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Cited by 319

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Folding of VSV G Protein: Sequential Interaction with BiP and Calnexin

Hammond, Craig, Helenius, Ari·1994·Science

Abstract

The endoplasmic reticulum (ER) contains molecular chaperones that facilitate the folding of proteins in mammalian cells. Biosynthetic labeling was used to study the interactions of two chaperones, BiP and calnexin, with vesicular stomatitis virus (VSV) glycoprotein (G protein). Coimmunoprecipitation of G protein with the chaperones showed that BiP bound maximally to early folding intermediates of G protein, whereas calnexin bound after a short lag to more folded molecules. Castanospermine, an inhibitor of ER glucosidases, blocked the binding of proteins to calnexin and inhibited G protein folding. Interaction with calnexin was necessary for efficient folding of G protein and for retention of partially folded forms.

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Crossref · 10.1126/science.7939687

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Metadata

Authors
Hammond, C., & Helenius, A.
Venue
Science
Published
1994-10-21
Volume
266
Issue
5184
Pages
456-458
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2034264764
Cited by
319
References
2
FWCI
11.92
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Folding of VSV G Protein: Sequential Interaction with BiP and Calnexin. https://app.cochat.ai/papers/10.1126/science.7939687
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Hammond, C., & Helenius, A. (1994). Folding of VSV G Protein: Sequential Interaction with BiP and Calnexin. Science. https://doi.org/10.1126/science.7939687

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

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.