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

Glycosylation of the N-terminal potential N-glycosylation sites in the human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI).

Glycoconjugate journal - 1 Dec 2000

Christensen L L, Bross P, Ørntoft T F

Abstract excerpt

Human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI) each contain four potential N-glycosylation sites (hFucTV: Asn60, Asn105, Asn167 and Asn198 and hFucTVI: Asn46, Asn91, Asn153 and Asn184). Glycosylation of the two N-terminal potential N-glycosylation sites (hFucTV: Asn60, Asn105 and hFucTVI: Asn46 and Asn91) have never been studied in detail. In the present study, we have analysed the glycosylation of...

Read the complete abstract on PubMed

Topics

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

Share to Asparagine
Share to COS Cells
Share to Enzyme Inhibitors

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Fucosyltransferases

Share to Glycosylation

Share to Mutagenesis, Site-Directed

Share to Structure-Activity Relationship

Share to Tunicamycin

Source

Identifiers

PMID: 11511810
DOI: 10.1023/a:1010917229243

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

Glycosylation of the N-terminal potential N-glycosylation sites in the human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI).PMID 11511810Read ↗

The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.Semantic proximity Read ↗

In‐depth comparison of N‐glycosylation of human plasma‐derived factor VIII and different recombinant products: from structure to clinical implicationsSemantic proximity Read ↗

N-glycosylation of recombinant human fucosyltransferase III is required for its in vivo folding in mammalian and insect cells.Semantic proximity Read ↗

N-glycans of core2 beta(1,6)-N-acetylglucosaminyltransferase-I (C2GnT-I) but not those of alpha(1,3)-fucosyltransferase-VII (FucT-VII) are required for the synthesis of functional P-selectin glycoprotein ligand-1 (PSGL-1): effects on P-, L- and E-selectin binding.Semantic proximity Read ↗

Specific N-linked glycosylation sites modulate synthesis and secretion of von Willebrand factor.Semantic proximity Read ↗

Phylogenetic and mutational analyses reveal key residues for UDP-glucuronic acid binding and activity of beta1,3-glucuronosyltransferase I (GlcAT-I).Semantic proximity Read ↗

Impact of host cell line choice on glycan profileSemantic proximity Read ↗

N-Glycosylation as a Tool to Study Antithrombin Secretion, Conformation, and Function.Semantic proximity Read ↗

N-glycosylation site occupancy of rat alpha-1,3-fucosyltransferase IV and the effect of glycosylation on enzymatic activity.Semantic proximity Read ↗

Two N-terminally truncated variants of human β-galactoside α2,6 sialyltransferase I with distinct properties for in vitro protein glycosylation.Semantic proximity Read ↗

In vivo analysis of the role of O-glycosylations of von Willebrand factor.Semantic proximity Read ↗

N-linked glycosylation of a subunit isoforms is critical for vertebrate vacuolar H+ -ATPase (V-ATPase) biosynthesis.Semantic proximity Read ↗

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