in the DNA binding region of a global staphylococcal virulence regulator affect its structure, function, and stability
Autor: Keya Sau, Sukhendu Mandal, Angshuman Bagchi, Soham Seal, Deeya Saha, Soumitra Polley, Semanti Ghosh, Avisek Mahapa, Debabrata Sinha, Subrata Sau
Publikováno v: International Journal of Biological Macromolecules. 113:1221-1232
SarA, a winged-helix DNA binding protein, is a global virulence regulator in Staphylococcus aureus. The putative DNA binding region of SarA is located between amino acid residues Leu 53 and Gln 97. Previous studies have demonstrated that residues at
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::52e1351cdb50ee959fa58869666c7fb0
https://doi.org/10.1016/j.ijbiomac.2018.03.045
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9
Removal of an atypical region from a staphylococcal cyclophilin affects its structure, function, stability, and shape
Autor: Debabrata Sinha, Subrata Sau, Tushar Chakraborty, Angshuman Bagchi, Soham Seal, Nilkanta Chowdhury, Ria Biswas
Publikováno v: International journal of biological macromolecules. 151
SaCyp, a cyclophilin having 197 amino acid residues, acts both as a protein-folding catalyst and a virulence factor in Staphylococcus aureus. Interestingly, a region, homologous to the SaCyp region carrying 121-148 amino acid residues, is present in
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3e88d6a58817303abbb73063459e527
https://pubmed.ncbi.nlm.nih.gov/31751734
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10
A staphylococcal cyclophilin carries a single domain and unfolds via the formation of an intermediate that preserves cyclosporin A binding activity
Autor: Subrata Sau, Soumitra Polley, Soham Seal
Publikováno v: PLoS ONE
PLoS ONE, Vol 14, Iss 3, p e0210771 (2019)
Cyclophilin (Cyp), a peptidyl-prolyl cis-trans isomerase (PPIase), acts as a virulence factor in many bacteria including Staphylococcus aureus. The enzymatic activity of Cyp is inhibited by cyclosporin A (CsA), an immunosuppressive drug. To precisely
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33bc0fa57d4aa55592d46eff2c4d3d0b
https://doi.org/10.1371/journal.pone.0210771
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