Hsp104 interacts with Hsp90 cochaperones in respiring yeast
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Disaggregases, molecular chaperones that resolubilize protein aggregatesStructural basis for intersubunit signaling in a protein disaggregating machineA Structural Model of the Sgt2 Protein and Its Interactions with Chaperones and the Get4/Get5 ComplexSpiral architecture of the Hsp104 disaggregase reveals the basis for polypeptide translocationSGT2 and MDY2 interact with molecular chaperone YDJ1 in Saccharomyces cerevisiaeThe Hsp70/90 cochaperone, Sti1, suppresses proteotoxicity by regulating spatial quality control of amyloid-like proteins.Functional interactions between Hsp90 and the co-chaperones Cns1 and Cpr7 in Saccharomyces cerevisiae.The Hsp90 cochaperones Cpr6, Cpr7, and Cns1 interact with the intact ribosomeFunctional similarity between the chloroplast translocon component, Tic40, and the human co-chaperone, Hsp70-interacting protein (Hip)Impact of acute metal stress in Saccharomyces cerevisiaeNuclear import of the glucocorticoid receptor-hsp90 complex through the nuclear pore complex is mediated by its interaction with Nup62 and importin betaNew insights into the mechanism of chloroplast protein import and its integration with protein quality control, organelle biogenesis and development.Synchrotron infrared microspectroscopy detecting the evolution of Huntington's disease neuropathology and suggesting unique correlates of dysfunction in white versus gray brain matter.Ssd1 is required for thermotolerance and Hsp104-mediated protein disaggregation in Saccharomyces cerevisiae.The Schizosaccharomyces pombe Hsp104 disaggregase is unable to propagate the [PSI] prion.Hsp90 nuclear accumulation in quiescence is linked to chaperone function and spore development in yeast.Coordinated Hsp110 and Hsp104 Activities Power Protein Disaggregation in Saccharomyces cerevisiae.In vivo monitoring of the prion replication cycle reveals a critical role for Sis1 in delivering substrates to Hsp104Sti1 regulation of Hsp70 and Hsp90 is critical for curing of Saccharomyces cerevisiae [PSI+] prions by Hsp104.The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically.Independent regulation of Hsp70 and Hsp90 chaperones by Hsp70/Hsp90-organizing protein Sti1 (Hop1).Loss of Hsp70 in Drosophila is pleiotropic, with effects on thermotolerance, recovery from heat shock and neurodegeneration.Effect of mutation of the tetratricopeptide repeat and asparatate-proline 2 domains of Sti1 on Hsp90 signaling and interaction in Saccharomyces cerevisiaeOverexpression of human virus surface glycoprotein precursors induces cytosolic unfolded protein response in Saccharomyces cerevisiae.Nucleotide-dependent interaction of Saccharomyces cerevisiae Hsp90 with the cochaperone proteins Sti1, Cpr6, and Sba1.Lessons from the genome sequence of Neurospora crassa: tracing the path from genomic blueprint to multicellular organism.Hsp90 inhibitors and drug resistance in cancer: the potential benefits of combination therapies of Hsp90 inhibitors and other anti-cancer drugsTetratricopeptide repeat cochaperones in steroid receptor complexesBiology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system.Functional analysis of conserved cis- and trans-elements in the Hsp104 protein disaggregating machineThe role of Sse1 in the de novo formation and variant determination of the [PSI+] prion.Fungal heat-shock proteins in human disease.Swa2, the yeast homolog of mammalian auxilin, is specifically required for the propagation of the prion variant [URE3-1].p23/Sba1p protects against Hsp90 inhibitors independently of its intrinsic chaperone activityProtein transport in organelles: The composition, function and regulation of the Tic complex in chloroplast protein import.Propagation of Saccharomyces cerevisiae [PSI+] prion is impaired by factors that regulate Hsp70 substrate bindingTowards a unifying mechanism for ClpB/Hsp104-mediated protein disaggregation and prion propagation.Mechanistic and Structural Insights into the Prion-Disaggregase Activity of Hsp104.Prion-specific Hsp40 function: The role of the auxilin homolog Swa2.Chaperone proteins select and maintain [PIN+] prion conformations in Saccharomyces cerevisiae.
P2860
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P2860
Hsp104 interacts with Hsp90 cochaperones in respiring yeast
description
2001 nî lūn-bûn
@nan
2001 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Hsp104 interacts with Hsp90 cochaperones in respiring yeast
@ast
Hsp104 interacts with Hsp90 cochaperones in respiring yeast
@en
Hsp104 interacts with Hsp90 cochaperones in respiring yeast
@nl
type
label
Hsp104 interacts with Hsp90 cochaperones in respiring yeast
@ast
Hsp104 interacts with Hsp90 cochaperones in respiring yeast
@en
Hsp104 interacts with Hsp90 cochaperones in respiring yeast
@nl
prefLabel
Hsp104 interacts with Hsp90 cochaperones in respiring yeast
@ast
Hsp104 interacts with Hsp90 cochaperones in respiring yeast
@en
Hsp104 interacts with Hsp90 cochaperones in respiring yeast
@nl
P2093
P2860
P1476
Hsp104 interacts with Hsp90 cochaperones in respiring yeast
@en
P2093
P2860
P304
P356
10.1128/MCB.21.22.7569-7575.2001
P407
P577
2001-11-01T00:00:00Z