Molecular structure of phospholipase D and regulatory mechanisms of its activity in plant and animal cells

Kód výsledku v 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>

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

Molecular structure of phospholipase D and regulatory mechanisms of its activity in plant and animal cells

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

Molecular structure of phospholipase D and regulatory mechanisms of its activity in plant and animal cells

Popis výsledku anglicky

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.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/GAP501%2F11%2F1654" target="_blank" >GAP501/11/1654: Fosfolipidová signální dráha, interakce s cytoskeletem a její funkce v odpovědi rostlin Arabidopsis thaliana na biotický stres</a><br>

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2012

Kód důvěrnosti údajů

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

Název periodika

Biochemistry-Moscow

ISSN

0006-2979

e-ISSN

—

Svazek periodika

77

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

14

Strana od-do

1-14

Kód UT WoS článku

000299897200001

EID výsledku v databázi Scopus

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