Chaperoning prions: the cellular machinery for propagating an infectious protein?
about
Prion switching in response to environmental stressA heritable switch in carbon source utilization driven by an unusual yeast prionActin, Membrane Trafficking and the Control of Prion Induction, Propagation and Transmission in YeastPotential roles for prions and protein-only inheritance in cancerHsp104-dependent remodeling of prion complexes mediates protein-only inheritanceProtein folding activity of ribosomal RNA is a selective target of two unrelated antiprion drugsUsing steered molecular dynamics to predict and assess Hsp70 substrate-binding domain mutants that alter prion propagationQualitative and quantitative multiplexed proteomic analysis of complex yeast protein fractions that modulate the assembly of the yeast prion Sup35pHeterologous prion interactions are altered by mutations in the prion protein Rnq1p.The Schizosaccharomyces pombe Hsp104 disaggregase is unable to propagate the [PSI] prion.Requirements of Hsp104p activity and Sis1p binding for propagation of the [RNQ(+)] prionGlobal transcript and phenotypic analysis of yeast cells expressing Ssa1, Ssa2, Ssa3 or Ssa4 as sole source of cytosolic Hsp70-Ssa chaperone activityUse of yeast as a system to study amyloid toxicity[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 Hsp104Assessment of inactivating stop codon mutations in forty Saccharomyces cerevisiae strains: implications for [PSI] prion- mediated phenotypes.Hsp40s specify functions of Hsp104 and Hsp90 protein chaperone machines.The prion hypothesis: from biological anomaly to basic regulatory mechanism.De novo appearance and "strain" formation of yeast prion [PSI+] are regulated by the heat-shock transcription factor.The sensitive [SWI (+)] prion: new perspectives on yeast prion diversity.Importance of the Hsp70 ATPase domain in yeast prion propagationMolecular chaperones and the assembly of the prion Ure2p in vitro.Strain conformation, primary structure and the propagation of the yeast prion [PSI+].Structural variants of yeast prions show conformer-specific requirements for chaperone activity.Variant-specific [PSI+] infection is transmitted by Sup35 polymers within [PSI+] aggregates with heterogeneous protein compositionInfluence of specific HSP70 domains on fibril formation of the yeast prion protein Ure2Specificity of the J-protein Sis1 in the propagation of 3 yeast prions.Mutational analysis of Sse1 (Hsp110) suggests an integral role for this chaperone in yeast prion propagation in vivo.Prion-prion interactionsPrion propagation by Hsp40 molecular chaperones.Prion and nonprion amyloids: a comparison inspired by the yeast Sup35 proteinTherapeutic interventions ameliorating prion disease.Prion-like propagation of cytosolic protein aggregates: insights from cell culture models.Pharmacological chaperone therapy for Gaucher disease: a patent review.The yeast prion protein Ure2: insights into the mechanism of amyloid formation.Are prions part of the dark matter of the cell?Patterns of [PSI (+) ] aggregation allow insights into cellular organization of yeast prion aggregates.The double life of the ribosome: When its protein folding activity supports prion propagation.SUP35 expression is enhanced in yeast containing [ISP+], a prion form of the transcriptional regulator Sfp1.Protein Folding Activity of the Ribosome is involved in Yeast Prion Propagation.
P2860
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P2860
Chaperoning prions: the cellular machinery for propagating an infectious protein?
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
2005年论文
@zh
2005年论文
@zh-cn
name
Chaperoning prions: the cellular machinery for propagating an infectious protein?
@ast
Chaperoning prions: the cellular machinery for propagating an infectious protein?
@en
type
label
Chaperoning prions: the cellular machinery for propagating an infectious protein?
@ast
Chaperoning prions: the cellular machinery for propagating an infectious protein?
@en
prefLabel
Chaperoning prions: the cellular machinery for propagating an infectious protein?
@ast
Chaperoning prions: the cellular machinery for propagating an infectious protein?
@en
P2860
P356
P1433
P1476
Chaperoning prions: the cellular machinery for propagating an infectious protein?
@en
P2093
Gary W Jones
Mick F Tuite
P2860
P304
P356
10.1002/BIES.20267
P407
P577
2005-08-01T00:00:00Z