The yeast Hsp110, Sse1p, exhibits high-affinity peptide binding.
about
Metazoan Hsp70-based protein disaggregases: emergence and mechanismsBiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functionsHsp70 nucleotide exchange factor Fes1 is essential for ubiquitin-dependent degradation of misfolded cytosolic proteins.Plasmodium falciparum heat shock protein 110 stabilizes the asparagine repeat-rich parasite proteome during malarial feversHierarchical functional specificity of cytosolic heat shock protein 70 (Hsp70) nucleotide exchange factors in yeast.[SWI], the prion formed by the chromatin remodeling factor Swi1, is highly sensitive to alterations in Hsp70 chaperone system activity.A nucleus-based quality control mechanism for cytosolic proteinsMutations in the Yeast Hsp70, Ssa1, at P417 Alter ATP Cycling, Interdomain Coupling, and Specific Chaperone Functions.Members of the Hsp70 Family Recognize Distinct Types of Sequences to Execute ER Quality Control.Cytolytic activity of the human papillomavirus type 16 E711-20 epitope-specific cytotoxic T lymphocyte is enhanced by heat shock protein 110 in HLA-A*0201 transgenic mice.Mutational analysis of Sse1 (Hsp110) suggests an integral role for this chaperone in yeast prion propagation in vivo.The large Hsp70 Grp170 binds to unfolded protein substrates in vivo with a regulation distinct from conventional Hsp70s.The role of the cytosolic HSP70 chaperone system in diseases caused by misfolding and aberrant trafficking of ion channelsUnique peptide substrate binding properties of 110-kDa heat-shock protein (Hsp110) determine its distinct chaperone activitySubstrate binding by the yeast Hsp110 nucleotide exchange factor and molecular chaperone Sse1 is not obligate for its biological activities.The metazoan protein disaggregase and amyloid depolymerase system: Hsp110, Hsp70, Hsp40, and small heat shock proteins.The four hydrophobic residues on the Hsp70 inter-domain linker have two distinct roles.Nucleotide exchange factors Fes1 and HspBP1 mimic substrate to release misfolded proteins from Hsp70.
P2860
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P2860
The yeast Hsp110, Sse1p, exhibits high-affinity peptide binding.
description
2008 nî lūn-bûn
@nan
2008 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
The yeast Hsp110, Sse1p, exhibits high-affinity peptide binding.
@ast
The yeast Hsp110, Sse1p, exhibits high-affinity peptide binding.
@en
The yeast Hsp110, Sse1p, exhibits high-affinity peptide binding.
@nl
type
label
The yeast Hsp110, Sse1p, exhibits high-affinity peptide binding.
@ast
The yeast Hsp110, Sse1p, exhibits high-affinity peptide binding.
@en
The yeast Hsp110, Sse1p, exhibits high-affinity peptide binding.
@nl
prefLabel
The yeast Hsp110, Sse1p, exhibits high-affinity peptide binding.
@ast
The yeast Hsp110, Sse1p, exhibits high-affinity peptide binding.
@en
The yeast Hsp110, Sse1p, exhibits high-affinity peptide binding.
@nl
P2093
P2860
P921
P1433
P1476
The yeast Hsp110, Sse1p, exhibits high-affinity peptide binding.
@en
P2093
Anthony P Petruso
Jeffrey L Brodsky
Jennifer L Goeckeler
Julia Aguirre
P2860
P304
P356
10.1016/J.FEBSLET.2008.05.047
P407
P577
2008-07-09T00:00:00Z