- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
1 Online-Ressource.
- Language
-
Englisch
- Bibliographic citation
-
The ribosome lowers the entropic penalty of protein folding ; volume:633 ; number:8028 ; day:7 ; month:8 ; year:2024 ; pages:232-239 ; date:9.2024
Nature; 633, Heft 8028 (7.8.2024), 232-239, 9.2024
- Creator
-
Streit, Julian O.
Bukvin, Ivana V.
Chan, Sammy H. S.
Bashir, Shahzad
Woodburn, Lauren F.
Włodarski, Tomasz
Figueiredo, Angelo Miguel
Jurkeviciute, Gabija
Sidhu, Haneesh K.
Hornby, Charity R.
Waudby, Christopher A.
Cabrita, Lisa D.
Cassaignau, Anaïs M. E.
Christodoulou, John
- Contributor
-
SpringerLink (Online service)
- DOI
-
10.1038/s41586-024-07784-4
- URN
-
urn:nbn:de:101:1-2412262123302.559037420610
- Rights
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:26 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
- Streit, Julian O.
- Bukvin, Ivana V.
- Chan, Sammy H. S.
- Bashir, Shahzad
- Woodburn, Lauren F.
- Włodarski, Tomasz
- Figueiredo, Angelo Miguel
- Jurkeviciute, Gabija
- Sidhu, Haneesh K.
- Hornby, Charity R.
- Waudby, Christopher A.
- Cabrita, Lisa D.
- Cassaignau, Anaïs M. E.
- Christodoulou, John
- SpringerLink (Online service)
Other Objects (12)
Ribosome Processivity and Co-translational Protein Folding
Molecular mechanisms of substrate selection and protein folding on the ribosome
Modulating co-translational protein folding by rational design and ribosome engineering
Disome-seq reveals widespread ribosome collisions that promote cotranslational protein folding
Co-translational protein folding by ribosome-associated chaperones: Ssb and RAC
Entropic herding
Resolving chaperone-assisted protein folding on the ribosome at the peptide level
Structural characterization of ribosomal complexes involved in ribosome biogenesis and protein folding
Structural remodeling of ribosome associated Hsp40-Hsp70 chaperones during co-translational folding
Endurance training lowers ribosome density despite increasing ribosome biogenesis markers in rodent skeletal muscle
The role of ribosome-associated chaperones in the folding of newly synthesized proteins
Author Correction: Modulating co-translational protein folding by rational design and ribosome engineering
Ribosome Processivity and Co-translational Protein Folding
Molecular mechanisms of substrate selection and protein folding on the ribosome
Modulating co-translational protein folding by rational design and ribosome engineering
Disome-seq reveals widespread ribosome collisions that promote cotranslational protein folding
Co-translational protein folding by ribosome-associated chaperones: Ssb and RAC
Entropic herding
Resolving chaperone-assisted protein folding on the ribosome at the peptide level
Structural characterization of ribosomal complexes involved in ribosome biogenesis and protein folding
Structural remodeling of ribosome associated Hsp40-Hsp70 chaperones during co-translational folding
Endurance training lowers ribosome density despite increasing ribosome biogenesis markers in rodent skeletal muscle
The role of ribosome-associated chaperones in the folding of newly synthesized proteins
Author Correction: Modulating co-translational protein folding by rational design and ribosome engineering
Ribosome Processivity and Co-translational Protein Folding
Molecular mechanisms of substrate selection and protein folding on the ribosome
Modulating co-translational protein folding by rational design and ribosome engineering
Disome-seq reveals widespread ribosome collisions that promote cotranslational protein folding
Co-translational protein folding by ribosome-associated chaperones: Ssb and RAC
Entropic herding
Resolving chaperone-assisted protein folding on the ribosome at the peptide level
Structural characterization of ribosomal complexes involved in ribosome biogenesis and protein folding
Structural remodeling of ribosome associated Hsp40-Hsp70 chaperones during co-translational folding
Endurance training lowers ribosome density despite increasing ribosome biogenesis markers in rodent skeletal muscle
The role of ribosome-associated chaperones in the folding of newly synthesized proteins