Reviews - 5d7q mentioned but not cited (1)
- SIRT1 and SIRT2 Activity Control in Neurodegenerative Diseases. Manjula R, Anuja K, Alcain FJ. Front Pharmacol 11 585821 (2020)
Articles - 5d7q mentioned but not cited (4)
- Seeding for sirtuins: microseed matrix seeding to obtain crystals of human Sirt3 and Sirt2 suitable for soaking. Rumpf T, Gerhardt S, Einsle O, Jung M. Acta Crystallogr F Struct Biol Commun 71 1498-1510 (2015)
- New chemical tools for probing activity and inhibition of the NAD+-dependent lysine deacylase sirtuin 2. Swyter S, Schiedel M, Monaldi D, Szunyogh S, Lehotzky A, Rumpf T, Ovádi J, Sippl W, Jung M. Philos Trans R Soc Lond B Biol Sci 373 20170083 (2018)
- Sirtuin 1 Inhibiting Thiocyanates (S1th)-A New Class of Isotype Selective Inhibitors of NAD+ Dependent Lysine Deacetylases. Wössner N, Alhalabi Z, González J, Swyter S, Gan J, Schmidtkunz K, Zhang L, Vaquero A, Ovaa H, Einsle O, Sippl W, Jung M. Front Oncol 10 657 (2020)
- Virtual Screening Combined with Enzymatic Assays to Guide the Discovery of Novel SIRT2 Inhibitors. Scarano N, Abbotto E, Musumeci F, Salis A, Brullo C, Fossa P, Schenone S, Bruzzone S, Cichero E. Int J Mol Sci 24 9363 (2023)
Reviews citing this publication (8)
- Lysine Acetylation Goes Global: From Epigenetics to Metabolism and Therapeutics. Ali I, Conrad RJ, Verdin E, Ott M. Chem Rev 118 1216-1252 (2018)
- The Current State of NAD+ -Dependent Histone Deacetylases (Sirtuins) as Novel Therapeutic Targets. Schiedel M, Robaa D, Rumpf T, Sippl W, Jung M. Med Res Rev 38 147-200 (2018)
- Sirtuins and their Biological Relevance in Aging and Age-Related Diseases. Zhao L, Cao J, Hu K, He X, Yun D, Tong T, Han L. Aging Dis 11 927-945 (2020)
- Guidelines for the successful generation of protein-ligand complex crystals. Müller I. Acta Crystallogr D Struct Biol 73 79-92 (2017)
- Human sirtuins: Structures and flexibility. Sacconnay L, Carrupt PA, Nurisso A. J Struct Biol 196 534-542 (2016)
- Opening the Selectivity Pocket in the Human Lysine Deacetylase Sirtuin2 - New Opportunities, New Questions. Robaa D, Monaldi D, Wössner N, Kudo N, Rumpf T, Schiedel M, Yoshida M, Jung M. Chem Rec 18 1701-1707 (2018)
- Virtual Screening in the Identification of Sirtuins' Activity Modulators. Abbotto E, Scarano N, Piacente F, Millo E, Cichero E, Bruzzone S. Molecules 27 5641 (2022)
- The roles of sirtuins in ferroptosis. Zeng J, Guo J, Huang S, Cheng Y, Luo F, Xu X, Chen R, Ma G, Wang Y. Front Physiol 14 1131201 (2023)
Articles citing this publication (6)
- Structural basis for the activation and inhibition of Sirtuin 6 by quercetin and its derivatives. You W, Zheng W, Weiss S, Chua KF, Steegborn C. Sci Rep 9 19176 (2019)
- Identification of Bichalcones as Sirtuin Inhibitors by Virtual Screening and In Vitro Testing. Karaman B, Alhalabi Z, Swyter S, Mihigo SO, Andrae-Marobela K, Jung M, Sippl W, Ntie-Kang F. Molecules 23 E416 (2018)
- Mechanism-based inhibitors of SIRT2: structure-activity relationship, X-ray structures, target engagement, regulation of α-tubulin acetylation and inhibition of breast cancer cell migration. Nielsen AL, Rajabi N, Kudo N, Lundø K, Moreno-Yruela C, Bæk M, Fontenas M, Lucidi A, Madsen AS, Yoshida M, Olsen CA. RSC Chem Biol 2 612-626 (2021)
- The crystal structure of the Leishmania infantum Silent Information Regulator 2 related protein 1: Implications to protein function and drug design. Ronin C, Costa DM, Tavares J, Faria J, Ciesielski F, Ciapetti P, Smith TK, MacDougall J, Cordeiro-da-Silva A, Pemberton IK. PLoS One 13 e0193602 (2018)
- Three-Component Aminoalkylations Yielding Dihydronaphthoxazine-Based Sirtuin Inhibitors: Scaffold Modification and Exploration of Space for Polar Side-Chains. Vojacek S, Beese K, Alhalabi Z, Swyter S, Bodtke A, Schulzke C, Jung M, Sippl W, Link A. Arch Pharm (Weinheim) 350 (2017)
- Substrate-Dependent Modulation of SIRT2 by a Fluorescent Probe, 1-Aminoanthracene. Bi D, Yang J, Hong JY, Parikh P, Hinds N, Infanti J, Lin H, Weiser BP. Biochemistry 59 3869-3878 (2020)