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231225s2017 xx |||||o 00| ||eng c |
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|a 10.1093/jxb/erx312
|2 doi
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|a pubmed25n0921.xml
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|a (DE-627)NLM276615174
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|a (NLM)28992300
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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 |
1 |
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|a Kim, Joo Yong
|e verfasserin
|4 aut
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| 245 |
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|a COP1 regulates plant growth and development in response to light at the post-translational level
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|c 2017
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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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| 500 |
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|a Date Completed 14.05.2018
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|a Date Revised 06.08.2019
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|a published: Print
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|a Citation Status MEDLINE
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|a © The Author 2017. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For permissions, please email: journals.permissionsoup.com.
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|a Photoreceptors perceive different wavelengths of light and transduce light signals downstream via a range of proteins. COP1, an E3 ubiquitin ligase, regulates light signaling by mediating the ubiquitination and subsequent proteasomal degradation of photoreceptors such as phytochromes and cryptochromes, as well as various development-related proteins including other light-responsive proteins. COP1 is itself regulated by direct interactions with several signaling molecules that modulate its activity. The control of photomorphogenesis by COP1 is also regulated by its localization to the cytoplasm in response to light. COP1 thus acts as a tightly regulated switch that determines whether development is skotomorphogenic or photomorphogenic. In this review, we discuss the effects of COP1 on the abundance and activity of various development-related proteins, including photoreceptors, and summarize the regulatory mechanisms that influence COP1 activity and stability in plants
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|a Journal Article
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|a COP1
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|a E3 ubiquitin ligase
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|a light
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|a photomorphogenesis
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|a ubiquitin
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|a ubiquitination
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|a Arabidopsis Proteins
|2 NLM
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|a Cryptochromes
|2 NLM
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| 650 |
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|a Photoreceptors, Plant
|2 NLM
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| 650 |
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|a Phytochrome
|2 NLM
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|a 11121-56-5
|2 NLM
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| 650 |
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|a AT2G32950 protein, Arabidopsis
|2 NLM
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| 650 |
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|a EC 2.3.2.27
|2 NLM
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| 650 |
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|a Ubiquitin-Protein Ligases
|2 NLM
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| 650 |
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|a EC 2.3.2.27
|2 NLM
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| 700 |
1 |
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|a Song, Jong Tae
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Seo, Hak Soo
|e verfasserin
|4 aut
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| 773 |
0 |
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|i Enthalten in
|t Journal of experimental botany
|d 1985
|g 68(2017), 17 vom: 13. Okt., Seite 4737-4748
|w (DE-627)NLM098182706
|x 1460-2431
|7 nnas
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| 773 |
1 |
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|g volume:68
|g year:2017
|g number:17
|g day:13
|g month:10
|g pages:4737-4748
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|u http://dx.doi.org/10.1093/jxb/erx312
|3 Volltext
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