Enhanced folding and processing of a disulfide mutant of the human asialoglycoprotein receptor H2b subunit.

doi:10.1074/jbc.270.34.20169

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Article

Enhanced folding and processing of a disulfide mutant of the human asialoglycoprotein receptor H2b subunit.

The Journal of biological chemistry - 25 Aug 1995

Yuk M H, Lodish H F

Abstract excerpt

Unfolded forms of the H2b subunit of the human asialoglycoprotein receptor, a galactose-specific C-type lectin, are degraded in the endoplasmic reticulum (ER), whereas folded forms of the protein can mature to the cell surface (Wikström, L., and Lodish, H. F. (1993) J. Biol. Chem. 268, 14412-1441...

Topics

3T3 Cells
Animals
Asialoglycoprotein Receptor
Asialoglycoproteins
Cell Membrane
Cysteine
Disulfides
Endoplasmic Reticulum
Fluorescent Antibody Technique
Golgi Apparatus
Humans
Kinetics

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mice

Mutagenesis, Site-Directed

Mutation

Orosomucoid

Protein Conformation

Protein Folding

Source

Open in PubMed

Identifiers

PMID: 7650036
DOI: 10.1074/jbc.270.34.20169

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-7650036-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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