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Cited by 222

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

Molecular Chaperones: The Plant Connection

Ellis, R. John·1990·Science

Abstract

Molecular chaperones are a family of unrelated proteins found in all types of cell. They mediate the correct assembly of other polypeptides, but are not components of the mature assembled structures. Chaperones function by binding specifically to interactive protein surfaces that are exposed transiently during many cellular processes and so prevent them from undergoing incorrect interactions that might produce nonfunctional structures. The concept of molecular chaperones originated largely from studies of the chloroplast enzyme rubisco, which fixes carbon dioxide in plant photosynthesis; the function of chaperones forces a rethinking of the principle of protein self-assembly.

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Metadata

Authors
Ellis, R. J.
Venue
Science
Published
1990-11-16
Volume
250
Issue
4983
Pages
954-959
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2102003825
Cited by
222
References
1
FWCI
11.21
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Molecular Chaperones: The Plant Connection. https://app.cochat.ai/papers/10.1126/science.250.4983.954
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Ellis, R. J. (1990). Molecular Chaperones: The Plant Connection. Science. https://doi.org/10.1126/science.250.4983.954

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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.