(Q38238640)

31 August 2017

title

Intermolecular disulfide-dependent redox signalling (English)

1 reference

31 August 2017

Harmjan R Vos

2

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Tobias B Dansen

object named as

Tobias B Dansen

series ordinal

3

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author name string

Marrit Putker

series ordinal

1

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31 August 2017

publication date

1 August 2014

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Biochemical Society Transactions

31 August 2017

published in

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31 August 2017

volume

42

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31 August 2017

issue

4

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31 August 2017

page(s)

971-978

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Signal transduction by reactive oxygen species

31 August 2017

cites work

1 reference

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Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine

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Cysteine sulfenic acid as an intermediate in disulfide bond formation and nonenzymatic protein folding

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Peroxiredoxin 1 functions as a signal peroxidase to receive, transduce, and transmit peroxide signals in mammalian cells

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Peroxiredoxin functions as a peroxidase and a regulator and sensor of local peroxides

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Disulfide Bond-mediated multimerization of Ask1 and its reduction by thioredoxin-1 regulate H(2)O(2)-induced c-Jun NH(2)-terminal kinase activation and apoptosis

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Identifiers

DOI

10.1042/BST20140097

1 reference

31 August 2017

1 reference