期刊
BIOCONJUGATE CHEMISTRY
卷 21, 期 10, 页码 1880-1889出版社
AMER CHEMICAL SOC
DOI: 10.1021/bc100266v
关键词
-
类别
资金
- National Institutes of Health [PHS 5R37 DK015556, NRSA 1 F30 ES016484-01, NRSA 5 T32 GM070421]
- David Robertson Fellowship
Bivalent small molecules composed of a targeting element and an element that recruits endogenous proteins have been shown to block protein-protein interactions in some systems. We have attempted to apply such an approach to disrupt the interaction of the estrogen receptor a with either its associated coactivators or its dimerization partner (i.e., another estrogen receptor). We show here that a conjugate capable of simultaneously binding both the estrogen receptor and a recruited protein (FK506 Binding Protein 12 kDa) is, however, incapable of disrupting the multimeric estrogen receptor dimer/coactivator complex both in vitro and in cell-based reporter gene assays. We postulate why it may not be possible to disrupt this particular protein-protein complex-as well as other systems having high topological tolerance-with such bivalent inhibitors.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据