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 …
F Hatahet, D Boyd, J Beckwith - … et Biophysica Acta (BBA)-Proteins and …, 2014 - Elsevier
The formation of structural disulfide bonds is essential for the function and stability of a great number of proteins, particularly those that are secreted. There exists a variety of dedicated …
C Schwechheimer, MJ Kuehn - Journal of bacteriology, 2013 - Am Soc Microbiol
Outer membrane vesicles (OMVs) are composed of outer membrane and periplasmic components and are ubiquitously secreted by Gram-negative bacteria. OMVs can …
SR Shouldice, B Heras, PM Walden… - Antioxidants & redox …, 2011 - liebertpub.com
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 …
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 …
Abstract Aims: The intracellular pathogen Burkholderia pseudomallei causes the disease melioidosis, a major source of morbidity and mortality in southeast Asia and northern …
IS Arts, G Ball, P Leverrier, S Garvis, V Nicolaes… - MBio, 2013 - Am Soc Microbiol
Disulfide bond formation is required for the folding of many bacterial virulence factors. However, whereas the Escherichia coli disulfide bond-forming system is well characterized …
By catalyzing oxidative protein folding, the bacterial disulfide bond protein A (DsbA) plays an essential role in the assembly of many virulence factors. Predictably, DsbA disruption affects …