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Ubiquitin Stability and the Lys 63‐Linked Polyubiquitination Site Are Compromised on Copper Binding
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Citations
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References
2007
Year
Met 1Protein AssemblyMolecular BiologyNeurochemical BiomarkersChemical BiologyAlzheimer's DiseaseProtein FoldingCopper BindingNeurologyNeuropathologyProtein ChemistryToxic AggregatesBiochemistryNeuropharmacologyNeurodegenerationPharmacologyPolyubiquitination Site AreNeurodegenerative DiseasesUbiquitin StabilityNatural SciencesMetalloproteinBioactive MetalNeuroscienceOxygen DonorMedicine
Appetite for copper: Ubiquitin is a hallmark of toxic aggregates in neurodegenerative disorders, where metal ions are believed to play a crucial role. Copper(II) ions have been found to bind to ubiquitin at a specific site involving the N-terminal nitrogen of Met 1 and three oxygen donor ligands in a tetragonal geometry. The affinity of this site for copper(II) is comparable to that of other amyloidogenic proteins involved in neurodegenerative disorders. Supporting information for this article is available on the WWW under http://www.wiley-vch.de/contents/jc_2002/2007/z701987_s.pdf or from the author. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.
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