Regeneration of peroxiredoxins during recovery after oxidative stress: only some overoxidized peroxiredoxins can be reduced during recovery after oxidative stress.
about
The peroxiredoxin repair proteinsReduction of Cysteine Sulfinic Acid in Peroxiredoxin by Sulfiredoxin Proceeds Directly through a Sulfinic Phosphoryl Ester IntermediateProtein Engineering of the Quaternary Sulfiredoxin{middle dot}Peroxiredoxin Enzyme{middle dot}Substrate Complex Reveals the Molecular Basis for Cysteine Sulfinic Acid PhosphorylationProteomic analysis identifies novel proteins of the Maurer's clefts, a secretory compartment delivering Plasmodium falciparum proteins to the surface of its host cellProteomics of the oxidative stress response induced by hydrogen peroxide and paraquat reveals a novel AhpC-like protein in Pseudomonas aeruginosaDual role of peroxiredoxin I in macrophage-derived foam cellsOxidative stress and protein oxidation in the brain of water drinking and alcohol drinking rats administered the HIV envelope protein, gp120Proteomics of the injured rat sciatic nerve reveals protein expression dynamics during regenerationEpididymis response partly compensates for spermatozoa oxidative defects in snGPx4 and GPx5 double mutant miceThe proteomic to biology inference, a frequently overlooked concern in the interpretation of proteomic data: a plea for functional validation.Proteomic detection of hydrogen peroxide-sensitive thiol proteins in Jurkat cellsInteraction of Ganoderma triterpenes with doxorubicin and proteomic characterization of the possible molecular targets of Ganoderma triterpenes.Peroxiredoxin post-translational modifications by redox messengersReduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-cys peroxiredoxins.Reactive oxygen and nitrogen species in steatotic hepatocytes: a molecular perspective on the pathophysiology of ischemia-reperfusion injury in the fatty liver.Sestrin2 decreases renal oxidative stress, lowers blood pressure, and mediates dopamine D2 receptor-induced inhibition of reactive oxygen species production.Proteomic profiling of differentially expressed proteins from Bax inhibitor-1 knockout and wild type mice.Increased oxidative stress and impaired antioxidant response in Lafora disease.Structural basis for the retroreduction of inactivated peroxiredoxins by human sulfiredoxinSignaling functions of reactive oxygen species.Novel oxidative modifications in redox-active cysteine residues.The Parkinson's disease protein DJ-1 is neuroprotective due to cysteine-sulfinic acid-driven mitochondrial localizationCold Atmospheric Plasma Treatment Induces Anti-Proliferative Effects in Prostate Cancer Cells by Redox and Apoptotic Signaling Pathways.Redox proteomics: identification and functional role of glutathionylated proteins.Oxidative stress response: a proteomic view.Tualang Honey Protects against BPA-Induced Morphological Abnormalities and Disruption of ERα, ERβ, and C3 mRNA and Protein Expressions in the Uterus of RatsAspects of the biological redox chemistry of cysteine: from simple redox responses to sophisticated signalling pathways.Peroxiredoxins play a major role in protecting Trypanosoma cruzi against macrophage- and endogenously-derived peroxynitrite.Cardiac peroxiredoxins undergo complex modifications during cardiac oxidant stress.Kinetic analysis of structural influences on the susceptibility of peroxiredoxins 2 and 3 to hyperoxidationPeroxiredoxin II expression and its association with oxidative stress and cell proliferation in human idiopathic pulmonary fibrosis.Mitochondrial peroxiredoxin 3 is more resilient to hyperoxidation than cytoplasmic peroxiredoxins.Sulfiredoxin Translocation into Mitochondria Plays a Crucial Role in Reducing Hyperoxidized Peroxiredoxin III.Novel protective mechanism against irreversible hyperoxidation of peroxiredoxin: Nalpha-terminal acetylation of human peroxiredoxin II.Molecular basis for the resistance of human mitochondrial 2-Cys peroxiredoxin 3 to hyperoxidationMolecular responses of mouse macrophages to copper and copper oxide nanoparticles inferred from proteomic analyses.Dissecting the integrative antioxidant and redox systems in plant mitochondria. Effect of stress and S-nitrosylationRedox regulation of mitochondrial function with emphasis on cysteine oxidation reactions.Lack of an efficient endoplasmic reticulum-localized recycling system protects peroxiredoxin IV from hyperoxidation.Mitochondrial peroxiredoxin involvement in antioxidant defence and redox signalling.
P2860
Q24652194-27D829DE-B58C-4F0D-A229-7BF27CA8B87BQ27650948-324E2F0B-E907-4BF8-918D-7CF805EFBD19Q27657723-8C725BA4-D208-495D-AF9D-71B9A6DDE5A3Q27973506-7ABC8CE3-7542-4651-AF66-BC9C7B088310Q28492540-AB73E04D-0FE4-4982-9F86-72FF69DEE4D1Q28505046-2874056D-609D-41F8-AE59-F2F95731E378Q28565475-8ED3350C-6328-4763-BA99-5597C5721107Q28567517-C7BB3D07-9653-4F1A-8155-4CECD3580047Q28728432-5DB70BB7-BE72-48E0-B318-54E3088888E8Q30700824-B9BD0E2E-5B53-4214-AC00-4C5411C41CCCQ33213431-29733412-2A07-4BCF-BCF9-98BEEABD1368Q33329230-9F463006-2CB5-4224-8819-3782E2033BADQ33857883-BECFED4F-81A5-4162-BC24-D041C0D7CCB6Q33983693-E11160D4-8A1A-47A5-8A78-18A4CEFB09E6Q34009236-57FFC309-F0A6-4AA6-951D-44EEEE488028Q34173690-B86A18C4-5BCF-45D7-87BD-D1F8CA26B4A2Q34317895-1DD19CF4-F7ED-4838-A145-565327C0B8EFQ34420455-55982C6D-3627-4009-BD0C-D105D4F53B7FQ34426006-5B470DF0-C840-459D-A82C-FC014453D5CCQ34482191-CDDE2DC9-30C7-4DA5-8B61-F762933A3CCDQ34616738-F7378140-4845-452B-8A4C-2B9044F3A139Q34836156-D1FA8587-DFE0-4D39-98D3-A93749FD8AF2Q35680270-07B37802-8389-4A6E-B216-A257C5DA3A2EQ36168403-83115B7F-D0D3-4EC8-998C-5E46C2C4A73AQ36322168-0B0F6CFB-6E22-4E0B-8332-B64A6A48EB57Q36405655-BC3D658A-A711-4766-894A-967A0A94AA5FQ36642755-FBA6E98F-57C7-46DA-9EA0-73F46A6C5B85Q36740177-C359D22A-2968-4A13-BA74-F32EED4A7462Q36807991-00D1420D-1774-43F3-BDFF-788AD7506BFEQ36876837-EC16CBCB-A0D6-4DDC-942D-16F241E96606Q36893845-35FC3B10-0889-44B0-AE5C-ABEA6FE48BA6Q37100400-CC455D73-FEAE-4ED9-8A21-08C83326FF06Q37136773-12D19B5C-2078-46B5-95AD-AAA275A869CEQ37185260-233A8753-A9B2-49C6-9DB6-A1D8F3E5C95FQ37226194-ED17AF25-D6F8-4D1E-ACB0-AAE3A0519991Q37289373-9F870E71-BAFD-4CBC-AC10-1361C350F40EQ37348617-7DD6FDDA-96B4-4341-86D7-3F6861E4A119Q37493001-546497A6-2B58-4AFF-9C06-E04612AE3988Q37608430-4F85C951-CFC4-4B46-89DF-B976BF2B14D6Q37660501-9DDA36A2-3567-484A-AEAA-3FC5971C1B62
P2860
Regeneration of peroxiredoxins during recovery after oxidative stress: only some overoxidized peroxiredoxins can be reduced during recovery after oxidative stress.
description
2003 nî lūn-bûn
@nan
2003 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հուլիսին 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
Regeneration of peroxiredoxins ...... covery after oxidative stress.
@ast
Regeneration of peroxiredoxins ...... covery after oxidative stress.
@en
type
label
Regeneration of peroxiredoxins ...... covery after oxidative stress.
@ast
Regeneration of peroxiredoxins ...... covery after oxidative stress.
@en
prefLabel
Regeneration of peroxiredoxins ...... covery after oxidative stress.
@ast
Regeneration of peroxiredoxins ...... covery after oxidative stress.
@en
P2093
P356
P1476
Regeneration of peroxiredoxins ...... covery after oxidative stress.
@en
P2093
Alain van Dorsselaer
Elsa Wagner
Mireille Chevallet
Sylvie Luche
Thierry Rabilloud
P304
37146-37153
P356
10.1074/JBC.M305161200
P407
P577
2003-07-08T00:00:00Z