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Arkadius Pichota
Researcher at Novartis Institute for Tropical Diseases
Publications - 3
Citations - 619
Arkadius Pichota is an academic researcher from Novartis Institute for Tropical Diseases. The author has contributed to research in topics: Druggability & Virus. The author has an hindex of 3, co-authored 3 publications receiving 558 citations. Previous affiliations of Arkadius Pichota include Novartis.
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Journal ArticleDOI
An adenosine nucleoside inhibitor of dengue virus
Zheng Yin,Zheng Yin,Yen Liang Chen,Wouter Schul,Qing Yin Wang,Feng Gu,Jeyaraj Duraiswamy,Ravinder Reddy Kondreddi,Pornwaratt Niyomrattanakit,Suresh B. Lakshminarayana,Anne Goh,Hao Ying Xu,Wei Liu,Boping Liu,Joanne Y.H. Lim,Chuan Young Ng,Min Qing,Chin Chin Lim,Andy Yip,Gang Wang,Wai Ling Chan,Hui Pen Tan,Kai Lin,Bo Zhang,Gang Zou,Kristen A. Bernard,Christine E. Garrett,Karen Beltz,Min Dong,Margaret Weaver,Handan He,Arkadius Pichota,Véronique Dartois,Thomas H. Keller,Pei Yong Shi +34 more
TL;DR: The results have proved the concept that a nucleoside inhibitor could be developed for potential treatment of flavivirus infections and suppressed peak viremia, reduced cytokine elevation, and completely prevented the infected mice from death.
Journal ArticleDOI
A practical view of 'druggability'
TL;DR: This review summarizes the recent advances in the field and examines the usefulness of 'the rules of the game' in practice from a medicinal chemist's standpoint.
Journal ArticleDOI
Peptide deformylase inhibitors of Mycobacterium tuberculosis: synthesis, structural investigations, and biological results.
Arkadius Pichota,Jeyaraj Duraiswamy,Zheng Yin,Thomas H. Keller,Jenefer Alam,Sarah Liung,Gladys Lee,Mei Ding,Gang Wang,Wai Ling Chan,Mark Schreiber,Ida Ma,David Beer,Xinyi Ngew,Kakoli Mukherjee,Mahesh Nanjundappa,Jeanette W. P. Teo,Pamela Thayalan,Amelia Yap,Thomas Dick,Wuyi Meng,Mei Xu,James Koehn,Shi-Hao Pan,Kirk Clark,Xiaoling Xie,Carolyn Shoen,Michael H. Cynamon +27 more
TL;DR: Structural-activity relationship and crystallographic data clarified the structural requirements for high enzyme potency and cell based potency of bacterial peptide deformylase.