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231225s2018 xx |||||o 00| ||eng c |
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|a 10.1016/j.jplph.2018.07.011
|2 doi
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|a pubmed25n0957.xml
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|a (DE-627)NLM287315797
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|a (NLM)30092447
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|a (PII)S0176-1617(18)30470-X
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|a DE-627
|b ger
|c DE-627
|e rakwb
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| 041 |
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|a eng
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| 100 |
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|a Nosek, Michał
|e verfasserin
|4 aut
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|a Withdrawal from functional Crassulacean acid metabolism (CAM) is accompanied by changes in both gene expression and activity of antioxidative enzymes
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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 26.10.2018
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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 Copyright © 2018 Elsevier GmbH. All rights reserved.
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|a In Mesembryanthemum crystallinum, crassulacean acid metabolism (CAM) is seemingly reversible, but unequivocal evidence for functional CAM withdrawal has yet to be shown. In this study, we confirmed the rapid downregulation of PEPC1 expression just 1 h after the removal of NaCl from the plant growth media. At the same time, the Δ malate values in desalted plants rapidly (1 d) re-established to values typical for C3 plants. This phenomenon allowed us to confirm functional CAM withdrawal in the desalted plants. Desalting altered the expression of the genes of the main antioxidative enzymes and/or the activity of their respective proteins; for catalase (CAT), both gene expression and protein activity were restored to levels observed in C3 plants in response to desalting, while for cooper-zinc superoxide dismutase (CuZnSOD) and ascorbate peroxidase (APX), only protein activity was restored. Therefore, we conclude that during the C3→CAM transition the CAM-specific antioxidative enzyme activity profile constitutes a transient and fully reversible response to abiotic stress
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|a Journal Article
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|a Antioxidants
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|a CAM reversibility
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|a Carboxylase
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|a Mesembryanthemum crystallinum
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|a Phosphoenolpyruvate carboxylase
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|a Salinity stress
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|a Antioxidants
|2 NLM
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|a Plant Proteins
|2 NLM
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|a Sodium Chloride
|2 NLM
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|a 451W47IQ8X
|2 NLM
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|a Ascorbate Peroxidases
|2 NLM
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| 650 |
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|a EC 1.11.1.11
|2 NLM
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| 650 |
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|a Catalase
|2 NLM
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| 650 |
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|a EC 1.11.1.6
|2 NLM
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| 650 |
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|a Superoxide Dismutase
|2 NLM
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| 650 |
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|a EC 1.15.1.1
|2 NLM
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| 700 |
1 |
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|a Gawrońska, Katarzyna
|e verfasserin
|4 aut
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| 700 |
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|a Rozpądek, Piotr
|e verfasserin
|4 aut
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| 700 |
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|a Szechyńska-Hebda, Magdalena
|e verfasserin
|4 aut
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| 700 |
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|a Kornaś, Andrzej
|e verfasserin
|4 aut
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| 700 |
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|a Miszalski, Zbigniew
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Journal of plant physiology
|d 1979
|g 229(2018) vom: 01. Okt., Seite 151-157
|w (DE-627)NLM098174622
|x 1618-1328
|7 nnas
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| 773 |
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|g volume:229
|g year:2018
|g day:01
|g month:10
|g pages:151-157
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|u http://dx.doi.org/10.1016/j.jplph.2018.07.011
|3 Volltext
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|d 229
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|h 151-157
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