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Structure of the insulin receptor-insulin complex by single-particle cryo-EM analysis.
Scapin, Giovanna; Dandey, Venkata P; Zhang, Zhening; Prosise, Winifred; Hruza, Alan; Kelly, Theresa; Mayhood, Todd; Strickland, Corey; Potter, Clinton S; Carragher, Bridget.
Afiliación
  • Scapin G; Merck & Co., Department of Biochemical Engineering & Structure, 2000 Galloping Hill Road, Kenilworth, New Jersey 07033, USA.
  • Dandey VP; Simons Electron Microscopy Center, National Resource for Automated Molecular Microscopy, New York Structural Biology Center, 89 Convent Avenue, New York, New York 10027, USA.
  • Zhang Z; Simons Electron Microscopy Center, National Resource for Automated Molecular Microscopy, New York Structural Biology Center, 89 Convent Avenue, New York, New York 10027, USA.
  • Prosise W; Merck & Co., Department of Biochemical Engineering & Structure, 2000 Galloping Hill Road, Kenilworth, New Jersey 07033, USA.
  • Hruza A; Merck & Co., Department of Biochemical Engineering & Structure, 2000 Galloping Hill Road, Kenilworth, New Jersey 07033, USA.
  • Kelly T; Merck & Co., Department of Biophysics, NMR & Protein Products Characterization, 2000 Galloping Hill Road, Kenilworth, New Jersey 07033, USA.
  • Mayhood T; Merck & Co., Department of Biophysics, NMR & Protein Products Characterization, 2000 Galloping Hill Road, Kenilworth, New Jersey 07033, USA.
  • Strickland C; Merck & Co., Department of Biochemical Engineering & Structure, 2000 Galloping Hill Road, Kenilworth, New Jersey 07033, USA.
  • Potter CS; Simons Electron Microscopy Center, National Resource for Automated Molecular Microscopy, New York Structural Biology Center, 89 Convent Avenue, New York, New York 10027, USA.
  • Carragher B; Simons Electron Microscopy Center, National Resource for Automated Molecular Microscopy, New York Structural Biology Center, 89 Convent Avenue, New York, New York 10027, USA.
Nature ; 556(7699): 122-125, 2018 04 05.
Article en En | MEDLINE | ID: mdl-29512653
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Receptor de Insulina / Microscopía por Crioelectrón / Multimerización de Proteína / Insulina Límite: Humans Idioma: En Revista: Nature Año: 2018 Tipo del documento: Article País de afiliación: Estados Unidos
Texto completo
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XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Receptor de Insulina / Microscopía por Crioelectrón / Multimerización de Proteína / Insulina Límite: Humans Idioma: En Revista: Nature Año: 2018 Tipo del documento: Article País de afiliación: Estados Unidos