Results 31 to 40 of about 5,725 (156)
Frontiers in Cellular and Infection Microbiology, 2017 Biofilm causes hospital-associated infections on indwelling medical devices. In Staphylococcus aureus, Biofilm formation is controlled by intricately coordinated network of regulating systems, of which the ATP-dependent protease ClpP shows an inhibitory ...
Qian Liu +9 more
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Frontiers in Microbiology, 2021 The ClpX ATPase is critical for resistance to cell envelope targeting antibiotics in Bacillus anthracis, however, it is unclear whether this is due to its function as an independent chaperone or as part of the ClpXP protease.
Lang Zou +5 more
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Mitofusin-2 Down-Regulation Predicts Progression of Non-Muscle Invasive Bladder Cancer
Diagnostics, 2021 Identification of markers predicting disease outcome is a major clinical issue for non-muscle invasive bladder cancer (NMIBC). The present study aimed to determine the role of the mitochondrial proteins Mitofusin-2 (Mfn2) and caseinolytic protease P ...
Antonella Cormio +9 more
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Metabolic Perturbations in a Bacillus subtilis clpP Mutant during Glucose Starvation
Metabolites, 2017 Proteolysis is essential for all living organisms to maintain the protein homeostasis and to adapt to changing environmental conditions. ClpP is the main protease in Bacillus subtilis, and forms complexes with different Clp ATPases.
Daniel Schultz +3 more
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eLife, 2020 The ClpXP degradation machine consists of a hexameric AAA+ unfoldase (ClpX) and a pair of heptameric serine protease rings (ClpP) that unfold, translocate, and subsequently degrade client proteins.
Zev A Ripstein +4 more
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ClpP: A distinctive family of cylindrical energy‐dependent serine proteases
FEBS Letters, 2007 Processes maintaining protein homeostasis in the cell are governed by the activities of molecular chaperones that mainly assist in the folding of polypeptide chains and by a large class of proteases that regulate protein levels through degradation. ClpP proteases define a distinctive family of cylindrical, energy‐dependent serine proteases that are ...
Yu, Angela Yeou Hsiung, Houry, Walid A.
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Frontiers in Molecular Biosciences, 2021 Rising antibiotic resistance urgently calls for the discovery and evaluation of novel antibiotic classes and unique antibiotic targets. The caseinolytic protease Clp emerged as an unprecedented target for antibiotic therapy 15 years ago when it was ...
Heike Brötz-Oesterhelt +2 more
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ClpA mediates directional translocation of substrate proteins into the ClpP protease [PDF]
Proceedings of the National Academy of Sciences, 2001 The intracellular degradation of many proteins is mediated in an ATP-dependent manner by large assemblies comprising a chaperone ring complex associated coaxially with a proteolytic cylinder, e.g., ClpAP, ClpXP, and HslUV in prokaryotes, and the 26S proteasome in eukaryotes.
B G, Reid +3 more
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Mitochondrial ClpP serine protease-biological function and emerging target for cancer therapy [PDF]
Cell Death & Disease, 2020 AbstractMitochondrial ClpP is a serine protease located in the mitochondrial matrix. This protease participates in mitochondrial protein quality control by degrading misfolded or damaged proteins, thus maintaining normal metabolic function. Mitochondrial ClpP is a stable heptamer ring with peptidase activity that forms a multimeric complex with the ATP-
Kazem Nouri, Yue Feng, Aaron D. Schimmer
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Structural insights into the Clp protein degradation machinery
mBioThe Clp protease system is important for maintaining proteostasis in bacteria. It consists of ClpP serine proteases and an AAA+ Clp-ATPase such as ClpC1.
Xiaolong Xu +5 more
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