Ontology highlight
ABSTRACT:
SUBMITTER: Yuan Z
PROVIDER: S-EPMC2998079 | biostudies-literature | 2010 Dec
REPOSITORIES: biostudies-literature
Yuan Zhigang Z Peng Lirong L Radhakrishnan Rangasudhagar R Seto Edward E
The Journal of biological chemistry 20101014 50
Histone deacetylase 9 (HDAC9), like most Class II HDACs, catalyzes the removal of acetyl moieties from the ε-amino groups of conserved lysine residues in the N-terminal tail of histones. Biologically, HDAC9 regulates a wide variety of normal and abnormal physiological functions, including cardiac growth, T-regulatory cell function, neuronal disorders, muscle differentiation, development, and cancer. In a biochemical approach to identify non-histone substrates of HDAC9, we found that HDAC9 co-pur ...[more]