Cotranslational protein folding on the ribosome monitored in real time-Reference-Cited by-同舟云学术

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Cotranslational protein folding on the ribosome monitored in real time

Published:2015-11-26 Issue:6264 Volume:350 Page:1104-1107
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Holtkamp W.,Kokic G.,Jager M.,Mittelstaet J.,Komar A. A.,Rodnina M. V.

Funder

Human Frontier Science Program

Deutsche Forschungsgemeinschaft

Max Planck Society

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference27 articles.

1. Monitoring cotranslational protein folding in mammalian cells at codon resolution

2. Structure and dynamics of a ribosome-bound nascent chain by NMR spectroscopy

3. Cotranslational structure acquisition of nascent polypeptides monitored by NMR spectroscopy

4. Nascent Membrane and Secretory Proteins Differ in FRET-Detected Folding Far inside the Ribosome and in Their Exposure to Ribosomal Proteins

5. Folding zones inside the ribosomal exit tunnel

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1. Mechanically rigid metallopeptide nanostructures achieved by highly efficient folding;Nature Synthesis;2024-09-05

2. Ribosome Tunnel Environment Drives the Formation of α-Helix during Cotranslational Folding;Journal of Chemical Information and Modeling;2024-08-16

3. The importance of the location of the N-terminus in successful protein folding in vivo and in vitro;Proceedings of the National Academy of Sciences;2024-08-15

4. The ribosome lowers the entropic penalty of protein folding;Nature;2024-08-07

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

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