The chemical biology of sirtuins

Developing diazirine-based chemical probes to identify histone modification ‘readers’ and ‘erasers’

(2015) Tangpo Yang et al.   Chemical Science

Selective Sirt2 inhibition by ligand-induced rearrangement of the active site

(2015) Tobias Rumpf et al.   Nature Communications

Integrative Chemical Biology Approaches for Identification and Characterization of “Erasers” for Fatty-Acid-Acylated Lysine Residues within Proteins

(2014) Zheng Liu et al.   ANGEWANDTE CHEMIE-INTERNATIONAL EDITION

A SIRT7-Dependent Acetylation Switch of GABPβ1 Controls Mitochondrial Function

(2014) Dongryeol Ryu et al.   Cell Metabolism

Lysine Glutarylation Is a Protein Posttranslational Modification Regulated by SIRT5

(2014) Minjia Tan et al.   Cell Metabolism

Chemical Biology Strategies for Posttranslational Control of Protein Function

(2014) Rishi Rakhit et al.   CHEMISTRY & BIOLOGY

Sirtuin inhibitors as anticancer agents

(2014) Jing Hu et al.   Future Medicinal Chemistry

Discovery of Potent and Selective Sirtuin 2 (SIRT2) Inhibitors Using a Fragment-Based Approach

(2014) Huaqing Cui et al.   JOURNAL OF MEDICINAL CHEMISTRY

Nonenzymatic Protein Acylation as a Carbon Stress Regulated by Sirtuin Deacylases

(2014) Gregory R. Wagner et al.   MOLECULAR CELL

The growing landscape of lysine acetylation links metabolism and cell signalling

(2014) Chunaram Choudhary et al.   NATURE REVIEWS MOLECULAR CELL BIOLOGY

A succinyl lysine-based photo-cross-linking peptide probe for Sirtuin 5

(2014) Karunakaran A. Kalesh et al.   ORGANIC & BIOMOLECULAR CHEMISTRY

Thiomyristoyl peptides as cell-permeable Sirt6 inhibitors

(2014) Bin He et al.   ORGANIC & BIOMOLECULAR CHEMISTRY

SIRT1 and other sirtuins in metabolism

(2014) Hung-Chun Chang et al.   TRENDS IN ENDOCRINOLOGY AND METABOLISM

Erasers of Histone Acetylation: The Histone Deacetylase Enzymes

(2014) E. Seto et al.   Cold Spring Harbor Perspectives in Biology

Identification of ‘erasers’ for lysine crotonylated histone marks using a chemical proteomics approach

(2014) Xiucong Bao et al.   eLife

Are sirtuin deacylase enzymes important modulators of mitochondrial energy metabolism?

(2013) Brenna Osborne et al.   BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS

Genealogy of an ancient protein family: the Sirtuins, a family of disordered members

(2013) Susan Costantini et al.   BMC EVOLUTIONARY BIOLOGY

An Update on Lysine Deacylases Targeting the Expanding “Acylome”

(2013) Christian A. Olsen   ChemMedChem

Widespread and Enzyme-independentNϵ-Acetylation andNϵ-Succinylation of Proteins in the Chemical Conditions of the Mitochondrial Matrix

(2013) Gregory R. Wagner et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Discovery of Thieno[3,2-d]pyrimidine-6-carboxamides as Potent Inhibitors of SIRT1, SIRT2, and SIRT3

(2013) Jeremy S. Disch et al.   JOURNAL OF MEDICINAL CHEMISTRY

The 2.5 Å Crystal Structure of the SIRT1 Catalytic Domain Bound to Nicotinamide Adenine Dinucleotide (NAD+) and an Indole (EX527 Analogue) Reveals a Novel Mechanism of Histone Deacetylase Inhibition

(2013) Xun Zhao et al.   JOURNAL OF MEDICINAL CHEMISTRY

SIRT4 Coordinates the Balance between Lipid Synthesis and Catabolism by Repressing Malonyl CoA Decarboxylase

(2013) Gaëlle Laurent et al.   MOLECULAR CELL

Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli

(2013) Brian T. Weinert et al.   MOLECULAR CELL

SIRT6 regulates TNF-α secretion through hydrolysis of long-chain fatty acyl lysine

(2013) Hong Jiang et al.   NATURE

Sorting out functions of sirtuins in cancer

(2013) M Roth et al.   ONCOGENE

Evidence for a Common Mechanism of SIRT1 Regulation by Allosteric Activators

(2013) B. P. Hubbard et al.   SCIENCE

Sirtuins in neurodegenerative diseases: an update on potential mechanisms

(2013) Sang-Won Min et al.   Frontiers in Aging Neuroscience

Quantitative Analysis of Histone Modifications: Formaldehyde Is a Source of Pathological N6-Formyllysine That Is Refractory to Histone Deacetylases

(2013) Bahar Edrissi et al.   PLoS Genetics

Sirtuin activators and inhibitors

(2012) José M. Villalba et al.   BIOFACTORS

Sirtuins: NAD+-dependent deacetylase mechanism and regulation

(2012) Anthony A Sauve et al.   CURRENT OPINION IN CHEMICAL BIOLOGY

Sirtuins as emerging anti-parasitic targets

(2012) Weiping Zheng   EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY

Sirtuin Catalysis and Regulation

(2012) Jessica L. Feldman et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Structural Basis for Sirtuin Activity and Inhibition

(2012) Hua Yuan et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

The Bicyclic Intermediate Structure Provides Insights into the Desuccinylation Mechanism of Human Sirtuin 5 (SIRT5)

(2012) Yeyun Zhou et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Azalysine Analogues as Probes for Protein Lysine Deacetylation and Demethylation

(2012) Blair C. R. Dancy et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Mechanism-based Modulator Discovery for Sirtuin-catalyzed Deacetylation Reaction

(2012) Weiping Zheng   MINI-REVIEWS IN MEDICINAL CHEMISTRY

Sirtuin 1 and Sirtuin 3: Physiological Modulators of Metabolism

(2012) Ruben Nogueiras et al.   PHYSIOLOGICAL REVIEWS

Plasmodium falciparum Sir2A Preferentially Hydrolyzes Medium and Long Chain Fatty Acyl Lysine

(2011) Anita Y. Zhu et al.   ACS Chemical Biology

A Direct Method for Site-Specific Protein Acetylation

(2011) Fupeng Li et al.   ANGEWANDTE CHEMIE-INTERNATIONAL EDITION

Medicinal Chemistry of Sirtuin Inhibitors

(2011) L. Chen   CURRENT MEDICINAL CHEMISTRY

SIRT1 Contains N- and C-terminal Regions That Potentiate Deacetylase Activity

(2011) Min Pan et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

The First Identification of Lysine Malonylation Substrates and Its Regulatory Enzyme

(2011) Chao Peng et al.   MOLECULAR & CELLULAR PROTEOMICS

Peptide Switch Is Essential for Sirt1 Deacetylase Activity

(2011) Hyeog Kang et al.   MOLECULAR CELL

Sirt5 Is a NAD-Dependent Protein Lysine Demalonylase and Desuccinylase

(2011) J. Du et al.   SCIENCE

Potent sirtuin inhibition bestowed by l-2-amino-7-carboxamidoheptanoic acid (l-ACAH), a Nε-acetyl-lysine analog

(2011) Brett M. Hirsch et al.   MedChemComm

SIRT3 Substrate Specificity Determined by Peptide Arrays and Machine Learning

(2010) Brian C. Smith et al.   ACS Chemical Biology

Catalysis and Mechanistic Insights into Sirtuin Activation

(2010) Kristin E. Dittenhafer-Reed et al.   CHEMBIOCHEM

Investigation of the Catalytic Mechanism of Sir2 Enzyme with QM/MM Approach: SN1 vs SN2?

(2010) Zhongjie Liang et al.   JOURNAL OF PHYSICAL CHEMISTRY B

Transition State of ADP-Ribosylation of Acetyllysine Catalyzed by Archaeoglobus fulgidus Sir2 Determined by Kinetic Isotope Effects and Computational Approaches

(2010) Yana Cen et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

SIRT Inhibitors Induce Cell Death and p53 Acetylation through Targeting Both SIRT1 and SIRT2

(2010) Barrie Peck et al.   MOLECULAR CANCER THERAPEUTICS

Amurensin G, a Potent Natural SIRT1 Inhibitor, Rescues Doxorubicin Responsiveness via Down-Regulation of Multidrug Resistance 1

(2010) W. K. Oh et al.   MOLECULAR PHARMACOLOGY

Mechanism-based affinity capture of sirtuins

(2010) Yana Cen et al.   ORGANIC & BIOMOLECULAR CHEMISTRY

Investigating the ADP-ribosyltransferase Activity of Sirtuins with NAD Analogues and32P-NAD†

(2009) Jintang Du et al.   BIOCHEMISTRY

Substrate specificity of SIRT1-catalyzed lysine Nε-deacetylation reaction probed with the side chain modified Nε-acetyl-lysine analogs

(2009) Nuttara Jamonnak et al.   BIOORGANIC CHEMISTRY

Crystal Structures of Human SIRT3 Displaying Substrate-induced Conformational Changes

(2009) Lei Jin et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Robust Fluorescent Detection of Protein Fatty-Acylation with Chemical Reporters

(2009) Guillaume Charron et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Sirtuin/Sir2 phylogeny, evolutionary considerations and structural conservation

(2009) Sebastian Greiss et al.   MOLECULES AND CELLS

Plasmodium falciparumSir2 is an NAD+-Dependent Deacetylase and an Acetyllysine-Dependent and Acetyllysine-Independent NAD+Glycohydrolase†

(2008) Jarrod B. French et al.   BIOCHEMISTRY

Discovery, In Vivo Activity, and Mechanism of Action of a Small-Molecule p53 Activator

(2008) Sonia Lain et al.   CANCER CELL

Highly Dissociative and Concerted Mechanism for the Nicotinamide Cleavage Reaction in Sir2Tm Enzyme Suggested by Ab Initio QM/MM Molecular Dynamics Simulations

(2008) Po Hu et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Structural Insights into Intermediate Steps in the Sir2 Deacetylation Reaction

(2008) William F. Hawse et al.   STRUCTURE