{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T22:47:36Z","timestamp":1791326856209,"version":"4.3.1"},"reference-count":37,"publisher":"Oxford University Press (OUP)","issue":"9","license":[{"start":{"date-parts":[[2021,1,20]],"date-time":"2021-01-20T00:00:00Z","timestamp":1611100800000},"content-version":"vor","delay-in-days":3063,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2012,10,24]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Plant activators are compounds, such as analogs of the defense hormone salicylic acid (SA), that protect plants from pathogens by activating the plant immune system. Although some plant activators have been widely used in agriculture, the molecular mechanisms of immune induction are largely unknown. Using a newly established high-throughput screening procedure that screens for compounds that specifically potentiate pathogen-activated cell death in Arabidopsis thaliana cultured suspension cells, we identified five compounds that prime the immune response. These compounds enhanced disease resistance against pathogenic Pseudomonas bacteria in Arabidopsis plants. Pretreatments increased the accumulation of endogenous SA, but reduced its metabolite, SA-O-\u03b2-d-glucoside. Inducing compounds inhibited two SA glucosyltransferases (SAGTs) in vitro. Double knockout plants that lack both SAGTs consistently exhibited enhanced disease resistance. Our results demonstrate that manipulation of the active free SA pool via SA-inactivating enzymes can be a useful strategy for fortifying plant disease resistance and may identify useful crop protectants.<\/jats:p>","DOI":"10.1105\/tpc.112.098343","type":"journal-article","created":{"date-parts":[[2012,9,8]],"date-time":"2012-09-08T03:59:12Z","timestamp":1347076752000},"page":"3795-3804","source":"Crossref","is-referenced-by-count":186,"title":["Novel Plant Immune-Priming Compounds Identified via High-Throughput Chemical Screening Target Salicylic Acid Glucosyltransferases in <i>Arabidopsis<\/i>\n\u00a0\n\u00a0"],"prefix":"10.1093","volume":"24","author":[{"given":"Yoshiteru","family":"Noutoshi","sequence":"first","affiliation":[{"name":"Research Core for Interdisciplinary Sciences, Okayama University, Kita-ku, Okayama 700-8530, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Masateru","family":"Okazaki","sequence":"additional","affiliation":[{"name":"Research Core for Interdisciplinary Sciences, Okayama University, Kita-ku, Okayama 700-8530, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tatsuya","family":"Kida","sequence":"additional","affiliation":[{"name":"Research Core for Interdisciplinary Sciences, Okayama University, Kita-ku, Okayama 700-8530, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yuta","family":"Nishina","sequence":"additional","affiliation":[{"name":"Research Core for Interdisciplinary Sciences, Okayama University, Kita-ku, Okayama 700-8530, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yoshihiko","family":"Morishita","sequence":"additional","affiliation":[{"name":"Kazusa DNA Research Institute, Kisarazu 292-0818, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Takumi","family":"Ogawa","sequence":"additional","affiliation":[{"name":"Kazusa DNA Research Institute, Kisarazu 292-0818, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hideyuki","family":"Suzuki","sequence":"additional","affiliation":[{"name":"Kazusa DNA Research Institute, Kisarazu 292-0818, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daisuke","family":"Shibata","sequence":"additional","affiliation":[{"name":"Kazusa DNA Research Institute, Kisarazu 292-0818, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yusuke","family":"Jikumaru","sequence":"additional","affiliation":[{"name":"RIKEN Plant Science Center, Tsurumi, Yokohama 230-0045, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Atsushi","family":"Hanada","sequence":"additional","affiliation":[{"name":"RIKEN Plant Science Center, Tsurumi, Yokohama 230-0045, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yuji","family":"Kamiya","sequence":"additional","affiliation":[{"name":"RIKEN Plant Science Center, Tsurumi, Yokohama 230-0045, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ken","family":"Shirasu","sequence":"additional","affiliation":[{"name":"RIKEN Plant Science Center, Tsurumi, Yokohama 230-0045, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2012,9,7]]},"reference":[{"key":"2021040706094567600_b1","doi-asserted-by":"crossref","first-page":"15724","DOI":"10.1074\/jbc.M801983200","article-title":"A kinetic analysis of regiospecific glucosylation by two glycosyltransferases of Arabidopsis thaliana: Domain swapping to introduce new activities","volume":"283","author":"Cartwright","year":"2008","journal-title":"J. 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