Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.
Career Basics

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Sci. STKE, 29 May 2001
Vol. 2001, Issue 84, p. tw3
[DOI: 10.1126/stke.2001.84.tw3]

EDITORS' CHOICE

CELL BIOLOGY Protein Aggregation and Degradation

Abstract:

Many neurodegenerative disorders are characterized by the prevalence of protein aggregates in the brain. These aggregates are often composed of proteins that have been modified by the addition of ubiquitin, a marker that should lead to degradation of the offending protein by a cytosolic proteolytic complex known as the proteasome. But are the aggregates a cause or a consequence of the disease process? Bence et al. (see the news story by Helmuth) now show that protein aggregation per se appears to inhibit the proteasomal protein degradation system.

N. F. Bence, R. M. Sampat, R. K. Kopito, Impairment of the ubiquitin-proteasome system by protein aggregation. Science 292, 1552-1555 (2001). [Abstract] [Full Text]

L. Helmuth, Protein clumps hijack cell's clearance system. Science 292, 1467-1468 (2001). [Full Text]

Citation: Protein Aggregation and Degradation. Sci. STKE 2001, tw3 (2001).

Read the Full Text

ADVERTISEMENT
Click Me!

ADVERTISEMENT
Click Me!

To Advertise     Find Products

Science Signaling. ISSN 1937-9145 (pre-2008: Science's STKE. ISSN 1525-8882)