Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation.
about
Molecular chaperones: guardians of the proteome in normal and disease statesMetazoan Hsp70-based protein disaggregases: emergence and mechanismsDisaggregases, molecular chaperones that resolubilize protein aggregatesYeast prions: structure, biology, and prion-handling systemsPrion Aggregates Are Recruited to the Insoluble Protein Deposit (IPOD) via Myosin 2-Based Vesicular TransportSingle-molecule analyses of the dynamics of heat shock protein 104 (Hsp104) and protein aggregates.Elements in nucleotide sensing and hydrolysis of the AAA+ disaggregation machine ClpB: a structure-based mechanistic dissection of a molecular motorYeast prions are useful for studying protein chaperones and protein quality controlCooperation of Hsp70 and Hsp100 chaperone machines in protein disaggregationAggregate-reactivation activity of the molecular chaperone ClpB from Ehrlichia chaffeensisThe Hsp104 N-terminal domain enables disaggregase plasticity and potentiationCoordinated Hsp110 and Hsp104 Activities Power Protein Disaggregation in Saccharomyces cerevisiae.Hsp104 overexpression cures Saccharomyces cerevisiae [PSI+] by causing dissolution of the prion seedsUsing Caenorhabditis elegans as a model system to study protein homeostasis in a multicellular organism.Metazoan Hsp70 machines use Hsp110 to power protein disaggregationDysregulation of the proteasome increases the toxicity of ALS-linked mutant SOD1.The effects of amino acid composition of glutamine-rich domains on amyloid formation and fragmentation.The Type II Hsp40 Sis1 cooperates with Hsp70 and the E3 ligase Ubr1 to promote degradation of terminally misfolded cytosolic protein.Heterologous gln/asn-rich proteins impede the propagation of yeast prions by altering chaperone availabilitySpatial quality control bypasses cell-based limitations on proteostasis to promote prion curing.Functional diversification of hsp40: distinct j-protein functional requirements for two prions allow for chaperone-dependent prion selectionHeterologous aggregates promote de novo prion appearance via more than one mechanism.Hsp70 clears misfolded kinases that partitioned into distinct quality-control compartments.Human Hsp70 Disaggregase Reverses Parkinson's-Linked α-Synuclein Amyloid Fibrils.Quantitative proteomics of the yeast Hsp70/Hsp90 interactomes during DNA damage reveal chaperone-dependent regulation of ribonucleotide reductase.The Symbiotic Performance of Chickpea Rhizobia Can Be Improved by Additional Copies of the clpB Chaperone GeneMutations in the Yeast Hsp70, Ssa1, at P417 Alter ATP Cycling, Interdomain Coupling, and Specific Chaperone Functions.Hsp40 function in yeast prion propagation: Amyloid diversity necessitates chaperone functional complexity.Prion aggregate structure in yeast cells is determined by the Hsp104-Hsp110 disaggregase machinery.Distinct Prion Domain Sequences Ensure Efficient Amyloid Propagation by Promoting Chaperone Binding or Processing In Vivo.ClpB N-terminal domain plays a regulatory role in protein disaggregationSwa2, the yeast homolog of mammalian auxilin, is specifically required for the propagation of the prion variant [URE3-1].Structural variants of yeast prions show conformer-specific requirements for chaperone activity.Schizosaccharomyces pombe disaggregation machinery chaperones support Saccharomyces cerevisiae growth and prion propagation.Heat shock protein (Hsp) 70 is an activator of the Hsp104 motor.Hsp70 biases the folding pathways of client proteins.Adenosine diphosphate restricts the protein remodeling activity of the Hsp104 chaperone to Hsp70 assisted disaggregationThe story of stolen chaperones: how overexpression of Q/N proteins cures yeast prions.Molecular chaperones and proteostasis regulation during redox imbalance.Physiological and environmental control of yeast prions.
P2860
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P2860
Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Hsp70 targets Hsp100 chaperone ...... ation and prion fragmentation.
@en
Hsp70 targets Hsp100 chaperone ...... ation and prion fragmentation.
@nl
type
label
Hsp70 targets Hsp100 chaperone ...... ation and prion fragmentation.
@en
Hsp70 targets Hsp100 chaperone ...... ation and prion fragmentation.
@nl
prefLabel
Hsp70 targets Hsp100 chaperone ...... ation and prion fragmentation.
@en
Hsp70 targets Hsp100 chaperone ...... ation and prion fragmentation.
@nl
P2860
P356
P1476
Hsp70 targets Hsp100 chaperone ...... ation and prion fragmentation.
@en
P2093
Jens Tyedmers
Juliane Winkler
P2860
P304
P356
10.1083/JCB.201201074
P407
P577
2012-08-01T00:00:00Z