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Cited by 242

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Cotranslational folding and calnexin binding during glycoprotein synthesis.

Open access
Chen, W, Helenius, J, Braakman, I, Helenius, A·1995·Proceedings of the National Academy of Sciences

Abstract

To analyze cotranslational folding of influenza hemagglutinin in the endoplasmic reticulum of live cells, we used short pulses of radiolabeling followed by immunoprecipitation and analysis with a two-dimensional SDS/polyacrylamide gel system which was nonreducing in the first dimension and reducing in the second. It separated nascent glycopolypeptides of different length and oxidation state. Evidence was obtained for cotranslational disulfide formation, generation of conformational epitopes, N-linked glycosylation, and oligosaccharide-dependent binding of calnexin, a membrane-bound chaperone that binds to incompletely folded glycoproteins via partially glucose-trimmed oligosaccharides. When glycosylation or oligosaccharide trimming was inhibited, the folding pathway was perturbed, suggesting a role for N-linked oligosaccharides and calnexin during translation of hemagglutinin.

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Metadata

Authors
Chen, W., Helenius, J., Braakman, I., & Helenius, A.
Venue
Proceedings of the National Academy of Sciences
Published
1995-07-03
Volume
92
Issue
14
Pages
6229-6233
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2089621623
Cited by
242
References
1
FWCI
6.03
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Cotranslational folding and calnexin binding during glycoprotein synthesis. https://app.cochat.ai/papers/10.1073/pnas.92.14.6229
The paper
Chen, W., Helenius, J., Braakman, I., & Helenius, A. (1995). Cotranslational folding and calnexin binding during glycoprotein synthesis. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.92.14.6229

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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