PMID

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Article Title

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Bivalent SIRT1 inhibitors.

Jiangsu University

Cyclic peptide-based potent and selective SIRT1/2 dual inhibitors harboring N

Jiangsu University

How much successful are the medicinal chemists in modulation of SIRT1: A critical review.

Guru Jambheshwar University of Science and Technology

5-((3-Amidobenzyl)oxy)nicotinamides as Sirtuin 2 Inhibitors.

University of Minnesota

Simple N(e)-thioacetyl-lysine-containing cyclic peptides exhibiting highly potent sirtuin inhibition.

Jiangsu University

Design, synthesis and structure-activity relationship studies of novel sirtuin 2 (SIRT2) inhibitors with a benzamide skeleton.

The University of Tokyo

Discovery of potent and selective sirtuin 2 (SIRT2) inhibitors using a fragment-based approach.

University of Minnesota

Development of pyrazolone and isoxazol-5-one cambinol analogues as sirtuin inhibitors.

Fred Hutchinson Cancer Research Center

Identification of novel SIRT2-selective inhibitors using a click chemistry approach.

Nagoya City University

Screen of pseudopeptidic inhibitors of human sirtuins 1-3: two lead compounds with antiproliferative effects in cancer cells.

University of Eastern Finland

Discovery of thieno[3,2-d]pyrimidine-6-carboxamides as potent inhibitors of SIRT1, SIRT2, and SIRT3.

Sirtris A Gsk

Discovery and mechanism study of SIRT1 activators that promote the deacetylation of fluorophore-labeled substrate.

Chinese Academy of Sciences

Inhibitors of the NAD(+)-Dependent Protein Desuccinylase and Demalonylase Sirt5.

TBA

SIRT1 modulation as a novel approach to the treatment of diseases of aging.

Sirtris A Gsk

Design, synthesis, and biological activity of a novel series of human sirtuin-2-selective inhibitors.

Kyoto Prefectural University of Medicine

Identification of a sirtuin 3 inhibitor that displays selectivity over sirtuin 1 and 2.

Universit£

Novel 3-arylideneindolin-2-ones as inhibitors of NAD+ -dependent histone deacetylases (sirtuins).

Ludwig-Maximilians-Universit£T M£Nchen

Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes.

Sirtris Pharmaceuticals

A mechanism-based potent sirtuin inhibitor containing Ne-thiocarbamoyl-lysine (TuAcK).

University of Akron

Synthesis and biological activity of splitomicin analogs targeted at human NAD(+)-dependent histone deacetylases (sirtuins).

Ernst-Moritz-Arndt University Greifswald

Identification of a cell-active non-peptide sirtuin inhibitor containing N-thioacetyl lysine.

Nagoya City University

Sirtuin 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson's disease.

Harvard Medical School

Discovery of novel compounds as potent activators of Sirt3.

Pmc Isochem

Discovery of indoles as potent and selective inhibitors of the deacetylase SIRT1.

Elixir Pharmaceuticals

Therapeutic Potential and Activity Modulation of the Protein Lysine Deacylase Sirtuin 5.

Sapienza University of Rome

Overview of SIRT5 as a potential therapeutic target: Structure, function and inhibitors.

China Pharmaceutical University

Potent and Specific Activators for Mitochondrial Sirtuins Sirt3 and Sirt5.

University of Bayreuth

Structure-Guided Design of a Small-Molecule Activator of Sirtuin-3 that Modulates Autophagy in Triple Negative Breast Cancer.

Sichuan University

Identification of isoform/domain-selective fragments from the selection of DNA-encoded dynamic library.

The University of Hong Kong

Discovery of Dihydro-1,4-Benzoxazine Carboxamides as Potent and Highly Selective Inhibitors of Sirtuin-1.

Max Planck Institute of Molecular Physiology

Discovery of new human Sirtuin 5 inhibitors by mimicking glutaryl-lysine substrates.

Xihua University

Simultaneous Inhibition of SIRT2 Deacetylase and Defatty-Acylase Activities via a PROTAC Strategy.

Cornell University

Discovery of 5-Benzylidene-2-phenyl-1,3-dioxane-4,6-diones as Highly Potent and Selective SIRT1 Inhibitors.

Chinese Academy of Sciences

Sensitive fluorogenic substrates for sirtuin deacylase inhibitor discovery.

Xihua University

A bicyclic pentapeptide-based highly potent and selective pan-SIRT1/2/3 inhibitor harboring N

Fudan University

Discovery of Potent Small-Molecule SIRT6 Activators: Structure-Activity Relationship and Anti-Pancreatic Ductal Adenocarcinoma Activity.

Sichuan University

Discovery of 5-(4-methylpiperazin-1-yl)-2-nitroaniline derivatives as a new class of SIRT6 inhibitors.

Sichuan University

Unexpected small molecules as novel SIRT2 suicide inhibitors.

Engineering Research Center For The Development and Application of Ethnic Medicine and Tcm (Ministry of Education)

An overview of Sirtuins as potential therapeutic target: Structure, function and modulators.

Sichuan University

Novel Lysine-Based Thioureas as Mechanism-Based Inhibitors of Sirtuin 2 (SIRT2) with Anticancer Activity in a Colorectal Cancer Murine Model.

TBA

Synthesis of certain benzothieno[3,2-d]pyrimidine derivatives as a selective SIRT2 inhibitors.

Cairo University

Extending Cross Metathesis To Identify Selective HDAC Inhibitors: Synthesis, Biological Activities, and Modeling.

Umr Cnrs 7285

Cyclic tripeptide-based potent human SIRT7 inhibitors.

Jiangsu University

Synthesis and in Vitro and in Vivo Biological Evaluation of Tissue-Specific Bisthiazole Histone Deacetylase (HDAC) Inhibitors.

Chinese Academy of Sciences

Identification of Diketopiperazine-Containing 2-Anilinobenzamides as Potent Sirtuin 2 (SIRT2)-Selective Inhibitors Targeting the "Selectivity Pocket", Substrate-Binding Site, and NAD

Kyoto Prefectural University of Medicine

Thienopyrimidinone Based Sirtuin-2 (SIRT2)-Selective Inhibitors Bind in the Ligand Induced Selectivity Pocket.

Imperial College

Human SIRT3 tripeptidic inhibitors containing N(?)-thioacetyl-lysine.

Jiangsu University

Development of Peptide-Based Sirtuin Defatty-Acylase Inhibitors Identified by the Fluorescence Probe, SFP3, That Can Efficiently Measure Defatty-Acylase Activity of Sirtuin.

Nagoya City University

Squaramides as novel class I and IIB histone deacetylase inhibitors for topical treatment of cutaneous t-cell lymphoma.

Nestle Skin Health R&D

Chemically Induced Degradation of Sirtuin 2 (Sirt2) by a Proteolysis Targeting Chimera (PROTAC) Based on Sirtuin Rearranging Ligands (SirReals).

University of Freiburg

X-ray crystal structure guided discovery of new selective, substrate-mimicking sirtuin 2 inhibitors that exhibit activities against non-small cell lung cancer cells.

West China School of Pharmacy

The mimics of N

School of Pharmacy

Discovery and Characterization of R/S-N-3-Cyanophenyl-N'-(6-tert-butoxycarbonylamino-3,4-dihydro-2,2-dimethyl-2H-1-benzopyran-4-yl)urea, a New Histone Deacetylase Class III Inhibitor Exerting Antiproliferative Activity against Cancer Cell Lines.

H�Pital Kirchberg

Discovery of 2-((4,6-dimethylpyrimidin-2-yl)thio)-N-phenylacetamide derivatives as new potent and selective human sirtuin 2 inhibitors.

Xihua University