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Chaperone substrate provides missing link for cancer drug discovery.
Byrd, Katherine M; Blagg, Brian S J.
Afiliación
  • Byrd KM; From the Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46545.
  • Blagg BSJ; From the Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46545.
J Biol Chem ; 293(7): 2381-2382, 2018 02 16.
Article en En | MEDLINE | ID: mdl-29453286
ABSTRACT
Both Hsp70 and Hsp90 chaperones are overexpressed in cancer, making them relevant targets for the development of cancer chemotherapeutics, but a lack of biomolecular readouts for Hsp70 inhibition has limited the pursuit of specific inhibitors for this enzyme. A new study from Cesa et al. identifies two inhibitors of apoptosis proteins (IAPs) as specific client substrates of Hsp70. These results establish biomarkers that can be utilized to monitor Hsp70 inhibition and provide a framework for future efforts to deconvolute chaperone networks.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Proteínas HSP90 de Choque Térmico / Proteínas HSP70 de Choque Térmico / Descubrimiento de Drogas / Neoplasias Límite: Humans Idioma: En Revista: J Biol Chem Año: 2018 Tipo del documento: Article

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Proteínas HSP90 de Choque Térmico / Proteínas HSP70 de Choque Térmico / Descubrimiento de Drogas / Neoplasias Límite: Humans Idioma: En Revista: J Biol Chem Año: 2018 Tipo del documento: Article