Conversion of a yeast prion protein to an infectious form in bacteria
about
Disease Transmission by Misfolded Prion-Protein Isoforms, Prion-Like Amyloids, Functional Amyloids and the Central DogmaSpreading of a prion domain from cell-to-cell by vesicular transport in Caenorhabditis elegansRebels with a cause: molecular features and physiological consequences of yeast prionsThe mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free systemPrion propagation can occur in a prokaryote and requires the ClpB chaperone.Prions in yeast.Generating extracellular amyloid aggregates using E. coli cells.Biofilm inhibitors that target amyloid proteins.Physiological and environmental control of yeast prions.Biological role of bacterial inclusion bodies: a model for amyloid aggregation.Modeling human neurodegenerative diseases in transgenic systems.RepA-WH1 prionoid: a synthetic amyloid proteinopathy in a minimalist hostTransfer of disrupted-in-schizophrenia 1 aggregates between neuronal-like cells occurs in tunnelling nanotubes and is promoted by dopamine.Prions on the run: How extracellular vesicles serve as delivery vehicles for self-templating protein aggregatesEngineered bacterial hydrophobic oligopeptide repeats in a synthetic yeast prion, [REP-PSI (+)].Mammalian prion amyloid formation in bacteria.Computational analysis of candidate prion-like proteins in bacteria and their role.Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria.Spatial regulation of coalesced protein assemblies: Lessons from yeast to diseases.The prion-like RNA-processing protein HNRPDL forms inherently toxic amyloid-like inclusion bodies in bacteria.Operational plasticity enables hsp104 to disaggregate diverse amyloid and nonamyloid clients.A novel secretion and online-cleavage strategy for production of cecropin A in Escherichia coli.The Rho Termination Factor of Clostridium botulinum Contains a Prion-Like Domain with a Highly Amyloidogenic Core.Aggregation interplay between variants of the RepA-WH1 prionoid in Escherichia coli.A bacterial global regulator forms a prion.Direct assessment in bacteria of prionoid propagation and phenotype selection by Hsp70 chaperone.CbtA toxin of Escherichia coli inhibits cell division and cell elongation via direct and independent interactions with FtsZ and MreBYeast prions form infectious amyloid inclusion bodies in bacteria.Fluorescent dye ProteoStat to detect and discriminate intracellular amyloid-like aggregates in Escherichia coli.Atomic insights into the genesis of cellular filaments by globular proteins
P2860
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P2860
Conversion of a yeast prion protein to an infectious form in bacteria
description
2010 nî lūn-bûn
@nan
2010 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Conversion of a yeast prion protein to an infectious form in bacteria
@ast
Conversion of a yeast prion protein to an infectious form in bacteria
@en
type
label
Conversion of a yeast prion protein to an infectious form in bacteria
@ast
Conversion of a yeast prion protein to an infectious form in bacteria
@en
prefLabel
Conversion of a yeast prion protein to an infectious form in bacteria
@ast
Conversion of a yeast prion protein to an infectious form in bacteria
@en
P2093
P2860
P356
P1476
Conversion of a yeast prion protein to an infectious form in bacteria
@en
P2093
Ann Hochschild
Jijun Dong
Sean J Garrity
Viknesh Sivanathan
P2860
P304
10596-10601
P356
10.1073/PNAS.0913280107
P407
P577
2010-05-19T00:00:00Z