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Exploring the Functional Consequences of Protein Backbone Alteration in Ubiquitin through Native Chemical Ligation.
Werner, Halina M; Estabrooks, Samuel K; Preston, G Michael; Brodsky, Jeffrey L; Horne, W Seth.
Afiliación
  • Werner HM; Department of Chemistry, University of Pittsburgh, 219 Parkman Avenue, Pittsburgh, PA, 15260, USA.
  • Estabrooks SK; Department of Biological Sciences, University of Pittsburgh, 219 Parkman Avenue, Pittsburgh, PA, 15260, USA.
  • Preston GM; Department of Biological Sciences, University of Pittsburgh, 219 Parkman Avenue, Pittsburgh, PA, 15260, USA.
  • Brodsky JL; Department of Biological Sciences, University of Pittsburgh, 219 Parkman Avenue, Pittsburgh, PA, 15260, USA.
  • Horne WS; Department of Chemistry, University of Pittsburgh, 219 Parkman Avenue, Pittsburgh, PA, 15260, USA.
Chembiochem ; 20(18): 2346-2350, 2019 09 16.
Article en En | MEDLINE | ID: mdl-31059184
Ubiquitin (Ub) plays critical roles in myriad protein degradation and signaling networks in the cell. We report herein Ub mimetics based on backbones that blend natural and artificial amino acid units. The variants were prepared by a modular route based on native chemical ligation. Biological assays show that some are enzymatically polymerized onto protein substrates, and that the resulting Ub tags are recognized for downstream pathways. These results advance the size and complexity of folded proteins mimicked by artificial backbones and expand the functional scope of such agents.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ubiquitinas Idioma: En Revista: Chembiochem Asunto de la revista: BIOQUIMICA Año: 2019 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Alemania
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ubiquitinas Idioma: En Revista: Chembiochem Asunto de la revista: BIOQUIMICA Año: 2019 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Alemania