Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor. - Wikidata - thesis-toulmin - TriplyDB

Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor.

Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor.

http://www.wikidata.org/entity/Q27940000

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Hsp105beta upregulates hsp70 gene expression through signal transducer and activator of transcription-3 Guidelines for the nomenclature of the human heat shock proteins Role of Heat-Shock Proteins in Cellular Function and in the Biology of Fungi Unfolding the Role of Large Heat Shock Proteins: New Insights and Therapeutic Implications Molecular chaperones: guardians of the proteome in normal and disease states The nucleotide exchange factors of Hsp70 molecular chaperones Metazoan Hsp70-based protein disaggregases: emergence and mechanisms Insights into the molecular mechanism of allostery in Hsp70s.Disaggregases, molecular chaperones that resolubilize protein aggregates BiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functions High molecular weight stress proteins: Identification, cloning and utilisation in cancer immunotherapy Modulation and elimination of yeast prions by protein chaperones and co-chaperones Insights into Hsp70 Chaperone Activity from a Crystal Structure of the Yeast Hsp110 Sse1 Crystal Structures of the 70-kDa Heat Shock Proteins in Domain Disjoining Conformation Structure of the Hsp110:Hsc70 nucleotide exchange machine.Structural analysis of the Sil1-Bip complex reveals the mechanism for Sil1 to function as a nucleotide-exchange factor Structure and function of Hip, an attenuator of the Hsp70 chaperone cycle Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s.Nucleotide binding by Lhs1p is essential for its nucleotide exchange activity and for function in vivo.The yeast Hsp110, Sse1p, exhibits high-affinity peptide binding.Prion-impairing mutations in Hsp70 chaperone Ssa1: effects on ATPase and chaperone activities.Characterization of Hsp70 binding and nucleotide exchange by the yeast Hsp110 chaperone Sse1.Hsp70 nucleotide exchange factor Fes1 is essential for ubiquitin-dependent degradation of misfolded cytosolic proteins.Sequential duplications of an ancient member of the DnaJ-family expanded the functional chaperone network in the eukaryotic cytosol.Plasmodium falciparum Hsp70-z, an Hsp110 homologue, exhibits independent chaperone activity and interacts with Hsp70-1 in a nucleotide-dependent fashion Nogo-A couples with Apg-1 through interaction and co-ordinate expression under hypoxic and oxidative stress Mammalian 105 kDa heat shock family proteins suppress hydrogen peroxide-induced apoptosis through a p38 MAPK-dependent mitochondrial pathway in HeLa cells Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro The HSP70 chaperone machinery: J proteins as drivers of functional specificity Plasmodium falciparum heat shock protein 110 stabilizes the asparagine repeat-rich parasite proteome during malarial fevers Heat shock proteins: cellular and molecular mechanisms in the central nervous system.ATP-induced conformational changes in Hsp70: molecular dynamics and experimental validation of an in silico predicted conformation.Molecular chaperone Hsp110 rescues a vesicle transport defect produced by an ALS-associated mutant SOD1 protein in squid axoplasm.Post-transcriptional regulation of the trypanosome heat shock response by a zinc finger protein.Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities.Progressive aggregation despite chaperone associations of a mutant SOD1-YFP in transgenic mice that develop ALS.Global transcript and phenotypic analysis of yeast cells expressing Ssa1, Ssa2, Ssa3 or Ssa4 as sole source of cytosolic Hsp70-Ssa chaperone activity Hierarchical functional specificity of cytosolic heat shock protein 70 (Hsp70) nucleotide exchange factors in yeast.Coordinated Hsp110 and Hsp104 Activities Power Protein Disaggregation in Saccharomyces cerevisiae.Analysis of chaperone mRNA expression in the adult mouse brain by meta analysis of the Allen Brain Atlas.

P2860

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P2860

Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor.

http://www.wikidata.org/entity/Q27940000

description

2006 nî lūn-bûn

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2006 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2006 թվականի հունիսին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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name

Chaperone network in the yeast ...... 70 nucleotide exchange factor.

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Chaperone network in the yeast ...... 70 nucleotide exchange factor.

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Chaperone network in the yeast ...... 70 nucleotide exchange factor.

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type

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Chaperone network in the yeast ...... 70 nucleotide exchange factor.

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Chaperone network in the yeast ...... 70 nucleotide exchange factor.

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Chaperone network in the yeast ...... 70 nucleotide exchange factor.

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prefLabel

Chaperone network in the yeast ...... 70 nucleotide exchange factor.

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Chaperone network in the yeast ...... 70 nucleotide exchange factor.

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Chaperone network in the yeast ...... 70 nucleotide exchange factor.

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SJ.EMBOJ.7601139

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The EMBO Journal

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Chaperone network in the yeast ...... 70 nucleotide exchange factor.

@en

P2093

Fernanda Rodriguez

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Heather Sadlish

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Holger Raviol

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Matthias P Mayer

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P2860

Functional organization of the yeast proteome by systematic analysis of protein complexes

Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors

Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK

A generic protein purification method for protein complex characterization and proteome exploration

Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p

The function of the yeast molecular chaperone Sse1 is mechanistically distinct from the closely related hsp70 family.

Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells.

Protein folding activity of Hsp70 is modified differentially by the hsp40 co-chaperones Sis1 and Ydj1.

Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase.

The refolding activity of the yeast heat shock proteins Ssa1 and Ssa2 defines their role in protein translocation

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16688211

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molecular chaperones

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