Neuroprotective alpha-cleavage of the human prion protein significantly impacts Cu(ii) coordination at its His111 site-Reference-Cited by-同舟云学术

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Neuroprotective alpha-cleavage of the human prion protein significantly impacts Cu(ii) coordination at its His111 site

Published:2018 Issue:28 Volume:47 Page:9274-9282
ISSN:1477-9226
Container-title:Dalton Transactions
language:en
Short-container-title:Dalton Trans.

Author:

Sánchez-López Carolina¹²³⁴,Fernández Claudio O.⁵⁶⁷⁸⁹,Quintanar Liliana¹²³⁴^ORCID

Affiliation:

1. Departamento de Química

2. Centro de Investigación y de Estudios Avanzados (Cinvestav)

3. Mexico City

4. Mexico

5. Max Planck Laboratory for Structural Biology

6. Chemistry and Molecular Biophysics of Rosario (MPLbioR

7. UNR-MPIbpC) and Instituto de Investigaciones para el Descubrimiento de Fármacos de Rosario (IIDEFAR

8. UNR-CONICET)

9. Universidad Nacional de Rosario

Abstract

Alpha-cleavage proteolytic processing of human prion protein significantly impacts its Cu(ii) coordination properties at the His111 site.

Funder

Consejo Nacional de Ciencia y Tecnología

Publisher

Royal Society of Chemistry (RSC)

Subject

Inorganic Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2018/DT/C7DT03400H

Reference39 articles.

1. Physiology of the Prion Protein

2. α-Cleavage of cellular prion protein

3. PrPC-related signal transduction is influenced by copper, membrane integrity and the alpha cleavage site

4. α-cleavage of the prion protein occurs in a late compartment of the secretory pathway and is independent of lipid rafts

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1. The role of d-block metal ions in neurodegenerative diseases;Comprehensive Inorganic Chemistry III;2023

2. β-cleavage of the human prion protein impacts Cu(II) coordination at its non-octarepeat region;Journal of Inorganic Biochemistry;2022-03

3. Dissecting the copper bioinorganic chemistry of the functional and pathological roles of the prion protein: Relevance in Alzheimer's disease and cancer;Current Opinion in Chemical Biology;2022-02

4. EPR of copper centers in the prion protein;Methods in Enzymology;2022

5. Amyloid β Perturbs Cu(II) Binding to the Prion Protein in a Site-Specific Manner: Insights into Its Potential Neurotoxic Mechanisms;Inorganic Chemistry;2021-05-27

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