Mechanisms and dynamics in the thiol/disulfide redox regulatory network: transmitters, sensors and targets

König J, Muthuramalingam M, Dietz K-J (2012)
Current opinion in plant biology 15(3): 261-268.

Journal Article | Published | English

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Abstract
Plant cells sense, weigh and integrate various endogenous and exogenous cues in order to optimize acclimation and resource allocation. The thiol/disulfide redox network appears to be in the core of this versatile integration process. In plant cells its complexity exceeds by far that of other organisms. Recent research has elucidated the multiplicity of the diversified input elements, transmitters (thioredoxin, glutaredoxins), targets and sensors (peroxiredoxins and other peroxidases), controlled processes and final acceptors (reactive oxygen species). An additional level of thiol/disulfide regulation is achieved by introducing dynamics in time and subcompartment and complex association. Copyright 2011 Elsevier Ltd. All rights reserved.
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König J, Muthuramalingam M, Dietz K-J. Mechanisms and dynamics in the thiol/disulfide redox regulatory network: transmitters, sensors and targets. Current opinion in plant biology. 2012;15(3):261-268.
König, J., Muthuramalingam, M., & Dietz, K. - J. (2012). Mechanisms and dynamics in the thiol/disulfide redox regulatory network: transmitters, sensors and targets. Current opinion in plant biology, 15(3), 261-268.
König, J., Muthuramalingam, M., and Dietz, K. - J. (2012). Mechanisms and dynamics in the thiol/disulfide redox regulatory network: transmitters, sensors and targets. Current opinion in plant biology 15, 261-268.
König, J., Muthuramalingam, M., & Dietz, K.-J., 2012. Mechanisms and dynamics in the thiol/disulfide redox regulatory network: transmitters, sensors and targets. Current opinion in plant biology, 15(3), p 261-268.
J. König, M. Muthuramalingam, and K.-J. Dietz, “Mechanisms and dynamics in the thiol/disulfide redox regulatory network: transmitters, sensors and targets”, Current opinion in plant biology, vol. 15, 2012, pp. 261-268.
König, J., Muthuramalingam, M., Dietz, K.-J.: Mechanisms and dynamics in the thiol/disulfide redox regulatory network: transmitters, sensors and targets. Current opinion in plant biology. 15, 261-268 (2012).
König, Janine, Muthuramalingam, Meenakumari, and Dietz, Karl-Josef. “Mechanisms and dynamics in the thiol/disulfide redox regulatory network: transmitters, sensors and targets”. Current opinion in plant biology 15.3 (2012): 261-268.
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Gollan PJ, Tikkanen M, Aro EM., Curr. Opin. Plant Biol. 27(), 2015
PMID: 26318477
Loss of APD1 in yeast confers hydroxyurea sensitivity suppressed by Yap1p transcription factor.
Tang HM, Pan K, Kong KY, Hu L, Chan LC, Siu KL, Sun H, Wong CM, Jin DY., Sci Rep 5(), 2015
PMID: 25600293
Nitrogen-use efficiency in maize (Zea mays L.): from 'omics' studies to metabolic modelling.
Simons M, Saha R, Guillard L, Clement G, Armengaud P, Canas R, Maranas CD, Lea PJ, Hirel B., J. Exp. Bot. 65(19), 2014
PMID: 24863438
Redox regulation of Arabidopsis mitochondrial citrate synthase.
Schmidtmann E, Konig AC, Orwat A, Leister D, Hartl M, Finkemeier I., Mol Plant 7(1), 2014
PMID: 24198232
Overexpression of chloroplast NADPH-dependent thioredoxin reductase in Arabidopsis enhances leaf growth and elucidates in vivo function of reductase and thioredoxin domains.
Toivola J, Nikkanen L, Dahlstrom KM, Salminen TA, Lepisto A, Vignols HF, Rintamaki E., Front Plant Sci 4(), 2013
PMID: 24115951
The conformational bases for the two functionalities of 2-cysteine peroxiredoxins as peroxidase and chaperone.
Konig J, Galliardt H, Jutte P, Schaper S, Dittmann L, Dietz KJ., J. Exp. Bot. 64(11), 2013
PMID: 23828546
Advances in purification and separation of posttranslationally modified proteins.
Cerny M, Skalak J, Cerna H, Brzobohaty B., J Proteomics 92(), 2013
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The hydrogen peroxide-sensitive proteome of the chloroplast in vitro and in vivo.
Muthuramalingam M, Matros A, Scheibe R, Mock HP, Dietz KJ., Front Plant Sci 4(), 2013
PMID: 23516120
Oxidative folding in chloroplasts.
Kieselbach T., Antioxid. Redox Signal. 19(1), 2013
PMID: 23289792
From top-down to bottom-up: computational modeling approaches for cellular redoxin networks.
Pillay CS, Hofmeyr JH, Mashamaite LN, Rohwer JM., Antioxid. Redox Signal. 18(16), 2013
PMID: 23249367
Mitochondrial energy and redox signaling in plants.
Schwarzlander M, Finkemeier I., Antioxid. Redox Signal. 18(16), 2013
PMID: 23234467
Inactivation of thioredoxin f1 leads to decreased light activation of ADP-glucose pyrophosphorylase and altered diurnal starch turnover in leaves of Arabidopsis plants.
Thormahlen I, Ruber J, von Roepenack-Lahaye E, Ehrlich SM, Massot V, Hummer C, Tezycka J, Issakidis-Bourguet E, Geigenberger P., Plant Cell Environ. 36(1), 2013
PMID: 22646759

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