Home > Publications database > Structural Determinants of the Prion Protein N-Terminus and Its Adducts with Copper Ions > print |
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245 | _ | _ | |a Structural Determinants of the Prion Protein N-Terminus and Its Adducts with Copper Ions |
260 | _ | _ | |a Basel |c 2019 |b Molecular Diversity Preservation International |
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520 | _ | _ | |a The N-terminus of the prion protein is a large intrinsically disordered region encompassing approximately 125 amino acids. In this paper, we review its structural and functional properties, with a particular emphasis on its binding to copper ions. The latter is exploited by the region’s conformational flexibility to yield a variety of biological functions. Disease-linked mutations and proteolytic processing of the protein can impact its copper-binding properties, with important structural and functional implications, both in health and disease progression. |
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700 | 1 | _ | |a Rossetti, Giulia |0 P:(DE-Juel1)145921 |b 1 |
700 | 1 | _ | |a Quintanar, Liliana |0 P:(DE-HGF)0 |b 2 |e Corresponding author |
700 | 1 | _ | |a Carloni, Paolo |0 P:(DE-Juel1)145614 |b 3 |e Corresponding author |
773 | _ | _ | |a 10.3390/ijms20010018 |g Vol. 20, no. 1, p. 18 - |0 PERI:(DE-600)2019364-6 |n 1 |p 18 |t International journal of molecular sciences |v 20 |y 2019 |x 1422-0067 |
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