Combining an Hsp70 inhibitor with either an N- or C-terminal Hsp90 inhibitor produces mechanistically distinct phenotypes

被引：13

作者：

Wang, Y. ^{[1
]}

McAlpine, S. R. ^{[1
]}

机构：

[1] Univ New S Wales, Dept Chem, Sydney, NSW 2052, Australia

来源：

ORGANIC & BIOMOLECULAR CHEMISTRY | 2015年 / 13卷 / 12期

关键词：

SHOCK-PROTEIN; 90; INDUCED APOPTOSIS; SMALL-MOLECULE; CANCER; SANSALVAMIDE; BINDING;

D O I：

10.1039/c5ob00147a

中图分类号：

O62 [有机化学];

学科分类号：

070303 ; 081704 ;

摘要：

Blocking the function of both heat shock protein 90 and 70 (Hsp90 and Hsp70) simultaneously limits these chaperones' cytoprotective effects on cancer cells. The unique phenotype associated with modulating Hsp90's C-terminus, when used in combination with Hsp70 inhibitors, produces a synergistic and highly relevant dual chemotherapy regimen.

引用

页码：3691 / 3698

页数：8

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