This page shows the publications co-authored by Olga Kandror and Alfred Goldberg.
Yeast adapt to near-freezing temperatures by STRE/Msn2,4-dependent induction of trehalose synthesis and certain molecular chaperones. Mol Cell. 2004 Mar 26; 13(6):771-81.
Trehalose synthesis is induced upon exposure of Escherichia coli to cold and is essential for viability at low temperatures. Proc Natl Acad Sci U S A. 2002 Jul 23; 99(15):9727-32.
Development of high throughput screening methods for inhibitors of ClpC1P1P2 from Mycobacteria tuberculosis. Anal Biochem. 2019 02 15; 567:30-37.
Trigger factor is induced upon cold shock and enhances viability of Escherichia coli at low temperatures. Proc Natl Acad Sci U S A. 1997 May 13; 94(10):4978-81.
Trigger factor associates with GroEL in vivo and promotes its binding to certain polypeptides. J Biol Chem. 1997 Jan 17; 272(3):1730-4.
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.
Trigger factor is involved in GroEL-dependent protein degradation in Escherichia coli and promotes binding of GroEL to unfolded proteins. EMBO J. 1995 Dec 01; 14(23):6021-7.
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.
Rapid degradation of an abnormal protein in Escherichia coli involves the chaperones GroEL and GroES. J Biol Chem. 1994 Sep 23; 269(38):23575-82.
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 Jan 25; 203(4).
The molecular chaperone DnaJ is required for the degradation of a soluble abnormal protein in Escherichia coli. J Biol Chem. 2001 Feb 09; 276(6):3920-8.
Acyldepsipeptide antibiotics kill mycobacteria by preventing the physiological functions of the ClpP1P2 protease. Mol Microbiol. 2016 07; 101(2):194-209.
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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