N-alpha-acetylation of &#945;-synuclein increases its helical folding propensity, GM1 binding specificity and resistance to aggregation.

Bartels, Tim; Kim, Nora C; Luth, Eric S; Selkoe, Dennis J

N-alpha-acetylation of α-synuclein increases its helical folding propensity, GM1 binding specificity and resistance to aggregation.

Bartels, Tim; Kim, Nora C; Luth, Eric S; Selkoe, Dennis J.

Afiliación

Bartels T; Center for Neurologic Diseases, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts, United States of America.
Kim NC; Center for Neurologic Diseases, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts, United States of America.
Luth ES; Center for Neurologic Diseases, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts, United States of America.
Selkoe DJ; Center for Neurologic Diseases, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts, United States of America.

PLoS One ; 9(7): e103727, 2014.

Article en En | MEDLINE | ID: mdl-25075858

Asunto(s)

Gangliósido G(M1)/química; Procesamiento Proteico-Postraduccional; alfa-Sinucleína/química; Acetilación; Amiloide/química; Humanos; Agregado de Proteínas; Unión Proteica; Pliegue de Proteína; Estructura Secundaria de Proteína; Termodinámica

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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Procesamiento Proteico-Postraduccional / Alfa-Sinucleína / Gangliósido G(M1) Tipo de estudio: Prognostic_studies Límite: Humans Idioma: En Revista: PLoS One Asunto de la revista: CIENCIA / MEDICINA Año: 2014 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos

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