ArticleCoordination chemistry reviews2012
The Rich Electrochemistry and Redox Reactions of the Copper Sites in the Cellular Prion Protein.
Article in Coordination chemistry reviews, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed.
- Analytical Methods Used in Determining Antioxidant Activity: A Review.International journal of molecular sciences · 2021Review
- Structural Determinants of the Prion Protein N-Terminus and Its Adducts with Copper Ions.International journal of molecular sciences · 2018Review
- Copper Redox Cycling Inhibits Aβ Fibre Formation and Promotes Fibre Fragmentation, while Generating a Dityrosine Aβ Dimer.Scientific reports · 2018Article
- Spectroscopic and Theoretical Study of Cu(I) Binding to His111 in the Human Prion Protein Fragment 106-115.Inorganic chemistry · 2016Article
- Insights on antioxidant assays for biological samples based on the reduction of copper complexes-the importance of analytical conditions.International journal of molecular sciences · 2014Article
- Evolutionary implications of metal binding features in different species' prion protein: an inorganic point of view.Biomolecules · 2014Review
- Review
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
This paper reviews recent electrochemical studies of the copper complexes of prion protein (PrP) and its related peptides, and correlates their redox behavior to chemical and biologically relevant reactions. Particular emphasis is placed on the difference in redox properties between copper in the octarepeat (OR) and the non-OR domains of PrP, as well as differences between the high and low copper occupancy states in the OR domain. Several discrepancies in literature concerning these differences are discussed and reconciled. The PrP copper complexes, in comparison to copper complexes of other amyloidogenic proteins/peptides, display a more diverse and richer redox chemistry. The specific protocols and caveats that need to be considered in studying the electrochemistry and redox reactions of copper complexes of PrP, PrP-derived peptides, and other related amyloidogenic proteins are summarized.
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Registered trials
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