Modeling and monitoring the effects of three partly conserved Ile residues in the dimerization domain of a Mip-like virulence factor from Escherichia coli
S Seal, T Chakraborty, S Polley, D Paul… - Journal of …, 2024 - Taylor & Francis
FKBP22, an Escherichia coli-made peptidyl-prolyl cis-trans isomerase, has shown
considerable homology with Mip-like virulence factors. While the C-terminal domain of this …
considerable homology with Mip-like virulence factors. While the C-terminal domain of this …
A staphylococcal cyclophilin carries a single domain and unfolds via the formation of an intermediate that preserves cyclosporin A binding activity
S Seal, S Polley, S Sau - Plos one, 2019 - journals.plos.org
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 …
many bacteria including Staphylococcus aureus. The enzymatic activity of Cyp is inhibited …
Dimerization ability, denaturation mechanism, and the stability of a staphylococcal phage repressor and its two domains
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 …
(CI) that harbors an N-terminal domain (NTD), and a C-terminal domain (CTD). Previously …