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Selective Inhibition of the Hsp90α Isoform.
Mishra, Sanket J; Khandelwal, Anuj; Banerjee, Monimoy; Balch, Maurie; Peng, Shuxia; Davis, Rachel E; Merfeld, Taylor; Munthali, Vitumbiko; Deng, Junpeng; Matts, Robert L; Blagg, Brian S J.
Afiliación
  • Mishra SJ; Department of Chemistry and Biochemistry, The University of Notre Dame, 305 McCourtney Hall, Notre Dame, IN, 46556, USA.
  • Khandelwal A; Department of Chemistry and Biochemistry, The University of Notre Dame, 305 McCourtney Hall, Notre Dame, IN, 46556, USA.
  • Banerjee M; Department of Chemistry and Biochemistry, The University of Notre Dame, 305 McCourtney Hall, Notre Dame, IN, 46556, USA.
  • Balch M; Department of Biochemistry and Molecular Biology, 246 Noble Research Center, Oklahoma State University, Stillwater, OK, 74078, USA.
  • Peng S; Department of Biochemistry and Molecular Biology, 246 Noble Research Center, Oklahoma State University, Stillwater, OK, 74078, USA.
  • Davis RE; Department of Chemistry and Biochemistry, The University of Notre Dame, 305 McCourtney Hall, Notre Dame, IN, 46556, USA.
  • Merfeld T; Department of Chemistry and Biochemistry, The University of Notre Dame, 305 McCourtney Hall, Notre Dame, IN, 46556, USA.
  • Munthali V; Department of Chemistry and Biochemistry, The University of Notre Dame, 305 McCourtney Hall, Notre Dame, IN, 46556, USA.
  • Deng J; Department of Biochemistry and Molecular Biology, 246 Noble Research Center, Oklahoma State University, Stillwater, OK, 74078, USA.
  • Matts RL; Department of Biochemistry and Molecular Biology, 246 Noble Research Center, Oklahoma State University, Stillwater, OK, 74078, USA.
  • Blagg BSJ; Department of Chemistry and Biochemistry, The University of Notre Dame, 305 McCourtney Hall, Notre Dame, IN, 46556, USA.
Angew Chem Int Ed Engl ; 60(19): 10547-10551, 2021 05 03.
Article en En | MEDLINE | ID: mdl-33621416
The 90 kDa heat shock protein (Hsp90) is a molecular chaperone that processes nascent polypeptides into their biologically active conformations. Many of these proteins contribute to the progression of cancer, and consequently, inhibition of the Hsp90 protein folding machinery represents an innovative approach toward cancer chemotherapy. However, clinical trials with Hsp90 N-terminal inhibitors have encountered deleterious side effects and toxicities, which appear to result from the pan-inhibition of all four Hsp90 isoforms. Therefore, the development of isoform-selective Hsp90 inhibitors is sought to delineate the pathological role played by each isoform. Herein, we describe a structure-based approach that was used to design the first Hsp90α-selective inhibitors, which exhibit >50-fold selectivity versus other Hsp90 isoforms.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas HSP90 de Choque Térmico / Neoplasias / Antineoplásicos Límite: Humans Idioma: En Revista: Angew Chem Int Ed Engl Año: 2021 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Alemania
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas HSP90 de Choque Térmico / Neoplasias / Antineoplásicos Límite: Humans Idioma: En Revista: Angew Chem Int Ed Engl Año: 2021 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Alemania