Substrate polypeptide presents a load on the apical domains of the chaperonin GroEL
Author:
Publisher
Proceedings of the National Academy of Sciences
Subject
Multidisciplinary
Reference44 articles.
1. Principles that Govern the Folding of Protein Chains
2. The Hsp70 and Hsp60 Chaperone Machines
3. Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein
4. Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under groes
5. Protein folding in the central cavity of the GroEL–GroES chaperonin complex
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1. Structural basis of substrate progression through the bacterial chaperonin cycle;Proceedings of the National Academy of Sciences;2023-12-08
2. From Microstates to Macrostates in the Conformational Dynamics of GroEL: A Single-Molecule Förster Resonance Energy Transfer Study;The Journal of Physical Chemistry Letters;2023-07-13
3. How soluble misfolded proteins bypass chaperones at the molecular level;Nature Communications;2023-06-21
4. Structural basis of substrate progression through the chaperonin cycle;2023-05-31
5. From Microstates to Macrostates in the Conformational Dynamics of GroEL: a Single-Molecule FRET Study;2023-03-25
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