MecA: A Multifunctional ClpP-Dependent and Independent Regulator in Gram-Positive Bacteria. [PDF]
Wen ZT, Ellepola K, Wu H.
europepmc +1 more source
Targeting mitochondrial ClpP: structural insights and therapeutic potential of ClpP agonists in cancer therapy. [PDF]
Kong M, Yu Y, Shao S, Zhang C.
europepmc +1 more source
Cell Sizes Matter for Industrial Bioproduction, a Case of Polyhydroxybutyrate. [PDF]
Chen YL +10 more
europepmc +1 more source
Structural insights into the Pseudomonas aeruginosa ClpP1•ClpP2 heterocomplex and its interactions with the AAA+ ClpX unfoldase. [PDF]
Ghanbarpour A +4 more
europepmc +1 more source
Molecular Glue-like Degraders of TEM β-Lactamases by Periplasmic Protease DegP
Taylor EK +7 more
europepmc +1 more source
Degradation of MinD Oscillator Complexes by Escherichia coli ClpXP [PDF]
MinD is a cell division ATPase in Escherichia coli that oscillates from pole to pole and regulates the spatial position of the cell division machinery. Together with MinC and MinE, the Min system restricts assembly of the FtsZ-ring to midcell, oscillating between the opposite ends of the cell and preventing FtsZ-ring misassembly at the poles.
Jodi L Camberg +2 more
exaly +6 more sources
The ClpXP Protease Contributes to Staphylococcus aureus Pneumonia [PDF]
Abstract Staphylococcus aureus is a leading cause of pneumonia. We show here that the ClpXP protease involved in protein turnover is important for pathogenesis in a murine model of acute pneumonia. Staphylococcus aureus lacking this protease is attenuated in vivo, being rapidly cleared from the airway and leading to decreased immune ...
Dane Parker, Lavoisier Akoolo
exaly +3 more sources
Discovery of Antibacterial Cyclic Peptides That Inhibit the ClpXP Protease [PDF]
AbstractA method to rapidly screen libraries of cyclic peptides in vivo for molecules with biological activity has been developed and used to isolate cyclic peptide inhibitors of the ClpXP protease. Fluorescence activated cell sorting was used in conjunction with a fluorescent reporter to isolate cyclic peptides that inhibit the proteolysis of tmRNA ...
Kenneth C Keiler +2 more
exaly +3 more sources
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A Specificity-Enhancing Factor for the ClpXP Degradation Machine
Science, 2000Events that stall bacterial protein synthesis activate the ssrA-tagging machinery, resulting in resumption of translation and addition of an 11-residue peptide to the carboxyl terminus of the nascent chain. This ssrA-encoded peptide tag marks the incomplete protein for degradation by the energy-dependent ClpXP protease.
I, Levchenko +3 more
openaire +2 more sources
Alternating Translocation of Protein Substrates From Both Ends of ClpXP Protease [PDF]
In ClpXP protease complexes, hexameric rings of the ATP-dependent ClpX chaperone stack on one or both faces of the double-heptameric rings of ClpP. We used electron microscopy to record the initial binding of protein substrates to ClpXP and their accumulation inside proteolytically inactive ClpP.
Joaquin Ortega +2 more
exaly +3 more sources

