SIR2/YDL042C Literature Guide Help

Other names published for SIR2: MAR1, YDL042C

SIR2 - Protein Physical Properties (12)

ReferenceOther Genes Addressed
Bheda P, et al.  (2012) Biotinylation of lysine method identifies acetylated histone H3 lysine 79 in Saccharomyces cerevisiae as a substrate for Sir2. Proc Natl Acad Sci U S A 109(16):E916-25
Tung SY, et al.  (2012) Chromatin affinity-precipitation using a small metabolic molecule: its application to analysis of O-acetyl-ADP-ribose. Cell Mol Life Sci 69(4):641-50
Oppikofer M, et al.  (2011) A dual role of H4K16 acetylation in the establishment of yeast silent chromatin.LID - 10.1038/emboj.2011.170 [doi] EMBO J ()
Du J, et al.  (2009) Investigating the ADP-ribosyltransferase activity of sirtuins with NAD analogues and 32P-NAD. Biochemistry 48(13):2878-90
Martino F, et al.  (2009) Reconstitution of yeast silent chromatin: multiple contact sites and O-AADPR binding load SIR complexes onto nucleosomes in vitro. Mol Cell 33(3):323-34
Sanders BD, et al.  (2009) Identification and characterization of novel sirtuin inhibitor scaffolds. Bioorg Med Chem 17(19):7031-41
Tong L, et al.  (2009) Hydrolase regulates NAD+ metabolites and modulates cellular redox. J Biol Chem 284(17):11256-66
Khan AN and Lewis PN  (2005) Unstructured Conformations Are a Substrate Requirement for the Sir2 Family of NAD-dependent Protein Deacetylases. J Biol Chem 280(43):36073-8
Schmidt MT, et al.  (2004) Coenzyme specificity of Sir2 protein deacetylases: implications for physiological regulation. J Biol Chem 279(38):40122-9
Bedalov A, et al.  (2003) NAD+-dependent deacetylase Hst1p controls biosynthesis and cellular NAD+ levels in Saccharomyces cerevisiae. Mol Cell Biol 23(19):7044-54
Gerber SA, et al.  (2003) Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS. Proc Natl Acad Sci U S A 100(12):6940-5
Ladurner AG, et al.  (2003) Bromodomains mediate an acetyl-histone encoded antisilencing function at heterochromatin boundaries. Mol Cell 11(2):365-76