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Endonuclease G interacts with histone H2B and DNA topoisomerase II alpha during apoptosis

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14330%2F12%3A00059138" target="_blank" >RIV/00216224:14330/12:00059138 - isvavai.cz</a>

  • Result on the web

    <a href="http://link.springer.com/article/10.1007%2Fs11010-011-1182-x" target="_blank" >http://link.springer.com/article/10.1007%2Fs11010-011-1182-x</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1007/s11010-011-1182-x" target="_blank" >10.1007/s11010-011-1182-x</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Endonuclease G interacts with histone H2B and DNA topoisomerase II alpha during apoptosis

  • Original language description

    During some apoptotic pathways, proteins apoptosis-inducing factor (AIF) and endonuclease G (EndoG) are released from the mitochondria and they translocate into the cell nuclei, where they probably participate in chromatin degradation together with othernuclear proteins. Exact mechanism of EndoG activity in cell nucleus is still unknown. We conducted a living-cell confocal fluorescence microscopy followed by an image analysis of fluorescence resonance energy transfer (FRET) to analyze the possibility of protein interactions of EndoG with histone H2B and human DNA topoisomerase II alpha (TOPO2a). Our results show that EndoG interacts with both these proteins during apoptotic cell death. Therefore, we can conclude that EndoG and TOPO2a may actively participate in apoptotic chromatin degradation. The possible existence of a degradation complex consisting of EndoG and TOPO2a and possibly other proteins like AIF and cyclophilin A have yet to be investigated.

  • Czech name

  • Czech description

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

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

    2012

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Mol Cell Biochem

  • ISSN

    0300-8177

  • e-ISSN

  • Volume of the periodical

    363

  • Issue of the periodical within the volume

    1-2

  • Country of publishing house

    DE - GERMANY

  • Number of pages

    7

  • Pages from-to

    301-307

  • UT code for WoS article

    000300888900030

  • EID of the result in the Scopus database