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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

SET and MYND domain containing 2

SMYD2, KMT3C, SET and MYND domain-containing protein-2
SET domain-containing proteins, such as SMYD2, catalyze lysine methylation (Brown et al., 2006 [PubMed 16805913]).[supplied by OMIM, Nov 2008] (from NCBI)
Top mentioned proteins: Histone, SET, p53, CAN, SMYD3
Papers on SMYD2
Quantitative profiling of the activity of protein lysine methyltransferase SMYD2 using SILAC-based proteomics.
Nguyen et al., United States. In Mol Cell Proteomics, Feb 2016
UNASSIGNED: The significance of non-histone lysine methylation in cell biology and human disease is an emerging area of research exploration, and the development of small molecule inhibitors that selectively and potently target enzymes that catalyze the addition of methyl-groups to lysine residues, such as the protein lysine mono-methyltransferase SMYD2, is an active area of drug discovery.
Purification of Histone Lysine Methyltransferase SMYD2 and Co-Crystallization with a Target Peptide from Estrogen Receptor α.
Yang et al., Detroit, United States. In Methods Mol Biol, Dec 2015
Methylation of estrogen receptor α by the histone lysine methyltransferase SMYD2 regulates ERα chromatin recruitment and its target gene expression.
Expression of histone methyltransferases as novel biomarkers for renal cell tumor diagnosis and prognostication.
Jerónimo et al., Porto, Portugal. In Epigenetics, Dec 2015
We found that the expression levels of 3 genes-SMYD2, SETD3, and NO66-was significantly altered in a set of RCTs, which was further validated in a large independent cohort.
Discovery of A-893, A New Cell-Active Benzoxazinone Inhibitor of Lysine Methyltransferase SMYD2.
Pappano et al., North Chicago, United States. In Acs Med Chem Lett, Jul 2015
A lack of useful small molecule tools has precluded thorough interrogation of the biological function of SMYD2, a lysine methyltransferase with known tumor-suppressor substrates.
LLY-507, a Cell-active, Potent, and Selective Inhibitor of Protein-lysine Methyltransferase SMYD2.
Vedadi et al., Toronto, Canada. In J Biol Chem, Jun 2015
SMYD2 is a lysine methyltransferase that catalyzes the monomethylation of several protein substrates including p53.
Dysregulation of AKT Pathway by SMYD2-Mediated Lysine Methylation on PTEN.
Hamamoto et al., Chicago, United States. In Neoplasia, Apr 2015
In this study, we demonstrated that the oncogenic protein lysine methyltransferase SET and MYND domain containing 2 (SMYD2) methylates PTEN at lysine 313 in vitro and in vivo.
The histone methyltransferase Smyd2 is a negative regulator of macrophage activation by suppressing interleukin 6 (IL-6) and tumor necrosis factor α (TNF-α) production.
Zheng et al., Suzhou, China. In J Biol Chem, Mar 2015
SET and MYND domain-containing 2 (Smyd2), a histone 3 lysine 4- and histone 3 lysine 36 (H3K36)-specific methyltransferase, plays critical roles in cardiac development and tumorigenesis.
A new test of computational protein design: predicting posttranslational modification specificity for the enzyme SMYD2.
Reynolds, Dallas, United States. In Structure, Feb 2015
In this issue of Structure, Lanouette and colleagues use a combination of computation and experiment to define a specificity motif for the lysine methyltransferase SMYD2.
Molecular Dynamics Simulation Reveals Correlated Inter-Lobe Motion in Protein Lysine Methyltransferase SMYD2.
Yang et al., Hat Yai, Thailand. In Plos One, 2014
Here we use the molecular dynamics simulation to investigate the still-poorly-understood SMYD2 dynamics.
BALL-SNP: combining genetic and structural information to identify candidate non-synonymous single nucleotide polymorphisms.
Keller et al., Saarbrücken, Germany. In Genome Med, 2014
Here, the analysis highlighted accumulation of variations in the genes JUP, VCL, and SMYD2.
Evolutionary History of the Smyd Gene Family in Metazoans: A Framework to Identify the Orthologs of Human Smyd Genes in Drosophila and Other Animal Species.
Galindo et al., Valencia, Spain. In Plos One, 2014
We have performed a phylogenetic analysis of Smyd protein sequences, and our results show that the extant metazoan Smyd genes can be classified in three main classes, Smyd3 (which includes chordate-specific Smyd1 and Smyd2 genes), Smyd4 and Smyd5.
SMYD proteins: key regulators in skeletal and cardiac muscle development and function.
Zhang et al., Baltimore, United States. In Anat Rec (hoboken), 2014
The Smyd family consists of five members including Smyd1, Smyd2, Smyd3, Smyd4, and Smyd5.
RB1 methylation by SMYD2 enhances cell cycle progression through an increase of RB1 phosphorylation.
Hamamoto et al., Tokyo, Japan. In Neoplasia, 2012
-dependent RB1 methylation at lysine 810 promotes cell cycle progression of cancer cells. Further study may explore SMYD2-dependent RB1 methylation as a potential therapeutic target in human cancer.
Structure of human SMYD2 protein reveals the basis of p53 tumor suppressor methylation.
Zhao et al., Shanghai, China. In J Biol Chem, 2011
SMYD2 has a role in specifically recognizing and regulating functions of p53 tumor suppressor through Lys-370 monomethylation
Structure of human lysine methyltransferase Smyd2 reveals insights into the substrate divergence in Smyd proteins.
Ding et al., Shanghai, China. In J Mol Cell Biol, 2011
Data report the crystal structure of the full-length human Smyd2 in complex with S-adenosyl-L-homocysteine (AdoHcy).
Proteomic analyses of the SMYD family interactomes identify HSP90 as a novel target for SMYD2.
Couture et al., Ottawa, Canada. In J Mol Cell Biol, 2011
Data highlights the ability of SMYD proteins to form unique protein complexes that may underlie their various biological functions and the SMYD2-mediated methylation of the key molecular chaperone HSP90.
Structural basis of substrate methylation and inhibition of SMYD2.
Keen et al., Waltham, United States. In Structure, 2011
Structural basis of substrate methylation and inhibition of SMYD2
Protein methylation: a new mechanism of p53 tumor suppressor regulation.
Chen et al., Davis, United States. In Histol Histopathol, 2008
Indeed, histone lysine methyltransferases KMT5 (Set9), KMT3C (Smyd2), and KMT5A (Set8) methylate p53 at specific C-terminal lysines.
p53 is regulated by the lysine demethylase LSD1.
Berger et al., Philadelphia, United States. In Nature, 2007
We find that, in vitro, LSD1 removes both monomethylation (K370me1) and dimethylation (K370me2) at K370, a previously identified Smyd2-dependent monomethylation site.
Repression of p53 activity by Smyd2-mediated methylation.
Berger et al., Philadelphia, United States. In Nature, 2006
results show that Smyd2 negatively regulates p53-responsive genes in a p53-dependent manner
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