34 articles for thisTarget
The following articles (labelled with PubMed ID or TBD) are for your review
PMID
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Article Title
Organization
Cyclic peptide-based potent and selective SIRT1/2 dual inhibitors harboring N
Jiangsu University
Substrates for efficient fluorometric screening employing the NAD-dependent sirtuin 5 lysine deacylase (KDAC) enzyme.
Technical University of Denmark
Design, synthesis and biological evaluation of 2,4,6- trisubstituted triazine derivatives as new nonpeptide small-molecule SIRT5 inhibitors.
Xihua University
Structure-Activity Relationship Studies of 2,4,5-Trisubstituted Pyrimidine Derivatives Leading to the Identification of a Novel and Potent Sirtuin 5 Inhibitor against Sepsis-Associated Acute Kidney Injury.
Xihua University
Pyrazolone derivatives as potent and selective small-molecule SIRT5 inhibitors.
University of Michigan
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
Development of hetero-triaryls as a new chemotype for subtype-selective and potent Sirt5 inhibition.
Ludwig-Maximilians University
Potent and Specific Activators for Mitochondrial Sirtuins Sirt3 and Sirt5.
University of Bayreuth
Identification of 2-hydroxybenzoic acid derivatives as selective SIRT5 inhibitors.
University of Michigan
Indirubin Derivatives as Dual Inhibitors Targeting Cyclin-Dependent Kinase and Histone Deacetylase for Treating Cancer.
Guizhou Medical University
Identification of isoform/domain-selective fragments from the selection of DNA-encoded dynamic library.
The University of Hong Kong
Discovery of new human Sirtuin 5 inhibitors by mimicking glutaryl-lysine substrates.
Xihua University
Identification of the subtype-selective Sirt5 inhibitor balsalazide through systematic SAR analysis and rationalization via theoretical investigations.
Ludwig-Maximilians 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
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
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
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
Potent and Selective Inhibitors of Human Sirtuin 5.
Martin-Luther-University Halle-Wittenberg
