Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Modification of the Campylobacter jejuni N-Linked Glycan by EptC Protein-mediated Addition of Phosphoethanolamine

3 Jul 2012

Abstract excerpt

Campylobacter jejuni is the major worldwide cause of bacterial gastroenteritis. C. jejuni possesses an extensive repertoire of carbohydrate structures that decorate both protein and non-protein surface-exposed structures. An N-linked glycosylation system encoded by the pgl gene cluster mediates the synthesis of a rigidly conserved heptasaccharide that is attached to protein substrates or released as free...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Bacteriophages and microbial interactions
Share to Salmonella and Campylobacter epidemiology
Share to Viral gastroenteritis research and epidemiology

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 22761430
DOI: 10.1074/jbc.m112.380212

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Modification of the Campylobacter jejuni N-Linked Glycan by EptC Protein-mediated Addition of PhosphoethanolaminePMID 22761430Read ↗

Identifying the targets and functions of N -linked protein glycosylation in Campylobacter jejuniSemantic proximity Read ↗

EptC of Campylobacter jejuni mediates phenotypes involved in host interactions and virulence.Semantic proximity Read ↗

Characterization of the structurally diverse N-linked glycans of Campylobacter species.Semantic proximity Read ↗

Crystallographic study of the phosphoethanolamine transferase EptC required for polymyxin resistance and motility in Campylobacter jejuni.Semantic proximity Read ↗

Comparative genomics analysis of completely sequenced microbial genomes reveals the ubiquity of N-linked glycosylation in prokaryotes.Semantic proximity Read ↗

N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli.Semantic proximity Read ↗

Functional analysis of the Campylobacter jejuni N-linked protein glycosylation pathway.Semantic proximity Read ↗

Biosynthesis of the N-linked glycan in Campylobacter jejuni and addition onto protein through block transfer.Semantic proximity Read ↗

Affinity-capture tandem mass spectrometric characterization of polyprenyl-linked oligosaccharides: tool to study protein N-glycosylation pathways.Semantic proximity Read ↗

Engineering the Campylobacter jejuni N-glycan to create an effective chicken vaccineSemantic proximity Read ↗

Functional characterization of the flagellar glycosylation locus in Campylobacter jejuni 81-176 using a focused metabolomics approach.Semantic proximity Read ↗

Increased efficiency of Campylobacter jejuni N-oligosaccharyltransferase PglB by structure-guided engineering.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.