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

Gradually glycosylated protein C mutants (Arg178Gln and Cys331Arg) are degraded by proteasome after mannose trimming.

Thrombosis and haemostasis - 1 Dec 2004

Nakahara Masako, Koyama Takatoshi, Nakazawa Fumie, Nishio Miwako, Shibamiya Aya, Hirosawa Shinsaku

Abstract excerpt

Proteins that fail to attain their correct three-dimensional structure are retained in the endoplasmic reticulum (ER) and eventually degraded within the cells. We investigated the degradation of mutant proteins, using naturally occurring protein C (PC) mutants (Arg178Gln and Cys331Arg) which lead to congenital deficiencies. Chinese hamster ovary (CHO) cells were transfected with normal or mutant expression...

Read the complete abstract on PubMed

Topics

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

Share to Asparagine
Share to Glutamine

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

Share to Immunoprecipitation

Share to Mannose

Share to Oligosaccharides

Share to Proteasome Endopeptidase Complex

Share to Proteasome Inhibitors

Share to Protein C

Source

Identifiers

PMID: 15583735
DOI: 10.1160/TH04-07-0403

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

Gradually glycosylated protein C mutants (Arg178Gln and Cys331Arg) are degraded by proteasome after mannose trimming.PMID 15583735Read ↗

[Proteasome degradation of protein C and plasmin inhibitor mutants: molecular mechanism of congenital protein deficiency].Semantic proximity Read ↗

Proteasome degradation of protein C and plasmin inhibitor mutants.Semantic proximity Read ↗

Multiple endoplasmic reticulum-associated pathways degrade mutant yeast carboxypeptidase Y in mammalian cells.Semantic proximity Read ↗

Enhanced folding and processing of a disulfide mutant of the human asialoglycoprotein receptor H2b subunit.Semantic proximity Read ↗

Superfolding of the partially unfolded core-glycosylated intermediate of human P-glycoprotein into the mature enzyme is promoted by substrate-induced transmembrane domain interactions.Semantic proximity Read ↗

ER-associated degradation relying on protein O-mannosylationSemantic proximity Read ↗

N-glycosylation is crucial for folding, trafficking, and stability of human tripeptidyl-peptidase I.Semantic proximity Read ↗

Gaucher disease due to saposin C deficiency is an inherited lysosomal disease caused by rapidly degraded mutant proteins.Semantic proximity Read ↗

Model-based analysis of N-glycosylation in Chinese hamster ovary cellsSemantic proximity Read ↗

The structural role of N-linked glycans on human glypican-1.Semantic proximity Read ↗

Molecular characterization of p.Asp77Gly and the novel p.Ala163Val and p.Ala163Glu mutations causing protein C deficiency.Semantic proximity Read ↗

Protein C-terminal variations impact proteostasis.Semantic proximity Read ↗

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