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231224s2012 xx |||||o 00| ||eng c |
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|a 10.1016/j.plantsci.2011.12.004
|2 doi
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|a pubmed24n0716.xml
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|a (DE-627)NLM214935663
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|a (NLM)22284714
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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 |
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|a Liu, Bing
|e verfasserin
|4 aut
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|a Musa paradisica RCI complements AtRCI and confers Na+ tolerance and K+ sensitivity in Arabidopsis
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|c 2012
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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 16.05.2012
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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 © 2011 Elsevier Ireland Ltd. All rights reserved.
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|a The mechanisms involved in Na⁺/K⁺ uptake and extrusion are important in plant salt tolerance. In this study, we investigated the physiological role of a plasma membrane (PM)-localized protein, MpRCI, from plantain in transgenic Arabidopsis under NaCl and KCl stress and determined its effect on PM fluidity and H⁺-ATPase activity. The MpRCI gene exhibited high homology to the AtRCI2 gene family in Arabidopsis and was therefore able to complement for loss of the yeast AtRCI2-related PMP3 gene. Results of phenotypic espial and atomic emission spectrophotometer (AES) assays indicated that MpRCI overexpression in the AtRCI2A knockout mutant with reduced shoot Na⁺ and increased K⁺ exhibited increased Na⁺-tolerance and K⁺-sensitivity under NaCl or KCl treatments, respectively. Furthermore, comparisons of PM fluidity and H⁺-ATPase activity in shoots, with expression or absence of MpRCI/AtRCI2A expression under NaCl or KCl stress, showed MpRCI maintained PM fluidity and H⁺-ATPase activity under stress conditions. Results suggest that MpRCI plays an essential role in Na⁺/K⁺ flux in plant cells
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a PMP3 protein, S cerevisiae
|2 NLM
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|a Plant Proteins
|2 NLM
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|a Proteolipids
|2 NLM
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|a Saccharomyces cerevisiae Proteins
|2 NLM
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|a Sodium Chloride
|2 NLM
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|a 451W47IQ8X
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|a Potassium Chloride
|2 NLM
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|a 660YQ98I10
|2 NLM
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|a Sodium
|2 NLM
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|a 9NEZ333N27
|2 NLM
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|a Proton-Translocating ATPases
|2 NLM
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|a EC 3.6.3.14
|2 NLM
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|a Potassium
|2 NLM
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|a RWP5GA015D
|2 NLM
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1 |
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|a Feng, Dongru
|e verfasserin
|4 aut
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|a Zhang, Bipei
|e verfasserin
|4 aut
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|a Mu, Peiqiang
|e verfasserin
|4 aut
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|a Zhang, Yang
|e verfasserin
|4 aut
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|a He, Yanming
|e verfasserin
|4 aut
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|a Qi, Kangbiao
|e verfasserin
|4 aut
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|a Wang, Jinfa
|e verfasserin
|4 aut
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| 700 |
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|a Wang, Hongbin
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Plant science : an international journal of experimental plant biology
|d 1985
|g 184(2012) vom: 29. März, Seite 102-11
|w (DE-627)NLM098174193
|x 1873-2259
|7 nnns
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| 773 |
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|g volume:184
|g year:2012
|g day:29
|g month:03
|g pages:102-11
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|u http://dx.doi.org/10.1016/j.plantsci.2011.12.004
|3 Volltext
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|a AR
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|d 184
|j 2012
|b 29
|c 03
|h 102-11
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