Molecular chaperones and the assembly of the prion Sup35p, an in vitro study.
about
Prion induction involves an ancient system for the sequestration of aggregated proteins and heritable changes in prion fragmentationHsp104-dependent remodeling of prion complexes mediates protein-only inheritanceHsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions.Prion-impairing mutations in Hsp70 chaperone Ssa1: effects on ATPase and chaperone activities.Qualitative and quantitative multiplexed proteomic analysis of complex yeast protein fractions that modulate the assembly of the yeast prion Sup35pHeritable yeast prions have a highly organized three-dimensional architecture with interfiber structures.Tunneling nanotube (TNT)-mediated neuron-to neuron transfer of pathological Tau protein assembliesThe number and transmission of [PSI] prion seeds (Propagons) in the yeast Saccharomyces cerevisiae.Function of SSA subfamily of Hsp70 within and across species varies widely in complementing Saccharomyces cerevisiae cell growth and prion propagation.Yeast prions assembly and propagation: contributions of the prion and non-prion moieties and the nature of assemblies.Substrate Discrimination by ClpB and Hsp104.A region within the C-terminal domain of Ure2p is shown to interact with the molecular chaperone Ssa1p by the use of cross-linkers and mass spectrometry.[SWI], the prion formed by the chromatin remodeling factor Swi1, is highly sensitive to alterations in Hsp70 chaperone system activity.Low activity of select Hsp104 mutants is sufficient to propagate unstable prion variantsIn vivo evidence for the fibrillar structures of Sup35 prions in yeast cells.Trans-species activity of a nonself recognition domain.Molecular chaperone Hsp104 can promote yeast prion generationImportance of the Hsp70 ATPase domain in yeast prion propagationInsight into molecular basis of curing of [PSI+] prion by overexpression of 104-kDa heat shock protein (Hsp104).The 26S Proteasome Degrades the Soluble but Not the Fibrillar Form of the Yeast Prion Ure2p In Vitro.Molecular chaperones and the assembly of the prion Ure2p in vitro.Molecular and functional characterization of the only known hemiascomycete ortholog of the carboxyl terminus of Hsc70-interacting protein CHIP in the yeast Yarrowia lipolytica.Unraveling infectious structures, strain variants and species barriers for the yeast prion [PSI+].A non-Q/N-rich prion domain of a foreign prion, [Het-s], can propagate as a prion in yeast.Prion aggregate structure in yeast cells is determined by the Hsp104-Hsp110 disaggregase machinery.Prions in yeast.Variant-specific [PSI+] infection is transmitted by Sup35 polymers within [PSI+] aggregates with heterogeneous protein compositionAxonal transport and secretion of fibrillar forms of α-synuclein, Aβ42 peptide and HTTExon 1Influence of specific HSP70 domains on fibril formation of the yeast prion protein Ure2Stress and prions: lessons from the yeast model.Heat shock protein (Hsp) 70 is an activator of the Hsp104 motor.Mutational analysis of Sse1 (Hsp110) suggests an integral role for this chaperone in yeast prion propagation in vivo.Prion-prion interactionsMultiple hsp70 isoforms in the eukaryotic cytosol: mere redundancy or functional specificity?Identification of a consensus motif in substrates bound by a Type I Hsp40.Prion propagation by Hsp40 molecular chaperones.Influence of Hsp70s and their regulators on yeast prion propagationHsp70 structure, function, regulation and influence on yeast prions.Infectious fold and amyloid propagation in Podospora anserina.Prion propagation: the role of protein dynamics
P2860
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P2860
Molecular chaperones and the assembly of the prion Sup35p, an in vitro study.
description
2006 nî lūn-bûn
@nan
2006 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Molecular chaperones and the assembly of the prion Sup35p, an in vitro study.
@ast
Molecular chaperones and the assembly of the prion Sup35p, an in vitro study.
@en
Molecular chaperones and the assembly of the prion Sup35p, an in vitro study.
@nl
type
label
Molecular chaperones and the assembly of the prion Sup35p, an in vitro study.
@ast
Molecular chaperones and the assembly of the prion Sup35p, an in vitro study.
@en
Molecular chaperones and the assembly of the prion Sup35p, an in vitro study.
@nl
prefLabel
Molecular chaperones and the assembly of the prion Sup35p, an in vitro study.
@ast
Molecular chaperones and the assembly of the prion Sup35p, an in vitro study.
@en
Molecular chaperones and the assembly of the prion Sup35p, an in vitro study.
@nl
P2860
P356
P1433
P1476
Molecular chaperones and the assembly of the prion Sup35p, an in vitro study.
@en
P2093
Joanna Krzewska
Ronald Melki
P2860
P304
P356
10.1038/SJ.EMBOJ.7600985
P407
P577
2006-02-09T00:00:00Z