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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

ClpX caseinolytic peptidase X homolog

Top mentioned proteins: ClpP, Clp, ATPase, CAN, TBX22
Papers on ClpX
Mitochondrial ClpP activity is required for cisplatin resistance in human cells.
Maurizi et al., Bethesda, United States. In Biochim Biophys Acta, Feb 2016
In human cells ClpP and ClpX are imported into the mitochondrial matrix, where they interact to form the ATP-dependent protease ClpXP and play a role in the mitochondrial unfolded protein response.
Mechanistic insights into bacterial AAA+ proteases and protein-remodelling machines.
Sauer et al., Cambridge, United States. In Nat Rev Microbiol, Jan 2016
In this Review, we discuss the structural and mechanistic features of AAA+ proteases and remodelling machines, focusing on the bacterial ClpXP and ClpX as paradigms.
Reversible Inhibitors Arrest ClpP in a Defined Conformational State that Can Be Revoked by ClpX Association.
Sieber et al., Garching bei München, Germany. In Angew Chem Int Ed Engl, Jan 2016
Strikingly, the conformational lock is overturned by binding of ClpX, an associated chaperone that enables proteolysis by substrate unfolding in the ClpXP complex.
Contributions of tropodithietic acid and biofilm formation to the probiotic activity of Phaeobacter inhibens.
Nelson et al., United States. In Bmc Microbiol, Dec 2015
RESULTS: Mutations in clpX (ATP-dependent ATPase) and exoP (an exopolysaccharide biosynthesis gene) were created by insertional mutagenesis using homologous recombination.
Stepwise decrease in daptomycin susceptibility in clinical Staphylococcus aureus isolates associated with an initial mutation in rpoB and a compensatory inactivation of the clpX gene.
Frees et al., Frederiksberg, Denmark. In Antimicrob Agents Chemother, Nov 2015
A subsequently acquired loss-of-function mutation in clpX partly alleviated the growth defect conferred by the rpoB mutation without changing antibiotic susceptibility.
Dissection of Axial-Pore Loop Function during Unfolding and Translocation by a AAA+ Proteolytic Machine.
Sauer et al., Cambridge, United States. In Cell Rep, Sep 2015
In the axial channels of ClpX and related hexameric AAA+ protein-remodeling rings, the pore-1 loops are thought to play important roles in engaging, mechanically unfolding, and translocating protein substrates.
Mitochondrial ClpX Activates a Key Enzyme for Heme Biosynthesis and Erythropoiesis.
Baker et al., Cambridge, United States. In Cell, Jun 2015
Among these chaperones is the AAA+ unfoldase ClpX, an important regulator of prokaryotic physiology with poorly defined function in the eukaryotic mitochondrion.
Transposon Mutagenesis Identifies Novel Genes Associated with Staphylococcus aureus Persister Formation.
Zhang et al., Shanghai, China. In Front Microbiol, 2014
We found 13 insertion mutants with significantly lower persister numbers under several stress conditions, including sdhA, sdhB, ureG, mnhG1, fbaA, ctaB, clpX, parE, HOU_0223, HOU_0587, HOU_2091, HOU_2315, and HOU_2346, which mapped into pathways of oxidative phosphorylation, TCA cycle, glycolysis, cell cycle, and ABC transporters, suggesting that these genes and pathways may play an important role in persister formation and survival.
Stochastic but highly coordinated protein unfolding and translocation by the ClpXP proteolytic machine.
Sauer et al., Nashville, United States. In Cell, 2014
We also present a mechanochemical model that accounts for single-molecule, biochemical, and structural results for our observation of enzymatic memory in translocation stepping, for the kinetics of translocation steps of different sizes, and for probabilistic but highly coordinated subunit activity within the ClpX ring.
Nucleotide binding and conformational switching in the hexameric ring of a AAA+ machine.
Sauer et al., Cambridge, United States. In Cell, 2013
ClpX, a AAA+ ring homohexamer, uses the energy of ATP binding and hydrolysis to power conformational changes that unfold and translocate target proteins into the ClpP peptidase for degradation.
Unfoldase-mediated protein translocation through an α-hemolysin nanopore.
Akeson et al., Santa Cruz, United States. In Nat Biotechnol, 2013
Here we describe controlled unfolding and translocation of proteins through the α-hemolysin (α-HL) pore using the AAA+ unfoldase ClpX.
ClpP: a structurally dynamic protease regulated by AAA+ proteins.
Ortega et al., Hamilton, Canada. In J Struct Biol, 2012
These enzymes assemble in complexes that combine the protease ClpP and the unfoldase, ClpA or ClpX.
ClpXP, an ATP-powered unfolding and protein-degradation machine.
Sauer et al., Cambridge, United States. In Biochim Biophys Acta, 2012
ClpXP consists of hexamers of a AAA+ ATPase (ClpX) and a tetradecameric peptidase (ClpP).
Structural and functional analysis of proteins by high-speed atomic force microscopy.
Sugiyama et al., Kyoto, Japan. In Adv Protein Chem Struct Biol, 2011
In this chapter, we describe the HS-AFM analysis of the dynamic molecular processes in photoactivated bacteriorhodopsin, membrane-mediated protein-protein interactions, ATP-induced conformational changes in purinergic receptors, the two-dimensional crystal structure of streptavidin, the nature of FtsZ polymers, the role of ClpX in the regulation of FtsZ polymer dynamics, the function of restriction enzymes, the action of motor proteins, the movement of TrCel7A on crystalline cellulose substrates, and the antimicrobial peptide activity on individual bacterial cells.
[Bacterial ClpX protease structure and function--a review].
Xie et al., Chongqing, China. In Wei Sheng Wu Xue Bao, 2010
ClpX is a member of Hsp100 (heat-shock protein) family which is conserved among organisms.
Diverse pore loops of the AAA+ ClpX machine mediate unassisted and adaptor-dependent recognition of ssrA-tagged substrates.
Sauer et al., Cambridge, United States. In Mol Cell, 2008
Results reveal that the ssrA tag interacts with different loops that form the top, middle, and lower portions of the central channel of the ClpX hexamer.
Human mitochondrial ClpP is a stable heptamer that assembles into a tetradecamer in the presence of ClpX.
Maurizi et al., Bethesda, United States. In J Biol Chem, 2005
hClpX can regulate the appearance of hClpP peptidase activity in mitochondria and might affect the nature of the degradation products released during ATP-dependent proteolytic cycles
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