The function of the yeast molecular chaperone Sse1 is mechanistically distinct from the closely related hsp70 family.
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The stress response against denatured proteins in the deletion of cytosolic chaperones SSA1/2 is different from heat-shock response in Saccharomyces cerevisiaeThe nucleotide exchange factors of Hsp70 molecular chaperonesMetazoan Hsp70-based protein disaggregases: emergence and mechanismsInsights into Hsp70 Chaperone Activity from a Crystal Structure of the Yeast Hsp110 Sse1Structure of the Hsp110:Hsc70 nucleotide exchange machine.Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s.A two-hybrid screen of the yeast proteome for Hsp90 interactors uncovers a novel Hsp90 chaperone requirement in the activity of a stress-activated mitogen-activated protein kinase, Slt2p (Mpk1p).The yeast Hsp110, Sse1p, exhibits high-affinity peptide binding.Characterization of Hsp70 binding and nucleotide exchange by the yeast Hsp110 chaperone Sse1.Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor.Overexpression, Purification and Characterisation of the Plasmodium falciparum Hsp70-z (PfHsp70-z) ProteinBinding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitroHsp110 is required for spindle length control.Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities.Hsp110 chaperones control client fate determination in the hsp70-Hsp90 chaperone system[SWI], the prion formed by the chromatin remodeling factor Swi1, is highly sensitive to alterations in Hsp70 chaperone system activity.The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free systemMetazoan Hsp70 machines use Hsp110 to power protein disaggregationAll in the family: atypical Hsp70 chaperones are conserved modulators of Hsp70 activity.Interaction between cell division proteins FtsE and FtsZ.Nucleotide exchange factors for Hsp70s are required for [URE3] prion propagation in Saccharomyces cerevisiae.Human heat shock protein 105/110 kDa (Hsp105/110) regulates biogenesis and quality control of misfolded cystic fibrosis transmembrane conductance regulator at multiple levels.Biology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system.Understanding the Mechanism of Thermotolerance Distinct From Heat Shock Response Through Proteomic Analysis of Industrial Strains of Saccharomyces cerevisiaeHsp70 targets a cytoplasmic quality control substrate to the San1p ubiquitin ligaseInsights into the structural dynamics of the Hsp110-Hsp70 interaction reveal the mechanism for nucleotide exchange activity.Mutational analysis of Sse1 (Hsp110) suggests an integral role for this chaperone in yeast prion propagation in vivo.The Hsp110 molecular chaperone stabilizes apolipoprotein B from endoplasmic reticulum-associated degradation (ERAD)Suppression of polyglutamine protein toxicity by co-expression of a heat-shock protein 40 and a heat-shock protein 110Hsp70 protein complexes as drug targets.The control of spindle length by Hsp70 and Hsp110 molecular chaperones.The secretory pathway: exploring yeast diversity.Structural mechanisms of chaperone mediated protein disaggregation.Unique 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.Chaperone expression profiles correlate with distinct physiological states of Plasmodium falciparum in malaria patients.The chaperone network connected to human ribosome-associated complexThe Hsp110 protein chaperone Sse1 is required for yeast cell wall integrity and morphogenesis.Interactions between Kar2p and its nucleotide exchange factors Sil1p and Lhs1p are mechanistically distinct.The molecular chaperone Sse1 and the growth control protein kinase Sch9 collaborate to regulate protein kinase A activity in Saccharomyces cerevisiae.
P2860
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P2860
The function of the yeast molecular chaperone Sse1 is mechanistically distinct from the closely related hsp70 family.
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2004 nî lūn-bûn
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2004 թուականի Մայիսին հրատարակուած գիտական յօդուած
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2004 թվականի մայիսին հրատարակված գիտական հոդված
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2004年の論文
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2004年論文
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2004年論文
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2004年論文
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2004年論文
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2004年論文
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2004年论文
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The function of the yeast mole ...... closely related hsp70 family.
@ast
The function of the yeast mole ...... closely related hsp70 family.
@en
The function of the yeast mole ...... closely related hsp70 family.
@nl
type
label
The function of the yeast mole ...... closely related hsp70 family.
@ast
The function of the yeast mole ...... closely related hsp70 family.
@en
The function of the yeast mole ...... closely related hsp70 family.
@nl
prefLabel
The function of the yeast mole ...... closely related hsp70 family.
@ast
The function of the yeast mole ...... closely related hsp70 family.
@en
The function of the yeast mole ...... closely related hsp70 family.
@nl
P2093
P2860
P356
P1476
The function of the yeast mole ...... closely related hsp70 family.
@en
P2093
Jeffrey L Brodsky
Jennifer L Goeckeler
Kevin A Morano
Lance Shaner
P2860
P304
21992-2001
P356
10.1074/JBC.M313739200
P407
P577
2004-05-21T00:00:00Z