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

ClpB caseinolytic peptidase B homolog

ClpB, SKD3
mouse homolog is a putative ATPase and member of the Clp/HSP104 family [RGD, Feb 2006] (from NCBI)
Top mentioned proteins: ATPase, HSP70, CAN, Clp, ACID
Papers on ClpB
ClpB N-terminal domain plays a regulatory role in protein disaggregation.
New
Kay et al., Toronto, Canada. In Proc Natl Acad Sci U S A, Jan 2016
ClpB/Hsp100 is an ATP-dependent disaggregase that solubilizes and reactivates protein aggregates in cooperation with the DnaK/Hsp70 chaperone system.
Gut Commensal E. coli Proteins Activate Host Satiety Pathways following Nutrient-Induced Bacterial Growth.
New
Impact
Fetissov et al., Rouen, France. In Cell Metab, Dec 2015
ClpB, a bacterial protein mimetic of α-MSH, was upregulated in the E. coli stationary phase, was detected in plasma proportional to ClpB DNA in feces, and stimulated firing rate of hypothalamic POMC neurons.
A fragment of the Escherichia coli ClpB heat-shock protein is a micromolar melanocortin 1 receptor agonist.
New
Haskell-Luevano et al., Minneapolis, United States. In Bioorg Med Chem Lett, Dec 2015
The Escherichia coli heat shock protein ClpB has previously been described as an antigen mimetic to the endogenous melanocortin agonist α-MSH.
Characterization of 5'UTR of rice ClpB-C/Hsp100 gene: evidence of its involvement in post-transcriptional regulation.
New
Grover et al., New Delhi, India. In Cell Stress Chaperones, Dec 2015
UNASSIGNED: Rice (Oryza sativa) ClpB-C (OsClpB-C) protein is expressed upon heat stress in vegetative tissues and constitutively in seeds.
Role of DnaK in HspR-HAIR interaction of Mycobacterium tuberculosis.
New
Batra et al., New Delhi, India. In Iubmb Life, Nov 2015
HspR is a negative regulator of expression of hsps, DnaK, ClpB, and Acr2 in M. tuberculosis.
Chaperone-assisted protein aggregate reactivation: Different solutions for the same problem.
Review
New
Muga et al., Bilbao, Spain. In Arch Biochem Biophys, Sep 2015
The oligomeric AAA+ chaperones Hsp104 in yeast and ClpB in bacteria are responsible for the reactivation of aggregated proteins, an activity essential for cell survival during severe stress.
Disaggregases, molecular chaperones that resolubilize protein aggregates.
Review
New
Ramos et al., Campinas, Brazil. In An Acad Bras Cienc, Aug 2015
The latter is a function of disaggregases, mainly represented by the ClpB/Hsp104 subfamily of molecular chaperones, that are ubiquitous in all organisms but, surprisingly, have no orthologs in the cytosol of metazoan cells.
Analysis of Linked Equilibria.
Lucius et al., Birmingham, United States. In Methods Enzymol, 2014
We have been studying two example members, Escherichia coli ClpA and ClpB.
Cooperation of Hsp70 and Hsp100 chaperone machines in protein disaggregation.
Review
Bukau et al., Heidelberg, Germany. In Front Mol Biosci, 2014
To counteract protein aggregation, bacteria, fungi, and plants encode a bi-chaperone system composed of ATP-dependent Hsp70 and hexameric Hsp100 (ClpB/Hsp104) chaperones, which rescue aggregated proteins and provide thermotolerance to cells.
PTEX component HSP101 mediates export of diverse malaria effectors into host erythrocytes.
Impact
Goldberg et al., Saint Louis, United States. In Nature, 2014
Here we show that export across the PVM requires heat shock protein 101 (HSP101), a ClpB-like AAA+ ATPase component of PTEX.
Structural mechanisms of chaperone mediated protein disaggregation.
Review
Sousa, San Antonio, United States. In Front Mol Biosci, 2013
The ClpB/Hsp104 and Hsp70 classes of molecular chaperones use ATP hydrolysis to dissociate protein aggregates and complexes, and to move proteins through membranes.
[Mycoplasma heat shock proteins and their genes].
Review
Borkhsenius et al., In Mikrobiologiia, 2013
Properties and functions of the most completely characterized mycoplasmal HSP are discussed: DnaK, DnaJ-like, GroEL/GroES, ClpB, and small heat shock proteins (sHSP).
Unraveling the mechanism of protein disaggregation through a ClpB-DnaK interaction.
Impact
Kay et al., Toronto, Canada. In Science, 2013
HSP-100 protein machines, such as ClpB, play an essential role in reactivating protein aggregates that can otherwise be lethal to cells.
Operational plasticity enables hsp104 to disaggregate diverse amyloid and nonamyloid clients.
Impact
Shorter et al., Philadelphia, United States. In Cell, 2012
Unexpectedly, prokaryotic ClpB subunits collaborate differently than Hsp104 and couple probabilistic substrate binding to cooperative ATP hydrolysis, which enhances disordered aggregate dissolution but sensitizes ClpB to inhibition and diminishes amyloid disaggregation.
DnaK-mediated association of ClpB to protein aggregates. A bichaperone network at the aggregate surface.
GeneRIF
Muga et al., Bilbao, Spain. In Febs Lett, 2009
formation of the DnaK-ClpB bichaperone network is a three step process
Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments.
GeneRIF
Bukau et al., Heidelberg, Germany. In Nat Struct Mol Biol, 2008
ClpB-DnaK reactivated all aggregated fusion proteins with similar efficiency, without unfolding native domains, demonstrating that partial threading of the misfolded moiety is sufficient to solubilize aggregates.
Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB.
Impact
Bukau et al., Heidelberg, Germany. In Cell, 2004
Cell survival under severe thermal stress requires the activity of the ClpB (Hsp104) AAA+ chaperone that solubilizes and reactivates aggregated proteins in concert with the DnaK (Hsp70) chaperone system.
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