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Prediction of localization and interactions of proteins involved in caspase-independent apoptosis

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14330%2F09%3A00036811" target="_blank" >RIV/00216224:14330/09:00036811 - isvavai.cz</a>

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    Prediction of localization and interactions of proteins involved in caspase-independent apoptosis

  • Original language description

    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). Another interesting protein is AIF-homologous mitochondrion-associated inducer of death (AMID). Heat shock protein HSP70-1, cyclophilin A and possibly DNA topoisomerase II alpha are also high candidate proteins that seem to take part at least in some part of caspase-independent apoptosis connected toAIF. We studied the structure, cellular localization, and interactions of these proteins in silico and also in cells using fluorescent microscopy. Bioinformatic predictions were conducted to analyze the interactions of some of the studied proteins with possible partners. We conducted molecular modeling of proteins with unknown 3D structures. These models were then refined by MolProbity server and employed in molecular docking simulations of interactions.

  • Czech name

  • Czech description

Classification

  • Type

    O - Miscellaneous

  • CEP classification

    EB - Genetics and molecular biology

  • OECD FORD branch

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

    2009

  • Confidentiality

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