(Q27656042)

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Analysis of the Structure and Function of YfcG from Escherichia coli Reveals an Efficient and Unique Disulfide Bond Reductase

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Analysis of the Structure and Function of YfcG from Escherichia coli Reveals an Efficient and Unique Disulfide Bond Reductase (English)

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1 reference

Megan C Wadington

1

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Jane E Ladner

series ordinal

2

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Nina V Stourman

series ordinal

3

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Joel M Harp

series ordinal

4

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Richard N Armstrong

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5

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language of work or name

English

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publication date

21 July 2009

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published in

Biochemistry

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volume

48

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issue

28

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page(s)

6559-61

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cites work

Conserved structural elements in glutathione transferase homologues encoded in the genome of Escherichia coli

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stated in

PubMed Central

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20 March 2017

Functional plasticity of a peroxidase allows evolution of diverse disulfide-reducing pathways

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PubMed Central

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29 September 2017

Thioredoxins and glutaredoxins as facilitators of protein folding.

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PubMed Central

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29 September 2017

Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria

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PubMed Central

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retrieved

29 September 2017

Structure, catalytic mechanism, and evolution of the glutathione transferases

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PubMed Central

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29 September 2017

Glutathionylspermidine metabolism in Escherichia coli.

1 reference

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PubMed Central

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29 September 2017

Molecular and cellular aspects of thiol-disulfide exchange.

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PubMed Central

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29 September 2017

Cloning, overexpression, and characterization of glutaredoxin 2, an atypical glutaredoxin from Escherichia coli

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PubMed Central

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retrieved

2 June 2018

Three distinct-type glutathione S-transferases from Escherichia coli important for defense against oxidative stress.

1 reference

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PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2996727

retrieved

27 November 2018

Identifiers

DOI

10.1021/BI9008825

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Fatcat ID

release_vsdciqou3zh65fhtp2w6fp3gvu

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ResearchGate publication ID

26302601

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(Q27656042)

Analysis of the Structure and Function of YfcG from Escherichia coli Reveals an Efficient and Unique Disulfide Bond Reductase

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