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  • Comprehensive Analysis of t... Comprehensive Analysis of the Human SH3 Domain Family Reveals a Wide Variety of Non-canonical Specificities
    Teyra, Joan; Huang, Haiming; Jain, Shobhit ... Structure, 10/2017, Volume: 25, Issue: 10
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    SH3 domains are protein modules that mediate protein-protein interactions in many eukaryotic signal transduction pathways. The majority of SH3 domains studied thus far act by binding to proline-rich ...
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2.
  • The structural basis for se... The structural basis for selective binding of non-methylated CpG islands by the CFP1 CXXC domain
    Min, Jinrong; Xu, Chao; Bian, Chuanbing ... Nature communications, 03/2011, Volume: 2, Issue: 1
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    CFP1 is a CXXC domain-containing protein and an essential component of the SETD1 histone H3K4 methyltransferase complex. CXXC domain proteins direct different chromatin-modifying activities to ...
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  • Structure and Biochemical F... Structure and Biochemical Functions of SIRT6
    Pan, Patricia W.; Feldman, Jessica L.; Devries, Mark K. ... Journal of biological chemistry/˜The œJournal of biological chemistry, 04/2011, Volume: 286, Issue: 16
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    SIRT6 is a member of the evolutionarily conserved sirtuin family of NAD+-dependent protein deacetylases and functions in genomic stability and transcriptional control of glucose metabolism. Early ...
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4.
  • Structural insights into tr... Structural insights into trans-histone regulation of H3K4 methylation by unique histone H4 binding of MLL3/4
    Liu, Yanli; Qin, Su; Chen, Tsai-Yu ... Nature communications, 01/2019, Volume: 10, Issue: 1
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    MLL3 and MLL4 are two closely related members of the SET1/MLL family of histone H3K4 methyltransferases and are responsible for monomethylating histone H3K4 on enhancers, which are essential in ...
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  • Structure of the catalytic ... Structure of the catalytic domain of EZH2 reveals conformational plasticity in cofactor and substrate binding sites and explains oncogenic mutations
    Wu, Hong; Zeng, Hong; Dong, Aiping ... PloS one, 12/2013, Volume: 8, Issue: 12
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    Polycomb repressive complex 2 (PRC2) is an important regulator of cellular differentiation and cell type identity. Overexpression or activating mutations of EZH2, the catalytic component of the PRC2 ...
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  • Discovery of Potent and Sel... Discovery of Potent and Selective Inhibitors for G9a-Like Protein (GLP) Lysine Methyltransferase
    Xiong, Yan; Li, Fengling; Babault, Nicolas ... Journal of medicinal chemistry, 03/2017, Volume: 60, Issue: 5
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    G9a-like protein (GLP) and G9a are highly homologous protein lysine methyltransferases (PKMTs) sharing approximately 80% sequence identity in their catalytic domains. GLP and G9a form a heterodimer ...
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  • A chemical probe selectivel... A chemical probe selectively inhibits G9a and GLP methyltransferase activity in cells
    Vedadi, Masoud; Barsyte-Lovejoy, Dalia; Liu, Feng ... Nature chemical biology, 07/2011, Volume: 7, Issue: 8
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    Protein lysine methyltransferases G9a and GLP modulate the transcriptional repression of a variety of genes via dimethylation of Lys9 on histone H3 (H3K9me2) as well as dimethylation of non-histone ...
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  • (R)-PFI-2 is a potent and s... (R)-PFI-2 is a potent and selective inhibitor of SETD7 methyltransferase activity in cells
    Barsyte-Lovejoy, Dalia; Li, Fengling; Oudhoff, Menno J. ... Proceedings of the National Academy of Sciences - PNAS, 09/2014, Volume: 111, Issue: 35
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    SET domain containing (lysine methyltransferase) 7 (SETD7) is implicated in multiple signaling and disease related pathways with a broad diversity of reported substrates. Here, we report the ...
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  • TP-064, a potent and select... TP-064, a potent and selective small molecule inhibitor of PRMT4 for multiple myeloma
    Nakayama, Kazuhide; Szewczyk, Magdalena M; Dela Sena, Carlo ... Oncotarget, 04/2018, Volume: 9, Issue: 26
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    Protein arginine methyltransferase (PRMT) 4 (also known as coactivator-associated arginine methyltransferase 1; CARM1) is involved in a variety of biological processes and is considered as a ...
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  • Structural basis for the regulatory role of the PPxY motifs in the thioredoxin-interacting protein TXNIP
    Liu, Yanli; Lau, Johnathan; Li, Weiguo ... Biochemical journal, 01/2016, Volume: 473, Issue: 2
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    TXNIP (thioredoxin-interacting protein) negatively regulates the antioxidative activity of thioredoxin and participates in pleiotropic cellular processes. Its deregulation is linked to various human ...
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