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231225s2018 xx |||||o 00| ||eng c |
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|a 10.1111/nph.15287
|2 doi
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|a pubmed24n0953.xml
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|a (DE-627)NLM285929135
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|a (NLM)29949665
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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| 100 |
1 |
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|a Qin, Jun
|e verfasserin
|4 aut
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| 245 |
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|a The Xanthomonas effector XopK harbours E3 ubiquitin-ligase activity that is required for virulence
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|c 2018
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 01.10.2019
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|a Date Revised 30.09.2020
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a © 2018 The Authors. New Phytologist © 2018 New Phytologist Trust.
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|a Xanthomonas oryzae pv. oryzae is the causative agent of rice bacterial leaf blight. While the type III secretion system of X. oryzae pv. oryzae is essential for virulence, the biochemical activities and virulence mechanisms of non-transcription activator-like (non-TAL) effectors delivered by this system are largely unknown. Here, by screening for non-TAL effectors that contribute to X. oryzae pv. oryzae virulence, we revealed that Xanthomonas outer protein K (XopK) inhibits pathogen-associated molecular pattern-triggered immunity upstream of mitogen-activated protein kinase cascades. Specifically, XopK interacted with and directly ubiquitinated rice somatic embryogenic receptor kinase 2 (OsSERK2), resulting in its degradation. Accordingly, mutation of a putative ubiquitin-conjugation enzyme (E2) binding site abolished XopK-induced degradation of OsSERK2 and compromised XopK-dependent virulence. As crucial immune regulators associated with a multitude of immune receptors, SERKs have been shown to be perturbed by Pseudomonas effectors via different mechanisms. Our study revealed a distinct perturbation mechanism of SERK activity via ubiquitination achieved by Xanthomonas non-TAL effector
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Xanthomonas
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|a OsSERK2
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|a effector
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|a plant immunity
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|a ubiquitination
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|a Bacterial Proteins
|2 NLM
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|a Pathogen-Associated Molecular Pattern Molecules
|2 NLM
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|a Plant Proteins
|2 NLM
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|a Ubiquitin-Protein Ligases
|2 NLM
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| 650 |
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|a EC 2.3.2.27
|2 NLM
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| 700 |
1 |
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|a Zhou, Xiaogang
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Sun, Lifan
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Wang, Kailun
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Yang, Fan
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Liao, Haicheng
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Rong, Wei
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Yin, Junjie
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Chen, Huamin
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Chen, Xuewei
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Zhang, Jie
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t The New phytologist
|d 1979
|g 220(2018), 1 vom: 15. Okt., Seite 219-231
|w (DE-627)NLM09818248X
|x 1469-8137
|7 nnns
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| 773 |
1 |
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|g volume:220
|g year:2018
|g number:1
|g day:15
|g month:10
|g pages:219-231
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|u http://dx.doi.org/10.1111/nph.15287
|3 Volltext
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|d 220
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|h 219-231
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