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231224s2011 xx |||||o 00| ||eng c |
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|a 10.1016/j.plantsci.2011.04.004
|2 doi
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|a pubmed25n0704.xml
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|a DE-627
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|e rakwb
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|a eng
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|a Malik, Saad I
|e verfasserin
|4 aut
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|a GSNOR-mediated de-nitrosylation in the plant defence response
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|c 2011
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
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|2 rdamedia
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|a ƒa Online-Ressource
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|a Date Completed 20.12.2011
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|a Date Revised 16.03.2022
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Crown Copyright © 2011. Published by Elsevier Ireland Ltd. All rights reserved.
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|a A key feature of the plant defence response is the transient engagement of a nitrosative burst, resulting in the synthesis of reactive nitrogen intermediates (RNIs). Specific, highly reactive cysteine (Cys) residues of low pK(a) are a major site of action for these intermediates. The addition of an NO moiety to a Cys thiol to form an S-nitrosothiol (SNO), is termed S-nitrosylation. This redox-based post-translational modification is emerging as a key regulator of protein function in plant immunity. Here we highlight recent advances in our understanding of de-nitrosylation, the mechanism that depletes protein SNOs, with a focus on S-nitrosoglutathione reductase (GSNOR). This enzyme controls total cellular S-nitrosylation indirectly during the defence response by turning over S-nitrosoglutathione (GSNO), a major cache of NO bioactivity
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Review
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|a S-Nitrosothiols
|2 NLM
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|a Nitric Oxide
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|a 31C4KY9ESH
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|a Aldehyde Oxidoreductases
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|a EC 1.2.-
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|a formaldehyde dehydrogenase, glutathione-independent
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|a Hussain, Adil
|e verfasserin
|4 aut
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|a Yun, Byung-Wook
|e verfasserin
|4 aut
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|a Spoel, Steven H
|e verfasserin
|4 aut
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|a Loake, Gary J
|e verfasserin
|4 aut
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|i Enthalten in
|t Plant science : an international journal of experimental plant biology
|d 1985
|g 181(2011), 5 vom: 15. Nov., Seite 540-4
|w (DE-627)NLM098174193
|x 1873-2259
|7 nnns
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|g volume:181
|g year:2011
|g number:5
|g day:15
|g month:11
|g pages:540-4
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|u http://dx.doi.org/10.1016/j.plantsci.2011.04.004
|3 Volltext
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