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

Retention and degradation of N-glycoproteins in the rough endoplasmic reticulum.

Bioscience reports - 1 Oct 1999

Duvet S, Dubuisson J, Ermonval M, Cacan R, Verbert A

Abstract excerpt

Recent studies have shown that newly synthesized proteins and glycoproteins are submitted to a quality control mechanism in the rough endoplasmic reticulum (ER). In this report we present two models: One model will illustrate a transient retention in rough ER leading to a further degradation of glycoproteins in the cytosol, (soluble alkaline phosphatase expressed in Man-P-Dol deficient CHO cells lines). The...

Read the complete abstract on PubMed

Topics

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

Share to Alkaline Phosphatase
Share to CHO Cells
Share to Chromatography, Affinity

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Chromatography, High Pressure Liquid

Share to Glycoproteins

Share to Golgi Apparatus

Share to Solubility

Share to Viral Envelope Proteins

Source

Identifiers

PMID: 10763816
DOI: 10.1023/a:1020228725997

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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

Retention and degradation of N-glycoproteins in the rough endoplasmic reticulum.PMID 10763816Read ↗

Processing by endoplasmic reticulum mannosidases partitions a secretion-impaired glycoprotein into distinct disposal pathways.Semantic proximity Read ↗

Characterization of Schizosaccharomyces pombe ER alpha-mannosidase: a reevaluation of the role of the enzyme on ER-associated degradation.Semantic proximity Read ↗

Reciprocal relationship between alpha1,2 mannosidase processing and reglucosylation in the rough endoplasmic reticulum of Man-P-Dol deficient cells.Semantic proximity Read ↗

Degradation of a short-lived glycoprotein from the lumen of the endoplasmic reticulum: the role of N-linked glycans and the unfolded protein response.Semantic proximity Read ↗

Evidence for stabilization of aquaporin-2 folding mutants by N-linked glycosylation in endoplasmic reticulum.Semantic proximity Read ↗

Recycling of proteins from the Golgi compartment to the ER in yeast.Semantic proximity Read ↗

Endomannosidase processes oligosaccharides of alpha1-antitrypsin and its naturally occurring genetic variants in the Golgi apparatus.Semantic proximity Read ↗

Formation of intracellular particles by hepatitis B virus large surface protein.Semantic proximity Read ↗

A misfolded protein conformation is not a sufficient condition for in vivo glucosylation by the UDP-Glc:glycoprotein glucosyltransferase.Semantic proximity Read ↗

An investigation of the role of transmembrane domains in Golgi protein retention.Semantic proximity Read ↗

Absence of nucleoside diphosphatase activities in the yeast secretory pathway does not abolish nucleotide sugar-dependent protein glycosylation.Semantic proximity Read ↗

Intracellular retention of hepatitis B virus surface protein mutants devoid of amino-terminal pre-S1 sequences.Semantic proximity Read ↗

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