Structure of the drug target ClpC1 unfoldase in action provides insights on antibiotic mechanism of action
Author:
Funder
European External Action Service
Horizon 2020
European Commission
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference37 articles.
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2. The active ClpP protease from M. tuberculosis is a complex composed of a heptameric ClpP1 and a ClpP2 ring;Akopian;EMBO J.,2012
3. Mycobacterium tuberculosis ClpP1 and ClpP2 function together in protein degradation and are required for viability in vitro and during infection;Raju;PLoS Pathog.,2012
4. The cyclic peptide ecumicin targeting CLpC1 is active against Mycobacterium tuberculosis in vivo;Gao;Antimicrob. Agents Chemother.,2015
5. Mutation analysis of the interactions between Mycobacterium tuberculosis caseinolytic protease C1 (ClpC1) and ecumicin;Jung;Int. J. Biol. Macromol.,2017
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2. Metabolites from Streptomyces aureus (VTCC43181) and Their Inhibition of Mycobacterium tuberculosis ClpC1 Protein;Molecules;2024-02-04
3. Discovery and Mechanistic Study of Novel Mycobacterium tuberculosis ClpP1P2 Inhibitors;Journal of Medicinal Chemistry;2023-12-13
4. Crystal structure of the N-terminal domain of MtClpC1 in complex with the anti-mycobacterial natural peptide Lassomycin;International Journal of Biological Macromolecules;2023-12
5. Correction: Structure of the drug target ClpC1 unfoldase in action provides insights on antibiotic mechanism of action;Journal of Biological Chemistry;2023-07
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