IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v440y2006i7083d10.1038_nature04543.html
   My bibliography  Save this article

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

Author

Listed:
  • Lucia Pastorino

    (Harvard Medical School)

  • Anyang Sun

    (Harvard Medical School
    Fudan University)

  • 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)

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.

Suggested Citation

  • 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 & Kun Ping Lu, 2006. "The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-β production," Nature, Nature, vol. 440(7083), pages 528-534, March.
    • Handle: RePEc:nat:nature:v:440:y:2006:i:7083:d:10.1038_nature04543
    DOI: 10.1038/nature04543
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature04543
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/nature04543?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:440:y:2006:i:7083:d:10.1038_nature04543. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.