Interakce apoptotických proteinů AIF a endonucleasa G analyzovaná pomocí bioinformatických predikcí, molekulárního dockingu a fluorescenční mikroskopií

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14330%2F08%3A00026398" target="_blank" >RIV/00216224:14330/08:00026398 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Interactions of apoptotic proteins AIF and endonuclease G analyzed by bioinformatic predictions, molecular docking, and fluorescent microscopy

Popis výsledku v původním jazyce

During apoptosis several mitochondrial proteins are released. Some of them participate in caspase-independent nuclear DNA degradation, especially apoptosis-inducing factor (AIF) and endonuclease G (endoG). We studied the structure, cellular localization,and interactions of several proteins in silico and in vitro using fluorescent microscopy. Bioinformatic predictions were conducted to analyze the presence of interaction sites in the studied proteins. We conducted molecular modeling of proteins with unknown 3D structure: endonuclease G, CPS-6, WAH-1, and heat shock protein 70-1. These models were then refined by MolProbity server and employed together with experimentally known 3D structures of other proteins like AIF and cyclophilin A in molecular docking simulations of interactions. Fluorescence resonance energy transfer (FRET) technique and consequent image analysis was used to evaluate the interactions of fluorescently labeled proteins in cells. Our results represent new information

Název v anglickém jazyce

Interactions of apoptotic proteins AIF and endonuclease G analyzed by bioinformatic predictions, molecular docking, and fluorescent microscopy

Popis výsledku anglicky

During apoptosis several mitochondrial proteins are released. Some of them participate in caspase-independent nuclear DNA degradation, especially apoptosis-inducing factor (AIF) and endonuclease G (endoG). We studied the structure, cellular localization,and interactions of several proteins in silico and in vitro using fluorescent microscopy. Bioinformatic predictions were conducted to analyze the presence of interaction sites in the studied proteins. We conducted molecular modeling of proteins with unknown 3D structure: endonuclease G, CPS-6, WAH-1, and heat shock protein 70-1. These models were then refined by MolProbity server and employed together with experimentally known 3D structures of other proteins like AIF and cyclophilin A in molecular docking simulations of interactions. Fluorescence resonance energy transfer (FRET) technique and consequent image analysis was used to evaluate the interactions of fluorescently labeled proteins in cells. Our results represent new information

Druh

O - Ostatní výsledky

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2008

Kód důvěrnosti údajů

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