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231224s2016 xx |||||o 00| ||eng c |
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|a 10.1016/j.jplph.2016.05.023
|2 doi
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|a pubmed24n0873.xml
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|a (DE-627)NLM261911112
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|a (NLM)27362847
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|a (PII)S0176-1617(16)30113-4
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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 Hashemi, Amenehsadat
|e verfasserin
|4 aut
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| 245 |
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|a Two-dimensional blue native/SDS-PAGE analysis of whole cell lysate protein complexes of rice in response to salt stress
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|c 2016
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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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|a Date Completed 10.04.2017
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|a Date Revised 30.09.2020
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Copyright © 2016 Elsevier GmbH. All rights reserved.
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|a To understand the biology of a plant in response to stress, insight into protein-protein interactions, which almost define cell behavior, is thought to be crucial. Here, we provide a comparative complexomics analysis of leaf whole cell lysate of two rice genotypes with contrasting responses to salt using two-dimensional blue native/SDS-PAGE (2D-BN/SDS-PAGE). We aimed to identify changes in subunit composition and stoichiometry of protein complexes elicited by salt. Using mild detergent for protein complex solubilization, we were able to identify 9 protein assemblies as hetero-oligomeric and 30 as homo-oligomeric complexes. A total of 20 proteins were identified as monomers in the 2D-BN/SDS-PAGE gels. In addition to identifying known protein complexes that confirm the technical validity of our analysis, we were also able to discover novel protein-protein interactions. Interestingly, an interaction was detected for glycolytic enzymes enolase (ENO1) and triosephosphate isomerase (TPI) and also for a chlorophyll a-b binding protein and RuBisCo small subunit. To show changes in subunit composition and stoichiometry of protein assemblies during salt stress, the differential abundance of interacting proteins was compared between salt-treated and control plants. A detailed exploration of some of the protein complexes provided novel insight into the function, composition, stoichiometry and dynamics of known and previously uncharacterized protein complexes in response to salt stress
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|a Journal Article
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|a 2D-BN/SDS-PAGE
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|a Complexomics
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|a Protein complexes
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|a Protein-protein interaction
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|a Rice
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|a Salt stress
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|a Cell Extracts
|2 NLM
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|a Detergents
|2 NLM
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| 650 |
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|a Multiprotein Complexes
|2 NLM
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| 650 |
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|a Plant Proteins
|2 NLM
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| 650 |
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|a Sodium Chloride
|2 NLM
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| 650 |
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|a 451W47IQ8X
|2 NLM
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| 700 |
1 |
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|a Gharechahi, Javad
|e verfasserin
|4 aut
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1 |
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|a Nematzadeh, Ghorbanali
|e verfasserin
|4 aut
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| 700 |
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|a Shekari, Faezeh
|e verfasserin
|4 aut
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|a Hosseini, Seyed Abdollah
|e verfasserin
|4 aut
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|a Salekdeh, Ghasem Hosseini
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Journal of plant physiology
|d 1979
|g 200(2016) vom: 01. Aug., Seite 90-101
|w (DE-627)NLM098174622
|x 1618-1328
|7 nnns
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| 773 |
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|g volume:200
|g year:2016
|g day:01
|g month:08
|g pages:90-101
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|u http://dx.doi.org/10.1016/j.jplph.2016.05.023
|3 Volltext
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