Human DNMT1 transition state structure.
Du, Quan; Wang, Zhen; Schramm, Vern L.
Proc Natl Acad Sci U S A
; 113(11): 2916-21, 2016 Mar 15.
Artigo em Inglês | MEDLINE | ID: mdl-26929335
Structure of the Dnmt1 Reader Module Complexed with a Unique Two-Mono-Ubiquitin Mark on Histone H3 Reveals the Basis for DNA Methylation Maintenance.
Rational Manipulation of DNA Methylation by Using Isotopically Reinforced Cytosine.
Electrochemical assay for the signal-on detection of human DNA methyltransferase activity.
[Dnmt2 is the Most Evolutionary Conserved and Enigmatic Cytosine DNA Methyltransferase in Eukaryotes].
Allosteric control of mammalian DNA methyltransferases - a new regulatory paradigm.
Targeted mutagenesis results in an activation of DNA methyltransferase 1 and confirms an autoinhibitory role of its RFTS domain.
Flexible double-headed cytosine-linked 2'-deoxycytidine nucleotides. Synthesis, polymerase incorporation to DNA and interaction with DNA methyltransferases.
Dual binding of chromomethylase domains to H3K9me2-containing nucleosomes directs DNA methylation in plants.
De novo DNA methyltransferase DNMT3A: Regulation of oligomeric state and mechanism of action in response to pH changes.
Structural insight into autoinhibition and histone H3-induced activation of DNMT3A.