Efficient demyristoylase activity of SIRT2 revealed by kinetic and structural studies.
about
Emerging therapeutic roles for NAD(+) metabolism in mitochondrial and age-related disordersPotential Modulation of Sirtuins by Oxidative StressThe role of sirtuins in cellular homeostasisA continuous sirtuin activity assay without any coupling to enzymatic or chemical reactions.Fatty acylation of proteins: The long and the short of it.The ɛ-Amino Group of Protein Lysine Residues Is Highly Susceptible to Nonenzymatic Acylation by Several Physiological Acyl-CoA Thioesters.Novel sirtuin inhibitory warheads derived from the N(ε)-acetyl-lysine analog L-2-amino-7-carboxamidoheptanoic acid.Proteomic analysis of fatty-acylated proteins.Investigating the Sensitivity of NAD+-dependent Sirtuin Deacylation Activities to NADHA SIRT2-Selective Inhibitor Promotes c-Myc Oncoprotein Degradation and Exhibits Broad Anticancer Activity.Altered DNA methylation associated with an abnormal liver phenotype in a cattle model with a high incidence of perinatal pathologies.Deacylation Mechanism by SIRT2 Revealed in the 1'-SH-2'-O-Myristoyl Intermediate Structure.Seeding for sirtuins: microseed matrix seeding to obtain crystals of human Sirt3 and Sirt2 suitable for soaking.The Current State of NAD(+) -Dependent Histone Deacetylases (Sirtuins) as Novel Therapeutic Targets.Sirtuins in Skin and Skin Cancers.Human Sirtuin 2 Localization, Transient Interactions, and Impact on the Proteome Point to Its Role in Intracellular Trafficking.An improved fluorogenic assay for SIRT1, SIRT2, and SIRT3.A Fluorescent Probe for Imaging Sirtuin Activity in Living Cells, Based on One-Step Cleavage of the Dabcyl Quencher.SIRT2 Reverses 4-Oxononanoyl Lysine Modification on Histones.Kinetic and Structural Basis for Acyl-Group Selectivity and NAD(+) Dependence in Sirtuin-Catalyzed DeacylationPotent mechanism-based sirtuin-2-selective inhibition by an in situ-generated occupant of the substrate-binding site, "selectivity pocket" and NAD+-binding site.HDAC8 Catalyzes the Hydrolysis of Long Chain Fatty Acyl Lysine.Sirtuin 2 Deficiency Increases Bacterial Phagocytosis by Macrophages and Protects from Chronic Staphylococcal Infection.SIRT2 and lysine fatty acylation regulate the transforming activity of K-Ras4a.Crystal structures of the mitochondrial deacylase Sirtuin 4 reveal isoform-specific acyl recognition and regulation features.SIRT7 Is an RNA-Activated Protein Lysine Deacylase.Thienopyrimidinone Based Sirtuin-2 (SIRT2)-Selective Inhibitors Bind in the Ligand Induced Selectivity Pocket.Development of Activity-Based Chemical Probes for Human Sirtuins.Crystal structures of SIRT3 reveal that the α2-α3 loop and α3-helix affect the interaction with long-chain acyl lysine.New chemical tools for probing activity and inhibition of the NAD+-dependent lysine deacylase sirtuin 2.Lysine benzoylation is a histone mark regulated by SIRT2Identification of a novel small molecule that inhibits deacetylase but not defatty-acylase reaction catalysed by SIRT2Acetylation of Mitochondrial Proteins in the Heart: The Role of SIRT3
P2860
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P2860
Efficient demyristoylase activity of SIRT2 revealed by kinetic and structural studies.
description
2015 nî lūn-bûn
@nan
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
2015年论文
@zh
2015年论文
@zh-cn
name
Efficient demyristoylase activity of SIRT2 revealed by kinetic and structural studies.
@en
Efficient demyristoylase activity of SIRT2 revealed by kinetic and structural studies.
@nl
type
label
Efficient demyristoylase activity of SIRT2 revealed by kinetic and structural studies.
@en
Efficient demyristoylase activity of SIRT2 revealed by kinetic and structural studies.
@nl
prefLabel
Efficient demyristoylase activity of SIRT2 revealed by kinetic and structural studies.
@en
Efficient demyristoylase activity of SIRT2 revealed by kinetic and structural studies.
@nl
P2093
P2860
P356
P1433
P1476
Efficient demyristoylase activity of SIRT2 revealed by kinetic and structural studies
@en
P2093
Pornpun Aramsangtienchai
Yan-Bin Teng
P2860
P2888
P356
10.1038/SREP08529
P407
P50
P577
2015-02-23T00:00:00Z