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|a pubmed24n0535.xml
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|a (DE-627)NLM160445884
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|a (NLM)16449373
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a Rodríguez-Navarro, Alonso
|e verfasserin
|4 aut
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|a High-affinity potassium and sodium transport systems in plants
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|c 2006
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|a Text
|b txt
|2 rdacontent
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|a ohne Hilfsmittel zu benutzen
|b n
|2 rdamedia
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|a Band
|b nc
|2 rdacarrier
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|a Date Completed 07.06.2006
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|a Date Revised 09.04.2022
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a All living cells have an absolute requirement for K+, which must be taken up from the external medium. In contrast to marine organisms, which live in a medium with an inexhaustible supply of K+, terrestrial life evolved in oligotrophic environments where the low supply of K+ limited the growth of colonizing plants. In these limiting conditions Na+ could substitute for K+ in some cellular functions, but in others it is toxic. In the vacuole, Na+ is not toxic and can undertake osmotic functions, reducing the total K+ requirements and improving growth when the lack of K+ is a limiting factor. Because of these physiological requirements, the terrestrial life of plants depends on high-affinity K+ uptake systems and benefits from high-affinity Na+ uptake systems. In plants, both systems have received extensive attention during recent years and a clear insight of their functions is emerging. Some plant HAK transporters mediate high-affinity K+ uptake in yeast, mimicking K+ uptake in roots, while other members of the same family may be K+ transporters in the tonoplast. In parallel with the HAK transporters, some HKT transporters mediate high-affinity Na+ uptake without cotransporting K+. HKT transporters have two functions: (i) to take up Na+ from the soil solution to reduce K+ requirements when K+ is a limiting factor, and (ii) to reduce Na+ accumulation in leaves by both removing Na+ from the xylem sap and loading Na+ into the phloem sap
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|a Journal Article
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|a Review
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|a Plant Proteins
|2 NLM
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|a Potassium Channels
|2 NLM
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|a Sodium Channels
|2 NLM
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|a Sodium
|2 NLM
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|a 9NEZ333N27
|2 NLM
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|a Adenosine Triphosphatases
|2 NLM
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|a EC 3.6.1.-
|2 NLM
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|a Potassium
|2 NLM
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|a RWP5GA015D
|2 NLM
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|a Rubio, Francisco
|e verfasserin
|4 aut
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|i Enthalten in
|t Journal of experimental botany
|d 1985
|g 57(2006), 5 vom: 15., Seite 1149-60
|w (DE-627)NLM098182706
|x 1460-2431
|7 nnns
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773 |
1 |
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|g volume:57
|g year:2006
|g number:5
|g day:15
|g pages:1149-60
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|d 57
|j 2006
|e 5
|b 15
|h 1149-60
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