A para-nitrophenol phosphonate probe labels distinct serine hydrolases of Arabidopsis.

Activity-based protein profiling represents a powerful methodology to probe the activity state of enzymes under various physiological conditions. Here we present the development of a para-nitrophenol phosphonate activity-based probe with structural similarities to the potent agrochemical paraoxon. W...

תיאור מלא

מידע ביבליוגרפי
Main Authors: Nickel, S, Kaschani, F, Colby, T, van der Hoorn, R, Kaiser, M
פורמט: Journal article
שפה:English
יצא לאור: 2012