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Mit domainia.

Mit domainia. Research Abstract Details 

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  • Mit domainia. Abstract Text:

    james h hurleyJames H Hurley,dong yangDong Yang,james h hurleyJames H Hurley,dong yangDong Yang,

    The AAA ATPase Vps4 disassembles the membrane-bound ESCRT-III lattice. Four recent publications show how Vps4 carries out this task in a partnership with another ESCRT-associated protein, Vta1. Vps4 and Vta1 both contain MIT domains, which bind to "MIT-interacting motifs" (MIMs) of ESCRT-III proteins. As new MIT domain proteins are rapidly being identified, these studies will likely have relevance well beyond Vps4.

    Mit domainia. Publishing Authors By Initials

    jh hurleyJH Hurley,d yangD Yang,jh hurleyJH Hurley,d yangD Yang,

    For similar abstracts research abstracts see: abstracts research

    PUBMED ID PMID:

    MEDLINE DATE:

    Mit domainia. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: Developmental cell

    VOLUME: 14

    Page Numbers: 6-8

    Journal Abbreviation: Dev. Cell

    ISSN: 1534-5807

    DAY: 15

    MONTH: Jan

    YEAR: 2008

    Mit domainia. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 101120028

    Mit domainia. Keywords Mesh Terms:

    KEYWORDS:

    MESH TERMS:

    Chemical & Substance for Abstract: Mit domainia. Information

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    Grant and Affiliation Information for Mit domainia.

    AFFILIATION: Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, U.S. Department of Health and Human Services, Bethesda, MD 20892, USA.

    Country: United States

    United States Research PublicationUnited States Research Publication

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    MEDLINETA: Dev Cell

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