Mechanism of histone methylation catalyzed by protein lysine methyltransferase SET7/9 and origin of product specificity.
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Epigenetic modifications and diabetic retinopathyModeling a new water channel that allows SET9 to dimethylate p53Structural origins for the product specificity of SET domain protein methyltransferasesSET7/9 Catalytic Mutants Reveal the Role of Active Site Water Molecules in Lysine Multiple MethylationStructural and biochemical studies of human lysine methyltransferase Smyd3 reveal the important functional roles of its post-SET and TPR domains and the regulation of its activity by DNA bindingCatalytic and functional roles of conserved amino acids in the SET domain of the S. cerevisiae lysine methyltransferase Set1Molecular basis for histone N-terminal methylation by NRMT1Facile synthesis of SAM-peptide conjugates through alkyl linkers targeting protein N-terminal methyltransferase 1QM/MM MD and free energy simulations of G9a-like protein (GLP) and its mutants: understanding the factors that determine the product specificityEpigenetic modifications of Keap1 regulate its interaction with the protective factor Nrf2 in the development of diabetic retinopathyDirect evidence for methyl group coordination by carbon-oxygen hydrogen bonds in the lysine methyltransferase SET7/9N-methylation of the amide bond by methyltransferase asm10 in ansamitocin biosynthesisA direct label-free MALDI-TOF mass spectrometry based assay for the characterization of inhibitors of protein lysine methyltransferases.Enzymatic mechanism and product specificity of SET-domain protein lysine methyltransferasesHow do SET-domain protein lysine methyltransferases achieve the methylation state specificity? Revisited by Ab initio QM/MM molecular dynamics simulations.Chemical mechanisms of histone lysine and arginine modificationsDirect interaction between the inhibitor 2 and ceramide via sphingolipid-protein binding is involved in the regulation of protein phosphatase 2A activity and signalingSphingolipids and cancer: ceramide and sphingosine-1-phosphate in the regulation of cell death and drug resistance.Structural Chemistry of Human SET Domain Protein Methyltransferases.The promise and failures of epigenetic therapies for cancer treatmentRegulatory variation: an emerging vantage point for cancer biology.QM/MM MD and free energy simulation study of methyl transfer processes catalyzed by PKMTs and PRMTs.Role of histone modifications and DNA methylation in the regulation of O6-methylguanine-DNA methyltransferase gene expression in human stomach cancer cells.Hyperoxia-induced methylation decreases RUNX3 in a newborn rat model of bronchopulmonary dysplasiaLysine Possesses the Optimal Chain Length for Histone Lysine Methyltransferase Catalysis.Molecular basis for histidine N1 position-specific methylation by CARNMT1.QM/MM free energy Simulations of an efficient Gluten Hydrolase (Kuma030) Implicate for a Reactant-State Based Protein-Design Strategy for General Acid/Base Catalysis.QM/MM-Methoden für biomolekulare Systeme
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P2860
Mechanism of histone methylation catalyzed by protein lysine methyltransferase SET7/9 and origin of product specificity.
description
2007 nî lūn-bûn
@nan
2007年の論文
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2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
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2007年论文
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2007年论文
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name
Mechanism of histone methylati ...... origin of product specificity.
@ast
Mechanism of histone methylati ...... origin of product specificity.
@en
type
label
Mechanism of histone methylati ...... origin of product specificity.
@ast
Mechanism of histone methylati ...... origin of product specificity.
@en
prefLabel
Mechanism of histone methylati ...... origin of product specificity.
@ast
Mechanism of histone methylati ...... origin of product specificity.
@en
P2860
P356
P1476
Mechanism of histone methylati ...... origin of product specificity.
@en
P2093
P2860
P304
P356
10.1073/PNAS.0702981104
P407
P577
2007-05-15T00:00:00Z