HST2/YPL015C Literature Guide Help

Other names published for HST2: YPL015C

HST2 - Protein Physical Properties (6)

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
Sanders BD, et al.  (2009) Identification and characterization of novel sirtuin inhibitor scaffolds. Bioorg Med Chem 17(19):7031-41
Khan AN and Lewis PN  (2006) Use of substrate analogs and mutagenesis to study substrate binding and catalysis in the Sir2 family of NAD-dependent protein deacetylases. J Biol Chem 281(17):11702-11
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