IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v540y2016i7633d10.1038_nature20590.html
   My bibliography  Save this article

Structure and regulation of the chromatin remodeller ISWI

Author

Listed:
  • Lijuan Yan

    (MOE Key Laboratory of Protein Science, Tsinghua University
    School of Life Science, Tsinghua University)

  • Li Wang

    (MOE Key Laboratory of Protein Science, Tsinghua University
    School of Life Science, Tsinghua University)

  • Yuanyuan Tian

    (MOE Key Laboratory of Protein Science, Tsinghua University
    School of Life Science, Tsinghua University)

  • Xian Xia

    (MOE Key Laboratory of Protein Science, Tsinghua University
    School of Life Science, Tsinghua University)

  • Zhucheng Chen

    (MOE Key Laboratory of Protein Science, Tsinghua University
    School of Life Science, Tsinghua University)

Abstract

The crystal structures of ISWI, the catalytic subunit of several chromatin remodelling complexes, and its complex with a histone H4 peptide are reported.

Suggested Citation

  • Lijuan Yan & Li Wang & Yuanyuan Tian & Xian Xia & Zhucheng Chen, 2016. "Structure and regulation of the chromatin remodeller ISWI," Nature, Nature, vol. 540(7633), pages 466-469, December.
    • Handle: RePEc:nat:nature:v:540:y:2016:i:7633:d:10.1038_nature20590
    DOI: 10.1038/nature20590
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature20590
    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/nature20590?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.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Chunli Yan & Thomas Dodd & Jina Yu & Bernice Leung & Jun Xu & Juntaek Oh & Dong Wang & Ivaylo Ivanov, 2021. "Mechanism of Rad26-assisted rescue of stalled RNA polymerase II in transcription-coupled repair," Nature Communications, Nature, vol. 12(1), pages 1-12, December.
    2. Yichen Zhong & Hakimeh Moghaddas Sani & Bishnu P. Paudel & Jason K. K. Low & Ana P. G. Silva & Stefan Mueller & Chandrika Deshpande & Santosh Panjikar & Xavier J. Reid & Max J. Bedward & Antoine M. Oi, 2022. "The role of auxiliary domains in modulating CHD4 activity suggests mechanistic commonality between enzyme families," Nature Communications, Nature, vol. 13(1), pages 1-17, December.

    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:540:y:2016:i:7633:d:10.1038_nature20590. 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.