The identification of protein disulfide isomerase, almost 50 years ago, opened the way to the
study of oxidative protein folding. Oxidative protein folding refers to the composite process …

Disulfide-bond formation is important for the correct folding of a great number of proteins that
are exported to the cell envelope of bacteria. Bacterial cells have evolved elaborate systems …

PDI catalyzes the oxidative folding of disulfide-containing proteins. However, the sequence
of reactions leading to a natively folded and oxidized protein remains unknown. Here we …

Gram-negative bacteria possess an outer membrane envelope consisting of an outer leaflet
of lipopolysaccharides, also called endotoxins, which protect the pathogen from …

Natural products containing nitrogen–nitrogen (N–N) bonds have attracted much attention
because of their bioactivities and chemical features. Several recent studies have revealed …

We have studied the proteome of the model plant Arabidopsis thaliana infected with a
necrotrophic fungal pathogen, Alternaria brassicicola. The Arabidopsis–A. brassicicola host …

Since its discovery in 1991, the bacterial periplasmic oxidative folding catalyst DsbA has
been the focus of intense research. Early studies addressed why it is so oxidizing and how it …

Microbes employ the thioredoxin system to defend against oxidative stress and ensure
correct disulfide bonding to maintain protein function. Listeria monocytogenes has been …

Recent years have witnessed a dramatic increase in bacterial antimicrobial resistance and a
decline in the development of novel antibiotics. New therapeutic strategies are urgently …

Aims: DsbA catalyzes disulfide bond formation in secreted and outer membrane proteins in
bacteria. In pathogens, DsbA is a major facilitator of virulence constituting a target for …