Ssa1 overexpression and [PIN(+)] variants cure [PSI(+)] by dilution of aggregates.
about
Prions, protein homeostasis, and phenotypic diversityDisaggregases, molecular chaperones that resolubilize protein aggregatesThe [RNQ+] prion: a model of both functional and pathological amyloidDifferences in the curing of [PSI+] prion by various methods of Hsp104 inactivationChemical-genetic profile analysis of five inhibitory compounds in yeast.Heritable yeast prions have a highly organized three-dimensional architecture with interfiber structures.Heat shock protein 104 (Hsp104)-mediated curing of [PSI+] yeast prions depends on both [PSI+] conformation and the properties of the Hsp104 homologs.Overexpression of the essential Sis1 chaperone reduces TDP-43 effects on toxicity and proteolysis.Analyzing the birth and propagation of two distinct prions, [PSI+] and [Het-s](y), in yeast.Low activity of select Hsp104 mutants is sufficient to propagate unstable prion variantsPrion-promoted phosphorylation of heterologous amyloid is coupled with ubiquitin-proteasome system inhibition and toxicity.Heterologous gln/asn-rich proteins impede the propagation of yeast prions by altering chaperone availabilityDestabilization and recovery of a yeast prion after mild heat shock.Newly identified prions in budding yeast, and their possible functions.Heterologous aggregates promote de novo prion appearance via more than one mechanism.Prions in yeast.The Paf1 complex subunit Rtf1 buffers cells against the toxic effects of [PSI+] and defects in Rkr1-dependent protein quality control in Saccharomyces cerevisiae.Human J-protein DnaJB6b Cures a Subset of Saccharomyces cerevisiae Prions and Selectively Blocks Assembly of Structurally Related Amyloids.Influence of specific HSP70 domains on fibril formation of the yeast prion protein Ure2Influence of Hsp70s and their regulators on yeast prion propagationPatterns of [PSI (+) ] aggregation allow insights into cellular organization of yeast prion aggregates.Regulation of the Hsp104 middle domain activity is critical for yeast prion propagation.[PIN+]ing down the mechanism of prion appearance.
P2860
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P2860
Ssa1 overexpression and [PIN(+)] variants cure [PSI(+)] by dilution of aggregates.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
2009年论文
@zh
2009年论文
@zh-cn
name
Ssa1 overexpression and [PIN
@nl
Ssa1 overexpression and [PIN(+)] variants cure [PSI(+)] by dilution of aggregates.
@en
type
label
Ssa1 overexpression and [PIN
@nl
Ssa1 overexpression and [PIN(+)] variants cure [PSI(+)] by dilution of aggregates.
@en
prefLabel
Ssa1 overexpression and [PIN
@nl
Ssa1 overexpression and [PIN(+)] variants cure [PSI(+)] by dilution of aggregates.
@en
P2860
P1476
Ssa1 overexpression and [PIN(+)] variants cure [PSI(+)] by dilution of aggregates.
@en
P2093
Joo Y Hong
Vidhu Mathur
P2860
P304
P356
10.1016/J.JMB.2009.04.063
P407
P577
2009-05-05T00:00:00Z