The elusive middle domain of Hsp104 and ClpB: location and function.
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Engineering and Evolution of Molecular Chaperones and Protein Disaggregases with Enhanced ActivityPrion-like domains as epigenetic regulators, scaffolds for subcellular organization, and drivers of neurodegenerative diseaseDisaggregases, molecular chaperones that resolubilize protein aggregatesThe Molecular Mechanism of Hsp100 Chaperone Inhibition by the Prion Curing Agent Guanidinium ChlorideHead-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregationFundamental Characteristics of AAA+ Protein Family Structure and FunctionEngineering enhanced protein disaggregases for neurodegenerative diseaseAggregate-reactivation activity of the molecular chaperone ClpB from Ehrlichia chaffeensisSuramin inhibits Hsp104 ATPase and disaggregase activityCharacterization of the molecular chaperone ClpB from the pathogenic spirochaete Leptospira interrogansThe tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease.Serine integrase chimeras with activity in E. coli and HeLa cells.The Symbiotic Performance of Chickpea Rhizobia Can Be Improved by Additional Copies of the clpB Chaperone GeneFunctional analysis of conserved cis- and trans-elements in the Hsp104 protein disaggregating machineReactivation of Aggregated Proteins by the ClpB/DnaK Bi-Chaperone System.Mechanistic Insights into Hsp104 Potentiation.Engineering therapeutic protein disaggregases.Differential Regulation of Genes Coding for Organelle and Cytosolic ClpATPases under Biotic and Abiotic Stresses in Wheat.Conserved distal loop residues in the Hsp104 and ClpB middle domain contact nucleotide-binding domain 2 and enable Hsp70-dependent protein disaggregation.ATP-driven molecular chaperone machines.ClpB/Hsp100 proteins and heat stress tolerance in plants.Mechanistic and Structural Insights into the Prion-Disaggregase Activity of Hsp104.Repurposing Hsp104 to Antagonize Seminal Amyloid and Counter HIV Infection.Yeast proteinopathy models: a robust tool for deciphering the basis of neurodegeneration.Reversing deleterious protein aggregation with re-engineered protein disaggregases.Regulation of the Hsp104 middle domain activity is critical for yeast prion propagation.Potentiated Hsp104 variants antagonize diverse proteotoxic misfolding events.Human TorsinA can function in the yeast cytosol as a molecular chaperone.Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation.The metazoan protein disaggregase and amyloid depolymerase system: Hsp110, Hsp70, Hsp40, and small heat shock proteins.Mechanically Watching the ClpXP Proteolytic Machinery.Isolation and Identification of Putative Protein Substrates of the AAA+ Molecular Chaperone ClpB from the Pathogenic Spirochaete Leptospira interrogans.Comparative roles of clpA and clpB in the survival of S. Typhimurium under stress and virulence in poultry.
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P2860
The elusive middle domain of Hsp104 and ClpB: location and function.
description
article científic
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article scientifique
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articol științific
@ro
articolo scientifico
@it
artigo científico
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artigo científico
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artigo científico
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artikel ilmiah
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artikull shkencor
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artículo científico
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name
The elusive middle domain of Hsp104 and ClpB: location and function.
@en
The elusive middle domain of Hsp104 and ClpB: location and function.
@nl
type
label
The elusive middle domain of Hsp104 and ClpB: location and function.
@en
The elusive middle domain of Hsp104 and ClpB: location and function.
@nl
prefLabel
The elusive middle domain of Hsp104 and ClpB: location and function.
@en
The elusive middle domain of Hsp104 and ClpB: location and function.
@nl
P2860
P1476
The elusive middle domain of Hsp104 and ClpB: location and function
@en
P2093
Morgan E Desantis
P2860
P356
10.1016/J.BBAMCR.2011.07.014
P407
P577
2011-07-24T00:00:00Z