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

N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli.

Science (New York, N.Y.) - 29 Nov 2002

Wacker Michael, Linton Dennis, Hitchen Paul G, Nita-Lazar Mihai, Haslam Stuart M, North Simon J, Panico Maria, Morris Howard R, Dell Anne, Wren Brendan W, Aebi Markus

Abstract excerpt

N-linked protein glycosylation is the most abundant posttranslation modification of secretory proteins in eukaryotes. A wide range of functions are attributed to glycan structures covalently linked to asparagine residues within the asparagine-X-serine/threonine consensus sequence (Asn-Xaa-Ser/Thr). We found an N-linked glycosylation system in the bacterium Campylobacter jejuni and demonstrate that a functional...

Read the complete abstract on PubMed

Topics

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

Share to Campylobacter jejuni
Share to Carbohydrate Conformation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Conjugation, Genetic

Share to Consensus Sequence

Share to Glycosyltransferases

Share to Lipoproteins

Share to Polysaccharides, Bacterial

Share to Transformation, Bacterial

Source

Identifiers

PMID: 12459590
DOI: 10.1126/science.298.5599.1790

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli.PMID 12459590Read ↗

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

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

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

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

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

Definition of the bacterial N-glycosylation site consensus sequence.Semantic proximity Read ↗

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

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

Bacterial protein N-glycosylation: new perspectives and applications.Semantic proximity Read ↗

Characterization of lipid-linked oligosaccharides by mass spectrometry.Semantic proximity Read ↗

Inverse metabolic engineering to improve Escherichia coli as an N‐glycosylation hostSemantic proximity Read ↗

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

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