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Article

Chaperone selection during glycoprotein translocation into the endoplasmic reticulum.

Science (New York, N.Y.) - 14 Apr 2000

Molinari M, Helenius A

Abstract excerpt

A variety of molecular chaperones and folding enzymes assist the folding of newly synthesized proteins in the endoplasmic reticulum. Here we investigated why some glycoproteins interact with the molecular chaperone BiP, and others with the calnexin/calreticulin pathway. The folding of Semliki forest virus glycoproteins and influenza hemagglutinin was studied in living cells. The initial choice of chaperone...

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

Share to Endoplasmic Reticulum Chaperone BiP

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Source

Identifiers

PMID: 10764645
DOI: 10.1126/science.288.5464.331

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.

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