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- Structure-based design, synthesis, and biological evaluation of novel piperine–resveratrol hybrids as antiproliferative agents targeting SIRT-2. Ahmed H. Tantawy, Xiang-Gao Meng, Adel A. Marzouk, Ali Fouad, Ahmed H. Abdelazeem, Bahaa G. M. Youssif, Hong Jiang, Man-Qun Wang
, RSC Adv.
, 2021
, 11
, 25738
- Development of a NanoBRET assay to validate inhibitors of Sirt2-mediated lysine deacetylation and defatty-acylation that block prostate cancer cell migration. A. Vogelmann, M. Schiedel, N. Wössner, A. Merz, D. Herp, S. Hammelmann, A. Colcerasa, G. Komaniecki, JY. Hong, M. Sum, E. Metzger, E. Neuwirt, L. Zhang, O. Einsle, O. Groß, R. Schüle, H. Lin, W. Sippl, M. Jung
, RSC Chem. Biol.
, 2022
, 3
, 468
- Recent advances in the development of histone deacylase SIRT2 inhibitors. Wenyu Yang, Wei Chen, Huilin Su, Rong Li, Chen Song, Zhouyu Wang, Lingling Yang
, RSC Adv.
, 2020
, 10
, 37382
- The chemical biology of sirtuins. Bing Chen, Wenwen Zang, Juan Wang, Yajun Huang, Yanhua He, Lingling Yan, Jiajia Liu, Weiping Zheng
, Chem. Soc. Rev.
, 2015
, 44
, 5246
- Selectivity hot-spots of sirtuin catalytic cores. Marco Daniele Parenti, Santina Bruzzone, Alessio Nencioni, Alberto Del Rio
, Mol. BioSyst.
, 2015
, 11
, 2263
- Genetic encoding of ε-N-l-lactyllysine for detecting delactylase activity in living cells. Yanan Sun, Yanchi Chen, Yaxin Xu, Yuqing Zhang, Minghao Lu, Manjia Li, Liyan Zhou, Tao Peng
, Chem. Commun.
, 2022
, 58
, 8544
- Crystallographic and SAR analyses reveal the high requirements needed to selectively and potently inhibit SIRT2 deacetylase and decanoylase. Ling-Ling Yang, Wei Xu, Jie Yan, Hui-Lin Su, Chen Yuan, Chao Li, Xing Zhang, Zhu-Jun Yu, Yu-Hang Yan, Yamei Yu, Qiang Chen, Zhouyu Wang, Lin Li, Shan Qian, Guo-Bo Li
, Med. Chem. Commun.
, 2019
, 10
, 164
- 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. Alexander L. Nielsen, Nima Rajabi, Norio Kudo, Kathrine Lundø, Carlos Moreno-Yruela, Michael Bæk, Martin Fontenas, Alessia Lucidi, Andreas S. Madsen, Minoru Yoshida, Christian A. Olsen
, RSC Chem. Biol.
, 2021
, 2
, 612
- Potent sirtuin inhibition with 1,2,5-trisubstituted benzimidazoles. Y. K. Yoon, H. Osman, T. S. Choon
, Med. Chem. Commun.
, 2016
, 7
, 2094
- Potent mechanism-based sirtuin-2-selective inhibition by an in situ-generated occupant of the substrate-binding site, “selectivity pocket” and NAD+-binding site. Paolo Mellini, Yukihiro Itoh, Hiroki Tsumoto, Ying Li, Miki Suzuki, Natsuko Tokuda, Taeko Kakizawa, Yuri Miura, Jun Takeuchi, Maija Lahtela-Kakkonen, Takayoshi Suzuki
, Chem. Sci.
, 2017
, 8
, 6400