Nature Search

New approach to determination of specific functions of platelet membrane sites

G. TOBELEM
S. LEVY-TOLEDANO
L. DEGOS
Research30 Sept 1976
Nature

Volume: 263, P: 427-429
Physiologically relevant reconstitution of iron-sulfur cluster biosynthesis uncovers persulfide-processing functions of ferredoxin-2 and frataxin

The mechanism of iron-sulfur (Fe-S) cluster biosynthesis is not fully understood. Here, the authors develop a physiologically relevant in vitro model of Fe-S cluster assembly, allowing them to elucidate the sequence of Fe-S cluster synthesis along with the respective roles of ferredoxin-2 and frataxin.

Sylvain Gervason
Djabir Larkem
Benoit D’Autréaux
ResearchOpen Access08 Aug 2019
Nature Communications

Volume: 10, P: 1-12
A scaffold protein that chaperones a cysteine-sulfenic acid in H₂O₂ signaling

The H₂O₂-responsive transcription factor Yap1 undergoes oxidative activation mediated by the peroxidase Orp1. In vitro reconstitution of the redox relay revealed a role for the Yap1-binding protein Ybp1 in promoting the formation of a ternary complex with Orp1 and Yap1 to enable redox transfer.

Antoine Bersweiler
Benoît D'Autréaux
Sophie Rahuel-Clermont
Research19 Jun 2017
Nature Chemical Biology

Volume: 13, P: 909-915
ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis

Reactive oxygen species (ROS) have been shown to be toxic but also function as signalling molecules. Recent studies have provided insights into the mechanisms that regulate ROS homeostasis and provide specificity in ROS signalling from prokaryotes to mammals.

Benoît D'Autréaux
Michel B. Toledano
Reviews01 Oct 2007
Nature Reviews Molecular Cell Biology

Volume: 8, P: 813-824
ATP-dependent reduction of cysteine–sulphinic acid by S. cerevisiae sulphiredoxin

Benoît Biteau
Jean Labarre
Michel B. Toledano
Research30 Oct 2003
Nature

Volume: 425, P: 980-984
Light-sensing via hydrogen peroxide and a peroxiredoxin

While yeasts lack dedicated photoreceptors, they nonetheless possess metabolic rhythms responsive to light. Here the authors find that light signalling in budding yeast involves the production of H₂O₂, which in turn regulates protein kinase A through a peroxiredoxin-thioredoxin redox relay.

Kristofer Bodvard
Ken Peeters
Mikael Molin
ResearchOpen Access24 Mar 2017
Nature Communications

Volume: 8, P: 1-11
Parsing protein sulfinic acid switches

The proteome-wide application of a probe that selectively labels cysteine residues oxidized to the sulfinic acid form reveals the mammalian S-sulfinylome and uncovers novel substrates of the sulfinyl reductase sulfiredoxin, opening yet unexplored realms of cysteine-based redox regulation.

Sophie Rahuel-Clermont
Michel B. Toledano
News & Views16 Oct 2018
Nature Chemical Biology

Volume: 14, P: 991-993
Mammalian frataxin directly enhances sulfur transfer of NFS1 persulfide to both ISCU and free thiols

The protein frataxin has a role in iron–sulfur clusters biosynthesis that is still elusive. Here, the authors present a novel alkylation assay for the detection of persulfide, an intermediate in this process, and describe the function of frataxin in the control of persulfide transfer.

Aubérie Parent
Xavier Elduque
Benoit D’Autréaux
Research19 Jan 2015
Nature Communications

Volume: 6, P: 1-12

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New approach to determination of specific functions of platelet membrane sites

Physiologically relevant reconstitution of iron-sulfur cluster biosynthesis uncovers persulfide-processing functions of ferredoxin-2 and frataxin

A scaffold protein that chaperones a cysteine-sulfenic acid in H₂O₂ signaling

ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis

ATP-dependent reduction of cysteine–sulphinic acid by S. cerevisiae sulphiredoxin

Light-sensing via hydrogen peroxide and a peroxiredoxin

Parsing protein sulfinic acid switches

Mammalian frataxin directly enhances sulfur transfer of NFS1 persulfide to both ISCU and free thiols

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