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231225s2001 xx |||||o 00| ||eng c |
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|a 10.1046/j.1469-8137.2001.00168.x
|2 doi
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|a pubmed24n1080.xml
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|a DE-627
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|e rakwb
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|a eng
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| 100 |
1 |
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|a Luan, Sheng
|e verfasserin
|4 aut
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| 245 |
1 |
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|a Protein tyrosine phosphatases in higher plants
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|c 2001
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| 336 |
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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| 338 |
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Revised 20.04.2021
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|a published: Print
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|a Citation Status PubMed-not-MEDLINE
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|a Reversible protein phosphorylation is the most common mechanism for cellular regulation in eukaryotic systems. Indeed, approximately 5% of the Arabidopsis genome encodes protein kinases and phosphatases. Among the thousands of such enzymes, only a small fraction has been examined experimentally. Studies have demonstrated that Ser/Thr phosphorylation and dephosphorylation play a key role in the regulation of plant physiology and development. However, function of tyrosine phosphorylation, despite the overwhelming importance in animals, has not been systematically studied in higher plants. As a result, it is still controversial whether tyrosine phosphorylation is important in plant signal transduction. Recently, the first two protein tyrosine phosphatases (PTPs) from a higher plant were characterized. A diverse group of genes encoding putative PTPs have been identified from the Arabidopsis genome sequence databases. Genetic analyses of various PTPs are underway and preliminary results have provided evidence that these PTPs serve critical functions in plant responses to stress signals and in plant development
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|a Journal Article
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|a signal transduction
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|a protein phosphatase
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|a stress response
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| 650 |
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|a tyrosine phosphorylation
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| 700 |
1 |
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|a Ting, Julie
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Gupta, Rajeev
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t The New phytologist
|d 1979
|g 151(2001), 1 vom: 20. Juli, Seite 155-164
|w (DE-627)NLM09818248X
|x 1469-8137
|7 nnns
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| 773 |
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|g volume:151
|g year:2001
|g number:1
|g day:20
|g month:07
|g pages:155-164
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|u http://dx.doi.org/10.1046/j.1469-8137.2001.00168.x
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|d 151
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|h 155-164
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