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In vivo deletion analysis of the architecture of a multiprotein complex of translation initiation factors

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F07%3A00088916" target="_blank" >RIV/61388971:_____/07:00088916 - isvavai.cz</a>

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    In vivo deletion analysis of the architecture of a multiprotein complex of translation initiation factors

  • Original language description

    Protein complexes play a critical role in virtually all cellular processes that have been studied to date. Comprehensive knowledge of the architecture of a protein complex of interest is, therefore, an important prerequisite for understanding its role inthe context of a particular pathway in which it participates. One of the possible approaches that has proven very useful in characterizing a protein complex is outlined in this chapter using the example of the eukaryotic initiation factor 3 (eIF3) and some of its binding partners. eIF3 is one of the major players in the translation initiation pathway because it orchestrates several crucial steps that ultimately conclude with formation of the 80S ribosome where the anticodon of methionyl-tRNAi Met base-pairs with the AUG start codon of the mRNA in the ribosomal P-site

  • Czech name

    In vivo deleční analýza architektury multiproteinového komplexu tvořeného iniciačními faktory

  • Czech description

    Práce pojednáva o studiu inciace translace a specifické úloze translačních iniciačních faktorů eIF1, 2, 3 a 5

Classification

  • Type

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

  • CEP classification

    EE - Microbiology, virology

  • OECD FORD branch

Result continuities

  • Project

  • Continuities

    Z - Vyzkumny zamer (s odkazem do CEZ)<br>N - Vyzkumna aktivita podporovana z neverejnych zdroju

Others

  • Publication year

    2007

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Methods in Enzymology

  • ISSN

    0076-6879

  • e-ISSN

  • Volume of the periodical

    431

  • Issue of the periodical within the volume

    -

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    18

  • Pages from-to

    15-32

  • UT code for WoS article

  • EID of the result in the Scopus database