An intrinsically disordered yeast prion arrests the cell cycle by sequestering a spindle pole body component.
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Dynamic JUNQ inclusion bodies are asymmetrically inherited in mammalian cell lines through the asymmetric partitioning of vimentinActin, Membrane Trafficking and the Control of Prion Induction, Propagation and Transmission in YeastThe Hsp70/90 cochaperone, Sti1, suppresses proteotoxicity by regulating spatial quality control of amyloid-like proteins.Polyglutamine toxicity in yeast induces metabolic alterations and mitochondrial defectsPolyglutamine-rich suppressors of huntingtin toxicity act upstream of Hsp70 and Sti1 in spatial quality control of amyloid-like proteins.Investigating the interactions of yeast prions: [SWI+], [PSI+], and [PIN+].Prion-promoted phosphorylation of heterologous amyloid is coupled with ubiquitin-proteasome system inhibition and toxicity.Defining the limits: Protein aggregation and toxicity in vivoHeterologous gln/asn-rich proteins impede the propagation of yeast prions by altering chaperone availabilityCAMELOT: A machine learning approach for coarse-grained simulations of aggregation of block-copolymeric protein sequences.Quantitative nature of overexpression experiments.Computational modeling of the relationship between amyloid and disease.Physiological and environmental control of yeast prions.Promiscuity as a functional trait: intrinsically disordered regions as central players of interactomes.Dynamic droplets: the role of cytoplasmic inclusions in stress, function, and disease.The frequency of yeast [PSI+] prion formation is increased during chronological ageing.The principle of conformational signaling.Prions, Chaperones, and Proteostasis in Yeast.A yeast model of optineurin proteinopathy reveals a unique aggregation pattern associated with cellular toxicity.A network of genes connects polyglutamine toxicity to ploidy control in yeastAutophagy protects against de novo formation of the [PSI+] prion in yeastMolecular mechanisms of spatial protein quality control.Prion puts yeast cells under arrest.Discovering Putative Prion-Like Proteins in : A Computational and Experimental Analysis
P2860
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P2860
An intrinsically disordered yeast prion arrests the cell cycle by sequestering a spindle pole body component.
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
An intrinsically disordered ye ...... a spindle pole body component.
@ast
An intrinsically disordered ye ...... a spindle pole body component.
@en
type
label
An intrinsically disordered ye ...... a spindle pole body component.
@ast
An intrinsically disordered ye ...... a spindle pole body component.
@en
prefLabel
An intrinsically disordered ye ...... a spindle pole body component.
@ast
An intrinsically disordered ye ...... a spindle pole body component.
@en
P2860
P356
P1476
An intrinsically disordered ye ...... a spindle pole body component.
@en
P2093
Sebastian Treusch
P2860
P304
P356
10.1083/JCB.201108146
P407
P577
2012-04-23T00:00:00Z