Ontology highlight
ABSTRACT:
SUBMITTER: Roszczenko P
PROVIDER: S-EPMC3463561 | biostudies-other | 2012
REPOSITORIES: biostudies-other
Roszczenko Paula P Radomska Katarzyna A KA Wywial Ewa E Collet Jean-Francois JF Jagusztyn-Krynicka Elzbieta K EK
PloS one 20121003 10
<h4>Background</h4>The formation of a disulfide bond between two cysteine residues stabilizes protein structure. Although we now have a good understanding of the Escherichia coli disulfide formation system, the machineries at work in other bacteria, including pathogens, are poorly characterized. Thus, the objective of this work was to improve our understanding of the disulfide formation machinery of Helicobacter pylori, a leading cause of ulcers and a risk factor for stomach cancer worldwide.<h4 ...[more]