Ontology highlight
ABSTRACT:
INSTRUMENT(S): Orbitrap Fusion Lumos
ORGANISM(S): Campylobacter Jejuni Subsp. Jejuni Nctc 11168 = Atcc 700819
SUBMITTER: Sherif Abouelhadid
LAB HEAD: Sherif Abouelhadid
PROVIDER: PXD011452 | Pride | 2021-09-08
REPOSITORIES: Pride
Action | DRS | |||
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PR486_SA_TMT_20180606-1.msf | Msf | |||
PR486_SA_TMT_20180606.raw | Raw |
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Abouelhadid Sherif S North Simon J SJ Hitchen Paul P Vohra Prerna P Chintoan-Uta Cosmin C Stevens Mark M Dell Anne A Cuccui Jon J Wren Brendan W BW
mBio 20190423 2
In eukaryotes, glycosylation plays a role in proteome stability, protein quality control, and modulating protein function; however, similar studies in bacteria are lacking. Here, we investigate the roles of general protein glycosylation systems in bacteria using the enteropathogen <i>Campylobacter jejuni</i> as a well-defined example. By using a quantitative proteomic strategy, we were able to monitor changes in the <i>C. jejuni</i> proteome when glycosylation is disrupted. We demonstrate that i ...[more]