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

Identification of the hydrophobic glycoproteins of Caenorhabditis elegans.

Glycobiology - 1 Oct 2005

Fan Xiaolian, She Yi-Min, Bagshaw Richard D, Callahan John W, Schachter Harry, Mahuran Don J

Abstract excerpt

Hydrophobic proteins such as integral membrane proteins are difficult to separate, and therefore to study, at a proteomics level. However, the Asn-linked (N-linked) carbohydrates (N-glycans) contained in membrane glycoproteins are important in differentiation, embryogenesis, inflammation, cancer and metastasis, and other vital cellular processes. Thus, the identification of these proteins and their sites of...

Read the complete abstract on PubMed

Topics

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

Share to Caenorhabditis elegans
Share to Caenorhabditis elegans Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Chromatography, High Pressure Liquid

Share to Glycoproteins

Share to Mutation

Share to Polysaccharides

Share to Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Share to Subcellular Fractions

Source

Identifiers

PMID: 15888633
DOI: 10.1093/glycob/cwi075

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification of the hydrophobic glycoproteins of Caenorhabditis elegans.PMID 15888633Read ↗

Mass spectrometric comparison of N-glycan profiles from Caenorhabditis elegans mutant embryos.Semantic proximity Read ↗

Modeling a congenital disorder of glycosylation type I in C. elegans: a genome-wide RNAi screen for N-glycosylation-dependent loci.Semantic proximity Read ↗

Deciphering endocytosis in Caenorhabditis elegans.Semantic proximity Read ↗

Functional analysis of glycosylation using Drosophila melanogaster.Semantic proximity Read ↗

Western Blot Analysis of C. elegans Proteins.Semantic proximity Read ↗

Ablation of N-acetylglucosaminyltransferases in Caenorhabditis induces expression of unusual intersected and bisected N-glycans.Semantic proximity Read ↗

The N's and O's of Drosophila glycoprotein glycobiology.Semantic proximity Read ↗

Comparisons of Caenorhabditis Fucosyltransferase Mutants Reveal a Multiplicity of Isomeric N-Glycan Structures.Semantic proximity Read ↗

Lipidomic and proteomic analysis of Caenorhabditis elegans lipid droplets and identification of ACS-4 as a lipid droplet-associated protein.Semantic proximity Read ↗

Pmr-1 gene affects susceptibility of Caenorhabditis elegans to Staphylococcus aureus infection through glycosylation and stress response pathways' alterations.Semantic proximity Read ↗

Caenorhabditis elegans syndecan (SDN-1) is required for normal egg laying and associates with the nervous system and the vulva.Semantic proximity Read ↗

Identification and molecular-genetic characterization of a LAMP/CD68-like protein from Caenorhabditis elegans.Semantic proximity Read ↗

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