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FUS Zigzags Its Way to Cross Beta.
Holehouse, Alex S; Pappu, Rohit V.
Afiliación
  • Holehouse AS; Department of Biomedical Engineering and Center for Biological Systems Engineering, Washington University in Saint Louis, Saint Louis, MO 63130, USA.
  • Pappu RV; Department of Biomedical Engineering and Center for Biological Systems Engineering, Washington University in Saint Louis, Saint Louis, MO 63130, USA. Electronic address: pappu@wustl.edu.
Cell ; 171(3): 499-500, 2017 10 19.
Article en En | MEDLINE | ID: mdl-29053965
ABSTRACT
The low-complexity domain (LCD) of the FUS protein forms concentration-dependent assemblies, including liquid droplets and fibril-based hydrogels. The molecular structures of FUS within different assemblies and their functional relevance are subjects of intense debate. Murray et al. report an atomic-level structural model for FUS LCD fibrils that answers some questions and raises new ones.
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Proteína FUS de Unión a ARN Idioma: En Revista: Cell Año: 2017 Tipo del documento: Article País de afiliación: Estados Unidos
Texto completo
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Proteína FUS de Unión a ARN Idioma: En Revista: Cell Año: 2017 Tipo del documento: Article País de afiliación: Estados Unidos