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

Defective threonine-linked glycosylation of human insulin-like growth factor in mutants of the yeast Saccharomyces cerevisiae.

Glycobiology - 1 Apr 1996

Finck M, Bergmann N, Jansson B, Ernst J F

Abstract excerpt

Mutants of the yeast Saccharomyces cerevisiae were identified, in which O-glycosylation at threonine 29 of a heterologous protein, human insulin-like growth factor (hIGF-1), is defective. In mutant M195, O-glycosylation of hIGF-1, but not of yeast proteins chitinase and a-agglutinin, was reduced; in mutant M577 yeast proteins were affected besides hIGF-1. The mutations of M195 and M577 did not affect viability...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Genes, Fungal
Share to Genetic Complementation Test

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

Share to Molecular Sequence Data

Share to Mutation

Share to Phenotype

Share to Recombinant Proteins

Share to Saccharomyces cerevisiae

Source

Identifiers

PMID: 8724139
DOI: 10.1093/glycob/6.3.313

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

Defective threonine-linked glycosylation of human insulin-like growth factor in mutants of the yeast Saccharomyces cerevisiae.PMID 8724139Read ↗

The PMT gene family: protein O-glycosylation in Saccharomyces cerevisiae is vital.Semantic proximity Read ↗

Glycoprotein biosynthesis in Saccharomyces cerevisiae: ngd29, an N-glycosylation mutant allelic to och1 having a defect in the initiation of outer chain formation.Semantic proximity Read ↗

Characterization of O-mannosyltransferase family in Schizosaccharomyces pombe.Semantic proximity Read ↗

Mnt2p and Mnt3p of Saccharomyces cerevisiae are members of the Mnn1p family of alpha-1,3-mannosyltransferases responsible for adding the terminal mannose residues of O-linked oligosaccharides.Semantic proximity Read ↗

Protein-O-glycosylation in yeast: protein-specific mannosyltransferases.Semantic proximity Read ↗

Studies on the N-glycosylation of the subunits of oligosaccharyl transferase in Saccharomyces cerevisiae.Semantic proximity Read ↗

Aspartic acid 252 and asparagine 185 are essential for activity of lipid N-acetylglucosaminylphosphate transferase.Semantic proximity Read ↗

Dolichol phosphate mannose synthase is required in vivo for glycosyl phosphatidylinositol membrane anchoring, O mannosylation, and N glycosylation of protein in Saccharomyces cerevisiae.Semantic proximity Read ↗

Proteolytic processing of a secreted glycoprotein and O-glycosylation of mannoproteins are affected in the N-glycosylation mutant Saccharomyces cerevisiae ldb1.Semantic proximity Read ↗

[Genetic regulation of N-glycosylation in yeast protein].Semantic proximity Read ↗

Isolation, characterization, and properties of Saccharomyces cerevisiae mnn mutants with nonconditional protein glycosylation defects.Semantic proximity Read ↗

Identification of defects in glycosylphosphatidylinositol anchor biosynthesis in the Thy-1 expression mutants.Semantic proximity Read ↗

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