IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v497y2013i7451d10.1038_nature12162.html
   My bibliography  Save this article

Mature HIV-1 capsid structure by cryo-electron microscopy and all-atom molecular dynamics

Author

Listed:
  • Gongpu Zhao

    (University of Pittsburgh School of Medicine
    Pittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine)

  • Juan R. Perilla

    (University of Illinois at Urbana-Champaign)

  • Ernest L. Yufenyuy

    (Pittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine
    Microbiology and Immunology, Vanderbilt University School of Medicine)

  • Xin Meng

    (University of Pittsburgh School of Medicine
    Pittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine)

  • Bo Chen

    (University of Central Florida)

  • Jiying Ning

    (University of Pittsburgh School of Medicine
    Pittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine)

  • Jinwoo Ahn

    (University of Pittsburgh School of Medicine
    Pittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine)

  • Angela M. Gronenborn

    (University of Pittsburgh School of Medicine
    Pittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine)

  • Klaus Schulten

    (University of Illinois at Urbana-Champaign)

  • Christopher Aiken

    (Pittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine
    Microbiology and Immunology, Vanderbilt University School of Medicine)

  • Peijun Zhang

    (University of Pittsburgh School of Medicine
    Pittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine
    Swanson School of Engineering)

Abstract

The structure of the HIV-1 capsid is analysed by cryo-electron microscopy and cryo-electron tomography, allowing presentation of an all-atom molecular dynamics model of the entire capsid.

Suggested Citation

  • Gongpu Zhao & Juan R. Perilla & Ernest L. Yufenyuy & Xin Meng & Bo Chen & Jiying Ning & Jinwoo Ahn & Angela M. Gronenborn & Klaus Schulten & Christopher Aiken & Peijun Zhang, 2013. "Mature HIV-1 capsid structure by cryo-electron microscopy and all-atom molecular dynamics," Nature, Nature, vol. 497(7451), pages 643-646, May.
    • Handle: RePEc:nat:nature:v:497:y:2013:i:7451:d:10.1038_nature12162
    DOI: 10.1038/nature12162
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature12162
    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/nature12162?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. Guido Schryen & Natalia Kliewer & Andreas Fink, 2020. "High Performance Business Computing," Business & Information Systems Engineering: The International Journal of WIRTSCHAFTSINFORMATIK, Springer;Gesellschaft für Informatik e.V. (GI), vol. 62(1), pages 1-3, February.
    2. Guochao Wei & Naseer Iqbal & Valentine V. Courouble & Ashwanth C. Francis & Parmit K. Singh & Arpa Hudait & Arun S. Annamalai & Stephanie Bester & Szu-Wei Huang & Nikoloz Shkriabai & Lorenzo Briganti , 2022. "Prion-like low complexity regions enable avid virus-host interactions during HIV-1 infection," Nature Communications, Nature, vol. 13(1), pages 1-19, December.
    3. Xiaojun Wei & Xiaoqin Wang & Zehui Zhang & Yuanyuan Luo & Zixin Wang & Wen Xiong & Piyush K. Jain & John R. Monnier & Hui Wang & Tony Y. Hu & Chuanbing Tang & Helmut Albrecht & Chang Liu, 2022. "A click chemistry amplified nanopore assay for ultrasensitive quantification of HIV-1 p24 antigen in clinical samples," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    4. Jordy Homing Lam & Aiichiro Nakano & Vsevolod Katritch, 2024. "Scalable computation of anisotropic vibrations for large macromolecular assemblies," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
    5. Yuta Sawanaka & Masahiro Yamashina & Hiroyoshi Ohtsu & Shinji Toyota, 2022. "A self-complementary macrocycle by a dual interaction system," Nature Communications, Nature, vol. 13(1), pages 1-8, 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:497:y:2013:i:7451:d:10.1038_nature12162. 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.