Protein degradation and protection against misfolded or damaged proteins
Alfred L. Goldberg ()
Additional contact information
Alfred L. Goldberg: Harvard Medical School
Nature, 2003, vol. 426, issue 6968, 895-899
Abstract:
Abstract The ultimate mechanism that cells use to ensure the quality of intracellular proteins is the selective destruction of misfolded or damaged polypeptides. In eukaryotic cells, the large ATP-dependent proteolytic machine, the 26S proteasome, prevents the accumulation of non-functional, potentially toxic proteins. This process is of particular importance in protecting cells against harsh conditions (for example, heat shock or oxidative stress) and in a variety of diseases (for example, cystic fibrosis and the major neurodegenerative diseases). A full understanding of the pathogenesis of the protein-folding diseases will require greater knowledge of how misfolded proteins are recognized and selectively degraded.
Date: 2003
References: Add references at CitEc
Citations: View citations in EconPapers (2)
Downloads: (external link)
https://www.nature.com/articles/nature02263 Abstract (text/html)
Access to the full text of the articles in this series is restricted.
Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.
Export reference: BibTeX
RIS (EndNote, ProCite, RefMan)
HTML/Text
Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:426:y:2003:i:6968:d:10.1038_nature02263
Ordering information: This journal article can be ordered from
https://www.nature.com/
DOI: 10.1038/nature02263
Access Statistics for this article
Nature is currently edited by Magdalena Skipper
More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().