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Showing 1–3 of 3 results
Advanced filters: Author: "Andreas G. Ladurner" Clear advanced filters

  • Chromatin-remodeling enzymes perform the formidable task of reorganizing the structure of a stable macromolecular assembly, the nucleosome. Recently published work demonstrates that the SNF2H chromatin remodeler distorts the histone octamer structure upon binding to the nucleosome, then taps into this induced plasticity to productively achieve nucleosome sliding.

    • Hari R Singh
    • Magdalena Murawska
    • Andreas G Ladurner
    News & Views
    Nature Structural & Molecular Biology
    Volume: 24, P: 341-343

  • A recent report shows that several 'poly-ADP-ribose-polymerases' may function exclusively as a family of endogenous mono-ADP-ribosyltransferases, providing a new, molecularly less complex and broadened cellular role for this elusive post-translational modification.

    • Susanne Till
    • Konstantina Diamantara
    • Andreas G Ladurner
    News & Views
    Nature Structural & Molecular Biology
    Volume: 15, P: 1243-1244

  • The human histone macroH2A.1.1 recruits activated PARP1 enzyme to chromatin through its poly(ADP-ribose)-binding macrodomain. New work shows that PARP1 and CBP can be displaced from chromatin in cancer cells that have lost macroH2A.1.1, thus leading to changes in histone H2B acetylation at cancer-relevant genes.

    • Gyula Timinszky
    • Andreas G Ladurner
    News & Views
    Nature Structural & Molecular Biology
    Volume: 21, P: 947-948