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Refolding of helical soluble α-synuclein through transient interaction with lipid interfaces.
Rovere, Matteo; Sanderson, John B; Fonseca-Ornelas, Luis; Patel, Dushyant S; Bartels, Tim.
Afiliación
  • Rovere M; Ann Romney Center for Neurologic Diseases, Brigham and Women's Hospital and Harvard Medical School, Boston, MA, USA.
  • Sanderson JB; Ann Romney Center for Neurologic Diseases, Brigham and Women's Hospital and Harvard Medical School, Boston, MA, USA.
  • Fonseca-Ornelas L; Ann Romney Center for Neurologic Diseases, Brigham and Women's Hospital and Harvard Medical School, Boston, MA, USA.
  • Patel DS; Ann Romney Center for Neurologic Diseases, Brigham and Women's Hospital and Harvard Medical School, Boston, MA, USA.
  • Bartels T; Ann Romney Center for Neurologic Diseases, Brigham and Women's Hospital and Harvard Medical School, Boston, MA, USA.
FEBS Lett ; 592(9): 1464-1472, 2018 05.
Article en En | MEDLINE | ID: mdl-29633780
ABSTRACT
α-Synuclein (αSyn) is a key player in the pathogenesis of Parkinson's disease and other synucleinopathies. Here, we report the existence of a novel soluble α-helical conformer of αSyn, obtained through transient interaction with lipid interfaces, and propose dynamic oligomerization as the mechanism underlying its stability. The conformational space of αSyn appears to be highly context-dependent, and lipid bilayers might thus play crucial roles as molecular chaperones in a cellular environment.
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Alfa-Sinucleína / Metabolismo de los Lípidos / Replegamiento Proteico Límite: Humans Idioma: En Revista: FEBS Lett Año: 2018 Tipo del documento: Article País de afiliación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Alfa-Sinucleína / Metabolismo de los Lípidos / Replegamiento Proteico Límite: Humans Idioma: En Revista: FEBS Lett Año: 2018 Tipo del documento: Article País de afiliación: Estados Unidos