28 articles for thisTarget
The following articles (labelled with PubMed ID or TBD) are for your review
PMID
Data
Article Title
Organization
Cyclic peptide-based potent and selective SIRT1/2 dual inhibitors harboring N
Jiangsu University
Quinazolinedione SIRT6 inhibitors sensitize cancer cells to chemotherapeutics.
University of Genoa
Design, synthesis, and pharmacological evaluations of pyrrolo[1,2-a]quinoxaline-based derivatives as potent and selective sirt6 activators.
University of Texas Medical Branch
The Pursuit of Enzyme Activation: A Snapshot of the Gold Rush.
Baylor College of Medicine
Therapeutic Potential and Activity Modulation of the Protein Lysine Deacylase Sirtuin 5.
Sapienza University of Rome
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
Structural Basis for Activation of Human Sirtuin 6 by Fluvastatin.
University of Bayreuth
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
An overview of Sirtuins as potential therapeutic target: Structure, function and modulators.
Sichuan University
Allosteric Modulator Discovery: From Serendipity to Structure-Based Design.
Shanghai Jiao-Tong University School of Medicine
Thienopyrimidinone Based Sirtuin-2 (SIRT2)-Selective Inhibitors Bind in the Ligand Induced Selectivity Pocket.
Imperial College
Human SIRT3 tripeptidic inhibitors containing N(ε)-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
Structural Basis of Sirtuin 6 Inhibition by the Hydroxamate Trichostatin A: Implications for Protein Deacylase Drug Development.
University of Bayreuth
SIRT6 inhibitors with salicylate-like structure show immunosuppressive and chemosensitizing effects.
University of Genoa
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
