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Andreas G. Ladurner
Researcher at Ludwig Maximilian University of Munich
Publications - 97
Citations - 8634
Andreas G. Ladurner is an academic researcher from Ludwig Maximilian University of Munich. The author has contributed to research in topics: Chromatin & Histone. The author has an hindex of 43, co-authored 94 publications receiving 7723 citations. Previous affiliations of Andreas G. Ladurner include Center for Integrated Protein Science Munich & European Bioinformatics Institute.
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Journal ArticleDOI
Structure and Function of a Human TAFII250 Double Bromodomain Module
TL;DR: In this article, it was shown that TAFII250, the largest subunit of TFIID, contains two tandem bromodomain modules that bind selectively to multiply acetylated histone H4 peptides.
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The macro domain is an ADP-ribose binding module
Georgios I. Karras,Georg Kustatscher,Heeran R Buhecha,Mark D. Allen,Céline Pugieux,Fiona Sait,Mark Bycroft,Andreas G. Ladurner +7 more
TL;DR: In this article, the authors provide biochemical and structural evidence that macro domains are high affinity binding modules for ADP-ribose nucleotide nucleotides and reveal a conserved ligand binding pocket among the macro domain fold.
Journal ArticleDOI
A macrodomain-containing histone rearranges chromatin upon sensing PARP1 activation.
Gyula Timinszky,Susanne Till,Paul O. Hassa,Michael Hothorn,Georg Kustatscher,Bianca Nijmeijer,Julien Colombelli,Matthias Altmeyer,Ernst H. K. Stelzer,Klaus Scheffzek,Michael O. Hottiger,Andreas G. Ladurner +11 more
TL;DR: Macrodomains are identified as modules that directly sense PARP activation in vivo and establish macroH2A histones as dynamic regulators of chromatin plasticity.
Journal ArticleDOI
The transcriptional cofactor complex CRSP is required for activity of the enhancer-binding protein Sp1.
TL;DR: A new human factor, CRSP, is described that is required together with the TAFIIs for transcriptional activation by Sp1, and the presence of common subunits in distinct cofactor complexes suggests a combinatorial mechanism of co-activator assembly during transcriptionalactivation.
Journal ArticleDOI
Poly(ADP-ribosyl)ation directs recruitment and activation of an ATP-dependent chromatin remodeler.
Aaron J. Gottschalk,Gyula Timinszky,Stephanie E. Kong,Jingji Jin,Yong Cai,Selene K. Swanson,Michael P. Washburn,Laurence Florens,Andreas G. Ladurner,Joan W. Conaway,Ronald C. Conaway +10 more
TL;DR: It is proposed that poly(ADP-ribosyl)ation of chromatin-associated Parp1 serves as a mechanism for targeting a SNF2 family remodeler to chromatin.