Аннотация:
A set of novel fragment-like catechol derivatives were identified as EphA2 inhibitors and were further profiled against a panel of 19 tyrosine kinases. In addition to EphA2, the recovered hits were active against EGFR, FGFR1, FGFR2, Abl and PDGFR-a, and according to molecular modelling studies catechol moiety was capable of forming two or more correlated hydrogen bonds with the kinase hinge region, suggesting prospects of its further optimization as an EphA2 inhibitor.
Тип публикации:
Статья
Язык публикации: английский
Образец цитирования:
V. S. Stroylov, T. V. Rakitina, F. N. Novikov, O. V. Stroganov, G. G. Chilov, A. V. Lipkin, “Novel fragment-like inhibitors of EphA2 obtained by experimental screening and modelling”, Mendeleev Commun., 20:5 (2010), 263–265
Образцы ссылок на эту страницу:
https://www.mathnet.ru/rus/mendc3059
https://www.mathnet.ru/rus/mendc/v20/i5/p263
Эта публикация цитируется в следующих 10 статьяx:
Alix Tröster, Michael DiPrima, Nathalie Jores, Denis Kudlinzki, Sridhar Sreeramulu, Santosh L. Gande, Verena Linhard, Damian Ludig, Alexander Schug, Krishna Saxena, Maria Reinecke, Stephanie Heinzlmeir, Matthias S. Leisegang, Jan Wollenhaupt, Frank Lennartz, Manfred S. Weiss, Bernhard Kuster, Giovanna Tosato, Harald Schwalbe, “Optimization of the Lead Compound NVP‐BHG712 as a Colorectal Cancer Inhibitor”, Chemistry A European J, 29:23 (2023)
Alix Tröster, Nathalie Jores, Konstantin S. Mineev, Sridhar Sreeramulu, Michael DiPrima, Giovanna Tosato, Harald Schwalbe, “Targeting EPHA2 with Kinase Inhibitors in Colorectal Cancer”, ChemMedChem, 18:23 (2023)
M. G. Medvedev, O. V. Stroganov, A. O. Dmitrienko, M. V. Panova, A. A. Lisov, I. Svitanko, F. N. Novikov, G. G. Chilov, “Reducing false-positive rates in virtual screening via cancellation of systematic errors in the scoring function”, Mendeleev Commun., 32:6 (2022), 735–738
Ф. Н. Новиков, В. С. Стройлов, И. В. Свитанько, В. Е. Небольсин, “Молекулярные основы патогенеза COVID-19”, Усп. хим., 89:8 (2020), 858–878; F. N. Novikov, V. S. Stroylov, I. Svitanko, V. E. Nebolsin, “Molecular foundations of COVID-19 pathogenesis”, Russian Chem. Reviews, 89:8 (2020), 858–878
Alix Tröster, Stephanie Heinzlmeir, Benedict‐Tilman Berger, Santosh L. Gande, Krishna Saxena, Sridhar Sreeramulu, Verena Linhard, Amir H. Nasiri, Michael Bolte, Susanne Müller, Bernhard Kuster, Guillaume Médard, Denis Kudlinzki, Harald Schwalbe, “NVP‐BHG712: Effects of Regioisomers on the Affinity and Selectivity toward the EPHrin Family”, ChemMedChem, 13:16 (2018), 1629
V. S. Stroylov, D. V. Katkov, I. Yu. Titov, O. V. Stroganov, F. N. Novikov, G. G. Chilov, I. Svitanko, “Modeling comparative selectivity profiles of kinase inhibitors using FEP/MD protocol”, Mendeleev Commun., 27:4 (2017), 349–351
Andrea Unzue, Karine Lafleur, Hongtao Zhao, Ting Zhou, Jing Dong, Peter Kolb, Johanna Liebl, Stefan Zahler, Amedeo Caflisch, Cristina Nevado, “Three stories on Eph kinase inhibitors: From in silico discovery to in vivo validation”, European Journal of Medicinal Chemistry, 112 (2016), 347
Yong Zhu, Ting Ran, Xin Chen, Jiaqi Niu, Shuang Zhao, Tao Lu, Weifang Tang, “Synthesis and Biological Evaluation of 1-(2-Aminophenyl)-3-arylurea Derivatives as Potential EphA2 and HDAC Dual Inhibitors”, Chem. Pharm. Bull., 64:8 (2016), 1136
Roberta Noberini, Ilaria Lamberto, Elena B. Pasquale, “Targeting Eph receptors with peptides and small molecules: Progress and challenges”, Seminars in Cell & Developmental Biology, 23:1 (2012), 51
L. V. Romashov, A. A. Zeifman, A. L. Zakharenko, F. N. Novikov, V. S. Stroylov, O. V. Stroganov, G. G. Chilov, S. N. Khodyreva, O. I. Lavrik, I. Yu. Titov, I. Svitanko, “Rational design and synthesis of new PARP1 inhibitors”, Mendeleev Commun., 22:1 (2012), 15–17