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231225s2019 xx |||||o 00| ||eng c |
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|a 10.1093/jxb/ery460
|2 doi
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|a pubmed25n0978.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 Cohen, Maja
|e verfasserin
|4 aut
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|a Plant serpin protease inhibitors
|b specificity and duality of function
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|c 2019
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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 15.06.2020
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|a Date Revised 15.06.2020
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|a published: Print
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|a Citation Status MEDLINE
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|a © The Author(s) 2019. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved.For permissions, please email: journals.permissionsoup.com.
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|a The serpins are a family of structurally conserved protease inhibitors found in all animal and plant kingdoms. After interaction with their cognate substrate(s), their native energetically stressed state is relaxed by hydrolysis, resulting in a semi-stable covalent bond that disables the protease. The inherent flexible serpin structure supports additional non-inhibitory functions. This review will focus on several biological functions attributed to plant serpins, ranging from specific cell death protease inhibitors to a stabilizing role for β-amylase in seeds. Functional conservation of a particular serpin type, the LR serpins, is suggested by its compelling ubiquity throughout the plant kingdom. The multiple target specificity of plant serpins including the LR serpins enables them to perform dual functions that are not mutually exclusive both as a regulator of cell death and as a protective anti-pathogenic protein
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Research Support, U.S. Gov't, Non-P.H.S.
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|a Review
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|a Cysteine and serine proteases
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|a plant cell death
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|a serpin
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|a Plant Proteins
|2 NLM
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| 650 |
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|a Protease Inhibitors
|2 NLM
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|a Serpins
|2 NLM
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|a Davydov, Olga
|e verfasserin
|4 aut
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|a Fluhr, Robert
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Journal of experimental botany
|d 1985
|g 70(2019), 7 vom: 12. Apr., Seite 2077-2085
|w (DE-627)NLM098182706
|x 1460-2431
|7 nnns
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| 773 |
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|g volume:70
|g year:2019
|g number:7
|g day:12
|g month:04
|g pages:2077-2085
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|u http://dx.doi.org/10.1093/jxb/ery460
|3 Volltext
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