The Octapeptide Repeats in Mammalian Prion Protein Constitute a pH-dependent Folding and Aggregation Site (Q27642560)

https://api.crossref.org/works/10.1016/J.JMB.2003.09.048

3 April 2024

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.048

3 April 2024

author name string

Ralph Zahn

full work available at URL

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language of work or name

English

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publication date

28 November 2003

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https://api.elsevier.com/content/article/PII:S0022283603012014?httpAccept=text/xml

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.048

https://api.elsevier.com/content/article/PII:S0022283603012014?httpAccept=text/plain

3 April 2024

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.048

Journal of Molecular Biology

3 April 2024

published in

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volume

334

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issue

3

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page(s)

477-88

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cites work

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Analysis of 27 mammalian and 9 avian PrPs reveals high conservation of flexible regions of the prion protein

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Heparin-like molecules bind differentially to prion-proteins and change their intracellular metabolic fate

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Identification of the heparan sulfate binding sites in the cellular prion protein

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Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible

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Molecular features of the copper binding sites in the octarepeat domain of the prion protein

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Identifiers