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

Analysis of Skp1 glycosylation and nuclear enrichment in Dictyostelium.

Glycobiology - 1 Apr 2001

Sassi S, Sweetinburgh M, Erogul J, Zhang P, Teng-Umnuay P, West C M

Abstract excerpt

Skp1 is a subunit of SCF-E3 ubiquitin ligases and other protein complexes in the nucleus and cytoplasm of yeast and mammalian cells. In Dictyostelium, Skp1 is partially modified by an unusual pentasaccharide O-linked to hydroxyproline143. This modification was found to be susceptible to known prolyl hydroxylase inhibitors based on M(r)-shift analysis using SDS-polyacrylamide gel electrophoresis/Western blotting....

Read the complete abstract on PubMed

Topics

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

Share to Active Transport, Cell Nucleus
Share to Dictyostelium
Share to Life Cycle Stages

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

Share to Ligases

Share to Procollagen-Proline Dioxygenase

Share to RNA, Protozoan

Share to S-Phase Kinase-Associated Proteins

Share to Spores

Source

Identifiers

PMID: 11358877
DOI: 10.1093/glycob/11.4.283

Genes

SDS

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

Analysis of Skp1 glycosylation and nuclear enrichment in Dictyostelium.PMID 11358877Read ↗

A non-Golgi alpha 1,2-fucosyltransferase that modifies Skp1 in the cytoplasm of Dictyostelium.Semantic proximity Read ↗

The Skp1 prolyl hydroxylase from Dictyostelium is related to the hypoxia-inducible factor-alpha class of animal prolyl 4-hydroxylases.Semantic proximity Read ↗

Prolyl hydroxylation- and glycosylation-dependent functions of Skp1 in O2-regulated development of Dictyostelium.Semantic proximity Read ↗

Prolyl 4-hydroxylase-1 mediates O2 signaling during development of Dictyostelium.Semantic proximity Read ↗

Biochemical and genetic analysis of an antigenic determinant found on N-linked oligosaccharides in Dictyostelium.Semantic proximity Read ↗

Characterization of a cytoplasmic glucosyltransferase that extends the core trisaccharide of the Toxoplasma Skp1 E3 ubiquitin ligase subunit.Semantic proximity Read ↗

A novel, putative MEK kinase controls developmental timing and spatial patterning in Dictyostelium and is regulated by ubiquitin-mediated protein degradation.Semantic proximity Read ↗

OSBPa, a predicted oxysterol binding protein of Dictyostelium, is required for regulated entry into culmination.Semantic proximity Read ↗

Biochemical and genetic analysis of the biosynthesis, sorting, and secretion of Dictyostelium lysosomal enzymes.Semantic proximity Read ↗

Alterations to N-linked oligosaccharides which affect intracellular transport rates and regulated secretion but not sorting of lysosomal acid phosphatase in Dictyostelium discoideum.Semantic proximity Read ↗

Cell-free N-glycosylation in Dictyostelium discoideum: analysis of wild-type and mutants defective in lipid-linked oligosaccharide biosynthesis.Semantic proximity Read ↗

Disruption of somitogenesis by a novel dominant allele of Lfng suggests important roles for protein processing and secretion.Semantic proximity Read ↗

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