Toxic effects of amyloid fibrils on cell membranes: the importance of ganglioside GM1-Reference-Cited by-同舟云学术

Toxic effects of amyloid fibrils on cell membranes: the importance of ganglioside GM1

Published:2011-11-09 Issue:2 Volume:26 Page:818-831
ISSN:0892-6638
Container-title:The FASEB Journal
language:en
Short-container-title:FASEB j.

Author:

Bucciantini Monica¹²,Nosi Daniele³,Forzan Mario⁴,Russo Edda¹,Calamai Martino⁵,Pieri Laura⁶,Formigli Lucia³,Quercioli Franco⁷,Soria Silvia⁸,Pavone Francesco⁵,Savistchenko Jimmy⁶,Melki Ronald⁴⁶,Stefani> Massimo¹²

Affiliation:

1. Department of Biochemical Sciences, and Forensic MedicineUniversity of Florence Florence Italy

2. Research Centre on the Molecular Basis of Neurodegeneration, and Forensic MedicineUniversity of Florence Florence Italy

3. Department of Anatomy, Histology, and Forensic MedicineUniversity of Florence Florence Italy

4. Department of Animal Pathology, Food Prophylaxis, and HygieneUniversity of Pisa Pisa Italy

5. European Laboratory for Nonlinear Spectroscopy (LENS)University of Florence Florence Italy

6. Laboratoire d'Enzymologie et Biochimie StructuralesCentre National de la Recherche Scientifique Gif sur Yvette France

7. National Institute of OpticsConsiglio Nazionale delle Ricerche Florence Research Area Florence Italy

8. Nello Carrara Institute of Applied PhysicsConsiglio Nazionale delle Ricerche Florence Research Area Florence Italy

Funder

Ente Cassa di Risparmio di Firenze

Agence Nationale de la Recherche

Seventh Framework Programme

Publisher

Wiley

Subject

Genetics,Molecular Biology,Biochemistry,Biotechnology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1096/fj.11-189381

Reference69 articles.

1. Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution

2. Protein Misfolding, Functional Amyloid, and Human Disease

3. Quantitative evaluation of congo red binding to amyloid-like proteins with a beta-pleated sheet conformation.

4. Techniques to study amyloid fibril formation in vitro

5. Protein aggregation and neurodegenerative disease

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