A5061979309- Sirtuins and Resveratrol in Medicine
- Autophagy in Disease and Therapy
- Histone Deacetylase Inhibitors Research
- PARP inhibition in cancer therapy
- Ubiquitin and proteasome pathways
- Synthesis and Catalytic Reactions
- Adenosine and Purinergic Signaling
- RNA modifications and cancer
- Porphyrin and Phthalocyanine Chemistry
- Cholinesterase and Neurodegenerative Diseases
- Metal-Catalyzed Oxygenation Mechanisms
- Trypanosoma species research and implications
- Calcium signaling and nucleotide metabolism
- Biochemical and Molecular Research
University of Freiburg
2021-2024
Istituto di Metodologie Chimiche
2018
Sapienza University of Rome
2018
Dysregulation of both tubulin deacetylases sirtuin 2 (Sirt2) and the histone deacetylase 6 (HDAC6) has been associated with pathogenesis cancer neurodegeneration, thus making these two enzymes promising targets for pharmaceutical intervention. Herein, we report design, synthesis, biological characterization first-in-class dual Sirt2/HDAC6 inhibitors as molecular tools inhibition deacetylation. Using biochemical
Sirtuin2 (Sirt2) with its NAD+-dependent deacetylase and defatty-acylase activities plays a central role in the regulation of specific cellular functions. Dysregulation Sirt2 activity has been associated pathogenesis many diseases, thus making promising target for pharmaceutical intervention. Herein, we present new high affinity selective Sirtuin-Rearranging Ligands (SirReals) that inhibit both Sirt2-dependent deacetylation defatty-acylation vitro cells. We show simultaneous inhibition...
The NAD+-dependent lysine deacylase sirtuin 2 (Sirt2) is involved in multiple pathological conditions such as cancer. Targeting Sirt2 has thus received an increased interest for therapeutic purposes. Furthermore, the orthologue from Schistosoma mansoni (SmSirt2) been considered potential treatment of neglected tropical disease schistosomiasis. We previously identified a 1,2,4-oxadiazole-based scaffold screening "Kinetobox" library dual inhibitor human (hSirt2) and SmSirt2. Herein, we...
Amino acid derivatives are oxidized by the <bold>1</bold>/H<sub>2</sub>O<sub>2</sub> system. A marked preference for aromatic over Cα–H and benzylic C–H oxidation is observed with phenylalanine.
Dysregulation of both tubulin deacetylases sirtuin 2 (Sirt2) and the histone deacetylase 6 (HDAC6) has been associated with pathogenesis cancer neurodegeneration, thus making these two enzymes promising targets for pharmaceutical intervention. Herein, we report design, synthesis, biological characterization first-in-class dual Sirt2/HDAC6 inhibitors as molecular tools inhibition deacetylation. Using biochemical in vitro assays cell-based methods target engagement, identified Mz325 (31) a...
Dysregulation of both tubulin deacetylases sirtuin 2 (Sirt2) and the histone deacetylase 6 (HDAC6) has been associated with pathogenesis cancer neurodegeneration, thus making these two enzymes promising targets for pharmaceutical intervention. Herein, we report design, synthesis, biological characterization first-in-class dual Sirt2/HDAC6 inhibitors as molecular tools inhibition deacetylation. Using biochemical in vitro assays cell-based methods target engagement, identified Mz325 (33) a...
The NAD+-dependent lysine deacylase Sirtuin2 (Sirt2) is involved in multiple pathological conditions, including cancer and targeting Sirt2 has thus received an increased interest for therapeutic purpose. Furthermore, addressing the ortholog from Schistosoma mansoni (SmSirt2) been considered potential treatment of neglected tropical disease schistosomiasis. We previously identified a 1,2,4-oxadiazole-based scaffold screening “Kinetobox” library as dual inhibitor human SmSirt2. Herein, we...
Dysregulation of both tubulin deacetylases sirtuin 2 (Sirt2) and the histone deacetylase 6 (HDAC6) has been associated with pathogenesis cancer neurodegeneration, thus making these two enzymes promising targets for pharmaceutical intervention. Herein, we report design, synthesis, biological characterization first-in-class dual Sirt2/HDAC6 inhibitors as molecular tools inhibition deacetylation. Using biochemical in vitro assays cell-based methods target engagement, identified Mz325 (31) a...
Sirtuin2 (Sirt2) with its NAD+-dependent deacetylase and defatty-acylase activities plays a central role in the regulation of specific cellular functions. Dysregulation Sirt2 activity has been associated pathogenesis many diseases, thus making promising target for pharmaceutical intervention. Herein, we present new high affinity selective Sirtuin-Rearranging Ligands (SirReals) that inhibit both Sirt2-dependent deacetylation defatty-acylation vitro cells. We show dual inhibition results...
The NAD+-dependent lysine deacylase Sirtuin2 (Sirt2) is involved in multiple pathological conditions, including cancer. Targeting Sirt2 has thus received an increased interest for therapeutic purpose, the ortholog from Schistosoma mansoni (SmSirt2) potential treatment of neglected tropical disease schistosomiasis. We previously identified a 1,2,4-oxadiazole-based scaffold screening “Kinetobox” library as inhibitor both human and SmSirt2. Herein, we describe structure-activity studies on...
Sirtuin2 (Sirt2) with its NAD+-dependent deacetylase and defatty-acylase activities plays a central role in the regulation of specific cellular functions. Dysregulation Sirt2 activity has been associated pathogenesis many diseases, thus making promising target for pharmaceutical intervention. Herein, we present new high affinity selective Sirtuin-Rearranging Ligands (SirReals) that inhibit both Sirt2-dependent deacetylation defatty-acylation vitro cells. We show simultaneous inhibition...