Published in Sci Rep on February 23, 2015
Kinetic and Structural Basis for Acyl-Group Selectivity and NAD(+) Dependence in Sirtuin-Catalyzed Deacylation. Biochemistry (2015) 1.00
Proteomic analysis of fatty-acylated proteins. Curr Opin Chem Biol (2015) 0.94
A SIRT2-Selective Inhibitor Promotes c-Myc Oncoprotein Degradation and Exhibits Broad Anticancer Activity. Cancer Cell (2016) 0.88
HDAC8 Catalyzes the Hydrolysis of Long Chain Fatty Acyl Lysine. ACS Chem Biol (2016) 0.82
Investigating the Sensitivity of NAD+-dependent Sirtuin Deacylation Activities to NADH. J Biol Chem (2016) 0.82
Fatty acylation of proteins: The long and the short of it. Prog Lipid Res (2016) 0.81
Potential Modulation of Sirtuins by Oxidative Stress. Oxid Med Cell Longev (2015) 0.81
SIRT2 Reverses 4-Oxononanoyl Lysine Modification on Histones. J Am Chem Soc (2016) 0.78
Seeding for sirtuins: microseed matrix seeding to obtain crystals of human Sirt3 and Sirt2 suitable for soaking. Acta Crystallogr F Struct Biol Commun (2015) 0.77
The role of sirtuins in cellular homeostasis. J Physiol Biochem (2016) 0.77
A continuous sirtuin activity assay without any coupling to enzymatic or chemical reactions. Sci Rep (2016) 0.77
Emerging therapeutic roles for NAD(+) metabolism in mitochondrial and age-related disorders. Clin Transl Med (2016) 0.77
An improved fluorogenic assay for SIRT1, SIRT2, and SIRT3. Org Biomol Chem (2016) 0.76
Altered DNA methylation associated with an abnormal liver phenotype in a cattle model with a high incidence of perinatal pathologies. Sci Rep (2016) 0.75
Human Sirtuin 2 Localization, Transient Interactions, and Impact on the Proteome Point to Its Role in Intracellular Trafficking. Mol Cell Proteomics (2016) 0.75
SIRT7 Is an RNA-Activated Protein Lysine Deacylase. ACS Chem Biol (2016) 0.75
A Fluorescent Probe for Imaging Sirtuin Activity in Living Cells, Based on One-Step Cleavage of the Dabcyl Quencher. Chembiochem (2016) 0.75
Deacylation Mechanism by SIRT2 Revealed in the 1'-SH-2'-O-Myristoyl Intermediate Structure. Cell Chem Biol (2017) 0.75
Potent mechanism-based sirtuin-2-selective inhibition by an in situ-generated occupant of the substrate-binding site, "selectivity pocket" and NAD(+)-binding site. Chem Sci (2017) 0.75
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Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem Biophys Res Commun (2000) 9.09
Mammalian sirtuins: biological insights and disease relevance. Annu Rev Pathol (2010) 8.55
The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. Mol Cell (2003) 8.34
Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins. Mol Biol Cell (2005) 6.79
Sirtuins as regulators of metabolism and healthspan. Nat Rev Mol Cell Biol (2012) 4.86
CBP/p300-mediated acetylation of histone H3 on lysine 56. Nature (2009) 4.83
Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase. Science (2011) 4.16
SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosis. Genes Dev (2006) 3.12
Ten years of NAD-dependent SIR2 family deacetylases: implications for metabolic diseases. Trends Pharmacol Sci (2010) 3.05
Identification of lysine succinylation as a new post-translational modification. Nat Chem Biol (2010) 2.87
The first identification of lysine malonylation substrates and its regulatory enzyme. Mol Cell Proteomics (2011) 2.83
Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome. Mol Cell (2012) 2.54
SIRT6 regulates TNF-α secretion through hydrolysis of long-chain fatty acyl lysine. Nature (2013) 2.52
SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways. Mol Cell (2013) 2.17
Protein lipidation. FEBS J (2007) 2.10
Activation of the protein deacetylase SIRT6 by long-chain fatty acids and widespread deacylation by mammalian sirtuins. J Biol Chem (2013) 2.03
Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways. Proc Natl Acad Sci U S A (2013) 2.01
Structure of a Sir2 enzyme bound to an acetylated p53 peptide. Mol Cell (2002) 2.00
SIRT5 regulates the mitochondrial lysine succinylome and metabolic networks. Cell Metab (2013) 1.70
Crystal structures of human SIRT3 displaying substrate-induced conformational changes. J Biol Chem (2009) 1.60
Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways. Mol Cell Proteomics (2012) 1.54
Plasmodium falciparum Sir2A preferentially hydrolyzes medium and long chain fatty acyl lysine. ACS Chem Biol (2011) 1.33
The tumor suppressor SirT2 regulates cell cycle progression and genome stability by modulating the mitotic deposition of H4K20 methylation. Genes Dev (2013) 1.29
Lysine-5 acetylation negatively regulates lactate dehydrogenase A and is decreased in pancreatic cancer. Cancer Cell (2013) 1.29
Identification of lysine succinylation substrates and the succinylation regulatory enzyme CobB in Escherichia coli. Mol Cell Proteomics (2013) 1.17
SIRT2 induces the checkpoint kinase BubR1 to increase lifespan. EMBO J (2014) 1.06
Structural and functional analysis of human SIRT1. J Mol Biol (2013) 1.01
Integrative chemical biology approaches for identification and characterization of "erasers" for fatty-acid-acylated lysine residues within proteins. Angew Chem Int Ed Engl (2014) 0.89
Thiomyristoyl peptides as cell-permeable Sirt6 inhibitors. Org Biomol Chem (2014) 0.87
SIRT2 regulates tumour hypoxia response by promoting HIF-1α hydroxylation. Oncogene (2014) 0.84