(Q27650585)

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Glutathionylation-triggered conformational changes of glutaredoxin Grx1 from the yeast Saccharomyces cerevisiae

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title

Glutathionylation-triggered conformational changes of glutaredoxin Grx1 from the yeast Saccharomyces cerevisiae (English)

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main subject

Saccharomyces cerevisiae

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author name string

Jiang Yu

series ordinal

1

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Nan-Nan Zhang

series ordinal

2

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Pei-Dong Yin

series ordinal

3

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Pei-Xin Cui

series ordinal

4

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Cong-Zhao Zhou

series ordinal

5

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language of work or name

English

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publication date

15 August 2008

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published in

Proteins

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volume

72

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issue

3

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page(s)

1077-83

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cites work

Thioredoxin or glutaredoxin in Escherichia coli is essential for sulfate reduction but not for deoxyribonucleotide synthesis

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Crossref

reference URL

https://api.crossref.org/works/10.1002%2FPROT.22096

retrieved

21 January 2018

Grx5 glutaredoxin plays a central role in protection against protein oxidative damage in Saccharomyces cerevisiae

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1002%2FPROT.22096

retrieved

21 January 2018

The yeast Saccharomyces cerevisiae contains two glutaredoxin genes that are required for protection against reactive oxygen species.

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1002%2FPROT.22096

retrieved

21 January 2018

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

1 reference

20 May 2022

https://opencitations.net/index/coci/api/v1/citations/10.1107/S0907444998003254

Roles of the glutathione- and thioredoxin-dependent reduction systems in the Escherichia coli and saccharomyces cerevisiae responses to oxidative stress.

1 reference

12 April 2024

https://opencitations.net/index/api/v1/citations/10.1146/ANNUREV.MICRO.54.1.439

Identifiers

DOI

10.1002/PROT.22096

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Fatcat ID

release_hykqhms6gnapdcwhyovqo2uo3m

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PubMed publication ID

18473363

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ResearchGate publication ID

5379019

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(Q27650585)

Glutathionylation-triggered conformational changes of glutaredoxin Grx1 from the yeast Saccharomyces cerevisiae

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