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231225s2022 xx |||||o 00| ||eng c |
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|a 10.1093/jxb/erab445
|2 doi
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|a pubmed24n1105.xml
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|a (DE-627)NLM331513404
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|a (NLM)34610124
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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 Duan, Zhikun
|e verfasserin
|4 aut
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| 245 |
1 |
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|a Probing membrane protein interactions and signaling molecule homeostasis in plants by Förster resonance energy transfer analysis
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|c 2022
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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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| 500 |
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|a Date Completed 27.01.2022
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|a Date Revised 27.01.2022
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|a published: Print
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|a Citation Status MEDLINE
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|a © The Author(s) 2021. 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 Membrane proteins have key functions in signal transduction, transport, and metabolism. Therefore, deciphering the interactions between membrane proteins provides crucial information on signal transduction and the spatiotemporal organization of protein complexes. However, detecting the interactions and behaviors of membrane proteins in their native environments remains difficult. Förster resonance energy transfer (FRET) is a powerful tool for quantifying the dynamic interactions and assembly of membrane proteins without disrupting their local environment, supplying nanometer-scale spatial information and nanosecond-scale temporal information. In this review, we briefly introduce the basic principles of FRET and assess the current state of progress in the development of new FRET techniques (such as FRET-FLIM, homo-FRET, and smFRET) for the analysis of plant membrane proteins. We also describe the various FRET-based biosensors used to quantify the homeostasis of signaling molecules and the active state of kinases. Furthermore, we summarize recent applications of these advanced FRET sensors in probing membrane protein interactions, stoichiometry, and protein clustering, which have shed light on the complex biological functions of membrane proteins in living 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 Review
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| 650 |
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|a Assembly stoichiometry
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| 650 |
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4 |
|a FRET
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| 650 |
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4 |
|a Förster resonance energy transfer
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| 650 |
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|a biosensors
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| 650 |
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4 |
|a membrane microdomains
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| 650 |
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4 |
|a membrane proteins
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| 650 |
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4 |
|a protein interactions
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| 650 |
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|a Membrane Proteins
|2 NLM
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| 700 |
1 |
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|a Li, Kaiwen
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Duan, Wenwen
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Zhang, Junli
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Xing, Jingjing
|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 73(2022), 1 vom: 05. Jan., Seite 68-77
|w (DE-627)NLM098182706
|x 1460-2431
|7 nnns
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| 773 |
1 |
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|g volume:73
|g year:2022
|g number:1
|g day:05
|g month:01
|g pages:68-77
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|u http://dx.doi.org/10.1093/jxb/erab445
|3 Volltext
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