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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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Dynamics of the ClpP serine protease: A model for self-compartmentalized proteases
Critical Reviews in Biochemistry and Molecular Biology, 2014ClpP is a highly conserved serine protease present in most bacterial species and in the mitochondria of mammalian cells. It forms a cylindrical tetradecameric complex arranged into two stacked heptamers. The two heptameric rings of ClpP enclose a roughly spherical proteolytic chamber of about 51 Å in diameter with 14 Ser-His-Asp proteolytic active ...
Kaiyin, Liu +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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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 development of small-molecule modulators for ClpP protease activity
Molecular BioSystems, 2017Deregulating ClpP activity either through inhibition or overactivation could lead to antibacterial activity.
Fei, Ye, Jiahui, Li, Cai-Guang, Yang
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Selektive Aktivierung der humanen caseinolytischen Protease P (ClpP)
Angewandte Chemie, 2018AbstractDie caseinolytische Protease P (ClpP) ist die proteolytische Komponente des Protein‐Abbau‐Komplexes ClpXP. Ihre genaue Funktion und Regulation sind größtenteils unerforscht. Hier stellen wir eine niedermolekulare Verbindung (D9) vor, die durch Nachahmung des natürlichen Chaperons ClpX als potenter und Spezies‐selektiver Aktivator der humanen ...
Matthias Stahl +9 more
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P-104: Targeting the mitochondrial protease CLPP in Multiple Myeloma
Clinical Lymphoma Myeloma and Leukemia, 2021Background Mitochondria are enticing potential targets against cancer, owing to their role as signaling hubs orchestrating key homeostatic functions. Of special interest is ClpP, a resident mitochondrial protease suggested to maintain OXPHOS by degrading damaged protein components and regulating the assembly of mito-ribosomes.
Tommaso Perini +9 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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A pH-Dependent Conformational Switch Controls N. meningitidis ClpP Protease Function
Journal of the American Chemical Society, 2020ClpPs are a conserved family of serine proteases that collaborate with ATP-dependent translocases to degrade protein substrates. Drugs targeting these enzymes have attracted interest for the treatment of cancer and bacterial infections due to their critical role in mitochondrial and bacterial proteostasis, respectively.
Zev A. Ripstein +3 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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