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

Protein glycosylation mutants of procyclic Trypanosoma brucei: defects in the asparagine-glycosylation pathway.

Glycobiology - 1 Feb 1999

Hwa K Y, Acosta-Serrano A, Khoo K H, Pearson T, Englund P T

Abstract excerpt

We employed a genetic approach to study protein glycosylation in the procyclic form of the parasite Trypanosoma brucei. Two different mutant parasites, ConA 1-1 and ConA 4-1, were isolated from mutagenized cultures by selecting cells which resisted killing or agglutination by concanavalin A. Both mutant cells show reduced concanavalin A binding. However, the mutants have different phenotypes, as indicated by the...

Read the complete abstract on PubMed

Topics

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

Share to Carbohydrate Sequence
Share to Drug Resistance
Share to Glycosylation

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

Share to Membrane Glycoproteins

Share to Molecular Sequence Data

Share to Mutation

Share to Protein Processing, Post-Translational

Share to Protozoan Proteins

Source

Identifiers

PMID: 9949195
DOI: 10.1093/glycob/9.2.181

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

Protein glycosylation mutants of procyclic Trypanosoma brucei: defects in the asparagine-glycosylation pathway.PMID 9949195Read ↗

Killing of Trypanosoma brucei by concanavalin A: structural basis of resistance in glycosylation mutants.Semantic proximity Read ↗

Structural analysis of the asparagine-linked glycans from the procyclic Trypanosoma brucei and its glycosylation mutants resistant to Concanavalin A killing.Semantic proximity Read ↗

Defects in the N-linked oligosaccharide biosynthetic pathway in a Trypanosoma brucei glycosylation mutant.Semantic proximity Read ↗

Deletion of the glucosidase II gene in Trypanosoma brucei reveals novel N-glycosylation mechanisms in the biosynthesis of variant surface glycoprotein.Semantic proximity Read ↗

Characterization, localization, essentiality, and high-resolution crystal structure of glucosamine 6-phosphate N-acetyltransferase from Trypanosoma brucei.Semantic proximity Read ↗

Transposon mutagenesis of Trypanosoma brucei identifies glycosylation mutants resistant to concanavalin A.Semantic proximity Read ↗

The N-glycan glucosidase system in Trypanosoma brucei.Semantic proximity Read ↗

Deletion of the TbALG3 gene demonstrates site-specific N-glycosylation and N-glycan processing in Trypanosoma brucei.Semantic proximity Read ↗

Identification and functional characterization of a highly divergent N-acetylglucosaminyltransferase I (TbGnTI) in Trypanosoma brucei.Semantic proximity Read ↗

Generation of a bloodstream form Trypanosoma brucei double glycosyltransferase null mutant competent in receptor-mediated endocytosis of transferrin.Semantic proximity Read ↗

Lectin-resistant CHO glycosylation mutants.Semantic proximity Read ↗

Disruption of Active Trans-Sialidase Genes Impairs Egress from Mammalian Host Cells and Generates Highly Attenuated Trypanosoma cruzi ParasitesSemantic proximity Read ↗

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