The effects of the cellular and infectious prion protein on the neuronal adaptor protein X11α

O'Sullivan, Jack; Comerford, Emma J.; Rachidi, Walid; Scott, Michael; Hooper, Nigel M.; McMahon, Hilary E.M.

doi:10.1016/j.bbagen.2015.08.010

Cited by 2 publications

(2 citation statements)

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“…The large number of possible combinations of copper ions allows for a wide range of copper coordination complexes, ranging from monodentate to hexadentate [190][191][192]. Importantly, Cu(I) has d 10 configurations and forms colorless and diamagnetic compounds, whereas Cu (II) has d 9 configurations and forms colored and paramagnetic compounds [10,11,[193][194][195][196][197][198][199][200][201][202][203]. There is an important difference in stability of Cu(I) and Cu (II) ions that strictly defines their biological role in the living organisms.…”

Section: Copper Ions In Nervous System Development and Neurodegeneratmentioning

confidence: 99%

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Using NMR spectroscopy to investigate the role played by copper in prion diseases

et al. 2020

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Prion diseases are a group of rare neurodegenerative disorders that develop as a result of the conformational conversion of normal prion protein (PrP C) to the disease-associated isoform (PrP Sc). The mechanism that actually causes disease remains unclear. However, the mechanism underlying the conformational transformation of prion protein is partially understood-in particular, there is strong evidence that copper ions play a significant functional role in prion proteins and in their conformational conversion. Various models of the interaction of copper ions with prion proteins have been proposed for the Cu (II)-binding, cell-surface glycoprotein known as prion protein (PrP). Changes in the concentration of copper ions in the brain have been associated with prion diseases and there is strong evidence that copper plays a significant functional role in the conformational conversion of PrP. Nevertheless, because copper ions have been shown to have both a positive and negative effect on prion disease onset, the role played by Cu (II) ions in these diseases remains a topic of debate. Because of the unique properties of paramagnetic Cu (II) ions in the magnetic field, their interactions with PrP can be tracked even at single atom resolution using nuclear magnetic resonance (NMR) spectroscopy. Various NMR approaches have been utilized to study the kinetic, thermodynamic, and structural properties of Cu (II)-PrP interactions. Here, we highlight the different models of copper interactions with PrP with particular focus on studies that use NMR spectroscopy to investigate the role played by copper ions in prion diseases.

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Section: Copper Ions In Nervous System Development and Neurodegeneratmentioning

confidence: 99%

“…This suggests that PrP is a target of copper-catalyzed oxidation and that this reaction leads to profound structural changes in the protein. Oxidation therefore must be taken into account as a potential side reaction when considering the role of copper in prion disease [52,53,202,203].…”

Section: Copper Ions In Nervous System Development and Neurodegeneratmentioning

confidence: 99%