Journal Article

FZJ-2015-03404

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Computational Studies on the Prion Protein

Rossetti, G.FZJ* ; Bongarzone, S. ; Carloni, P. (Corresponding Author)FZJ*

2013
Bentham Science Publishers Spring House, Pa.

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Please use a persistent id in citations: doi:10.2174/15680266113136660170

Abstract: Prion diseases are rare neurodegenerative diseases characterized by the conversion of the prion protein from its native state (PrPC) towards the so-called 'scrapie form', rich in β-strands. Computational approaches, here briefly reviewed, are instrumental to understand the intrinsic instability of PrPC fold and how the latter is affected by mutations, binding of metals as well as by different environmental conditions, such as pH and temperature. These studies also provide a structural basis for the binding of anti-prion compounds, which may block the conversion to the scrapie form and, consequently, may inhibit fibril formation.

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Contributing Institute(s):

1. Computational Biomedicine (IAS-5)
2. Jülich Supercomputing Center (JSC)
3. GRS (GRS)

Research Program(s):

1. 411 - Computational Science and Mathematical Methods (POF2-411) (POF2-411)

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Database coverage:
; BIOSIS Previews ; BIOSIS Reviews Reports And Meetings ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; SCOPUS ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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