Structural and dynamical determinants of a β-sheet-enriched intermediate involved in amyloid fibrillar assembly of human prion protein-Reference-Cited by-同舟云学术

Structural and dynamical determinants of a β-sheet-enriched intermediate involved in amyloid fibrillar assembly of human prion protein

Published:2022 Issue:35 Volume:13 Page:10406-10427
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Russo Luigi¹^ORCID,Salzano Giulia²^ORCID,Corvino Andrea¹,Bistaffa Edoardo³,Moda Fabio³,Celauro Luigi²^ORCID,D'Abrosca Gianluca¹,Isernia Carla¹^ORCID,Milardi Danilo⁴^ORCID,Giachin Gabriele⁵,Malgieri Gaetano¹,Legname Giuseppe²⁶,Fattorusso Roberto¹^ORCID

Affiliation:

1. Department of Environmental, Biological and Pharmaceutical Science and Technology, University of Campania Luigi Vanvitelli, Caserta, Italy

2. Laboratory of Prion Biology, Department of Neuroscience, Scuola Internazionale Superiore di Studi Avanzati (SISSA), Trieste, Italy

3. Fondazione IRCCS Istituto Neurologico Carlo Besta, Division of Neurology 5 and Neuropathology, Milano, Italy

4. Institute of Crystallography, National Research Council, Catania, Italy

5. Department of Chemical Sciences (DiSC), University of Padua, Padova, Italy

6. ELETTRA Laboratory, Sincrotrone Trieste S.C.p.A., Basovizza, Trieste, Italy

Abstract

The N-ter domain in HuPrP regulates the folding mechanism by tuning the long-range μs–ms dynamics. Removal of the N-ter domain triggers the formation of a stable β-enriched intermediate state inducing amyloid aggregates with HuPrPSc seeding activity.

Funder

Ministero dell’Istruzione, dell’Università e della Ricerca

Ministero della Salute

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2022/SC/D2SC00345G

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4. PrPC Controls via Protein Kinase A the Direction of Synaptic Plasticity in the Immature Hippocampus

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