Non-infectious aggregates of the prion protein react with several PrPSc-directed antibodies. (Q46734839)

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3 January 2020

title

Non-infectious aggregates of the prion protein react with several PrPSc-directed antibodies (English)

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3 January 2020

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10

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3 January 2020

Emiliano Biasini

1

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3 January 2020

Roberto Chiesa

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3 January 2020

4

Laura Solforosi

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3 January 2020

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M Esa Seegulam

2

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3 January 2020

Brianna N Patti

3

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Andrea Z Medrano

5

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3 January 2020

Heather M Christensen

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Assunta Senatore

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3 January 2020

R Anthony Williamson

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3 January 2020

language of work or name

English

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publication date

1 June 2008

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Journal of Neurochemistry

3 January 2020

number of pages

15

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based on heuristic

inferred from page(s)

published in

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3 January 2020

volume

105

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3 January 2020

issue

6

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page(s)

2190-2204

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GFP-tagged prion protein is correctly localized and functionally active in the brains of transgenic mice.

3 January 2020

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Two mutant prion proteins expressed in cultured cells acquire biochemical properties reminiscent of the scrapie isoform.

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Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol

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Selective and efficient immunoprecipitation of the disease-associated form of the prion protein can be mediated by nonspecific interactions between monoclonal antibodies and scrapie-associated fibrils

21 January 2018

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Motif-grafted antibodies containing the replicative interface of cellular PrP are specific for PrPSc

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Pathologic prion protein is specifically recognized in situ by a novel PrP conformational antibody.

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