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Temporal coordination of the transcription factor response to H₂O₂ stress

H₂O₂ stress is known to activate a slew of transcription factors that restore redox balance. Here, the authors use live-cell imaging and single-cell analysis to reveal that the transcription factors that are activated and their timing of activation is dose dependent.

Elizabeth Jose
Woody March-Steinman
Andrew L. Paek
ResearchOpen Access23 Apr 2024
Nature Communications

Volume: 15, P: 1-17
A fast and specific fluorescent probe for thioredoxin reductase that works via disulphide bond cleavage

Thioredoxin reductase (TrxR) plays a crucial part in regulating cellular redox homeostasis. Here, the authors developed a fluorescent probe composed of a five-membered disulphide, a coumarin fluorophore and a urea linker that detects TrxR activity with fast response and high selectivity.

Xinming Li
Baoxin Zhang
Jianguo Fang
ResearchOpen Access21 Jun 2019
Nature Communications

Volume: 10, P: 1-12
A role for annexin A2 in scaffolding the peroxiredoxin 2–STAT3 redox relay complex

Peroxiredoxin 2 (Prx2) was previously shown to transfer H₂O₂-derived oxidative equivalents to STAT3, generating disulfide-linked dimers and tetramers. Here the authors show that the interaction between Prx2 and STAT3 at the plasma membrane is mediated by the membrane chaperone annexin A2; suggesting that the redox relay complex is part of a membrane signaling domain.

Deepti Talwar
Joris Messens
Tobias P. Dick
ResearchOpen Access09 Sept 2020
Nature Communications

Volume: 11, P: 1-11
Quantitative assessment of the determinant structural differences between redox-active and inactive glutaredoxins

Glutaredoxins play a central role in numerous biological processes including cellular redox homeostasis and Fe-S cluster biogenesis. Here the authors establish the molecular basis for glutaredoxin redox catalysis through comprehensive biochemical and structural analyses.

Linda Liedgens
Jannik Zimmermann
Marcel Deponte
ResearchOpen Access07 Apr 2020
Nature Communications

Volume: 11, P: 1-18
Oxidative stress, protein damage and repair in bacteria

Oxidative damage can have a devastating effect on the structure and activity of proteins, leading to cell death. This Review discusses how bacteria repair oxidized proteins and highlights the importance of these repair systems in physiology and virulence.

Benjamin Ezraty
Alexandra Gennaris
Jean-François Collet
Reviews19 Apr 2017
Nature Reviews Microbiology

Volume: 15, P: 385-396
Pan msr gene deleted strain of Salmonella Typhimurium suffers oxidative stress, depicts macromolecular damage and attenuated virulence

Raj Sahoo
Tapan Kumar Singh Chauhan
Manish Mahawar
ResearchOpen Access09 Dec 2023
Scientific Reports

Volume: 13, P: 1-14
Structural and mechanistic basis for redox sensing by the cyanobacterial transcription regulator RexT

The DNA binding and H₂O₂ sensing mechanisms are revealed for RexT, a transcriptional regulator found in cyanobacteria of the Nostocales order.

Bin Li
Minshik Jo
Jennifer Bridwell-Rabb
ResearchOpen Access28 Mar 2022
Communications Biology

Volume: 5, P: 1-15
Low expression of the PPARγ-regulated gene thioredoxin-interacting protein accompanies human melanoma progression and promotes experimental lung metastases

Patrick Meylan
Christine Pich
Liliane Michalik
ResearchOpen Access12 Apr 2021
Scientific Reports

Volume: 11, P: 1-17
Thyroxine binding to type III iodothyronine deiodinase

Craig A. Bayse
Eric S. Marsan
Alexis T. Tran-Thompson
ResearchOpen Access21 Sept 2020
Scientific Reports

Volume: 10, P: 1-10
Interaction of the GntR-family transcription factor Sll1961 with thioredoxin in the cyanobacterium Synechocystis sp. PCC 6803

Junichi Kujirai
Sato Nanba
Yukako Hihara
ResearchOpen Access27 Apr 2018
Scientific Reports

Volume: 8, P: 1-11
Structural variability of E. coli thioredoxin captured in the crystal structures of single-point mutants

Martín E. Noguera
Diego S. Vazquez
Javier Santos
ResearchOpen Access09 Feb 2017
Scientific Reports

Volume: 7, P: 1-12
Catalytic Thr or Ser Residue Modulates Structural Switches in 2-Cys Peroxiredoxin by Distinct Mechanisms

Carlos A. Tairum
Melina Cardoso Santos
Marcos A. de Oliveira
ResearchOpen Access15 Sept 2016
Scientific Reports

Volume: 6, P: 1-12
Cell-mediated reduction of human β-defensin 1: a major role for mucosal thioredoxin

S U Jaeger
B O Schroeder
J Wehkamp
ResearchOpen Access10 Apr 2013
Mucosal Immunology

Volume: 6, P: 1179-1190
Acceleration of protein folding by four orders of magnitude through a single amino acid substitution

Daniel J. A. Roderer
Martin A. Schärer
Rudi Glockshuber
ResearchOpen Access30 Jun 2015
Scientific Reports

Volume: 5, P: 1-16
The conserved Trp114 residue of thioredoxin reductase 1 has a redox sensor-like function triggering oligomerization and crosslinking upon oxidative stress related to cell death

J Xu
S E Eriksson
E S J Arnér
ResearchOpen Access22 Jan 2015
Cell Death & Disease

Volume: 6, P: e1616
The disruption of the rod-derived cone viability gene leads to photoreceptor dysfunction and susceptibility to oxidative stress

T Cronin
W Raffelsberger
T Léveillard
Research05 Feb 2010
Cell Death & Differentiation

Volume: 17, P: 1199-1210

Search

Temporal coordination of the transcription factor response to H₂O₂ stress

A fast and specific fluorescent probe for thioredoxin reductase that works via disulphide bond cleavage

A role for annexin A2 in scaffolding the peroxiredoxin 2–STAT3 redox relay complex

Quantitative assessment of the determinant structural differences between redox-active and inactive glutaredoxins

Oxidative stress, protein damage and repair in bacteria

Pan msr gene deleted strain of Salmonella Typhimurium suffers oxidative stress, depicts macromolecular damage and attenuated virulence

Structural and mechanistic basis for redox sensing by the cyanobacterial transcription regulator RexT

Low expression of the PPARγ-regulated gene thioredoxin-interacting protein accompanies human melanoma progression and promotes experimental lung metastases

Thyroxine binding to type III iodothyronine deiodinase

Interaction of the GntR-family transcription factor Sll1961 with thioredoxin in the cyanobacterium Synechocystis sp. PCC 6803

Structural variability of E. coli thioredoxin captured in the crystal structures of single-point mutants

Catalytic Thr or Ser Residue Modulates Structural Switches in 2-Cys Peroxiredoxin by Distinct Mechanisms

Cell-mediated reduction of human β-defensin 1: a major role for mucosal thioredoxin

Acceleration of protein folding by four orders of magnitude through a single amino acid substitution

The conserved Trp114 residue of thioredoxin reductase 1 has a redox sensor-like function triggering oligomerization and crosslinking upon oxidative stress related to cell death

The disruption of the rod-derived cone viability gene leads to photoreceptor dysfunction and susceptibility to oxidative stress

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