Variant-specific [PSI+] infection is transmitted by Sup35 polymers within [PSI+] aggregates with heterogeneous protein composition
about
Amyloid-mediated sequestration of essential proteins contributes to mutant huntingtin toxicity in yeastModulation and elimination of yeast prions by protein chaperones and co-chaperonesAmyloid cannot resist identificationDifferences in the curing of [PSI+] prion by various methods of Hsp104 inactivationPrion Aggregates Are Recruited to the Insoluble Protein Deposit (IPOD) via Myosin 2-Based Vesicular TransportMolecular chaperones and stress-inducible protein-sorting factors coordinate the spatiotemporal distribution of protein aggregates.Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions.The Hsp70 homolog Ssb is essential for glucose sensing via the SNF1 kinase networkYeast prions are useful for studying protein chaperones and protein quality controlAmyloid-associated activity contributes to the severity and toxicity of a prion phenotypeHeterologous cross-seeding mimics cross-species prion conversion in a yeast model.Sensitivity-enhanced NMR reveals alterations in protein structure by cellular milieusGPI anchoring facilitates propagation and spread of misfolded Sup35 aggregates in mammalian cells.Heritable yeast prions have a highly organized three-dimensional architecture with interfiber structures.Disease-associated mutant ubiquitin causes proteasomal impairment and enhances the toxicity of protein aggregates.Prion dynamics and the quest for the genetic determinant in protein-only inheritanceOverexpression of the essential Sis1 chaperone reduces TDP-43 effects on toxicity and proteolysis.Interdependence of amyloid formation in yeast: implications for polyglutamine disorders and biological functions.Analyzing the birth and propagation of two distinct prions, [PSI+] and [Het-s](y), in yeast.[SWI], the prion formed by the chromatin remodeling factor Swi1, is highly sensitive to alterations in Hsp70 chaperone system activity.In vivo monitoring of the prion replication cycle reveals a critical role for Sis1 in delivering substrates to Hsp104The effect of red pigment on the amyloidization of yeast proteins.Prion formation and polyglutamine aggregation are controlled by two classes of genes.In vivo evidence for the fibrillar structures of Sup35 prions in yeast cells.Prion-promoted phosphorylation of heterologous amyloid is coupled with ubiquitin-proteasome system inhibition and toxicity.Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humansHsp40s specify functions of Hsp104 and Hsp90 protein chaperone machines.Defining the limits: Protein aggregation and toxicity in vivoHeterologous gln/asn-rich proteins impede the propagation of yeast prions by altering chaperone availabilityTrans-species activity of a nonself recognition domain.Spatial quality control bypasses cell-based limitations on proteostasis to promote prion curing.Suicidal [PSI+] is a lethal yeast prion.Dominant prion mutants induce curing through pathways that promote chaperone-mediated disaggregation.Destabilization and recovery of a yeast prion after mild heat shock.Functional diversification of hsp40: distinct j-protein functional requirements for two prions allow for chaperone-dependent prion selectionHeterologous aggregates promote de novo prion appearance via more than one mechanism.Prion aggregate structure in yeast cells is determined by the Hsp104-Hsp110 disaggregase machinery.Prions in yeast.Prion-Associated Toxicity is Rescued by Elimination of Cotranslational Chaperones.Study of amyloids using yeast
P2860
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P2860
Variant-specific [PSI+] infection is transmitted by Sup35 polymers within [PSI+] aggregates with heterogeneous protein composition
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Variant-specific [PSI+] infect ...... erogeneous protein composition
@ast
Variant-specific [PSI+] infect ...... erogeneous protein composition
@en
type
label
Variant-specific [PSI+] infect ...... erogeneous protein composition
@ast
Variant-specific [PSI+] infect ...... erogeneous protein composition
@en
prefLabel
Variant-specific [PSI+] infect ...... erogeneous protein composition
@ast
Variant-specific [PSI+] infect ...... erogeneous protein composition
@en
P2860
P356
P1476
Variant-specific [PSI+] infect ...... erogeneous protein composition
@en
P2093
Janet E Richmond
Susan W Liebman
P2860
P304
P356
10.1091/MBC.E08-01-0078
P577
2008-03-19T00:00:00Z