The 13Å Structure of a Chaperonin GroEL–Protein Substrate Complex by Cryo-electron Microscopy
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Structural Biology
Reference27 articles.
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4. Allosteric control by ATP of non-folded protein binding to GroEL;Yifrach;J. Mol. Biol.,1996
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1. Friends in need: How chaperonins recognize and remodel proteins that require folding assistance;Frontiers in Molecular Biosciences;2022-11-21
2. Three-dimensional motions of GroEL during substrate protein recognition;2022-09-16
3. Electron scattering properties of biological macromolecules and their use for cryo-EM map sharpening;Faraday Discussions;2022
4. Chaperonin-assisted protein folding: a chronologue;Quarterly Reviews of Biophysics;2020
5. A two-domain folding intermediate of RuBisCO in complex with the GroEL chaperonin;International Journal of Biological Macromolecules;2018-10
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