Cage-like complexes that protect folding proteins visualized in cells

Wagner, Jonathan; Bracher, Andreas

doi:10.1038/d41586-024-02926-0

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Cage-like complexes that protect folding proteins visualized in cells

Wagner, J., & Bracher, A. (2024). Cage-like complexes that protect folding proteins visualized in cells. Nature. doi:10.1038/d41586-024-02926-0.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0010-0E14-9 Version Permalink: https://hdl.handle.net/21.11116/0000-0010-0E15-8

Genre: Journal Article

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Creators:
Wagner, Jonathan^{1, 2}, Author
Bracher, Andreas¹, Author

Affiliations:
1Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565152
2Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, Am Klopferspitz 18, 82152 Martinsried, DE, ou_1565142

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Free keywords: Science & Technology - Other Topics; Cell biology; Structural biology;

Abstract: The bacterial chaperonin complex - consisting of the proteins GroEL and GroES - assists the folding of newly synthesized proteins by transiently encapsulating them in a nanometre-scale cage. Visualizing this process using cryo-electron tomography in the intact cellular environment provides insights into the chaperonin reaction cycle in vivo.

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Language(s): eng - English

Dates: Date issued: 2024-11-09

Publication Status: Issued

Pages: 2

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Table of Contents: -

Rev. Type: Peer

Identifiers: ISI: 001336278700003
DOI: 10.1038/d41586-024-02926-0

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Title: Nature

Abbreviation : Nature

Source Genre: Journal

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Publ. Info: London : Nature Publishing Group

Pages: - Volume / Issue: - Sequence Number: - Start / End Page: - Identifier: ISSN: 0028-0836
CoNE: https://pure.mpg.de/cone/journals/resource/954925427238