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

A novel variant form of murine beta-1, 6-N-acetylglucosaminyltransferase forming branches in poly-N-acetyllactosamines.

Glycobiology - 1 Oct 2000

Chen G Y, Kurosawa N, Muramatsu T

Abstract excerpt

A novel form of murine beta-1,6-N:-acetylglucosaminyltransferase that forms branches in poly-N:-acetyllactosamines (designated as IGnT B) was cloned based on sequence homology to the known IGnT (designated as IGnT A). When expressed as proteins, IGnT B showed higher specific activity than IGnT A. The C-terminal 1/4 of IGnT B was identical to that of IGnT A, while the rest of the predicted sequences showed 63%...

Read the complete abstract on PubMed

Topics

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

Share to Alternative Splicing
Share to Carbohydrate Conformation
Share to Carbohydrate Sequence

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

Share to Cloning, Molecular

Share to N-Acetylglucosaminyltransferases

Share to Polysaccharides

Share to Sequence Analysis, DNA

Share to Substrate Specificity

Source

Identifiers

PMID: 11030746
DOI: 10.1093/glycob/10.10.1001

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

A novel variant form of murine beta-1, 6-N-acetylglucosaminyltransferase forming branches in poly-N-acetyllactosamines.PMID 11030746Read ↗

Characterization of mouse sialyltransferase genes: their evolution and diversity.Semantic proximity Read ↗

Cloning and expression of a human gene encoding an N-acetylgalactosamine- 2,6-sialyltransferase (ST6GalNAc I): a candidate for synthesis of cancer-associated sialyl-Tn antigensSemantic proximity Read ↗

Aberrant N-glycosylation in cancer: MGAT5 and β1,6-GlcNAc branched N-glycans as critical regulators of tumor development and progression.Semantic proximity Read ↗

A novel I-branching beta-1,6-N-acetylglucosaminyltransferase involved in human blood group I antigen expression.Semantic proximity Read ↗

α2-6–Linked Sialic Acids on N-Glycans Modulate Carcinoma Differentiation <i>In vivo</i>Semantic proximity Read ↗

UDP-GlcNAc 2-Epimerase/ManNAc Kinase (GNE): A Master Regulator of Sialic Acid Synthesis.Semantic proximity Read ↗

GALNT2 suppresses malignant phenotypes through IGF-1 receptor and predicts favorable prognosis in neuroblastoma.Semantic proximity Read ↗

O-acetylated Gangliosides as Targets for Cancer ImmunotherapySemantic proximity Read ↗

Elevated mRNA level of hST6Gal I and hST3Gal V positively correlates with the high risk of pediatric acute leukemia.Semantic proximity Read ↗

A multipotential β-1,6- N -acetylglucosaminyl-transferase is encoded by bovine herpesvirus type 4Semantic proximity Read ↗

Sialylation is involved in cell fate decision during development, reprogramming and cancer progressionSemantic proximity Read ↗

Isolation, characterization and inactivation of the mouse Mgat3 gene: the bisecting N-acetylglucosamine in asparagine-linked oligosaccharides appears dispensable for viability and reproduction.Semantic proximity Read ↗

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