The nucleotide exchange factors of Hsp70 molecular chaperones
about
Insights into the molecular mechanism of allostery in Hsp70s.Coordinated Hsp110 and Hsp104 Activities Power Protein Disaggregation in Saccharomyces cerevisiae.Reconstitution of a Mycobacterium tuberculosis proteostasis network highlights essential cofactor interactions with chaperone DnaK.Methyl CpG level at distal part of heat-shock protein promoter HSP70 exhibits epigenetic memory for heat stress by modulating recruitment of POU2F1-associated nucleosome-remodeling deacetylase (NuRD) complex.Backbone and methyl resonance assignments of the 42 kDa human Hsc70 nucleotide binding domain in the ADP state.The Role of Co-chaperones in Synaptic Proteostasis and Neurodegenerative Disease.The Role of the Multifunctional BAG3 Protein in Cellular Protein Quality Control and in Disease.UBL/BAG-domain co-chaperones cause cellular stress upon overexpression through constitutive activation of Hsf1.Evolution of an intricate J-protein network driving protein disaggregation in eukaryotes.Substrate binding by the yeast Hsp110 nucleotide exchange factor and molecular chaperone Sse1 is not obligate for its biological activities.Differential Targeting of Hsp70 Heat Shock Proteins HSPA6 and HSPA1A with Components of a Protein Disaggregation/Refolding Machine in Differentiated Human Neuronal Cells following Thermal Stress.Components of a mammalian protein disaggregation/refolding machine are targeted to nuclear speckles following thermal stress in differentiated human neuronal cells.Conformation transitions of the polypeptide-binding pocket support an active substrate release from Hsp70s.Molecular biology: Mature proteins braced by a chaperone.An Update on Sec61 Channel Functions, Mechanisms, and Related Diseases.The FKBP51 Glucocorticoid Receptor Co-Chaperone: Regulation, Function, and Implications in Health and Disease.BAG3-mediated proteostasis at a glance.Thermodynamic Bounds on the Ultra- and Infra-affinity of Hsp70 for Its Substrates.The absence of specific yeast heat-shock proteins leads to abnormal aggregation and compromised autophagic clearance of mutant Huntingtin proteins.Bap (Sil1) regulates the molecular chaperone BiP by coupling release of nucleotide and substrate.Nucleotide exchange factors Fes1 and HspBP1 mimic substrate to release misfolded proteins from Hsp70.
P2860
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P2860
The nucleotide exchange factors of Hsp70 molecular chaperones
description
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name
The nucleotide exchange factors of Hsp70 molecular chaperones
@ast
The nucleotide exchange factors of Hsp70 molecular chaperones
@en
The nucleotide exchange factors of Hsp70 molecular chaperones
@nl
type
label
The nucleotide exchange factors of Hsp70 molecular chaperones
@ast
The nucleotide exchange factors of Hsp70 molecular chaperones
@en
The nucleotide exchange factors of Hsp70 molecular chaperones
@nl
prefLabel
The nucleotide exchange factors of Hsp70 molecular chaperones
@ast
The nucleotide exchange factors of Hsp70 molecular chaperones
@en
The nucleotide exchange factors of Hsp70 molecular chaperones
@nl
P2860
P356
P1476
The nucleotide exchange factors of Hsp70 molecular chaperones
@en
P2093
Andreas Bracher
Jacob Verghese
P2860
P356
10.3389/FMOLB.2015.00010
P407
P577
2015-01-01T00:00:00Z