The SET-domain protein superfamily: protein lysine methyltransferases
By Shane C. Dillon, Xing Zhang, R. Trievel, Xiaodong Cheng. Genome Biology, 2005
761 citations recorded by the source corpus.
The SET-domain protein methyltransferase superfamily includes all but one of the proteins known to methylate histones on lysine. Histone methylation is important in the regulation of chromatin and gene expression.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/31752a87c61cd02c74ea7b940bfa9dba3bd51cbb
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Molecular Biology
- V. Richon
- R. Pollock
- M. Scott
- J. Simon
- Inanç Birol
- Marco A. Marra
- Jacqueline E. Schein
- Sohrab P. Shah
Citations in the corpus
- Histone Lysine Methylation Dynamics: Establishment, Regulation, and Biological Impact (2012, neutral): “This became known as the F/Y switch, which is important for determining the specificity and extent of lysine methylation (Dillon et al., 2005).”
- Regulation of nucleosome dynamics by histone modifications (2013, neutral): “Many histone methyltransferases are proposed to act in a processive fashion—that is, a single methyltransferase performs multiple rounds of methylation on a single residue 51,52 .”
- Coordinated activities of wild-type plus mutant EZH2 drive tumor-associated hypertrimethylation of lysine 27 on histone H3 (H3K27) in human B-cell lymphomas (2010, background): “For example, when tyrosine 245 of recombinant SET7/9 wasmutated to alanine, a change in substrate specificity, similar to what is reported here for EZH2 Y641 mutations, was observed (19).”
- Somatic mutation of EZH2 (Y641) in Follicular and Diffuse Large B-cell Lymphomas of Germinal Center Origin (2010, positive): “Our model indicates that Tyr641 interacts with the lysine 27 side chain of the H3 histone tail, as has been suggested in other SET domain protein”
- Roles of the EZH2 histone methyltransferase in cancer epigenetics. (2008, background): “Structure determinations of ther SET domains have revealed an unusual “thread-the-needle” tructure, called a pseudoknot ([18,19] for reviews).”