Multiple glutathione disulfide removal pathways mediate cytosolic redox homeostasis. (Q27939956)

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20 February 2020

title

Multiple glutathione disulfide removal pathways mediate cytosolic redox homeostasis (English)

1 reference

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20 February 2020

main subject

Thioredoxin TRX2 YGR209C

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ATP-binding cassette glutathione S-conjugate transporter YCF1 YDR135C

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Glutathione-disulfide reductase GLR1 YPL091W

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Dithiol glutaredoxin GRX2 YDR513W

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1 reference

1

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20 February 2020

author name string

Daria Ezeriņa

2

1 reference

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20 February 2020

Theresa N E Amoako

3

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20 February 2020

Jan Riemer

4

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20 February 2020

Matthias Seedorf

5

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20 February 2020

Tobias P Dick

6

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20 February 2020

language of work or name

English

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publication date

16 December 2012

1 reference

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20 February 2020

published in

Nature Chemical Biology

2 references

1 December 2016

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20 February 2020

volume

9

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20 February 2020

page(s)

119-125

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20 February 2020

issue

2

1 reference

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The multidrug resistance protein MRP1 mediates the release of glutathione disulfide from rat astrocytes during oxidative stress

20 February 2020

cites work

1 reference

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The NADPH-dependent thioredoxin system constitutes a functional backup for cytosolic glutathione reductase in Arabidopsis

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Substitution of the thioredoxin system for glutathione reductase in Drosophila melanogaster

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Glutaredoxins catalyze the reduction of glutathione by dihydrolipoamide with high efficiency

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Structural and kinetic analysis of Saccharomyces cerevisiae thioredoxin Trx1: implications for the catalytic mechanism of GSSG reduced by the thioredoxin system

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Glutathione is an essential metabolite required for resistance to oxidative stress in the yeast Saccharomyces cerevisiae.

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Molecular mechanisms and clinical implications of reversible protein S-glutathionylation

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A glutathione reductase mutant of yeast accumulates high levels of oxidized glutathione and requires thioredoxin for growth

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Monitoring disulfide bond formation in the eukaryotic cytosol

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Imaging dynamic redox changes in mammalian cells with green fluorescent protein indicators

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Real-time imaging of the intracellular glutathione redox potential.

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Measuring E(GSH) and H2O2 with roGFP2-based redox probes.

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The yeast CLC protein counteracts vesicular acidification during iron starvation

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Fluorescent protein-based redox probes

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In vivo mapping of hydrogen peroxide and oxidized glutathione reveals chemical and regional specificity of redox homeostasis.

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Redox-sensitive YFP sensors monitor dynamic nuclear and cytosolic glutathione redox changes

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Free aminothiols, glutathione redox state and protein mixed disulphides in aging Drosophila melanogaster

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Measuring the poise of thiol/disulfide couples in vivo

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Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple

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Redox characteristics of the eukaryotic cytosol

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Glutathione transport is a unique function of the ATP-binding cassette protein ABCG2.

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ABC transporters in Saccharomyces cerevisiae and their interactors: new technology advances the biology of the ABCC (MRP) subfamily

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Ycf1p attenuates basal level oxidative stress response in Saccharomyces cerevisiae

21 January 2018

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The Rho1 GTPase acts together with a vacuolar glutathione S-conjugate transporter to protect yeast cells from oxidative stress

21 January 2018

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The thioredoxin-thioredoxin reductase system can function in vivo as an alternative system to reduce oxidized glutathione in Saccharomyces cerevisiae

21 January 2018

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21 January 2018

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21 January 2018

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12 December 2020

Cellular Redox: A Modulator of Intestinal Epithelial Cell Proliferation

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12 December 2020

Yeast glutathione reductase. I. Spectrophotometric and kinetic studies of its interaction with reduced nicotinamide adenine dinucleotide

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12 December 2020

Assay for quantitative determination of glutathione and glutathione disulfide levels using enzymatic recycling method

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12 December 2020

Cytoplasmic glutathione redox status determines survival upon exposure to the thiol-oxidant 4,4â ²-dipyridyl disulfide

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12 December 2020

Identifiers

DOI

10.1038/NCHEMBIO.1142

2 references

Consolidated OpenCitations Corpus – April 2017

2627435

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23242256%20AND%20SRC:MED&resulttype=core&format=json

Dimensions Publication ID

20 February 2020

1019117833

0 references

2627435

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

2 references

2627435

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23242256%20AND%20SRC:MED&resulttype=core&format=json