Harvard Catalyst Profiles

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Olga Kandror, Ph.D.

Co-Author

This page shows the publications co-authored by Olga Kandror and Alfred Goldberg.
Connection Strength

2.201
  1. 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.
    View in: PubMed
    Score: 0.300
  2. 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.
    View in: PubMed
    Score: 0.267
  3. Development of high throughput screening methods for inhibitors of ClpC1P1P2 from Mycobacteria tuberculosis. Anal Biochem. 2019 02 15; 567:30-37.
    View in: PubMed
    Score: 0.208
  4. 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.
    View in: PubMed
    Score: 0.187
  5. Trigger factor associates with GroEL in vivo and promotes its binding to certain polypeptides. J Biol Chem. 1997 Jan 17; 272(3):1730-4.
    View in: PubMed
    Score: 0.183
  6. 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.
    View in: PubMed
    Score: 0.171
  7. 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.
    View in: PubMed
    Score: 0.169
  8. 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.
    View in: PubMed
    Score: 0.160
  9. 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.
    View in: PubMed
    Score: 0.155
  10. 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.
    View in: PubMed
    Score: 0.129
  11. ClpX Is Essential and Activated by Single-Strand DNA Binding Protein in Mycobacteria. J Bacteriol. 2021 01 25; 203(4).
    View in: PubMed
    Score: 0.060
  12. 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.
    View in: PubMed
    Score: 0.059
  13. Acyldepsipeptide antibiotics kill mycobacteria by preventing the physiological functions of the ClpP1P2 protease. Mol Microbiol. 2016 07; 101(2):194-209.
    View in: PubMed
    Score: 0.043
  14. The cyclic peptide ecumicin targeting ClpC1 is active against Mycobacterium tuberculosis in vivo. Antimicrob Agents Chemother. 2015 Feb; 59(2):880-9.
    View in: PubMed
    Score: 0.039
  15. 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.
    View in: PubMed
    Score: 0.038
  16. 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.
    View in: PubMed
    Score: 0.032
Connection Strength
The connection strength for co-authors is the sum of the scores for each of their shared publications.

Publication scores are based on many factors, including how long ago they were written and whether the person is a first or senior author.
Funded by the NIH National Center for Advancing Translational Sciences through its Clinical and Translational Science Awards Program, grant number UL1TR002541.