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ClpP: A structurally dynamic protease regulated by AAA+ proteins
Journal of Structural Biology, 2012Proteolysis is an important process for many aspects of bacterial physiology. Clp proteases carry out a large proportion of protein degradation in bacteria. These enzymes assemble in complexes that combine the protease ClpP and the unfoldase, ClpA or ClpX.
Joaquin Ortega, Alba Guarné
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A novel class of Plasmodial ClpP protease inhibitors as potential antimalarial agents
Bioorganic and Medicinal Chemistry, 2017The prokaryotic ATP-dependent ClpP protease, localized in the relict plastid of malaria parasite, represents a potential drug target. In the present study, we utilized in silico structure-based screening and medicinal chemistry approaches to identify a novel pyrimidine series of compounds inhibiting P.
Asif Mohmmed +2 more
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The Mechanism of Caseinolytic Protease (ClpP) Inhibition
Angewandte Chemie - International Edition, 2013Christian Hedberg +2 more
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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
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The development of small-molecule modulators for ClpP protease activity
Molecular BioSystems, 2016Abstract The global spread of antibiotic resistance among important human pathogens emphasizes the need to find new antibacterial drugs with a novel mode of action. The ClpP protease has been shown to demonstrate its pivotal importance to both the survival and the virulence of pathogenic bacteria during host infection.
Fei, Ye, Jiahui, Li, Cai-Guang, Yang
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The Role of ClpP Protease in Bacterial Pathogenesis and Human Diseases
ACS Chemical Biology, 2018In prokaryotic cells and eukaryotic organelles, the ClpP protease plays an important role in proteostasis. The disruption of the ClpP function has been shown to influence the infectivity and virulence of a number of bacterial pathogens. More recently, ClpP has been found to be involved in various forms of carcinomas and in Perrault syndrome, which is ...
Vaibhav Bhandari +5 more
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Mitochondrial protease ClpP supplementation ameliorates diet-induced NASH in mice
Journal of Hepatology, 2022Mitochondrial dysfunction is considered a pathogenic linker in the development of non-alcoholic steatohepatitis (NASH). Inappropriate mitochondrial protein-quality control, possibly induced by insufficiency of the mitochondrial matrix caseinolytic protease P (ClpP), can potentially cause mitochondrial dysfunction.
Sung-E Choi +13 more
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Human ClpP protease, a promising therapy target for diseases of mitochondrial dysfunction
Drug Discovery Today, 2021Human caseinolytic protease P (HsClpP), an ATP-dependent unfolding peptidase protein in the mitochondrial matrix, controls protein quality, regulates mitochondrial metabolism, and maintains the integrity and enzyme activity of the mitochondrial respiratory chain (RC).
Baozhu Luo +4 more
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Journal of the American Chemical Society, 2013
Over 100 protease inhibitors are currently used in the clinics, and most of them use blockage of the active site for their mode of inhibition. Among the protease drug targets are several enzymes for which the correct multimeric assembly is crucial to their activity, such as the proteasome and the HIV protease.
Malte Gersch +4 more
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Over 100 protease inhibitors are currently used in the clinics, and most of them use blockage of the active site for their mode of inhibition. Among the protease drug targets are several enzymes for which the correct multimeric assembly is crucial to their activity, such as the proteasome and the HIV protease.
Malte Gersch +4 more
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
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