about
GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system.Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALSSequential tethering of Golgins and catalysis of SNAREpin assembly by the vesicle-tethering protein p115A direct role for GRASP65 as a mitotically regulated Golgi stacking factorPhosphorylation of the vesicle-tethering protein p115 by a casein kinase II-like enzyme is required for Golgi reassembly from isolated mitotic fragmentsEngineering and Evolution of Molecular Chaperones and Protein Disaggregases with Enhanced ActivityPrion-like domains as epigenetic regulators, scaffolds for subcellular organization, and drivers of neurodegenerative diseaseChaperones in NeurodegenerationDiscovery and characterization of an endogenous CXCR4 antagonistSpiral architecture of the Hsp104 disaggregase reveals the basis for polypeptide translocationHsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions.Engineering enhanced protein disaggregases for neurodegenerative diseasePrions as adaptive conduits of memory and inheritanceSuramin inhibits Hsp104 ATPase and disaggregase activityThe Hsp104 N-terminal domain enables disaggregase plasticity and potentiationHsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities.The Surprising Role of Amyloid Fibrils in HIV InfectionMembrane traffic: do cones mark sites of fission?Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLSThe 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.Fission yeast does not age under favorable conditions, but does so after stress.Hsp104 suppresses polyglutamine-induced degeneration post onset in a drosophila MJD/SCA3 model.Isolating potentiated Hsp104 variants using yeast proteinopathy modelsA yeast functional screen predicts new candidate ALS disease genesA cellular system that degrades misfolded proteins and protects against neurodegenerationA molecular tweezer antagonizes seminal amyloids and HIV infection.Epigallocatechin-3-gallate rapidly remodels PAP85-120, SEM1(45-107), and SEM2(49-107) seminal amyloid fibrils.Hsp104 drives "protein-only" positive selection of Sup35 prion strains encoding strong [PSI(+)].Inhibition of RNA lariat debranching enzyme suppresses TDP-43 toxicity in ALS disease modelsMechanistic Insights into Hsp104 Potentiation.Direct and selective elimination of specific prions and amyloids by 4,5-dianilinophthalimide and analogsStress granules as crucibles of ALS pathogenesis.Hsp104 antagonizes alpha-synuclein aggregation and reduces dopaminergic degeneration in a rat model of Parkinson diseaseEngineering therapeutic protein disaggregases.Hsp104: a weapon to combat diverse neurodegenerative disorders.Prion proteostasis: Hsp104 meets its supporting castConserved distal loop residues in the Hsp104 and ClpB middle domain contact nucleotide-binding domain 2 and enable Hsp70-dependent protein disaggregation.N-terminal domains elicit formation of functional Pmel17 amyloid fibrils
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description
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
James Shorter
@ast
James Shorter
@en
James Shorter
@es
James Shorter
@nl
James Shorter
@sl
type
label
James Shorter
@ast
James Shorter
@en
James Shorter
@es
James Shorter
@nl
James Shorter
@sl
prefLabel
James Shorter
@ast
James Shorter
@en
James Shorter
@es
James Shorter
@nl
James Shorter
@sl
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P2798
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0000-0001-5269-8533