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Showing 1 to 7 of 7 for “"Hsp104"”.
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Energy Stress Causes Chaperones to Assemble Into Cytoplasmic Complexes
… and fungi have a potent disaggregase, named Hsp104 in Saccharomyces cerevisiae. Recently, heat-induced aggregates, termed Q-bodies, were found to contain three molecular chaperones: Hsp70, Hsp104, and Hsp42. Their coalescence from small puncta into larger inclusions required Hsp104. During …
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Stress-Induced Targeting of Molecular Chaperones In The Yeast Saccharomyces Cerevisiae
… program. The yeast molecular chaperone Hsp104 is a member of the Hsp100 superfamily of AAA+ ATPases. Unlike the Hsp90 family of chaperones, Hsp104 is not restricted to a specific set of client proteins, but rather assists in reactivating stress-denatured proteins by solubilizing protein …
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Assessing the role of Hsp70 in prion propagation in Saccharomyces cerevisiae
… shock proteins (HSP) such as Hsp40, Hsp70 and Hsp104, are essential for prion propagation in yeast. Hsp70 is a highly conserved protein composed of an N-terminal ATPase domain, a peptide-binding domain (PBD) and a C-terminal domain. In this study we describe a genetic screen that identifies an …
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Thiol-Based Misfolding: Linking Redox Balance to Cytosolic Proteostasis
… stress responses and recruits chaperones such as Hsp104 and Tsa1. These chaperones assist in clearing existing aggregates and preventing further damage. Above all, protein aggregation as a result of exposure to thiol-specific stress extends to human cells, thus establishing a conserved mechanism …
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Functional significance of Hsp70 post-translational modification in prion propagation and cellular function
… role for molecular chaperones, namely Hsp70 and Hsp104. The Hsp70 chaperone family and its associated co-chaperones are highly conserved from yeast to mammals. A major function of Hsp70 is to prevent the aggregation of denatured proteins by binding to exposed hydrophobic regions and preventing …
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Deciphering Functional Significance of Substrate-Binding Domain of Ssa1 on Heat-Shock Response and Prion Propagation
… interactions with co-chaperones, especially Hsp104 and Hsp26, but decreased the interactions with Sup35. Degradation of the SBD in vivo is dependent on the action of vacuolar carboxypeptidase (Pep4) rather than the proteasome and occurs in WT cells at high temperature. Finally, SBD …
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Dictyostelium als Wirtsmodell und Funktionsanalyse des Virulenzfaktors Mip aus Legionella pneumophila
… zählen die Chaperone ClpB (heat shock protein Hsp104), β’-COP (coat protein) und drei calciumbindende Proteine. Nach Einteilung in funktionelle Kategorien, konnte gezeigt werden, dass viele Gene reguliert werden, deren Produkte am Aminosäure-Metabolismus beteiligt sind oder bei denen es sich um …