Kinetics and redox-sensitive oligomerisation reveal negative subunit cooperativity in tryparedoxin peroxidase of Trypanosoma brucei brucei.
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The peroxiredoxin repair proteinsStructural Evidence that Peroxiredoxin Catalytic Power Is Based on Transition-State StabilizationMitochondrial redox metabolism in trypanosomatids is independent of tryparedoxin activityThe mycobacterial thioredoxin peroxidase can act as a one-cysteine peroxiredoxinBroad specificity AhpC-like peroxiredoxin and its thioredoxin reductant in the sparse antioxidant defense system of Treponema pallidum.Nitration transforms a sensitive peroxiredoxin 2 into a more active and robust peroxidase.Peroxiredoxins in parasites.Substrate specificity and redox potential of AhpC, a bacterial peroxiredoxinCardiac peroxiredoxins undergo complex modifications during cardiac oxidant stress.Kinetic analysis of structural influences on the susceptibility of peroxiredoxins 2 and 3 to hyperoxidationOxidant sensing by reversible disulfide bond formationMolecular basis for the resistance of human mitochondrial 2-Cys peroxiredoxin 3 to hyperoxidationMono- and dithiol glutaredoxins in the trypanothione-based redox metabolism of pathogenic trypanosomes.Structural insights into the enzymes of the trypanothione pathway: targets for antileishmaniasis drugs.Enzymatic mechanism controls redox-mediated protein-DNA interactions at the replication origin of kinetoplast DNA minicircles.Depletion of the thioredoxin homologue tryparedoxin impairs antioxidative defence in African trypanosomes.Antitumor quinol PMX464 is a cytocidal anti-trypanosomal inhibitor targeting trypanothione metabolism.High throughput screening against the peroxidase cascade of African trypanosomes identifies antiparasitic compounds that inactivate tryparedoxin.Structural and electrostatic asymmetry at the active site in typical and atypical peroxiredoxin dimers.The dithiol glutaredoxins of african trypanosomes have distinct roles and are closely linked to the unique trypanothione metabolism.Catalytic mechanism of the glutathione peroxidase-type tryparedoxin peroxidase of Trypanosoma brucei.Verification of the interaction of a tryparedoxin peroxidase with tryparedoxin by ESI-MS/MS.Trypanosoma brucei and Trypanosoma cruzi tryparedoxin peroxidases catalytically detoxify peroxynitrite via oxidation of fast reacting thiols.The cytosolic or the mitochondrial glutathione peroxidase-type tryparedoxin peroxidase is sufficient to protect procyclic Trypanosoma brucei from iron-mediated mitochondrial damage and lysis.Tryparedoxin peroxidase-deficiency commits trypanosomes to ferroptosis-type cell deathThiol Peroxidases of Trypanosomatids
P2860
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P2860
Kinetics and redox-sensitive oligomerisation reveal negative subunit cooperativity in tryparedoxin peroxidase of Trypanosoma brucei brucei.
description
2003 nî lūn-bûn
@nan
2003 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Kinetics and redox-sensitive o ...... of Trypanosoma brucei brucei.
@ast
Kinetics and redox-sensitive o ...... of Trypanosoma brucei brucei.
@en
type
label
Kinetics and redox-sensitive o ...... of Trypanosoma brucei brucei.
@ast
Kinetics and redox-sensitive o ...... of Trypanosoma brucei brucei.
@en
prefLabel
Kinetics and redox-sensitive o ...... of Trypanosoma brucei brucei.
@ast
Kinetics and redox-sensitive o ...... of Trypanosoma brucei brucei.
@en
P2093
P2860
P356
P1433
P1476
Kinetics and redox-sensitive o ...... of Trypanosoma brucei brucei.
@en
P2093
Birgit Hofmann
Hans-Jürgen Hecht
Heike Budde
Josef Wissing
Leopold Flohé
Matthias Stehr
P2860
P304
P356
10.1515/BC.2003.069
P577
2003-04-01T00:00:00Z