Molecular structure of phospholipase D and regulatory mechanisms of its activity in plant and animal cells
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61389030%3A_____%2F12%3A00380581" target="_blank" >RIV/61389030:_____/12:00380581 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1134/S0006297912010014" target="_blank" >http://dx.doi.org/10.1134/S0006297912010014</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1134/S0006297912010014" target="_blank" >10.1134/S0006297912010014</a>
Alternative languages
Result language
angličtina
Original language name
Molecular structure of phospholipase D and regulatory mechanisms of its activity in plant and animal cells
Original language description
Phospholipase D (PLD) catalyzes hydrolysis of phospholipids with production of phosphatidic acid, which often acts as secondary messenger of transduction of intracellular signals. This review summarizes data of leading laboratories on specific features of organization and regulation of PLD activity in plant and animal cells. The main structural domains of PLD (C2, PX, PH), the active site, and other functionally important parts of the enzyme are discussed. Regulatory mechanisms of PLD activity are characterized in detail. Studies associated with molecular design, analysis, and synthesis of new nontoxic substances capable of inhibiting different PLD isoenzymes in vivo are shown to be promising for biotechnology and medicine.
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
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
<a href="/en/project/GAP501%2F11%2F1654" target="_blank" >GAP501/11/1654: Phospholipid signaling and interaction with microtubule/actin cytoskeleton in biotic stress response of Arabidopsis thaliana</a><br>
Continuities
Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2012
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Biochemistry-Moscow
ISSN
0006-2979
e-ISSN
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Volume of the periodical
77
Issue of the periodical within the volume
1
Country of publishing house
US - UNITED STATES
Number of pages
14
Pages from-to
1-14
UT code for WoS article
000299897200001
EID of the result in the Scopus database
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