EconPapers    
Economics at your fingertips  
 

Pinning down phosphorylated tau

Michel Goedert ()
Additional contact information
Michel Goedert: MRC Laboratory of Molecular Biology

Nature, 1999, vol. 399, issue 6738, 739-740

Abstract: A defining characteristic of certain neurodegenerative diseases is the formation of filamentous deposits of a microtubule-associated protein called tau, in an abnormal hyperphosphorylated form. New work shows that this form of tau can bind to a prolyl isomerase called Pin1, and that this interaction restores the biological activity of phosphorylated tau. This discovery could open the way to developing therapeutic compounds that reduce the pool of functionally impaired tau.

Date: 1999
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/21550 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:399:y:1999:i:6738:d:10.1038_21550

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/21550

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 ().

 
Page updated 2025-03-19
Handle: RePEc:nat:nature:v:399:y:1999:i:6738:d:10.1038_21550