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231224s2016 xx |||||o 00| ||eng c |
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|a 10.1111/nph.14014
|2 doi
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|a pubmed24n0879.xml
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|a eng
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| 100 |
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|a Ma, Jun
|e verfasserin
|4 aut
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| 245 |
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|a Endoplasmic reticulum-associated N-glycan degradation of cold-upregulated glycoproteins in response to chilling stress in Arabidopsis
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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
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|2 rdacarrier
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|a Date Completed 26.01.2018
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|a Date Revised 21.03.2022
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a © 2016 The Authors. New Phytologist © 2016 New Phytologist Trust.
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|a N-glycosylation has a great impact on glycoprotein structure, conformation, stability, solubility, immunogenicity and enzyme activity. Structural characterization of N-glycoproteome has been challenging but can provide insights into the extent of protein folding and surface topology. We describe a highly sensitive proteomics method for large-scale identification and quantification of glycoproteins in Arabidopsis through (15) N-metabolic labeling, selective enrichment of glycopeptides, data-dependent MS/MS analysis and automated database searching. In-house databases of Arabidopsis glycoproteins and glycopeptides containing Asn-X-Ser/Thr/Cys motifs were constructed by reducing 20% and 90% of the public database size, respectively, to enable a rapid analysis of large datasets for comprehensive identification and quantification of glycoproteins and heterogeneous N-glycans in a complex mixture. Proteome-wide analysis identified c. 100 stress-related N-glycoproteins, of which the endoplasmic reticulum (ER) resident proteins were examined to be up-regulated. Quantitative measurements provided a molecular signature specific to glycoproteins for determining the degree of plant stress at low temperature. Structural N-glycoproteomics following time-course cold treatments revealed the stress-responsive degradation of high-mannose type N-glycans in ER in response to chilling stress, which may aid in elucidating the cellular mechanisms of protein relocation, transport, trafficking, misfolding and degradation under stress conditions
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Arabidopsis
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|a chilling stress
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|a endoplasmic reticulum (ER)
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|a glycoproteomics
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|a liquid chromatography-tandem mass spectrometry
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|a Arabidopsis Proteins
|2 NLM
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|a Glycopeptides
|2 NLM
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| 650 |
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|a Glycoproteins
|2 NLM
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| 650 |
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|a Polysaccharides
|2 NLM
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| 700 |
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|a Wang, Dinghe
|e verfasserin
|4 aut
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| 700 |
1 |
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|a She, Jessica
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Li, Jianming
|e verfasserin
|4 aut
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| 700 |
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|a Zhu, Jian-Kang
|e verfasserin
|4 aut
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| 700 |
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|a She, Yi-Min
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t The New phytologist
|d 1979
|g 212(2016), 1 vom: 25. Okt., Seite 282-96
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|x 1469-8137
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|g volume:212
|g year:2016
|g number:1
|g day:25
|g month:10
|g pages:282-96
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|u http://dx.doi.org/10.1111/nph.14014
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