Regulation of Traslantion During In Vitro Maturation of Bovine Oocytes: The Role of MAP Kinase, eIF4E (Cap Binding Protein) Phosphorylation, and eIF4E-BP1.
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985904%3A_____%2F02%3A21023126" target="_blank" >RIV/67985904:_____/02:21023126 - 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
Regulation of Traslantion During In Vitro Maturation of Bovine Oocytes: The Role of MAP Kinase, eIF4E (Cap Binding Protein) Phosphorylation, and eIF4E-BP1.
Original language description
Meiotic maturation of mammalian oocytes (transition from prophase I to metaphase II) is accompanied by complex changes in the protein phosphorylation pattern. we show, that during meiotic maturation of bovine oocyre, the translantion initiation factor, eIF4E (the cap binding protein), gradually becomes phosphorylated. This substantial phosphorylation begins at the time of germinal vesicle breakdown (GVBD) and continues to the metaphase II stage.
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
EB - Genetics and molecular biology
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2002
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Biology of Reproduction
ISSN
0006-3363
e-ISSN
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Volume of the periodical
66
Issue of the periodical within the volume
N/A
Country of publishing house
US - UNITED STATES
Number of pages
9
Pages from-to
1274-1282
UT code for WoS article
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EID of the result in the Scopus database
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