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Engineering and Evolution of Molecular Chaperones and Protein Disaggregases with Enhanced ActivityEngineering enhanced protein disaggregases for neurodegenerative diseaseSuramin inhibits Hsp104 ATPase and disaggregase activityHeat shock proteins: cellular and molecular mechanisms in the central nervous system.The Surprising Role of Amyloid Fibrils in HIV InfectionThe mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free systemPotentiated Hsp104 variants suppress toxicity of diverse neurodegenerative disease-linked proteins.The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease.Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humansHsp104 suppresses polyglutamine-induced degeneration post onset in a drosophila MJD/SCA3 model.Isolating potentiated Hsp104 variants using yeast proteinopathy modelsInsight into molecular basis of curing of [PSI+] prion by overexpression of 104-kDa heat shock protein (Hsp104).Dictyostelium discoideum has a highly Q/N-rich proteome and shows an unusual resilience to protein aggregation.Swa2, the yeast homolog of mammalian auxilin, is specifically required for the propagation of the prion variant [URE3-1].Mechanistic Insights into Hsp104 Potentiation.Biochemical characterization of protein quality control mechanisms during disease progression in the C22 mouse model of CMT1A.Emergence and natural selection of drug-resistant prions.Mechanisms of amyloid fibril formation--focus on domain-swapping.The elusive middle domain of Hsp104 and ClpB: location and function.Mechanistic and Structural Insights into the Prion-Disaggregase Activity of Hsp104.Repurposing Hsp104 to Antagonize Seminal Amyloid and Counter HIV Infection.Expanding role of molecular chaperones in regulating α-synuclein misfolding; implications in Parkinson's disease.Yeast proteinopathy models: a robust tool for deciphering the basis of neurodegeneration.RNA-binding proteins with prion-like domains in health and disease.Prion formation by a yeast GLFG nucleoporin.Purification of hsp104, a protein disaggregase.Prion-like disorders: blurring the divide between transmissibility and infectivity.Reversing deleterious protein aggregation with re-engineered protein disaggregases.Countering amyloid polymorphism and drug resistance with minimal drug cocktails.Operational plasticity enables hsp104 to disaggregate diverse amyloid and nonamyloid clients.Global stress response in a prokaryotic model of DJ-1-associated Parkinsonism.A new perspective on Hsp104-mediated propagation and curing of the yeast prion [PSI (+) ].A non-transcriptional role for the glucocorticoid receptor in mediating the cell stress response.Surface adsorption considerations when working with amyloid fibrils in multiwell plates and Eppendorf tubesDisparate Mutations Confer Therapeutic Gain of Hsp104 Function.The metazoan protein disaggregase and amyloid depolymerase system: Hsp110, Hsp70, Hsp40, and small heat shock proteins.Variant-specific and reciprocal Hsp40 functions in Hsp104-mediated prion elimination.Dehydrins in maritime pine (Pinus pinaster) and their expression related to drought stress responseAmyloid assembly and disassemblyStudying Huntington's Disease in Yeast: From Mechanisms to Pharmacological Approaches
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description
article científic
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article scientifique
@fr
articolo scientifico
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artigo científico
@pt
bilimsel makale
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scientific article published on February 2010
@en
vedecký článok
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vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
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name
Applying Hsp104 to protein-misfolding disorders.
@en
Applying Hsp104 to protein-misfolding disorders.
@nl
type
label
Applying Hsp104 to protein-misfolding disorders.
@en
Applying Hsp104 to protein-misfolding disorders.
@nl
prefLabel
Applying Hsp104 to protein-misfolding disorders.
@en
Applying Hsp104 to protein-misfolding disorders.
@nl
P2860
P356
P1476
Applying Hsp104 to protein-misfolding disorders
@en
P2093
Mimi Cushman
Shilpa Vashist
P2860
P356
10.1139/O09-121
P577
2010-02-01T00:00:00Z