The N-Terminal Tandem Repeat Region of Human Prion Protein Reduces Copper: Role of Tryptophan Residues
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference21 articles.
1. Molecular Biology of Prion Diseases
2. PATHOLOGIC CONFORMATIONS OF PRION PROTEINS
3. Separation and properties of cellular and scrapie prion proteins.
4. N-terminal truncation of the scrapie-associated form of PrP by lysosomal protease(s): implications regarding the site of conversion of PrP to the protease-resistant state
5. Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins
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2. Substitutions of PrP N-terminal histidine residues modulate scrapie disease pathogenesis and incubation time in transgenic mice;PLOS ONE;2017-12-08
3. Prion protein facilitates retinal iron uptake and is cleaved at the β-site: Implications for retinal iron homeostasis in prion disorders;Scientific Reports;2017-08-29
4. An improved Bathocuproine assay for accurate valence identification and quantification of copper bound by biomolecules;Analytical Biochemistry;2016-03
5. Properties of the indole ring in metal complexes. A comparison with the phenol ring;Journal of Inorganic Biochemistry;2015-07
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