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dc.contributor.authorEmwas, Abdul-Hamid M.
dc.contributor.authorAl-Talla, Zeyad
dc.contributor.authorGuo, Xianrong
dc.contributor.authorAl-Ghamdi, Suliman
dc.contributor.authorAl-Masri, Harbi Tomah
dc.date.accessioned2015-08-12T09:01:07Z
dc.date.available2015-08-12T09:01:07Z
dc.date.issued2013-02-24
dc.identifier.issn07491581
dc.identifier.pmid23436479
dc.identifier.doi10.1002/mrc.3936
dc.identifier.urihttp://hdl.handle.net/10754/566051
dc.description.abstractCopper 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.
dc.description.sponsorshipWe 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.
dc.publisherWiley-Blackwell
dc.subjectcopper
dc.subjectEPR
dc.subjectneurodegenerative disorder
dc.subjectNMR
dc.subjectprion
dc.titleUtilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases
dc.typeArticle
dc.contributor.departmentImaging and Characterization Core Lab
dc.contributor.departmentAnalytical Core Lab
dc.contributor.departmentAdvanced Nanofabrication, Imaging and Characterization Core Lab
dc.identifier.journalMagnetic Resonance in Chemistry
dc.contributor.institutionFaculty of Applied Sciences, Department of Applied Chemistry, Taibah University, Madinah 1343, Saudi Arabia
kaust.personEmwas, Abdul-Hamid M.
kaust.personAl-Talla, Zeyad
kaust.personGuo, Xianrong


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