Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product
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Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediateRegulation of peroxiredoxin I activity by Cdc2-mediated phosphorylationMutations in LRRK2 increase phosphorylation of peroxiredoxin 3 exacerbating oxidative stress-induced neuronal deathA method for detection of overoxidation of cysteines: peroxiredoxins are oxidized in vivo at the active-site cysteine during oxidative stressStructures of tryparedoxins revealing interaction with trypanothioneCrystal structure of the quorum-sensing protein LuxS reveals a catalytic metal siteThe crystal structure of Mycobacterium tuberculosis alkylhydroperoxidase AhpD, a potential target for antitubercular drug designThe tetrameric structure of Haemophilus influenza hybrid Prx5 reveals interactions between electron donor and acceptor proteinsTryparedoxins from Crithidia fasciculata and Trypanosoma brucei: photoreduction of the redox disulfide using synchrotron radiation and evidence for a conformational switch implicated in functionCrystal structure of Escherichia coli thiol peroxidase in the oxidized state: insights into intramolecular disulfide formation and substrate binding in atypical 2-Cys peroxiredoxinsDimer-oligomer interconversion of wild-type and mutant rat 2-Cys peroxiredoxin: disulfide formation at dimer-dimer interfaces is not essential for decamerizationStructure of the sulphiredoxin–peroxiredoxin complex reveals an essential repair embraceThe crystal structure of the C45S mutant of annelidArenicola marinaperoxiredoxin 6 supports its assignment to the mechanistically typical 2-Cys subfamily without any formation of toroid-shaped decamersStructural Basis for a Distinct Catalytic Mechanism in Trypanosoma brucei Tryparedoxin PeroxidaseMoonlighting by Different Stressors: Crystal Structure of the Chaperone Species of a 2-Cys PeroxiredoxinCrystal structure of mammalian selenocysteine-dependent iodothyronine deiodinase suggests a peroxiredoxin-like catalytic mechanismATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin.Peroxiredoxin 1 - an antioxidant enzyme in cancerHuman peroxiredoxin 1 and 2 are not duplicate proteins: the unique presence of CYS83 in Prx1 underscores the structural and functional differences between Prx1 and Prx2Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acidCharacterization of the Mycobacterium tuberculosis H37Rv alkyl hydroperoxidase AhpC points to the importance of ionic interactions in oligomerization and activityThe AhpC and AhpD antioxidant defense system of Mycobacterium tuberculosisDifferential cellular and subcellular localization of heme-binding protein 23/peroxiredoxin I and heme oxygenase-1 in rat liverMice with targeted mutation of peroxiredoxin 6 develop normally but are susceptible to oxidative stressGenome-wide analysis of putative peroxiredoxin in unicellular and filamentous cyanobacteriaStructural and biochemical characterization of a mitochondrial peroxiredoxin from Plasmodium falciparumOxidative stress-dependent structural and functional switching of a human 2-Cys peroxiredoxin isotype II that enhances HeLa cell resistance to H2O2-induced cell death.Phosphorylation and concomitant structural changes in human 2-Cys peroxiredoxin isotype I differentially regulate its peroxidase and molecular chaperone functions.A novel peroxiredoxin of the plant Sedum lineare is a homologue of Escherichia coli bacterioferritin co-migratory protein (Bcp)Kinetics and redox-sensitive oligomerisation reveal negative subunit cooperativity in tryparedoxin peroxidase of Trypanosoma brucei brucei.Augmented expression of peroxiredoxin VI in rat lung and kidney after birth implies an antioxidative role.Biomphalaria glabrata peroxiredoxin: effect of schistosoma mansoni infection on differential gene regulation.Specific expression profile and prognostic significance of peroxiredoxins in grade II-IV astrocytic brain tumors.Crystallization and preliminary crystallographic analysis of mouse peroxiredoxin II with significant pseudosymmetry.Peroxiredoxin 1 (Prx1) is a dual-function enzyme by possessing Cys-independent catalase-like activityRedox-regulated chaperones.The 2-Cys peroxiredoxin alkyl hydroperoxide reductase c binds heme and participates in its intracellular availability in Streptococcus agalactiae.The plant-specific function of 2-Cys peroxiredoxin-mediated detoxification of peroxides in the redox-hierarchy of photosynthetic electron flux.T-LAK cell-originated protein kinase (TOPK) phosphorylation of Prx1 at Ser-32 prevents UVB-induced apoptosis in RPMI7951 melanoma cells through the regulation of Prx1 peroxidase activity.Molecular mechanism of the reduction of cysteine sulfinic acid of peroxiredoxin to cysteine by mammalian sulfiredoxin.
P2860
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P2860
Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product
description
1999 nî lūn-bûn
@nan
1999 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Crystal structure of a multifu ...... ration-associated gene product
@ast
Crystal structure of a multifu ...... ration-associated gene product
@en
Crystal structure of a multifu ...... ration-associated gene product
@nl
type
label
Crystal structure of a multifu ...... ration-associated gene product
@ast
Crystal structure of a multifu ...... ration-associated gene product
@en
Crystal structure of a multifu ...... ration-associated gene product
@nl
prefLabel
Crystal structure of a multifu ...... ration-associated gene product
@ast
Crystal structure of a multifu ...... ration-associated gene product
@en
Crystal structure of a multifu ...... ration-associated gene product
@nl
P2093
P2860
P921
P356
P1476
Crystal structure of a multifu ...... ration-associated gene product
@en
P2093
N Nagahara
T Hakoshima
P2860
P304
P356
10.1073/PNAS.96.22.12333
P407
P577
1999-10-26T00:00:00Z