Results 171 to 180 of about 18,135 (204)
A Conformational Switch Underlies ClpP Protease Function
Angewandte Chemie - International Edition, 2011 A “breathing” protein: The first structure of the virulence regulator and heat shock protein ClpP from Staphylococcus aureus reveals a previously unobserved compressed state of the ClpP barrel. A conformational switch in the active center “handle region” results in closure of the active sites and opening of equatorial pores.
Thomas Böttcher, Stephan A Sieber
exaly +5 more sources
ClpP Protease, a Promising Antimicrobial Target [PDF]
International Journal of Molecular Sciences, 2019 The caseinolytic protease proteolytic subunit (ClpP) is a serine protease playing an important role in proteostasis of eukaryotic organelles and prokaryotic cells. Alteration of ClpP function has been proved to affect the virulence and infectivity of a number of pathogens.
Carlos Moreno-Cinos +2 more
exaly +4 more sources
Mitochondrial ClpP-Mediated Proteolysis Induces Selective Cancer Cell Lethality [PDF]
Cancer Cell, 2019 The mitochondrial caseinolytic protease P (ClpP) plays a central role in mitochondrial protein quality control by degrading misfolded proteins. Using genetic and chemical approaches, we showed that hyperactivation of the protease selectively kills cancer cells, independently of p53 status, by selective degradation of its respiratory chain protein ...
Jo Ishizawa, Ondrej Halgas, Ran Zhao
exaly +3 more sources
Some of the next articles are maybe not open access.
Related searches:
Related searches:
The Mechanism of Caseinolytic Protease (ClpP) Inhibition
Angewandte Chemie - International Edition, 2013Malte Gersch +2 more
exaly +4 more sources
Selective Activation of Human Caseinolytic Protease P (ClpP)
Angewandte Chemie - International Edition, 2018AbstractCaseinolytic protease P (ClpP) is the proteolytic component of the ClpXP protein degradation complex. Eukaryotic ClpP was recently found to act within the mitochondria‐specific unfolded protein response (UPRmt). However, its detailed function and dedicated regulation remain largely unexplored.
Matthias Stahl +2 more
exaly +3 more sources
Substrates and interactors of the ClpP protease in the mitochondria
Current Opinion in Chemical Biology, 2022 The ClpP protease is found across eukaryotic and prokaryotic organisms. It is well-characterized in bacteria where its function is important in maintaining protein homeostasis. Along with its ATPase partners, it has been shown to play critical roles in the regulation of enzymes involved in important cellular pathways.
Walid A Houry
exaly +3 more sources
The activated ClpP peptidase forcefully grips a protein substrate
Biophysical Journal, 2022ATPases associated with diverse cellular activities (AAA+) proteases power the maintenance of protein homeostasis by coupling ATP hydrolysis to mechanical protein unfolding, translocation, and ultimately degradation. Although ATPase activity drives a large portion of the mechanical work these molecular machines perform, how the peptidase contributes to
Steven D, Walker, Adrian O, Olivares
openaire +2 more sources
Barrel-shaped ClpP Proteases Display Attenuated Cleavage Specificities
ACS Chemical Biology, 2015ClpP is a self-compartmentalizing protease with crucial roles in bacterial and mitochondrial protein quality control. Although the ClpP homocomplex is composed of 14 equivalent active sites, it degrades a multitude of substrates to small peptides, demonstrating its capability to carry out diverse cleavage reactions.
Malte, Gersch +6 more
openaire +2 more sources
The ClpP Peptidase Forcefully Grips Protein Substrates
2022ABSTRACTATPases Associated with diverse cellular Activities (AAA+) proteases power the maintenance of protein homeostasis by coupling ATP hydrolysis to mechanical protein unfolding, translocation, and ultimately degradation. Though ATPase activity drives a large portion of the mechanical work these molecular machines perform, how the peptidase ...
Steven D. Walker, Adrian O. Olivares
openaire +1 more source
Characterization of mouse Clpp protease cDNA, gene, and protein
Mammalian Genome, 2000Mutations that cause accumulation or rapid degradation owing to protein misfolding are a frequent cause of inherited disease in humans. In Escherichia coli, Clpp protease is one of the components of the protein quality control system that handles misfolded proteins.
Andresen, B S +7 more
openaire +3 more sources