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    Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases

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    Type
    Article
    Authors
    Emwas, Abdul-Hamid M.
    Al-Talla, Zeyad
    Guo, Xianrong
    Al-Ghamdi, Suliman
    Al-Masri, Harbi Tomah
    KAUST Department
    Advanced Nanofabrication, Imaging and Characterization Core Lab
    Analytical Chemistry Core Lab
    Analytical Core Lab
    Imaging and Characterization Core Lab
    Date
    2013-02-24
    Online Publication Date
    2013-02-24
    Print Publication Date
    2013-05
    Permanent link to this record
    http://hdl.handle.net/10754/566051
    
    Metadata
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    Abstract
    Copper is an essential nutrient for the normal development of the brain and nervous system, although the hallmark of several neurological diseases is a change in copper concentrations in the brain and central nervous system. Prion protein (PrP) is a copper-binding, cell-surface glycoprotein that exists in two alternatively folded conformations: a normal isoform (PrPC) and a disease-associated isoform (PrPSc). Prion diseases are a group of lethal neurodegenerative disorders that develop as a result of conformational conversion of PrPC into PrPSc. The pathogenic mechanism that triggers this conformational transformation with the subsequent development of prion diseases remains unclear. It has, however, been shown repeatedly that copper plays a significant functional role in the conformational conversion of prion proteins. In this review, we focus on current research that seeks to clarify the conformational changes associated with prion diseases and the role of copper in this mechanism, with emphasis on the latest applications of NMR and EPR spectroscopy to probe the interactions of copper with prion proteins. Copyright © 2013 John Wiley & Sons, Ltd.
    Citation
    Emwas, A.-H. M., Al-Talla, Z. A., Guo, X., Al-Ghamdi, S., & Al-Masri, H. T. (2013). Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases. Magnetic Resonance in Chemistry, 51(5), 255–268. doi:10.1002/mrc.3936
    Sponsors
    We thank King Abdullah University of Science and Technology (KAUST) for the financial support. Special thanks to Dr. Jamil Saad from the University of Alabama at Birmingham, USA, and Dr. Virginia Unkefer from KAUST for their assistance and helpful remarks.
    Publisher
    Wiley
    Journal
    Magnetic Resonance in Chemistry
    DOI
    10.1002/mrc.3936
    PubMed ID
    23436479
    ae974a485f413a2113503eed53cd6c53
    10.1002/mrc.3936
    Scopus Count
    Collections
    Articles; Analytical Chemistry Core Lab; Imaging and Characterization Core Lab

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