about
Facilitated aggregation of FG nucleoporins under molecular crowding conditionsYeast prions and human prion-like proteins: sequence features and prediction methodsProteomic screening for amyloid proteinsDisordered proteinaceous machinesProtein aggregation behavior regulates cyclin transcript localization and cell-cycle controlPrions, amyloids, and RNA: Pieces of a puzzle.Investigating the interactions of yeast prions: [SWI+], [PSI+], and [PIN+].Defining the limits: Protein aggregation and toxicity in vivoIncreasing prion propensity by hydrophobic insertion.Altering nuclear pore complex function impacts longevity and mitochondrial function in S. cerevisiaeInteraction networks of prion, prionogenic and prion-like proteins in budding yeast, and their role in gene regulationThe Structure and Dynamics of Higher-Order Assemblies: Amyloids, Signalosomes, and Granules.Physiological and environmental control of yeast prions.Toxic PRn poly-dipeptides encoded by the C9orf72 repeat expansion block nuclear import and export.The effects of glutamine/asparagine content on aggregation and heterologous prion induction by yeast prion-like domains.The selective permeability barrier in the nuclear pore complexAnalysis of [SWI+ ] formation and propagation events.Prion-like proteins and their computational identification in proteomes.Expanding the yeast prion world: Active prion conversion of non-glutamine/asparagine-rich Mod5 for cell survival.The copper transport-associated protein Ctr4 can form prion-like epigenetic determinants in Schizosaccharomyces pombe.Feedback control of prion formation and propagation by the ribosome-associated chaperone complexSystematic analysis of barrier-forming FG hydrogels from Xenopus nuclear pore complexes.Tau-er of PowerTDP-43 pathology disrupts nuclear pore complexes and nucleocytoplasmic transport in ALS/FTD.Analysis of Small Critical Regions of Swi1 Conferring Prion Formation, Maintenance, and Transmission.A brief overview of the Swi1 prion-[SWI+]Dynamics in the solid-state: perspectives for the investigation of amyloid aggregates, membrane proteins and soluble protein complexesSequence features governing aggregation or degradation of prion-like proteinsProtein Co-Aggregation Related to Amyloids: Methods of Investigation, Diversity, and Classification
P2860
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P2860
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年学术文章
@wuu
2012年学术文章
@zh-cn
2012年学术文章
@zh-hans
2012年学术文章
@zh-my
2012年学术文章
@zh-sg
2012年學術文章
@yue
2012年學術文章
@zh
2012年學術文章
@zh-hant
name
Prion formation by a yeast GLFG nucleoporin.
@en
Prion formation by a yeast GLFG nucleoporin.
@nl
type
label
Prion formation by a yeast GLFG nucleoporin.
@en
Prion formation by a yeast GLFG nucleoporin.
@nl
prefLabel
Prion formation by a yeast GLFG nucleoporin.
@en
Prion formation by a yeast GLFG nucleoporin.
@nl
P2093
P2860
P356
P1433
P1476
Prion formation by a yeast GLFG nucleoporin
@en
P2093
Jessica R Wright
Michael Rexach
Susan Lindquist
P2860
P304
P356
10.4161/PRI.20199
P577
2012-05-07T00:00:00Z