Results 171 to 180 of about 13,032 (201)
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The Role of ClpP in Protein Expression of Streptococcus pneumoniae
Current Microbiology, 2011Previous reports suggest that ClpP proteolytic activity is important not only for cell physiology but also for regulation of virulence properties of Streptococcus pneumoniae (S. pneumoniae). In order to get a more comprehensive picture of the role of ClpP protease on protein expression in S. pneumoniae D39 and how it relates to physiology and virulence,
Qun, Zhang +6 more
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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
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Polyphasic studies that used phospholipid fatty acid analysis (PLFA) in conjunction with community level physiological profiling (CLPP) or PCR-based molecular methods were analyzed in order to evaluate the power of each strategy to detect treatment ...
Matthias C. Rillig +2 more
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Mechanism of Allosteric Activation in Human Mitochondrial ClpP Protease
Abstract Human ClpP protease contributes to mitochondrial protein quality control by degrading misfolded proteins. ClpP is overexpressed in cancers such as acute myeloid leukemia (AML), where its inhibition leads to the accumulation of damaged respiratory chain subunits and cell death.
Siavash Vahidi +2 more
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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.
John A, Alexopoulos +2 more
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The Structural Basis for the Activation and Peptide Recognition of Bacterial ClpP
Journal of Molecular Biology, 2008ClpP and its ATPase compartment, ClpX or ClpA, remove misfolded proteins in cells and are of utmost importance in protein quality control. The ring hexamers of ClpA or ClpX recognize, unfold, and translocate target substrates into the degradation chamber of the double-ring tetradecamer of ClpP.
Dong Young, Kim, Kyeong Kyu, Kim
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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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Role of ClpP in biofilm formation and virulence of Staphylococcus epidermidis
Microbes and Infection, 2007Infections caused by the leading nosocomial pathogen Staphylococcus epidermidis are characterized by biofilm formation on implanted medical devices. However, the molecular basis of biofilm formation and its regulation are not completely understood.
Chongzhen, Wang +6 more
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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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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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