Published in
Royal Society of Chemistry, Chemical Science, 2(8), p. 1592-1600, 2017
DOI: 10.1039/c6sc03438a
Links
- Royal Society of Chemistry
- [europepmc.org] | PDF
- [mediatum.ub.tum.de] | PDF
- [www.ncbi.nlm.nih.gov] | PDF
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Insights into ClpXP proteolysis: heterooligomerization and partial deactivation enhance chaperone affinity and substrate turnover in Listeria monocytogenes
Journal article published in 2017 by
Dóra Balogh,
Maria Dahmen,
Matthias Stahl 
,
Marcin Poreba,
Malte Gersch,
Marcin Drag,
Stephan A. Sieber
,
Marcin Poreba,
Malte Gersch,
Marcin Drag,
Stephan A. Sieber
This paper is made freely available by the publisher.
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Abstract
Caseinolytic protease fromListeriaexploits two paths of proteolytic stimulation: heterooligomerization and partial inhibitor binding both enhance ClpX chaperone affinity.