Crowding activates ClpB and enhances its association with DnaK for efficient protein aggregate reactivation.

scientific article

Crowding activates ClpB and enhances its association with DnaK for efficient protein aggregate reactivation. is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1016/J.BPJ.2014.03.042
P8608Fatcat IDrelease_c774jjr3tbhjvebds4ldndv7wa
P932PMC publication ID4017315
P698PubMed publication ID24806934
P5875ResearchGate publication ID262148107

P50authorGerman RivasQ59545857
Arturo MugaQ39715467
Carlos AlfonsoQ42649560
P2093author name stringFernando Moro
Garbiñe Celaya
Ianire Martín
P2860cites workEffects of macromolecular crowding on protein folding and aggregationQ24529974
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Structure, function, and folding of phosphoglycerate kinase are strongly perturbed by macromolecular crowdingQ28294869
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Macromolecular crowding extended to a heptameric system: the Co-chaperonin protein 10.Q30155628
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Conformational stability of the full-atom hexameric model of the ClpB chaperone from Escherichia coli.Q54399538
Effect of High Concentration of Inert Cosolutes on the Refolding of an EnzymeQ61174613
Evaluation of uncertainties for parameters in binding studies: the sum-of-squares profile and Monte Carlo estimationQ69595149
Purification and properties of the dnaJ replication protein of Escherichia coliQ69892745
Direct observation of the self-association of dilute proteins in the presence of inert macromolecules at high concentration via tracer sedimentation equilibrium: theory, experiment, and biological significanceQ78021416
A quantitative analysis of the effect of nucleotides and the M domain on the association equilibrium of ClpBQ83394361
DnaK-mediated association of ClpB to protein aggregates. A bichaperone network at the aggregate surfaceQ84447521
CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregationQ33929489
Analysis of heterogeneous interactionsQ34076334
Crowding effects on EcoRV kinetics and bindingQ34172022
How crowded is the cytoplasm?Q34268384
Molecular chaperone functions in protein folding and proteostasisQ34349321
Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB.Q34369100
Protein aggregation in crowded environments.Q34532811
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Quantitative characterization of polymer-polymer, protein-protein, and polymer-protein interaction via tracer sedimentation equilibriumQ36370509
Beyond the second virial coefficient: Sedimentation equilibrium in highly non-ideal solutionsQ36370518
Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperonesQ36390259
Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104.Q36398218
Quantitative assessment of the relative contributions of steric repulsion and chemical interactions to macromolecular crowding.Q36570261
Association equilibrium of the HIV-1 capsid protein in a crowded medium reveals that hexamerization during capsid assembly requires a functional C-domain dimerization interfaceQ36621915
Motor mechanism for protein threading through Hsp104.Q37209865
Impact of reconstituted cytosol on protein stability.Q37353199
Clp chaperone-proteases: structure and function.Q37592458
Hsp70 chaperone dynamics and molecular mechanismQ38135145
Molecular chaperones: avoiding the crowdQ41585985
Quantification of excluded volume effects on the folding landscape of Pseudomonas aeruginosa apoazurin in vitroQ42956128
Nucleotide utilization requirements that render ClpB active as a chaperoneQ43189809
Energetics of nucleotide-induced DnaK conformational statesQ43193112
Non-linear effects of macromolecular crowding on enzymatic activity of multi-copper oxidaseQ43236942
Requirement for GroEL/GroES-dependent protein folding under nonpermissive conditions of macromolecular crowdingQ43951834
Interdomain interaction through helices A and B of DnaK peptide binding domainQ44264738
Characterization of a trap mutant of the AAA+ chaperone ClpB.Q44477296
Development of a homogeneous fluorescence anisotropy assay to monitor and measure FtsZ assembly in solution.Q44478385
Non-ideal tracer sedimentation equilibrium: a powerful tool for the characterization of macromolecular interactions in crowded solutions.Q45054740
Solubilization of aggregated proteins by ClpB/DnaK relies on the continuous extraction of unfolded polypeptidesQ45181636
The heat-shock protein ClpB in Escherichia coli is a protein-activated ATPaseQ45232404
Unraveling the mechanism of protein disaggregation through a ClpB-DnaK interaction.Q46035197
Coupling and dynamics of subunits in the hexameric AAA+ chaperone ClpB.Q46699925
Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery.Q47239818
Screening and evaluation of small organic molecules as ClpB inhibitors and potential antimicrobialsQ47739500
Sedimentation equilibrium in a solution containing an arbitrary number of solute species at arbitrary concentrations: theory and application to concentrated solutions of ribonuclease.Q47884653
Physicochemical determinants of chaperone requirements.Q54387037
P433issue9
P407language of work or nameEnglishQ1860
P1104number of pages11
P304page(s)2017-2027
P577publication date2014-05-01
P1433published inBiophysical JournalQ2032955
P1476titleCrowding activates ClpB and enhances its association with DnaK for efficient protein aggregate reactivation
P478volume106

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cites work (P2860)
Q52324439Activation of the DnaK-ClpB Complex is Regulated by the Properties of the Bound Substrate.
Q41625613ClpB dynamics is driven by its ATPase cycle and regulated by the DnaK system and substrate proteins
Q40590160Stress Conditions Induced by Carvacrol and Cinnamaldehyde on Acinetobacter baumannii.
Q58554573The amino-terminal domain of ClpB protein plays a crucial role in its substrate disaggregation activity
Q27012942What macromolecular crowding can do to a protein