Journal
ORGANIC & BIOMOLECULAR CHEMISTRY
Volume 15, Issue 45, Pages 9595-9598Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c7ob02562a
Keywords
-
Categories
Funding
- National Institutes of Health [GM110208, GM122459]
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available