1404459-19-3Relevant academic research and scientific papers
Light-switched inhibitors of protein tyrosine phosphatase PTP1B based on phosphonocarbonyl phenylalanine as photoactive phosphotyrosine mimetic
Wagner, Stefan,Schütz, Anja,Rademann, J?rg
, p. 2839 - 2847 (2015)
Phosphopeptide mimetics containing the 4-phosphonocarbonyl phenylalanine (pcF) as a photo-active phosphotyrosine isoster are developed as potent, light-switchable inhibitors of the protein tyrosine phosphatase PTP1B. The photo-active inhibitors 6-10 are d
Benzoylphosphonate-based photoactive phosphopeptide mimetics for modulation of protein tyrosine phosphatases and highly specific labeling of SH2 domains
Horatscheck, André,Wagner, Stefan,Ortwein, Jutta,Kim, Boo Geun,Lisurek, Michael,Beligny, Samuel,Schütz, Anja,Rademann, J?rg
, p. 9441 - 9447 (2012/10/29)
A light switch for phosphotyrosine- recognizing proteins: Irradiation of the bioisosteric benzoylphosphonate suffices to "turn off" the activity of target proteins and to label them covalently (see scheme). Photoactive bioisosters may find applications in functional cell biology, bioanalytics, and proteome research.
