Prion aggregate structure in yeast cells is determined by the Hsp104-Hsp110 disaggregase machinery.
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Prion Aggregates Are Recruited to the Insoluble Protein Deposit (IPOD) via Myosin 2-Based Vesicular TransportCoordinated Hsp110 and Hsp104 Activities Power Protein Disaggregation in Saccharomyces cerevisiae.Mechanistic and Structural Insights into the Prion-Disaggregase Activity of Hsp104.ER stress causes widespread protein aggregation and prion formation.The Role of Co-chaperones in Synaptic Proteostasis and Neurodegenerative Disease.Selective aggregation of the splicing factor Hsh155 suppresses splicing upon genotoxic stress.The absence of specific yeast heat-shock proteins leads to abnormal aggregation and compromised autophagic clearance of mutant Huntingtin proteins.A Liquid to Solid Phase Transition Underlying Pathological Huntingtin Exon1 Aggregation.Chaperones caught partying with prions.
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P2860
Prion aggregate structure in yeast cells is determined by the Hsp104-Hsp110 disaggregase machinery.
description
2015 nî lūn-bûn
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2015年の論文
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2015年論文
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2015年論文
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2015年論文
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2015年論文
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2015年論文
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2015年论文
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2015年论文
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name
Prion aggregate structure in y ...... Hsp110 disaggregase machinery.
@ast
Prion aggregate structure in y ...... Hsp110 disaggregase machinery.
@en
type
label
Prion aggregate structure in y ...... Hsp110 disaggregase machinery.
@ast
Prion aggregate structure in y ...... Hsp110 disaggregase machinery.
@en
prefLabel
Prion aggregate structure in y ...... Hsp110 disaggregase machinery.
@ast
Prion aggregate structure in y ...... Hsp110 disaggregase machinery.
@en
P2860
P356
P1476
Prion aggregate structure in y ...... Hsp110 disaggregase machinery.
@en
P2093
Daniel Clare
Jonathan O'Driscoll
P2860
P304
P356
10.1083/JCB.201505104
P407
P50
P577
2015-10-05T00:00:00Z