The human prion protein α2 helix: A thermodynamic study of its conformational preferences-Reference-Cited by-同舟云学术

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The human prion protein α2 helix: A thermodynamic study of its conformational preferences

Published:2005-02-01 Issue:1 Volume:59 Page:72-79
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Bioinformatics
language:en
Short-container-title:Proteins

Author:

Tizzano Barbara,Palladino Pasquale,De Capua Antonia,Marasco Daniela,Rossi Filomena,Benedetti Ettore,Pedone Carlo,Ragone Raffaele,Ruvo Menotti

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

Reference54 articles.

1. A proposed structural model for amyloid fibril elongation: domain swapping forms an interdigitating β-structure polymer;Sinha;Protein Eng,2001

2. Prions;Prusiner;Proc Natl Acad Sci USA,1998

3. Deadly conformations-protein misfolding in prion disease;Horwich;Cell,1977

4. Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins;Pan;Proc Natl Acad Sci USA,1993

5. NMR structure of the mouse prion protein domain PrP(121-231);Riek;Nature,1996

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