(Q47291762)

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A eukaryotic-like sulfiredoxin involved in oxidative stress responses and in the reduction of the sulfinic form of 2-Cys peroxiredoxin in the cyanobacterium Anabaena PCC 7120.

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3 February 2020

A eukaryotic-like sulfiredoxin involved in oxidative stress responses and in the reduction of the sulfinic form of 2-Cys peroxiredoxin in the cyanobacterium Anabaena PCC 7120 (English)

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Europe PubMed Central

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3 February 2020

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3 February 2020

Cheng-Cai Zhang

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3 February 2020

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Céline Boileau

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3 February 2020

Céline Brochier-Armanet

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3 February 2020

Annick Janicki

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3 February 2020

Amel Latifi

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3 February 2020

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8 June 2011

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3 February 2020

New Phytologist

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3 February 2020

191

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3 February 2020

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3 February 2020

1108-1118

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3 February 2020

Gapped BLAST and PSI-BLAST: a new generation of protein database search programs

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Use of a conditionally lethal gene in Anabaena sp. strain PCC 7120 to select for double recombinants and to entrap insertion sequences

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Sulfiredoxin: a potential therapeutic agent?

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WoLF PSORT: protein localization predictor

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The sulfinic acid switch in proteins

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Two enzymes in one; two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function

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Molecular mechanism of the reduction of cysteine sulfinic acid of peroxiredoxin to cysteine by mammalian sulfiredoxin

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RETRACTED: TREEFINDER: a powerful graphical analysis environment for molecular phylogenetics

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The peroxiredoxin repair proteins

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Reduction of Cysteine Sulfinic Acid in Peroxiredoxin by Sulfiredoxin Proceeds Directly through a Sulfinic Phosphoryl Ester Intermediate

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Identification of intact protein thiosulfinate intermediate in the reduction of cysteine sulfinic acid in peroxiredoxin by human sulfiredoxin

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21 January 2018

Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120.

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Reaction mechanism of plant 2-Cys peroxiredoxin. Role of the C terminus and the quaternary structure

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Clustal W and Clustal X version 2.0

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