Structural Rearrangements at Physiological pH: Nuclear Magnetic Resonance Insights from the V210I Human Prion Protein Mutant-Reference-Cited by-同舟云学术

Structural Rearrangements at Physiological pH: Nuclear Magnetic Resonance Insights from the V210I Human Prion Protein Mutant

Published:2012-09-12 Issue:38 Volume:51 Page:7465-7474
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Biljan Ivana¹,Ilc Gregor¹²,Giachin Gabriele³,Plavec Janez¹²⁴,Legname Giuseppe³⁵

Affiliation:

1. Slovenian NMR Centre, National Institute of Chemistry, Hajdrihova 19, SI-1000 Ljubljana, Slovenia

2. EN→FIST Centre of Excellence, Dunajska 156, SI-1001 Ljubljana, Slovenia

3. Laboratory of Prion Biology, Department of Neuroscience, Scuola Internazionale Superiore di Studi Avanzati (SISSA), via Bonomea 265, Trieste, Italy

4. Faculty of Chemistry and Chemical Technology, University of Ljubljana, Aškerčeva cesta 5, SI-1000 Ljubljana, Slovenia

5. ELETTRA Laboratory, Sincrotrone Trieste S.C.p.A., I-34149 Basovizza, Trieste, Italy

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi3009856

Reference54 articles.

1. Legname, G., Giachin, G., and Benetti, F. (2012) Structural Studies of Prion Proteins and Prions, Non-fibrillar Amyloidogenic Protein Assemblies: Common Cytotoxins Underlying Degenerative Diseases(Rahimi, F. and Bitan, G., Eds.) pp289–317,Springer,Dordrecht, The Netherlands.

2. NMR characterization of the full-length recombinant murine prion protein, m PrP(23-231)

3. NMR solution structure of the human prion protein

4. The prion protein and lipid rafts (Review)

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