期刊
ORGANIC & BIOMOLECULAR CHEMISTRY
卷 15, 期 45, 页码 9595-9598出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c7ob02562a
关键词
-
资金
- National Institutes of Health [GM110208, GM122459]
Protein tyrosine phosphatases (PTPs) have been challenging targets for inhibitor design, because all PTPs share a highly conserved active site structure, which is positively charged and requires negatively charged moieties for tight binding. In this study, we developed cell-permeable bicyclic peptidyl inhibitors against T-cell PTP (TCPTP), which feature a cell-penetrating motif in one ring and a target-binding sequence in the second ring.
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