(Q51187977)

1 April 2018

title

In vitro assay for fragmentation of amyloid fibers of yeast prion protein. (English)

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1 April 2018

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Yuji Inoue

1

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1 April 2018

Masasuke Yoshida

series ordinal

2

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1 April 2018

publication date

1 May 2006

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1 April 2018

published in

Methods

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1 April 2018

volume

39

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1 April 2018

issue

1

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1 April 2018

page(s)

56-60

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1 April 2018

Novel proteinaceous infectious particles cause scrapie

cites work

1 reference

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[URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae

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A neuronal isoform of the aplysia CPEB has prion-like properties

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Rnq1: an epigenetic modifier of protein function in yeast

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The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog

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Ψ, A cytoplasmic suppressor of super-suppressor in yeast

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Support for the prion hypothesis for inheritance of a phenotypic trait in yeast

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Propagation of the yeast prion-like [psi+] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor

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Evidence for the prion hypothesis: induction of the yeast [PSI+] factor by in vitro- converted Sup35 protein

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Scrapie prions aggregate to form amyloid-like birefringent rods

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Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae.

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Synthetic mammalian prions

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beta-Helix is a likely core structure of yeast prion Sup35 amyloid fibers.

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Strong growth polarity of yeast prion fiber revealed by single fiber imaging

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Conformational diversity in a yeast prion dictates its seeding specificity

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Assembly of the yeast prion Ure2p into protein fibrils. Thermodynamic and kinetic characterization

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Mechanism of prion propagation: amyloid growth occurs by monomer addition

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Structure and replication of yeast prions

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Yeast [PSI+] Prion Aggregates Are Formed by Small Sup35 Polymers Fragmented by Hsp104

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Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers

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Hsp104 binds to yeast Sup35 prion fiber but needs other factor(s) to sever it.

7 January 2021

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Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]

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Interactions of the chaperone Hsp104 with yeast Sup35 and mammalian PrP.

7 January 2021

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Conformational variations in an infectious protein determine prion strain differences

7 January 2021

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Strains of [PSI(+)] are distinguished by their efficiencies of prion-mediated conformational conversion

7 January 2021

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A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion

7 January 2021

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Nucleated conformational conversion and the replication of conformational information by a prion determinant

7 January 2021

1 reference

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10.1016/J.YMETH.2006.04.002

7 January 2021

Identifiers

DOI

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1 April 2018

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1 April 2018