The curious case of opossum prion: a physicochemical study on copper(ii) binding to the bis-decarepeat fragment from the protein N-terminal domain-Reference-Cited by-同舟云学术

The curious case of opossum prion: a physicochemical study on copper(ii) binding to the bis-decarepeat fragment from the protein N-terminal domain

Published:2019 Issue:47 Volume:48 Page:17533-17543
ISSN:1477-9226
Container-title:Dalton Transactions
language:en
Short-container-title:Dalton Trans.

Author:

Magrì Antonio¹²³⁴,Tabbì Giovanni¹²³⁴,Cucci Lorena Maria⁵⁶⁷⁴,Satriano Cristina⁵⁶⁷⁴^ORCID,Pietropaolo Adriana⁸⁹¹⁰⁴^ORCID,Malgieri Gaetano¹¹¹²¹³¹⁴⁴,Isernia Carla¹¹¹²¹³¹⁴⁴^ORCID,La Mendola Diego¹⁵¹⁶¹⁷⁴^ORCID

Affiliation:

1. Institute of Crystallography

2. National Research Council (CNR)

3. 95126 Catania

4. Italy

5. Department of Chemical Sciences

6. University of Catania

7. Catania

8. Department of Health Sciences

9. University of Catanzaro

10. 88100 Catanzaro

11. Department of Environmental

12. Biological and Pharmaceutical Science and Technology

13. University of Campania “L. Vanvitelli”

14. 81100 Caserta

15. Department of Pharmacy

16. University of Pisa

17. 56126 Pisa

Abstract

The opossum prion tandem repeat peptide binds copper ions differently from the analogous sequence of human prion, inducing different interactions with supported lipid bilayers.

Publisher

Royal Society of Chemistry (RSC)

Subject

Inorganic Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2019/DT/C9DT02510C

Reference79 articles.

1. Pathogenic mechanisms of prion protein, amyloid-β and α-synuclein misfolding: the prion concept and neurotoxicity of protein oligomers

2. Attempt to Untangle the Prion-Like Misfolding Mechanism for Neurodegenerative Diseases

3. Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases

4. The function of the cellular prion protein in health and disease

5. More than Just a Phase: Prions at the Crossroads of Epigenetic Inheritance and Evolutionary Change

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