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

Recycling cell surface glycoproteins undergo limited oligosaccharide reprocessing in LEC1 mutant Chinese hamster ovary cells.

Glycobiology - 1 Dec 1998

Reichner J S, Helgemo S L, Hart G W

Abstract excerpt

The ability of particular cell surface glycoproteins to recycle and become exposed to individual Golgi enzymes has been demonstrated. This study was designed to determine whether endocytic trafficking includes significant reentry into the overall oligosaccharide processing pathway. The Lec1 mutant of Chinese hamster ovary (CHO) cells lack N -acetylglucosaminyltransferase I (GlcNAc-TI) activity resulting in...

Read the complete abstract on PubMed

Topics

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

Share to CHO Cells
Share to Cricetinae
Share to Enzyme Inhibitors

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

Share to Kinetics

Share to Membrane Glycoproteins

Share to Mutation

Share to Phenotype

Source

Identifiers

PMID: 9858639
DOI: 10.1093/glycob/8.12.1173

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Recycling cell surface glycoproteins undergo limited oligosaccharide reprocessing in LEC1 mutant Chinese hamster ovary cells.PMID 9858639Read ↗

Glycomics profiling of Chinese hamster ovary cell glycosylation mutants reveals N-glycans of a novel size and complexity.Semantic proximity Read ↗

Activity of recycling Golgi mannosyltransferases in the yeast endoplasmic reticulum.Semantic proximity Read ↗

A subclass of cell surface carbohydrates revealed by a CHO mutant with two glycosylation mutations.Semantic proximity Read ↗

Independent Lec1A CHO glycosylation mutants arise from point mutations in N-acetylglucosaminyltransferase I that reduce affinity for both substrates. Molecular consequences based on the crystal structure of GlcNAc-TI.Semantic proximity Read ↗

Five Lec1 CHO cell mutants have distinct Mgat1 gene mutations that encode truncated N-acetylglucosaminyltransferase I.Semantic proximity Read ↗

Mistargeting of the lectin ERGIC-53 to the endoplasmic reticulum of HeLa cells impairs the secretion of a lysosomal enzyme.Semantic proximity Read ↗

Evidence for core 2 to core 1 O-glycan remodeling during the recycling of MUC1.Semantic proximity Read ↗

CHO cells provide access to novel N-glycans and developmentally regulated glycosyltransferases.Semantic proximity Read ↗

Arrested maturing multivesicular endosomes observed in a Chinese hamster ovary cell mutant, LEX2, isolated by repeated flow-cytometric cell sorting.Semantic proximity Read ↗

Exploring the outcome of genetic modifications of glycosylation in cultured cell lines by concurrent isolation of the major classes of vertebrate glycans.Semantic proximity Read ↗

Preliminary characterization of a Chinese hamster ovary cell glycosylation mutant isolated by screening for low intracellular lysosomal enzyme activity.Semantic proximity Read ↗

Cell surface counter receptors are essential components of the unconventional export machinery of galectin-1.Semantic proximity Read ↗

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