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Article

Oligomerization and interacellular localization of the glycoprotein receptor ERGIC-53 is independent of disulfide bonds.

Journal of molecular biology - 2 Dec 2005

Neve Etienne P A, Lahtinen Ulla, Pettersson Ralf F

Abstract excerpt

ERGIC-53 is a type I transmembrane lectin facilitating the efficient export of a subset of secretory glycoproteins from the endoplasmic reticulum. Previous results have shown that ERGIC-53 is present as reduction-sensitive homo-oligomers, i.e. as a balanced mixture of disulfide-linked hexamers and dimers, with the two cysteine residues located close to the transmembrane domain playing a crucial role in...

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PMID: 16257008
DOI: 10.1016/j.jmb.2005.09.077

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Oligomerization and interacellular localization of the glycoprotein receptor ERGIC-53 is independent of disulfide bonds.PMID 16257008Read ↗

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