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References from Structural bioinformatic analysis of DsbA proteins and their pathogenicity associated substrates. Local targets link to admitted publications; unresolved targets remain external evidence.
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The Salmonella SPI1 type three secretion system responds to periplasmic disulfide bond status via the flagellar apparatus and the RcsCDB system
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A periplasmic protein disulfide oxidoreductase is required for transformation of Haemophilus influenzae Rd
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Inactivation of DsbA, but not DsbC and DsbD, affects the intracellular survival and virulence of Shigella flexneri
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Structural and Functional Characterization of DsbC, a Protein Involved in Disulfide Bond Formation in Escherichia coli
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The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation
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Why is DsbA such an oxidizing disulfide catalyst?
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Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization
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On the role of the cis-proline residue in the active site of DsbA
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The uncharged surface features surrounding the active site of Escherichia coli DsbA are conserved and are implicated in peptide binding
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Catalytic mechanism of DsbA and its comparison with that of protein disulfide isomerase
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Characterization of disulfide exchange between DsbA and HtrA proteins from Escherichia coli
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Four structural subclasses of the antivirulence drug target disulfide oxidoreductase DsbA provide a platform for design of subclass-specific inhibitors
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Crystal structure of the dithiol oxidase DsbA enzyme from proteus mirabilis bound non-covalently to an active site peptide ligand
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The 1.2 Å resolution crystal structure of TcpG, the Vibrio cholerae DsbA disulfide-forming protein required for pilus and cholera-toxin production
2012 · External reference
Comparative sequence, structure and redox analyses of Klebsiella pneumoniae DsbA show that anti-virulence target DsbA enzymes fall into distinct classes
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10.1089/ars.2009.2736
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Staphylococcus aureus DsbA does not have a destabilizing disulfide. A new paradigm for bacterial oxidative folding
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A single dipeptide sequence modulates the redox properties of a whole enzyme family
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Structure of TcpG, the DsbA protein folding catalyst from Vibrio cholerae11Edited by I. A. Wilson
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Structural and Biochemical Characterization of Xylella fastidiosa DsbA Family Members: New Insights into the Enzyme−Substrate Interaction
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Virulence of the Melioidosis Pathogen Burkholderia pseudomallei Requires the Oxidoreductase Membrane Protein DsbB
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Theoretical insights into the mechanism for thiol/disulfide exchange
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Preferential binding of an unfolded protein to DsbA
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