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
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DOI - Digital Object Identifier
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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
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Result continuities
Project
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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
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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
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EID of the result in the Scopus database
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