Modulating co-translational protein folding by rational design and ribosome engineering
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
-
2041-1723
- Extent
-
Online-Ressource
- Language
-
Englisch
- Notes
-
online resource.
- Bibliographic citation
-
Modulating co-translational protein folding by rational design and ribosome engineering ; volume:13 ; number:1 ; day:22 ; month:7 ; year:2022 ; pages:1-14 ; date:12.2022
Nature Communications ; 13, Heft 1 (22.7.2022), 1-14, 12.2022
- Creator
-
Ahn, Minkoo
Włodarski, Tomasz
Mitropoulou, Alkistis
Chan, Sammy H. S.
Sidhu, Haneesh
Plessa, Elena
Becker, Thomas A.
Budisa, Nediljko
Waudby, Christopher A.
Beckmann, Roland
Cassaignau, Anaïs M. E.
Cabrita, Lisa D.
Christodoulou, John
- Contributor
-
SpringerLink (Online service)
- DOI
-
10.1038/s41467-022-31906-z
- URN
-
urn:nbn:de:101:1-2022120521034677787618
- Rights
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:22 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Ahn, Minkoo
- Włodarski, Tomasz
- Mitropoulou, Alkistis
- Chan, Sammy H. S.
- Sidhu, Haneesh
- Plessa, Elena
- Becker, Thomas A.
- Budisa, Nediljko
- Waudby, Christopher A.
- Beckmann, Roland
- Cassaignau, Anaïs M. E.
- Cabrita, Lisa D.
- Christodoulou, John
- SpringerLink (Online service)
Other Objects (12)
Author Correction: Modulating co-translational protein folding by rational design and ribosome engineering
Ribosome Processivity and Co-translational Protein Folding
Co-translational protein folding by ribosome-associated chaperones: Ssb and RAC
Structural remodeling of ribosome associated Hsp40-Hsp70 chaperones during co-translational folding
Impact of translation speed on co-translational protein folding and ribosome associated factor recruitment
The ribosome lowers the entropic penalty of protein folding
Co-Translational Protein Folding and Sorting in Chloroplasts
Structural basis of translational recycling and bacterial ribosome rescue
Molecular mechanisms of substrate selection and protein folding on the ribosome
Disome-seq reveals widespread ribosome collisions that promote cotranslational protein folding
The bacterial ribosome : testing a new concept for translational initiation
Resolving chaperone-assisted protein folding on the ribosome at the peptide level
Author Correction: Modulating co-translational protein folding by rational design and ribosome engineering
Ribosome Processivity and Co-translational Protein Folding
Co-translational protein folding by ribosome-associated chaperones: Ssb and RAC
Structural remodeling of ribosome associated Hsp40-Hsp70 chaperones during co-translational folding
Impact of translation speed on co-translational protein folding and ribosome associated factor recruitment
The ribosome lowers the entropic penalty of protein folding
Co-Translational Protein Folding and Sorting in Chloroplasts
Structural basis of translational recycling and bacterial ribosome rescue
Molecular mechanisms of substrate selection and protein folding on the ribosome
Disome-seq reveals widespread ribosome collisions that promote cotranslational protein folding
The bacterial ribosome : testing a new concept for translational initiation
Resolving chaperone-assisted protein folding on the ribosome at the peptide level
Author Correction: Modulating co-translational protein folding by rational design and ribosome engineering
Ribosome Processivity and Co-translational Protein Folding
Co-translational protein folding by ribosome-associated chaperones: Ssb and RAC
Structural remodeling of ribosome associated Hsp40-Hsp70 chaperones during co-translational folding
Impact of translation speed on co-translational protein folding and ribosome associated factor recruitment
The ribosome lowers the entropic penalty of protein folding
Co-Translational Protein Folding and Sorting in Chloroplasts
Structural basis of translational recycling and bacterial ribosome rescue
Molecular mechanisms of substrate selection and protein folding on the ribosome
Disome-seq reveals widespread ribosome collisions that promote cotranslational protein folding
The bacterial ribosome : testing a new concept for translational initiation