Design and Synthesis of 24-Fluorinated Bafilomycin Analogue as an NMR Probe with Potent Inhibitory Activity to Vacuolar-type ATPase
Author:
Affiliation:
1. Graduate School of Science, Osaka University
2. ERATO, Lipid Active Structure Project, Japan Science and Technology Agency
3. Faculty of Life and Environmental Sciences, University of Tsukuba
Publisher
The Chemical Society of Japan
Subject
General Chemistry
Link
http://www.journal.csj.jp/doi/pdf/10.1246/cl.131099
Reference29 articles.
1. Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology
2. Structural bases of physiological functions and roles of the vacuolar H+-ATPase
3. The structure of the bafilomycins, a new group of macrolide antibiotics
4. Metabolic products of microorganisms. 224. Bafilomycins, a new group of macrolide antibiotics. Production, isolation, chemical structure and biological activity.
5. Concanamycin A, the Specific Inhibitor of V-ATPases, Binds to the Vo Subunit c
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3. Bafilomycin analogue site-specifically fluorinated at the pharmacophore macrolactone ring has potent vacuolar-type ATPase inhibitory activity;Tetrahedron Letters;2016-06
4. Modification of Bafilomycin Structure to Efficiently Synthesize Solid-State NMR Probes that Selectively Bind to Vacuolar-Type ATPase;Chemistry - An Asian Journal;2015-01-21
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