Copper<sup>2+</sup> Binding to &#945;-Synuclein. Histidine50 Can Form a Ternary Complex with Cu<sup>2+</sup> at the N-Terminus but Not a Macrochelate.

Tian, Yao; Stanyon, Helen F; Barritt, Joseph D; Mayet, Uroosa; Patel, Pelak; Karamani, Elena; Fusco, Giuliana; Viles, John H

Copper²⁺ Binding to α-Synuclein. Histidine50 Can Form a Ternary Complex with Cu²⁺ at the N-Terminus but Not a Macrochelate.

Tian, Yao; Stanyon, Helen F; Barritt, Joseph D; Mayet, Uroosa; Patel, Pelak; Karamani, Elena; Fusco, Giuliana; Viles, John H.

Afiliación

Tian Y; School of Biological and Chemical Sciences , Queen Mary, University of London Mile End Road , London E1 4NS , United Kingdom.
Stanyon HF; School of Biological and Chemical Sciences , Queen Mary, University of London Mile End Road , London E1 4NS , United Kingdom.
Barritt JD; School of Biological and Chemical Sciences , Queen Mary, University of London Mile End Road , London E1 4NS , United Kingdom.
Mayet U; Department of Life Sciences , Imperial College London , London SW7 2AZ , United Kingdom.
Patel P; School of Biological and Chemical Sciences , Queen Mary, University of London Mile End Road , London E1 4NS , United Kingdom.
Karamani E; School of Biological and Chemical Sciences , Queen Mary, University of London Mile End Road , London E1 4NS , United Kingdom.
Fusco G; School of Biological and Chemical Sciences , Queen Mary, University of London Mile End Road , London E1 4NS , United Kingdom.
Viles JH; Centre for Misfolding Diseases, Department of Chemistry , University of Cambridge , Cambridge CB1 1EW , United Kingdom.

Inorg Chem ; 58(22): 15580-15589, 2019 Nov 18.

Article en En | MEDLINE | ID: mdl-31697492

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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Inorg Chem Año: 2019 Tipo del documento: Article País de afiliación: Reino Unido Pais de publicación: Estados Unidos

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