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Structure of the immature retroviral capsid at 8 angstrom resolution by cryo-electron microscopy

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F12%3A00381079" target="_blank" >RIV/61388963:_____/12:00381079 - isvavai.cz</a>

  • Alternative codes found

    RIV/60461373:22330/12:43894097

  • Result on the web

    <a href="http://dx.doi.org/10.1038/nature11169" target="_blank" >http://dx.doi.org/10.1038/nature11169</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1038/nature11169" target="_blank" >10.1038/nature11169</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Structure of the immature retroviral capsid at 8 angstrom resolution by cryo-electron microscopy

  • Original language description

    The assembly of retroviruses such as HIV-1 is driven by oligomerization of their major structural protein, Gag. Gag is a multi-domain polyprotein including three conserved folded domains MA (matrix), CA (capsid) and NC (nucleocapsid). Assembly of an infectious virion proceeds in two stages. In the first stage, Gag oligomerization into a hexameric protein lattice leads to formation of an incomplete, roughly spherical protein shell that buds through the plasma membrane of the infected cell to release an enveloped immature virus particle. In the second stage, cleavage of Gag by the viral protease leads to rearrangement of the particle interior, converting the non-infectious immature virus particle into a mature infectious virion. The immature Gag shell acts as the pivotal intermediate in assembly and is a potential target for anti-retroviral drugs both to inhibit virus assembly and to disrupt virus maturation. Detailed structural information on the immature Gag shell has not been availabl

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    Z - Vyzkumny zamer (s odkazem do CEZ)

Others

  • Publication year

    2012

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Nature

  • ISSN

    0028-0836

  • e-ISSN

  • Volume of the periodical

    487

  • Issue of the periodical within the volume

    7407

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    5

  • Pages from-to

    385-389

  • UT code for WoS article

    000306506500047

  • EID of the result in the Scopus database