The DOI matches its Crossref record; 84 of the 84 references it cites were found in a registry or an index.
Copper and the Prion Protein: Methods, Structures, Function, and Disease
Open accessAbstract
The transmissible spongiform encephalopathies (TSEs) arise from conversion of the membrane-bound prion protein from PrP C to PrP Sc. Examples of the TSEs include mad cow disease, chronic wasting disease in deer and elk, scrapie in goats and sheep, and kuru and Creutzfeldt-Jakob disease in humans. Although the precise function of PrP C in healthy tissues is not known, recent research demonstrates that it binds Cu(II) in an unusual and highly conserved region of the protein termed the octarepeat domain. This review describes recent connections between copper and PrP C, with an emphasis on the electron paramagnetic resonance elucidation of the specific copper-binding sites, insights into PrP C function, and emerging connections between copper and prion disease.
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Cites
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The cellular prion protein binds copper in vivo
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Cited by
Physiology of the prion protein
Linden, R., Martins, V. R., Prado, M. A. M., Cammarota, M., Izquierdo, I., & Brentani, R. R. (2008) · Physiological Reviews · doi:10.1152/physrev.00007.2007 · Cited by 617
Stys, P. K., You, H., & Zamponi, G. W. (2012) · The Journal of Physiology · doi:10.1113/jphysiol.2011.225276 · Cited by 115
Neurodegenerative diseases and exposure to the environmental metals Mn, Pb, and Hg
Charlet, L., Chapron, Y., Faller, P., Kirsch, R., Stone, A. T., & Baveye, P. C. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.05.012 · Cited by 92
Multiple effects of copper on NMDA receptor currents
Marchetti, C., Baranowska-Bosiacka, I., & Gavazzo, P. (2014) · Brain Research · doi:10.1016/j.brainres.2013.10.029 · Cited by 37
The N Terminus of α‐Synuclein Forms Cu II ‐Bridged Oligomers
Drew, S. C. (2015) · Chemistry – A European Journal · doi:10.1002/chem.201500236 · Cited by 26
Metadata
- Authors
- Millhauser, G. L.
- Venue
- Annual Review of Physical Chemistry
- Publisher
- Annual Reviews
- Published
- 2007-05-01
- Volume
- 58
- Issue
- 1
- Pages
- 299-320
- ISSN
- 0066-426X (ISSN-L)
- 1545-1593
- OpenAlex
- W2126111700
- Cited by
- 263
- References
- 84
- FWCI
- 1.11
- Type
- journal article
- Language
- en
- Open access
- green
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- Millhauser, G. L. (2007). Copper and the Prion Protein: Methods, Structures, Function, and Disease. Annual Review of Physical Chemistry. https://doi.org/10.1146/annurev.physchem.58.032806.104657
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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