Mutational analysis of Sse1 (Hsp110) suggests an integral role for this chaperone in yeast prion propagation in vivo.
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Plasmodium falciparum Hsp70-z, an Hsp110 homologue, exhibits independent chaperone activity and interacts with Hsp70-1 in a nucleotide-dependent fashionGlobal transcript and phenotypic analysis of yeast cells expressing Ssa1, Ssa2, Ssa3 or Ssa4 as sole source of cytosolic Hsp70-Ssa chaperone activityCoordinated Hsp110 and Hsp104 Activities Power Protein Disaggregation in Saccharomyces cerevisiae.Dancing through Life: Molecular Dynamics Simulations and Network-Centric Modeling of Allosteric Mechanisms in Hsp70 and Hsp110 Chaperone Proteins.Prion aggregate structure in yeast cells is determined by the Hsp104-Hsp110 disaggregase machinery.Prions, Chaperones, and Proteostasis in Yeast.The metazoan protein disaggregase and amyloid depolymerase system: Hsp110, Hsp70, Hsp40, and small heat shock proteins.Hsp104 disaggregase at normal levels cures many [PSI+] prion variants in a process promoted by Sti1p, Hsp90, and Sis1p.
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Mutational analysis of Sse1 (Hsp110) suggests an integral role for this chaperone in yeast prion propagation in vivo.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 07 August 2013
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Mutational analysis of Sse1 (H ...... ast prion propagation in vivo.
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Mutational analysis of Sse1
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type
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Mutational analysis of Sse1 (H ...... ast prion propagation in vivo.
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Mutational analysis of Sse1
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prefLabel
Mutational analysis of Sse1 (H ...... ast prion propagation in vivo.
@en
Mutational analysis of Sse1
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Mutational analysis of Sse1 (H ...... east prion propagation in vivo
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Ciara Moran
Gemma K Kinsella
Sarah Perrett
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10.1534/G3.113.007112
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2013-08-07T00:00:00Z