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Effect of posttranslational modifications on enzyme function and assembly

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F13%3A10190110" target="_blank" >RIV/00216208:11310/13:10190110 - isvavai.cz</a>

  • Alternative codes found

    RIV/61388971:_____/13:00422889

  • Result on the web

    <a href="http://dx.doi.org/10.1016/j.jprot.2013.03.025" target="_blank" >http://dx.doi.org/10.1016/j.jprot.2013.03.025</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.jprot.2013.03.025" target="_blank" >10.1016/j.jprot.2013.03.025</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Effect of posttranslational modifications on enzyme function and assembly

  • Original language description

    The detailed examination of enzyme molecules by mass spectrometry and other techniques continues to identify hundreds of distinct PTMs. Recently, global analyses of enzymes using methods of contemporary proteomics revealed widespread distribution of PTMson many key enzymes distributed in all cellular compartments. Critically, patterns of multiple enzymatic and nonenzymatic PTMs within a single enzyme are now functionally evaluated providing a holistic picture of a macromolecule interacting with low molecular mass compounds, some of them being substrates, enzyme regulators, or activated precursors for enzymatic and nonenzymatic PTMs. Multiple PTMs within a single enzyme molecule and their mutual interplays are critical for the regulation of catalytic activity. Full understanding of this regulation will require detailed structural investigation of enzymes, their structural analogs, and their complexes. Further, proteomics is now integrated with molecular genetics, transcriptomics, and o

  • 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

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2013

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Journal of Proteomics

  • ISSN

    1874-3919

  • e-ISSN

  • Volume of the periodical

    92

  • Issue of the periodical within the volume

    Special issue SI

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    30

  • Pages from-to

    80-109

  • UT code for WoS article

    000328518000007

  • EID of the result in the Scopus database