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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Control of substrate gating and translocation into ClpP by channel residues and ClpX binding [PDF]
, 2010 ClpP is a self-compartmentalized protease, which has very limited degradation activity unless it associates with ClpX to form ClpXP or with ClpA to form ClpAP.
Barkow +60 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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Crystal structure of Mycobacterium tuberculosis ClpP1P2 suggests a model for peptidase activation by AAA+ partner binding and substrate delivery [PDF]
, 2014 Caseinolytic peptidase P (ClpP), a double-ring peptidase with 14 subunits, collaborates with ATPases associated with diverse activities (AAA+) partners to execute ATP-dependent protein degradation.
Carney, Daniel W. +3 more
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Mitochondrial Quality Control in Age-Related Pulmonary Fibrosis. [PDF]
, 2020 Idiopathic pulmonary fibrosis (IPF) is age-related interstitial lung disease of unknown etiology. About 100,000 people in the U.S have IPF, with a 3-year median life expectancy post-diagnosis.
Cuevas-Mora, Karina +2 more
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Protein purification to analyze AAA+ proteolytic machine in vitro [PDF]
, 2011 The ATP-dependent ClpXP protease of Escherichia coli consists of two subunits, the ClpP subunit, which has the proteolytic activity and the AAA+ motor ClpX, which mechanically unfolds and translocates substrates for ClpP degradation.
Rojas, Diego F.
core +2 more sources
Highly Dynamic Interactions Maintain Kinetic Stability of the ClpXP Protease During the ATP-Fueled Mechanical Cycle [PDF]
, 2016 The ClpXP protease assembles in a reaction in which an ATP-bound ring hexamer of ClpX binds to one or both heptameric rings of the ClpP peptidase. Contacts between ClpX IGF-loops and clefts on a ClpP ring stabilize the complex.
Amor, Alvaro Jorge +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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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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