Prion infectivity is encoded exclusively within the structure of proteinase K-resistant fragments of synthetically generated recombinant PrPSc

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Location: Deutsche Nationalbibliothek Frankfurt am Main

ISSN: 2051-5960

Extent: Online-Ressource

Language: Englisch

Notes: online resource.

Bibliographic citation: Prion infectivity is encoded exclusively within the structure of proteinase K-resistant fragments of synthetically generated recombinant PrPSc ; volume:6 ; number:1 ; day:24 ; month:4 ; year:2018 ; pages:1-8 ; date:12.2018
Acta Neuropathologica Communications ; 6, Heft 1 (24.4.2018), 1-8, 12.2018

Creator: Wang, Fei

Contributor: Wang, Xinhe
Abskharon, Romany
Ma, Jiyan
SpringerLink (Online service)

DOI: 10.1186/s40478-018-0534-0

URN: urn:nbn:de:101:1-2018070102254417787369

Rights: Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 15.08.2025, 7:38 AM CEST

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Wang, Fei
Wang, Xinhe
Abskharon, Romany
Ma, Jiyan
SpringerLink (Online service)

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Wide distribution of prion infectivity in the peripheral tissues of vCJD and sCJD patients

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$Prion subcellular fractionation reveals infectivity spectrum, with a high titre-low PrPreslevel disparity$

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Inflammatory response of microglia to prions is controlled by sialylation of PrPSc

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Prion infectivity is encoded exclusively within the structure of proteinase K-resistant fragments of synthetically generated recombinant PrPSc

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Other Objects (12)

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Stability of BSE infectivity towards heat treatment even after proteolytic removal of prion protein

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Prion protein amino acid sequence influences formation of authentic synthetic PrPSc

Inflammatory response of microglia to prions is controlled by sialylation of PrPSc

Wide distribution of prion infectivity in the peripheral tissues of vCJD and sCJD patients

Evaluation of a combinatorial approach to prion inactivation using an oxidizing agent, SDS, and proteinase K

PrPSc spreading patterns in the brain of sheep linked to different prion types

Hereditary E200K mutation within the prion protein gene alters human iPSC derived cardiomyocyte function

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The Absence of Prion-Like Infectivity in Mice expressing Prion Protein-Like Protein

Screening anti-prion compounds and diagnosing prion diseases by amplifying PrPSc in vitro

Prions prions prions

Stability of BSE infectivity towards heat treatment even after proteolytic removal of prion protein

Prion subcellular fractionation reveals infectivity spectrum, with a high titre-low PrPreslevel disparity

Prion protein amino acid sequence influences formation of authentic synthetic PrPSc

Inflammatory response of microglia to prions is controlled by sialylation of PrPSc

Wide distribution of prion infectivity in the peripheral tissues of vCJD and sCJD patients

Evaluation of a combinatorial approach to prion inactivation using an oxidizing agent, SDS, and proteinase K

PrPSc spreading patterns in the brain of sheep linked to different prion types

Hereditary E200K mutation within the prion protein gene alters human iPSC derived cardiomyocyte function

Prion infectivity: From risk assessment to inactivation

The Absence of Prion-Like Infectivity in Mice expressing Prion Protein-Like Protein

Screening anti-prion compounds and diagnosing prion diseases by amplifying PrPSc in vitro

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Stability of BSE infectivity towards heat treatment even after proteolytic removal of prion protein

Prion subcellular fractionation reveals infectivity spectrum, with a high titre-low PrPreslevel disparity

Prion protein amino acid sequence influences formation of authentic synthetic PrPSc

Inflammatory response of microglia to prions is controlled by sialylation of PrPSc

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PrPSc spreading patterns in the brain of sheep linked to different prion types

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