Infectious fold and amyloid propagation in Podospora anserina. - Wikidata - awgldk - TriplyDB

Infectious fold and amyloid propagation in Podospora anserina.

Infectious fold and amyloid propagation in Podospora anserina.

http://www.wikidata.org/entity/Q37375820

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Insights into intragenic and extragenic effectors of prion propagation using chimeric prion proteins.Solid-state NMR spectroscopy reveals that E. coli inclusion bodies of HET-s(218-289) are amyloids.

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P2860

Infectious fold and amyloid propagation in Podospora anserina.

http://www.wikidata.org/entity/Q37375820

description

article científic

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article scientifique

@fr

articolo scientifico

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artigo científico

@pt

bilimsel makale

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scientific article published on 28 January 2007

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Infectious fold and amyloid propagation in Podospora anserina.

@en

Infectious fold and amyloid propagation in Podospora anserina.

@nl

type

label

Infectious fold and amyloid propagation in Podospora anserina.

@en

Infectious fold and amyloid propagation in Podospora anserina.

@nl

prefLabel

Infectious fold and amyloid propagation in Podospora anserina.

@en

Infectious fold and amyloid propagation in Podospora anserina.

@nl

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Infectious fold and amyloid propagation in Podospora anserina.

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P2093

Marie-Lise Maddelein

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P2860

Amyloid aggregates of the HET-s prion protein are infectious.

Structure of the cross-beta spine of amyloid-like fibrils

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

Comparative analysis of programmed cell death pathways in filamentous fungi

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

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

Prions in Saccharomyces and Podospora spp.: protein-based inheritance.

Conformational transition occurring upon amyloid aggregation of the HET-s prion protein of Podospora anserina analyzed by hydrogen/deuterium exchange and mass spectrometry.

The sequences appended to the amyloid core region of the HET-s prion protein determine higher-order aggregate organization in vivo.

Prions: infectious proteins with genetic properties.

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44-47

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scholarly article

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10.4161/PRI.1.1.4083

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1

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1

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2007-01-28T00:00:00Z

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23934041

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19164904

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2633707

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