Antimicrobial Agents and Chemotherapy · 2019 · 118 citations · 36 references
Life SciencesMicrobiologyMolecular BiologyAntimicrobial ResistanceDrug DiscoveryProtein BiochemistryAntibacterial PharmacologyAntimicrobial PeptidesEnzyme InhibitionProtein DegradationProteolytic ProcessingTuberculosis PharmacotherapyAntibacterial PeptidesAntimicrobial Peptide ActivityCyclic PeptidesLead Compound DiscoveryMycobacterium Tuberculosis InfectionMycobacterium Tuberculosis PathogenesisProtein Degradation ResistanceProteolytic Pathways
(V13, H77, and F80). RUFI also significantly decreased the proteolytic capabilities of the ClpC1/P1/P2 complex to degrade casein, while having no significant effect on the ATPase activity of ClpC1. This represents a marked difference from ecumicin, which inhibits ClpC1 proteolysis but stimulates the ATPase activity, thereby providing evidence that although these peptides share ClpC1 as a macromolecular target, their downstream effects are distinct, likely due to differences in binding.
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MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) Software Version 4.0
Koichiro Tamura, Joel T. Dudley, M Nei et al. · Molecular Biology and Evolution · 2007 · 28.8K citations · Full text
Global tuberculosis report (2014)
L.A. Gabbasova, E.R. Experts Who · 2014 · 13.2K citations