This page shows the publications co-authored by Olga Kandror and Tatos Akopian.
Cleavage Specificity of Mycobacterium tuberculosis ClpP1P2 Protease and Identification of Novel Peptide Substrates and Boronate Inhibitors with Anti-bacterial Activity. J Biol Chem. 2015 Apr 24; 290(17):11008-20.
The active ClpP protease from M. tuberculosis is a complex composed of a heptameric ClpP1 and a ClpP2 ring. EMBO J. 2012 Mar 21; 31(6):1529-41.
ClpX Is Essential and Activated by Single-Strand DNA Binding Protein in Mycobacteria. J Bacteriol. 2021 01 25; 203(4).
Pyrazinamide triggers degradation of its target aspartate decarboxylase. Nat Commun. 2020 04 03; 11(1):1661.
Development of high throughput screening methods for inhibitors of ClpC1P1P2 from Mycobacteria tuberculosis. Anal Biochem. 2019 02 15; 567:30-37.
An Antibacterial ß-Lactone Kills Mycobacterium tuberculosis by Disrupting Mycolic Acid Biosynthesis. Angew Chem Int Ed Engl. 2018 01 02; 57(1):348-353.
Acyldepsipeptide antibiotics kill mycobacteria by preventing the physiological functions of the ClpP1P2 protease. Mol Microbiol. 2016 07; 101(2):194-209.
Structure and Functional Properties of the Active Form of the Proteolytic Complex, ClpP1P2, from Mycobacterium tuberculosis. J Biol Chem. 2016 Apr 01; 291(14):7465-76.
The cyclic peptide ecumicin targeting ClpC1 is active against Mycobacterium tuberculosis in vivo. Antimicrob Agents Chemother. 2015 Feb; 59(2):880-9.
Lassomycin, a ribosomally synthesized cyclic peptide, kills mycobacterium tuberculosis by targeting the ATP-dependent protease ClpC1P1P2. Chem Biol. 2014 Apr 24; 21(4):509-518.
Mycobacterium tuberculosis ClpP1 and ClpP2 function together in protein degradation and are required for viability in vitro and during infection. PLoS Pathog. 2012 Feb; 8(2):e1002511.
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