| Data suggest that SMYD2-mediated estrogen receptor alpha (ERalpha) protein methylation and p300/cAMP response element-binding protein-binding protein-dependent ERalpha acetylation play an important role in the estrogen-induced gene expression profiles. | Regulation of estrogen receptor α by histone methyltransferase SMYD2-mediated protein methylation.
Zhang X, Tanaka K, Yan J, Li J, Peng D, Jiang Y, Yang Z, Barton MC, Wen H, Shi X., Free PMC Article | 01/4/2014 |
| -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. | RB1 methylation by SMYD2 enhances cell cycle progression through an increase of RB1 phosphorylation.
Cho HS, Hayami S, Toyokawa G, Maejima K, Yamane Y, Suzuki T, Dohmae N, Kogure M, Kang D, Neal DE, Ponder BA, Yamaue H, Nakamura Y, Hamamoto R., Free PMC Article | 11/17/2012 |
| Data report the crystal structure of the full-length human Smyd2 in complex with S-adenosyl-L-homocysteine (AdoHcy). | Structure of human lysine methyltransferase Smyd2 reveals insights into the substrate divergence in Smyd proteins.
Xu S, Zhong C, Zhang T, Ding J. | 03/17/2012 |
| 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. | Proteomic analyses of the SMYD family interactomes identify HSP90 as a novel target for SMYD2.
Abu-Farha M, Lanouette S, Elisma F, Tremblay V, Butson J, Figeys D, Couture JF. | 03/17/2012 |
| SMYD2 has a role in specifically recognizing and regulating functions of p53 tumor suppressor through Lys-370 monomethylation | Structure of human SMYD2 protein reveals the basis of p53 tumor suppressor methylation.
Wang L, Li L, Zhang H, Luo X, Dai J, Zhou S, Gu J, Zhu J, Atadja P, Lu C, Li E, Zhao K., Free PMC Article | 01/14/2012 |
| Structural basis of substrate methylation and inhibition of SMYD2 | Structural basis of substrate methylation and inhibition of SMYD2.
Ferguson AD, Larsen NA, Howard T, Pollard H, Green I, Grande C, Cheung T, Garcia-Arenas R, Cowen S, Wu J, Godin R, Chen H, Keen N. | 12/31/2011 |
| Substrate specificity and product analysis studies established SMYD2 as a monomethyltransferase that prefers nonmethylated p53 peptide substrate. | Biochemical characterization of human SET and MYND domain-containing protein 2 methyltransferase.
Wu J, Cheung T, Grande C, Ferguson AD, Zhu X, Theriault K, Code E, Birr C, Keen N, Chen H. | 09/24/2011 |
| SMYD2 gene expression is decreased in both classic and follicular variants of papillary thyroid carcinoma. | Differential expression of a set of genes in follicular and classic variants of papillary thyroid carcinoma.
Igci YZ, Arslan A, Akarsu E, Erkilic S, Igci M, Oztuzcu S, Cengiz B, Gogebakan B, Cakmak EA, Demiryurek AT. | 04/26/2011 |
| RB monomethylation at lysine 860 by SMYD2 provides a direct binding site for L3MBTL1. | Methylation of the retinoblastoma tumor suppressor by SMYD2.
Saddic LA, West LE, Aslanian A, Yates JR 3rd, Rubin SM, Gozani O, Sage J., Free PMC Article | 01/1/2011 |
| SMYD2 plays an important role in tumor cell proliferation through its activation/overexpression and highlight its usefulness as a prognosticator and potential therapeutic target in ESCC. | Overexpression of SMYD2 relates to tumor cell proliferation and malignant outcome of esophageal squamous cell carcinoma.
Komatsu S, Imoto I, Tsuda H, Kozaki KI, Muramatsu T, Shimada Y, Aiko S, Yoshizumi Y, Ichikawa D, Otsuji E, Inazawa J. | 01/21/2010 |
| Observational study of gene-disease association. (HuGE Navigator) | Coeliac disease-associated risk variants in TNFAIP3 and REL implicate altered NF-kappaB signalling.
Trynka G, Zhernakova A, Romanos J, Franke L, Hunt KA, Turner G, Bruinenberg M, Heap GA, Platteel M, Ryan AW, de Kovel C, Holmes GK, Howdle PD, Walters JR, Sanders DS, Mulder CJ, Mearin ML, Verbeek WH, Trimble V, Stevens FM, Kelleher D, Barisani D, Bardella MT, McManus R, van Heel DA, Wijmenga C. | 04/1/2009 |
| The combination of the SMYD2 interactome with the gene expression data suggests that some of the genes regulated by SMYD2 are closely associated with SMYD2-interacting proteins. | The tale of two domains: proteomics and genomics analysis of SMYD2, a new histone methyltransferase.
Abu-Farha M, Lambert JP, Al-Madhoun AS, Elisma F, Skerjanc IS, Figeys D. | 01/21/2010 |