The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-β production

Lucia Pastorino, Anyang Sun, Pei-Jung Lu, Xiao Zhen Zhou, Martin Balastik, Greg Finn, Gerburg Wulf, Jormay Lim, Shi-Hua Li, Xiaojiang Li, Weiming Xia, Linda K. Nicholson and Kun Ping Lu ()
Additional contact information
Lucia Pastorino: Harvard Medical School
Anyang Sun: Harvard Medical School
Pei-Jung Lu: Kaohsiung Veterans General Hospital
Xiao Zhen Zhou: Harvard Medical School
Martin Balastik: Harvard Medical School
Greg Finn: Harvard Medical School
Gerburg Wulf: Harvard Medical School
Jormay Lim: Harvard Medical School
Shi-Hua Li: Emory University
Xiaojiang Li: Emory University
Weiming Xia: Harvard Medical School
Linda K. Nicholson: Cornell University
Kun Ping Lu: Harvard Medical School

Nature, 2006, vol. 440, issue 7083, 528-534

Abstract: Pin number Alzheimer's disease pathology is characterized by the presence of plaques of amyloid β-peptides and neurofibrillary tangles of tau protein. The Pin1 proline isomerase, known to restore the function of defective tau protein, is now emerging as a possible link between tangle and plaque pathologies. New work points to amyloid precursor protein as a Pin1 target, providing insight into the pathogenic process, as well as possible new drug targets.

Date: 2006
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/nature04543 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:440:y:2006:i:7083:d:10.1038_nature04543

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

DOI: 10.1038/nature04543

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 ().