Folding mechanisms steer the amyloid fibril formation propensity of highly homologous proteins-Reference-Cited by-同舟云学术

Folding mechanisms steer the amyloid fibril formation propensity of highly homologous proteins

Published:2018 Issue:13 Volume:9 Page:3290-3298
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Malgieri Gaetano¹²³⁴^ORCID,D'Abrosca Gianluca¹²³⁴^ORCID,Pirone Luciano⁵⁶⁷⁴,Toto Angelo⁸⁹¹⁰⁴,Palmieri Maddalena¹²³⁴,Russo Luigi¹²³⁴,Sciacca Michele Francesco Maria⁵⁶¹¹⁴,Tatè Rosarita¹²⁶¹³⁴,Sivo Valeria¹²³⁴,Baglivo Ilaria¹²³⁴,Majewska Roksana¹²³⁴^ORCID,Coletta Massimo¹⁴¹⁵¹⁰⁴,Pedone Paolo Vincenzo¹²³⁴,Isernia Carla¹²³⁴,De Stefano Mario¹²³⁴,Gianni Stefano⁸⁹¹⁰⁴,Pedone Emilia Maria⁵⁶⁷⁴^ORCID,Milardi Danilo⁵⁶¹¹⁴^ORCID,Fattorusso Roberto¹²³⁴^ORCID

Affiliation:

1. Department of Environmental, Biological and Pharmaceutical Sciences and Technologies

2. University of Campania “Luigi Vanvitelli”

3. 81100 Caserta

4. Italy

5. Institute of Biostructures and Bioimaging

6. CNR

7. 80134 Naples

8. Department of Biochemical Sciences “Alessandro Rossi Fanelli”

9. University of Rome “La Sapienza”

10. Roma

11. 95125 Catania

12. Institute of Genetics and Biophysics “Adriano Buzzati-Traverso”

13. 80131 Napoli

14. Department of Clinical Sciences and Translational Medicine

15. University of Rome “Tor Vergata”

Abstract

Understanding the molecular determinants of fibrillogenesis by studying the aggregation propensities of high homologous proteins with different folding pathways.

Funder

Sapienza Università di Roma

Ministero dell’Istruzione, dell’Università e della Ricerca

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2018/SC/C8SC00166A

Reference43 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