A methylation and phosphorylation switch between an adjacent lysine and serine determines human DNMT1 stability

Nature Structural and Molecular Biology

Volumn 18, Issue 1, 2011, Pages 42-49

  Estéve, Pierre Olivier ^a   Chang, Yanqi ^b   Samaranayake, Mala ^a   Upadhyay, Anup K ^b   Horton, John R ^b   Feehery, George R ^a   Cheng, Xiaodong ^b   Pradhan, Sriharsa ^a  

^a NEW ENGLAND BIOLABS   (United States)

^b EMORY UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DNA METHYLTRANSFERASE 1; LYSINE; PROTEIN KINASE B; PROTEIN METHYLTRANSFERASE; SERINE;

ARTICLE; CONTROLLED STUDY; DNA METHYLATION; DNA SYNTHESIS; ENZYME MODIFICATION; ENZYME PHOSPHORYLATION; ENZYME STABILITY; GENE OVEREXPRESSION; HUMAN; HUMAN CELL; MAMMAL CELL; PRIORITY JOURNAL; PROTEIN METHYLATION; STRUCTURE ANALYSIS;

CRYSTALLOGRAPHY, X-RAY; DNA (CYTOSINE-5-)-METHYLTRANSFERASE; DNA METHYLATION; GENOME, HUMAN; HISTONE-LYSINE N-METHYLTRANSFERASE; HUMANS; LYSINE; METHYLATION; MODELS, MOLECULAR; PHOSPHORYLATION; PROTEIN STABILITY; PROTEIN STRUCTURE, TERTIARY; PROTO-ONCOGENE PROTEINS C-AKT; SERINE;

MAMMALIA;

EID: 78650981194     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.1939     Document Type: Article

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