Interest in protein disulfide bond formation has recently increased because of the prominent
role of disulfide bonds in bacterial virulence and survival. The first discovered pathway that …

A deluge of whole-genome sequencing has begun to give insights into the patterns and
processes of microbial evolution, but genome sequences have accrued in a haphazard …

Disulfide bonds are important for the stability and function of many secreted proteins. In
Gram-negative bacteria, these linkages are catalyzed by thiol-disulfide oxidoreductases …

Secreted proteins constitute a reservoir of virulence factors. Here, an in silico analysis of the
secretome of 15 S. aureus reference strains is presented revealing that about 30% of the …

S taphylococcus aureus is a major human pathogen. Hospital infections caused by
methicillin‐resistant strains (MRSA), which have acquired resistance to a broad spectrum of …

Enterococcus faecalis, a Gram-positive bacterium, and Candida albicans, a polymorphic
fungus, are common constituents of the microbiome as well as increasingly problematic …

The Gram‐positive pathogen C orynebacterium diphtheriae exports through the Sec
apparatus many extracellular proteins that include the key virulence factors diphtheria toxin …

Extracytoplasmic thiol-disulfide oxidoreductases (TDORs) catalyze the oxidation, reduction,
and isomerization of protein disulfide bonds. Although these processes have been …

Disulfide bonds are important for the stability of many extracellular proteins, including
bacterial virulence factors. Formation of these bonds is catalyzed by thiol-disulfide …

Mechanisms of disulfide bond formation in the human pathogen Streptococcus pyogenes
are currently unknown. To date, no disulfide bond-forming thiol-disulfide oxidoreductase …