22 Papers
87 Citations
Ragna Sack is an academic researcher from Friedrich Miescher Institute for Biomedical Research. The author has contributed to research in topics: Chromatin & Histone methyltransferase. The author has an hindex of 17, co-authored 22 publications.
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Papers
Histone Methylation by PRC2 Is Inhibited by Active Chromatin Marks
Frank W. Schmitges,Archana B. Prusty,Mahamadou Faty,Alexandra Stützer,Gondichatnahalli M. Lingaraju,Jonathan Aiwazian,Ragna Sack,Daniel Hess,Ling Li,Shaolian Zhou,Richard D. Bunker,Urs Wirth,Tewis Bouwmeester,Andreas Bauer,Nga Ly-Hartig,Kehao Zhao,Ho Man Chan,Justin Gu,Heinz Gut,Wolfgang Fischle,Jürg Müller,Nicolas H. Thomä +21 more
TL;DR: It is found that H3K4me3 inhibits PRC2 activity in an allosteric fashion assisted by the Su(z)12 C terminus, which provides the molecular basis of histone H3 N terminus recognition by thePRC2 Nurf55-Su( z)12 submodule.
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The mammalian TRIM-NHL protein TRIM71/LIN-41 is a repressor of mRNA function.
TL;DR: The results reveal strong similarities between TRIM71 and Drosophila BRAT, the best-studied TRIM-NHL protein and a well-documented translational repressor, suggesting that BRAT and TRIM 71 are part of a family of mRNA repressors regulating proliferation and differentiation.
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DNA methylation and normal chromosome behavior in Neurospora depend on five components of a histone methyltransferase complex, DCDC.
Zachary A. Lewis,Keyur K. Adhvaryu,Shinji Honda,Anthony L. Shiver,Marijn Knip,Ragna Sack,Eric U. Selker +6 more
TL;DR: Data support a two-step mechanism for H3K9 methylation in Neurospora crassa, and revealed DCDC, a previously unknown protein complex including DIM-5, D IM-7,DIM-9, CUL4, and DDB1, which forms multiple complexes with distinct functions.
Direct protein-protein interaction of 11β-hydroxysteroid dehydrogenase type 1 and hexose-6-phosphate dehydrogenase in the endoplasmic reticulum lumen
Atanas G. Atanasov,Lyubomir G. Nashev,Laurent Gelman,Balázs Legeza,Ragna Sack,Reto Portmann,Alex Odermatt +6 more
TL;DR: Using three different methods, strong evidence is provided that the functional coupling between 11beta-HSD1 and H6PDH involves a direct physical interaction of the two proteins.
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Absolute Quantification of Histone PTM Marks by MRM-Based LC-MS/MS
Jun Gao,Rijing Liao,Yanyan Yu,Huili Zhai,Yingqi Wang,Ragna Sack,Antoine H.F.M. Peters,Antoine H.F.M. Peters,Jiajia Chen,Haiping Wu,Zheng Huang,Min Hu,Wei Qi,Chris Lu,Peter Atadja,Counde Oyang,En Li,Wei Yi,Shaolian Zhou +18 more
TL;DR: This method has been used to study translocated NSD2 (a histone lysine methyltransferase that catalyzes the histoneLysine 36 methylation) function with its overexpression in KMS11 multiple myeloma cells and successfully quantitated both individual and combinatorial histone marks.
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