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231224s2012 xx |||||o 00| ||eng c |
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|a 10.1093/jxb/err310
|2 doi
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|a pubmed24n0708.xml
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|a (DE-627)NLM212394282
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|a (NLM)22016431
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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 Lyzenga, Wendy J
|e verfasserin
|4 aut
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|a Abiotic stress tolerance mediated by protein ubiquitination
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|c 2012
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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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|2 rdacarrier
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|a Date Completed 10.01.2014
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|a Date Revised 16.03.2022
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Plant growth and development is largely influenced by ubiquitin-mediated regulation of protein stability. Specificity of the ubiquitination pathway is controlled mainly by the substrate-recruiting E3 ubiquitin ligases, and consequently, E3 ligases control numerous cellular processes. Recent evidence that ubiquitination plays a critical role in regulating plant responses to abiotic stresses has launched intensive efforts to identify E3 ligases that mediate plant tolerance of adverse environmental conditions. Most stress-related E3 ligases identified to date facilitate responses to environmental stimuli by modulating the abundance of key downstream stress-responsive transcription factors. In this review, the regulatory roles of ubiquitin during the plant's response to abiotic stress are summarized and highlighted
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Review
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|a Plant Proteins
|2 NLM
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|a Transcription Factors
|2 NLM
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|a Abscisic Acid
|2 NLM
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|a 72S9A8J5GW
|2 NLM
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|a Ubiquitin-Protein Ligases
|2 NLM
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|a EC 2.3.2.27
|2 NLM
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|a Proteasome Endopeptidase Complex
|2 NLM
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|a EC 3.4.25.1
|2 NLM
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|a ATP dependent 26S protease
|2 NLM
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|a EC 3.4.99.-
|2 NLM
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|a Stone, Sophia L
|e verfasserin
|4 aut
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|i Enthalten in
|t Journal of experimental botany
|d 1985
|g 63(2012), 2 vom: 01. Jan., Seite 599-616
|w (DE-627)NLM098182706
|x 1460-2431
|7 nnns
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|g volume:63
|g year:2012
|g number:2
|g day:01
|g month:01
|g pages:599-616
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|u http://dx.doi.org/10.1093/jxb/err310
|3 Volltext
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