Cotranslational Protein Folding inside the Ribosome Exit Tunnel-Reference-Cited by-同舟云学术

Cotranslational Protein Folding inside the Ribosome Exit Tunnel

Published:2015-09 Issue:10 Volume:12 Page:1533-1540
ISSN:2211-1247
Container-title:Cell Reports
language:en
Short-container-title:Cell Reports

Author:

Nilsson Ola B.,Hedman Rickard,Marino Jacopo,Wickles Stephan,Bischoff Lukas,Johansson Magnus,Müller-Lucks Annika,Trovato Fabio,Puglisi Joseph D.,O’Brien Edward P.,Beckmann Roland,von Heijne Gunnar

Publisher

Elsevier BV

Subject

General Biochemistry, Genetics and Molecular Biology

Reference41 articles.

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2. SecM-stalled ribosomes adopt an altered geometry at the peptidyl transferase center;Bhushan;PLoS Biol.,2011

3. Molecular basis for the ribosome functioning as an L-tryptophan sensor;Bischoff;Cell Rep.,2014

4. Translocon “pulling” of nascent SecM controls the duration of its translational pause and secretion-responsive secA regulation;Butkus;J. Bacteriol.,2003

5. Cotranslational folding inhibits translocation from within the ribosome-Sec61 translocon complex;Conti;Nat. Struct. Mol. Biol.,2014

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1. Reconstituted Cell-free Translation Systems for Exploring Protein Folding and Aggregation;Journal of Molecular Biology;2024-10

2. Single-residue effects on the behavior of a nascent polypeptide chain inside the ribosome exit tunnel;2024-08-20

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4. Resolving chaperone-assisted protein folding on the ribosome at the peptide level;Nature Structural & Molecular Biology;2024-07-10

5. Mechanism of chaperone coordination during cotranslational protein folding in bacteria;Molecular Cell;2024-07