(Q37761769)

22 August 2017

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title

Identification by MS/MS of disulfides produced by a functional redox transition (English)

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22 August 2017

2

Stefano Toppo

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22 August 2017

6

Fulvio Ursini

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22 August 2017

5

Matilde Maiorino

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22 August 2017

Pierluigi Mauri

1

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22 August 2017

Antonella De Palma

series ordinal

3

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22 August 2017

Louise Benazzi

series ordinal

4

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22 August 2017

language of work or name

English

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publication date

1 January 2010

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22 August 2017

published in

Methods in Enzymology

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22 August 2017

volume

473

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22 August 2017

page(s)

217-225

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Structural basis of the redox switch in the OxyR transcription factor

22 August 2017

cites work

1 reference

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A thiol peroxidase is an H2O2 receptor and redox-transducer in gene activation

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Signaling functions of reactive oxygen species.

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Protein disulfide bond determination by mass spectrometry

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7 January 2021

The disulfide bond formation (Dsb) system

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7 January 2021

The thioredoxin specificity of Drosophila GPx: a paradigm for a peroxiredoxin-like mechanism of many glutathione peroxidases.

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7 January 2021

Versatility of selenium catalysis in PHGPx unraveled by LC/ESI-MS/MS.

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7 January 2021

Sulfur-centered radical formation from the antioxidant dihydrolipoic acid

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7 January 2021

A Disulphide Interchange Reaction

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7 January 2021

Identification and characterization of a selenoprotein family containing a diselenide bond in a redox motif

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7 January 2021

Catalytic mechanisms and specificities of glutathione peroxidases: variations of a basic scheme

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7 January 2021

The catalytic site of glutathione peroxidases.

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7 January 2021

The mycobacterial thioredoxin peroxidase can act as a one-cysteine peroxiredoxin

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7 January 2021

pH dependence of the isomerase activity of protein disulfide isomerase: insights into its functional relevance

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https://api.crossref.org/works/10.1016%2FS0076-6879%2810%2973011-1

7 January 2021

Disulfides as redox switches: from molecular mechanisms to functional significance

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2810%2973011-1

7 January 2021

10.1016/S0076-6879(10)73011-1

Identifiers

DOI

1 reference

22 August 2017

1 reference