| Literature DB >> 26196061 |
Abstract
Pin1 regulates the levels and functions of phosphoproteins by catalyzing phosphorylation-dependent cis/trans isomerization of peptidyl-prolyl bonds. Previous Pin1 inhibitors contained phosphoamino acids, which are metabolically unstable and have poor membrane permeability. In this work, we report a cell-permeable and metabolically stable nonphosphorylated bicyclic peptide as a potent and selective Pin1 inhibitor, which inhibited the intracellular Pin1 activity in cultured mammalian cells but had little effect on other isomerases such as Pin4, FKBP12, or cyclophilin A.Entities:
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Year: 2015 PMID： 26196061 PMCID： PMC4594195 DOI： 10.1021/acs.jmedchem.5b00411
Source DB: PubMed Journal: J Med Chem ISSN： 0022-2623 Impact factor: 7.446