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Ring finger E3 ubiqutin ligase CBL protein and its functional roles and mutations in myeloid malignancies

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00023736%3A_____%2F17%3A00011737" target="_blank" >RIV/00023736:_____/17:00011737 - isvavai.cz</a>

  • Result on the web

    <a href="https://www.novapublishers.com/catalog/product_info.php?products_id=61057" target="_blank" >https://www.novapublishers.com/catalog/product_info.php?products_id=61057</a>

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    Ring finger E3 ubiqutin ligase CBL protein and its functional roles and mutations in myeloid malignancies

  • Original language description

    The E3 ubiquitin ligases facilitate substrate specificity and isopeptide bond formation between C-terminal glycine residue of ubiquitin (Gly 76) and a lysine residue in the target protein. This work reviews several new insights, discusses emerging roles and analyzes clinical implications of uniquitin ligases.

  • Czech name

  • Czech description

Classification

  • Type

    C - Chapter in a specialist book

  • CEP classification

  • OECD FORD branch

    30205 - Hematology

Result continuities

  • Project

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2017

  • Confidentiality

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

Data specific for result type

  • Book/collection name

    Ubiquitin ligase: new insights, emerging roles and clinical implications

  • ISBN

    978-1-53610-912-2

  • Number of pages of the result

    8

  • Pages from-to

    "chapter 4"

  • Number of pages of the book

    69

  • Publisher name

    Nova Science Publishers

  • Place of publication

    New York

  • UT code for WoS chapter