Structural and enzymatic evidence for the methylation of the ACK1 tyrosine kinase by the histone lysine methyltransferase SETD2
Author:
Funder
Université de Paris
ANR
Institut Pasteur
Centre National de la Recherche Scientifique
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference33 articles.
1. Set2 methylation of histone H3 lysine 36 suppresses histone exchange on transcribed genes;Venkatesh;Nature,2012
2. Histone lysine methyltransferases in biology and disease;Husmann;Nat. Struct. Mol. Biol.,2019
3. SETD2 is required for DNA double-strand break repair and activation of the p53-mediated checkpoint;Carvalho;Elife,2014
4. Identification of functional cooperative mutations of SETD2 in human acute leukemia;Zhu;Nat. Genet.,2014
5. Structure/function analysis of recurrent mutations in SETD2 protein reveals a critical and conserved role for a SET domain residue in maintaining protein stability and histone H3 lys-36 trimethylation;Hacker;J. Biol. Chem.,2016
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