Structure and activity of enzymes that remove histone modifications
- 2 November 2005
- journal article
- review article
- Published by Elsevier in Current Opinion in Structural Biology
- Vol. 15 (6) , 673-680
- https://doi.org/10.1016/j.sbi.2005.10.006
Abstract
No abstract availableKeywords
This publication has 49 references indexed in Scilit:
- An essential role for CoREST in nucleosomal histone 3 lysine 4 demethylationNature, 2005
- Splicing regulates NAD metabolite binding to histone macroH2ANature Structural & Molecular Biology, 2005
- Histone demethylation catalysed by LSD1 is a flavin‐dependent oxidative processFEBS Letters, 2005
- Maintenance of Low Histone Ubiquitylation by Ubp10 Correlates with Telomere-Proximal Sir2 Association and Gene SilencingMolecular Cell, 2005
- H2B Ubiquitin Protease Ubp8 and Sgf11 Constitute a Discrete Functional Module within the Saccharomyces cerevisiae SAGA ComplexMolecular and Cellular Biology, 2005
- Histone Demethylation Mediated by the Nuclear Amine Oxidase Homolog LSD1Cell, 2004
- Crystal Structures of Arginine Deiminase with Covalent Reaction Intermediates: Implications for Catalytic MechanismStructure, 2004
- Molecular Evolution of the Histone Deacetylase Family: Functional Implications of Phylogenetic AnalysisPublished by Elsevier ,2004
- Structure and Substrate Binding Properties of cobB, a Sir2 Homolog Protein Deacetylase from Escherichia coliJournal of Molecular Biology, 2004
- Structure of SET domain proteins: a new twist on histone methylationTrends in Biochemical Sciences, 2003