Plant redox proteomics

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Plant redox proteomics. / Navrot, Nicolas; Finnie, Christine; Svensson, Birte; Hägglund, Per.

In: Journal of Proteomics, Vol. 74, No. 8, 2011, p. 1450-1462.

Research output: Contribution to journal › Review › Research › peer-review

Harvard

Navrot, N, Finnie, C, Svensson, B & Hägglund, P 2011, 'Plant redox proteomics', Journal of Proteomics, vol. 74, no. 8, pp. 1450-1462. https://doi.org/10.1016/j.jprot.2011.03.008

APA

Navrot, N., Finnie, C., Svensson, B., & Hägglund, P. (2011). Plant redox proteomics. Journal of Proteomics, 74(8), 1450-1462. https://doi.org/10.1016/j.jprot.2011.03.008

Vancouver

Navrot N, Finnie C, Svensson B, Hägglund P. Plant redox proteomics. Journal of Proteomics. 2011;74(8):1450-1462. https://doi.org/10.1016/j.jprot.2011.03.008

Author

Navrot, Nicolas ; Finnie, Christine ; Svensson, Birte ; Hägglund, Per. / Plant redox proteomics. In: Journal of Proteomics. 2011 ; Vol. 74, No. 8. pp. 1450-1462.

Bibtex

@article{bb835ce244e54031983b4ac6400d4247,
title = "Plant redox proteomics",
abstract = "In common with other aerobic organisms, plants are exposed to reactive oxygen species resulting in formation of post-translational modifications related to protein oxidoreduction (redox PTMs) that may inflict oxidative protein damage. Accumulating evidence also underscores the importance of redox PTMs in regulating enzymatic activities and controlling biological processes in plants. Notably, proteins controlling the cellular redox state, e.g. thioredoxin and glutaredoxin, appear to play dual roles to maintain oxidative stress resistance and regulate signal transduction pathways via redox PTMs. To get a comprehensive overview of these types of redox-regulated pathways there is therefore an emerging interest to monitor changes in redox PTMs on a proteome scale. Compared to some other PTMs, e.g. protein phosphorylation, redox PTMs have received less attention in plant proteome analysis, possibly due to technical challenges such as with maintaining the in vivo redox states of proteins and the lability of certain PTMs, e.g. nitrosylations, during sample preparation and mass spectrometric analysis. The present review article provides an overview of the recent developments in the emerging area of plant redox proteomics.",
keywords = "Ascorbate, Glutaredoxin, Oxidative stress, Reactive nitrogen species, Reactive oxygen species, Redox, Thioredoxin",
author = "Nicolas Navrot and Christine Finnie and Birte Svensson and Per H{\"a}gglund",
year = "2011",
doi = "10.1016/j.jprot.2011.03.008",
language = "English",
volume = "74",
pages = "1450--1462",
journal = "Journal of Proteomics",
issn = "1874-3919",
publisher = "Elsevier",
number = "8",

}

RIS

TY - JOUR

T1 - Plant redox proteomics

AU - Navrot, Nicolas

AU - Finnie, Christine

AU - Svensson, Birte

AU - Hägglund, Per

PY - 2011

Y1 - 2011

N2 - In common with other aerobic organisms, plants are exposed to reactive oxygen species resulting in formation of post-translational modifications related to protein oxidoreduction (redox PTMs) that may inflict oxidative protein damage. Accumulating evidence also underscores the importance of redox PTMs in regulating enzymatic activities and controlling biological processes in plants. Notably, proteins controlling the cellular redox state, e.g. thioredoxin and glutaredoxin, appear to play dual roles to maintain oxidative stress resistance and regulate signal transduction pathways via redox PTMs. To get a comprehensive overview of these types of redox-regulated pathways there is therefore an emerging interest to monitor changes in redox PTMs on a proteome scale. Compared to some other PTMs, e.g. protein phosphorylation, redox PTMs have received less attention in plant proteome analysis, possibly due to technical challenges such as with maintaining the in vivo redox states of proteins and the lability of certain PTMs, e.g. nitrosylations, during sample preparation and mass spectrometric analysis. The present review article provides an overview of the recent developments in the emerging area of plant redox proteomics.

AB - In common with other aerobic organisms, plants are exposed to reactive oxygen species resulting in formation of post-translational modifications related to protein oxidoreduction (redox PTMs) that may inflict oxidative protein damage. Accumulating evidence also underscores the importance of redox PTMs in regulating enzymatic activities and controlling biological processes in plants. Notably, proteins controlling the cellular redox state, e.g. thioredoxin and glutaredoxin, appear to play dual roles to maintain oxidative stress resistance and regulate signal transduction pathways via redox PTMs. To get a comprehensive overview of these types of redox-regulated pathways there is therefore an emerging interest to monitor changes in redox PTMs on a proteome scale. Compared to some other PTMs, e.g. protein phosphorylation, redox PTMs have received less attention in plant proteome analysis, possibly due to technical challenges such as with maintaining the in vivo redox states of proteins and the lability of certain PTMs, e.g. nitrosylations, during sample preparation and mass spectrometric analysis. The present review article provides an overview of the recent developments in the emerging area of plant redox proteomics.

KW - Ascorbate

KW - Glutaredoxin

KW - Oxidative stress

KW - Reactive nitrogen species

KW - Reactive oxygen species

KW - Redox

KW - Thioredoxin

U2 - 10.1016/j.jprot.2011.03.008

DO - 10.1016/j.jprot.2011.03.008

M3 - Review

C2 - 21406256

AN - SCOPUS:79961011220

VL - 74

SP - 1450

EP - 1462

JO - Journal of Proteomics

JF - Journal of Proteomics

SN - 1874-3919

IS - 8

ER -

ID: 240160289