Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation
about
Cloning and characterization of AOEB166, a novel mammalian antioxidant enzyme of the peroxiredoxin familyHepatitis C virus core protein-induced loss of LZIP function correlates with cellular transformationIdentification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediateProteomics analysis of cellular response to oxidative stress. Evidence for in vivo overoxidation of peroxiredoxins at their active siteNuclear and cytoplasmic peroxiredoxin-1 differentially regulate NF-kappaB activitiesMixed lineage kinase LZK and antioxidant protein-1 activate NF-kappaB synergisticallyDifferential expression, localization and activity of two alternatively spliced isoforms of human APC regulator CDH1A method for detection of overoxidation of cysteines: peroxiredoxins are oxidized in vivo at the active-site cysteine during oxidative stressRefined mapping of X-linked reticulate pigmentary disorder and sequencing of candidate genesMutational analysis of Peroxiredoxin IV: exclusion of a positional candidate for multinodular goitre.Specific TATAA and bZIP requirements suggest that HTLV-I Tax has transcriptional activity subsequent to the assembly of an initiation complexFish Peroxiredoxins and Their Role in ImmunityThe high resolution crystal structure of recombinant Crithidia fasciculata tryparedoxin-IThe crystal structure of Mycobacterium tuberculosis alkylhydroperoxidase AhpD, a potential target for antitubercular drug designCrystal structure of a novel human peroxidase enzyme at 2.0 A resolutionLoss of yeast peroxiredoxin Tsa1p induces genome instability through activation of the DNA damage checkpoint and elevation of dNTP levelsMitochondria of Saccharomyces cerevisiae contain one-conserved cysteine type peroxiredoxin with thioredoxin peroxidase activity.Peroxiredoxin-null yeast cells are hypersensitive to oxidative stress and are genomically unstable.ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin.The putative glutathione peroxidase gene of Plasmodium falciparum codes for a thioredoxin peroxidaseTranscriptional regulation of the antioxidant protein 2 gene, a thiol-specific antioxidant, by lens epithelium-derived growth factor to protect cells from oxidative stressHIV-1 antiviral activity of recombinant natural killer cell enhancing factors, NKEF-A and NKEF-B, members of the peroxiredoxin familyInactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acidGlutaredoxin-dependent peroxiredoxin from poplar: protein-protein interaction and catalytic mechanismExpression of peroxiredoxin 1 and 4 promotes human lung cancer malignancyPotential biomarkers for the clinical prognosis of severe dengueProteome changes in human bronchoalveolar cells following styrene exposure indicate involvement of oxidative stress in the molecular-response mechanismThioredoxins, glutaredoxins, and peroxiredoxins--molecular mechanisms and health significance: from cofactors to antioxidants to redox signalingIdentification and characterization of alternatively transcribed form of peroxiredoxin IV gene that is specifically expressed in spermatids of postpubertal mouse testisCloning of the peroxiredoxin gene family in rats and characterization of the fourth memberRat lung peroxiredoxins I and II are differentially regulated during development and by hyperoxiaDifferential cellular and subcellular localization of heme-binding protein 23/peroxiredoxin I and heme oxygenase-1 in rat liverMolecular cloning and characterization of a mitochondrial selenocysteine-containing thioredoxin reductase from rat liverMolecular characterization of a newly identified heme-binding protein induced during differentiation of urine erythroleukemia cellsMice with targeted mutation of peroxiredoxin 6 develop normally but are susceptible to oxidative stressGene expression profiling in hepatic tissue of newly weaned pigs fed pharmacological zinc and phytase supplemented diets.Proteomic analysis of differential protein expression in primary hepatocytes induced by EGF, tumour necrosis factor alpha or the peroxisome proliferator nafenopin.Cyclophilin a binds to peroxiredoxins and activates its peroxidase activity.Nuclear heat shock response and novel nuclear domain 10 reorganization in respiratory syncytial virus-infected a549 cells identified by high-resolution two-dimensional gel electrophoresisAnalysis of NOD2-mediated proteome response to muramyl dipeptide in HEK293 cells.
P2860
Q22010651-44C648B1-A76D-466F-9C94-F8C5F8A92CF8Q22253188-981570DB-11BF-4668-937C-0319E0A28C9DQ22253468-7416C30D-AFBA-44B3-81C0-E6FF27E587F2Q24292492-E9105EDC-F7A4-4216-A165-35B83B8C3C15Q24316248-17B78073-4E28-4D5C-AF18-E5217B1BD3BBQ24337381-0F988B31-E56D-413D-8D54-69AF45B44E2AQ24530195-DEDA383F-EB89-4231-A7FA-B05DDA1C03FDQ24534471-1B93082A-B598-4640-9211-C89A7DA5E025Q24645679-901C0224-84DC-45AD-85B0-9A588B343D37Q24798271-D679F07D-E07C-4CE4-ADB4-E22F7102970AQ24798610-6B63CC32-0601-49DF-8BEE-729FE5BB6583Q26774985-16A0F236-4247-497B-834F-E994FB11F92BQ27619480-4DE70122-46DF-4298-8D8C-E4E88B716C40Q27638528-BDF0E2C7-BADB-4DCB-9C63-7246949462EEQ27757619-B4A007E8-1EFF-406A-9CC5-9BF4DAEF1334Q27936718-CB426935-1224-4F52-AA7A-39EE273E92C0Q27936999-ED5E939D-F653-44E2-9C01-00F5D7222D14Q27939536-758B853D-1ADA-4897-A98D-36F1A3E53F3DQ27939560-30CF91A5-0E9D-4D43-A646-9C138F31F5E3Q27976484-1A621E80-5DBD-4AFD-AFB4-FEA367EF759EQ28202183-6F159392-1C12-47FE-A384-2AA43CED5EB1Q28214202-1B01B2EC-D635-46DB-8C38-E35A1A77A41AQ28216839-1C6FC406-28FB-4C2F-B58F-3AEB70C2C0D3Q28217838-B09717DB-1EAC-4033-A96D-CB182F1C9E23Q28248261-BC1A8C6E-6948-4A88-9AD5-03AEA4E2A9A9Q28298525-E4A26B01-9C61-410C-B2B3-131756CCCAF6Q28389343-D7B8997D-F080-4E79-96E1-D363498BA6F8Q28389739-B727F625-CDC5-4ABA-B474-384852E4018EQ28507042-10C3648E-4325-4BA6-A0B6-289479E9BCE7Q28569349-C78B15FB-57D6-4F73-A6AE-E7BF3E26DA75Q28571347-9A20A14F-3D7B-4A11-8EA1-D0377824E81BQ28576971-43DE2710-B27D-49C4-BAF9-530F6843D688Q28578397-7DABC64B-24FA-4A3E-81C7-59E6AD508B94Q28586057-999F90A0-013F-462A-ACFD-DB797599B60FQ28587822-560D6C7A-93CC-43F3-9F91-D1154E5F09C9Q30847805-DD0C5C77-F7ED-41F9-A5C1-2275CA458F46Q30886686-4D7D6208-2C79-4B59-B257-1B7539B4F41FQ30991292-196AD27A-A622-406A-9732-B9B96EDB1796Q31120475-FB9BDA8C-4A57-44F3-9B08-72240C222DCAQ33226252-5E062B16-5C8C-45E4-82C4-22B72B412866
P2860
Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation
description
1997 nî lūn-bûn
@nan
1997 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation
@ast
Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation
@en
Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation
@en-gb
Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation
@nl
type
label
Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation
@ast
Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation
@en
Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation
@en-gb
Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation
@nl
prefLabel
Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation
@ast
Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation
@en
Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation
@en-gb
Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation
@nl
P2093
P921
P3181
P356
P1476
Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation
@en
P2093
P304
P3181
P356
10.1074/JBC.272.49.30952
P407
P577
1997-12-05T00:00:00Z