@article {H. Richau:2010:1570-1646:328,
title = "Studies on Plant-Pathogen Interactions Using Activity-based Proteomics",
journal = "Current Proteomics",
parent_itemid = "infobike://ben/cp",
publishercode ="ben",
year = "2010",
volume = "7",
number = "4",
publication date ="2010-12-01T00:00:00",
pages = "328-336",
itemtype = "ARTICLE",
issn = "1570-1646",
url = "https://www.ingentaconnect.com/content/ben/cp/2010/00000007/00000004/art00010",
doi = "doi:10.2174/157016410793611800",
keyword = "Phytophthora infestans, Cladosporium fulvum, PLCP, SylA, Activity-based protein profiling, zymograms, fluorophosphonate, N-terminal threonine, AVR2, PLCP inhibitor E-64, cysteine protease, methylestrases MES2, Papain-like cysteine protease, pathogen effectors, MES3, Pseudomonas syringae, activity-based probes, Botrytis cinerea, EPICs, ABPP, oomycete, Programmed cell death, plant pathogen interactions, Serine hydrolase, proteasome, serine hydrolases, Serine hydrolases, S-formyl glutathione hydrolase",
author = "H. Richau, Kerstin and A.L. van der Hoorn, Renier",
abstract = "To accelerate functional annotation of proteins with a role during plant-pathogen interactions it is essential to monitor activities of proteins rather than the abundance of transcripts and proteins, since many proteins are posttranslationally regulated during antagonistic interactions. Activity-based protein profiling (ABPP) displays the active proteome using small molecule probes that react with the active site of proteins in an activity-dependent manner. ABPP is a simple and powerful functional proteomics approach that has made important contributions to studies on immune responses and plant-pathogen interactions. ABPP revealed up-regulated proteasome activities during immune responses, and displayed differential serine hydrolase activities of both host and pathogen during infection. Furthermore, ABPP in the presence of putative inhibitors demonstrated that pathogens from different kingdoms produce effectors that suppress different proteolytic activities of the host. Taken together, these examples show that ABPP is a simple and robust way to capture functional information beyond standard proteomic techniques. ",
}