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The EMBO Journal|January 10, 2013
Dimerization of Sir3 via its C-terminal winged helix domain is essential for yeast heterochromatin formationMariano Oppikofer, Stephanie Kueng, Jeremy J Keusch, et al.Folding & Design|January 1, 1996
Towards the complete structural characterization of a protein folding pathway: the structures of the denatured, transition and native states for the association/folding of two complementary fragments of cleaved chymotrypsin inhibitor 2. Direct evidence for a nucleation-condensation mechanismJ L Neira, B Davis, A G Ladurner, et al.Cell|June 11, 2013
Structures of Drosophila cryptochrome and mouse cryptochrome1 provide insight into circadian functionAnna Czarna, Alex Berndt, Hari Raj Singh, et al.Oncogene|August 4, 2009
Histone macroH2A isoforms predict the risk of lung cancer recurrenceJ C Sporn, G Kustatscher, T Hothorn, et al.Journal of Molecular Biology|April 25, 1997
Following co-operative formation of secondary and tertiary structure in a single protein moduleJ L Neira, L S Itzhaki, A G Ladurner, et al.Current Biology : CB|July 7, 2007
The chromatin-remodeling factor FACT contributes to centromeric heterochromatin independently of RNAiErwan Lejeune, Miriam Bortfeld, Sharon A White, et al.Biomedicine & Pharmacotherapy = Biomedecine & Pharmacotherapie|December 14, 2004
Cholesteryl ester transfer protein TaqIB polymorphism and its relation to parameters of the insulin resistance syndrome in an Austrian cohortR Weitgasser, G Galvan, L Malaimare, et al.Proceedings of the National Academy of Sciences of the United States of America|February 28, 2009
Combining affinity purification by ADP-ribose-binding macro domains with mass spectrometry to define the mammalian ADP-ribosyl proteomeNadia Dani, Annalisa Stilla, Adriano Marchegiani, et al.European Journal of Neurology|January 27, 2010
Decision-making for and impact of early immunomodulatory treatment: the Austrian Clinically Isolated Syndrome Study (ACISS)F Fazekas, U Baumhackl, T Berger, et al.The EMBO Journal|May 20, 2005
The macro domain is an ADP-ribose binding moduleGeorgios I Karras, Georg Kustatscher, Heeran R Buhecha, et al.Pageof 20