about
Inhibition of the c-Jun N-terminal kinase/AP-1 and NF-kappaB pathways by PICOT, a novel protein kinase C-interacting protein with a thioredoxin homology domainEnzymatic reduction of disulfide bonds in lysosomes: characterization of a gamma-interferon-inducible lysosomal thiol reductase (GILT)Redox regulation by Nrf2: gatekeeping for the basal and diabetes-induced expression of thioredoxin interacting proteinIdentification of a novel thioredoxin-related transmembrane proteinCharacterization of Sptrx, a novel member of the thioredoxin family specifically expressed in human spermatozoaAn alternative splicing variant of the selenoprotein thioredoxin reductase is a modulator of estrogen signalingIdentification and characterization of TRP14, a thioredoxin-related protein of 14 kDa. New insights into the specificity of thioredoxin functionNovel insight into the mechanism of the vitamin K oxidoreductase (VKOR): electron relay through Cys43 and Cys51 reduces VKOR to allow vitamin K reduction and facilitation of vitamin K-dependent protein carboxylationERp16, an endoplasmic reticulum-resident thiol-disulfide oxidoreductase: biochemical properties and role in apoptosis induced by endoplasmic reticulum stressSalmonella type III secretion effector SlrP is an E3 ubiquitin ligase for mammalian thioredoxinThe genome of Melanoplus sanguinipes entomopoxvirusGamma-carboxyglutamate-containing proteins and the vitamin K-dependent carboxylaseMammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1.The redox state of SECIS binding protein 2 controls its localization and selenocysteine incorporation functionRedox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzymeThree-dimensional structure of a mammalian thioredoxin reductase: implications for mechanism and evolution of a selenocysteine-dependent enzymeATL-derived factor (ADF), an IL-2 receptor/Tac inducer homologous to thioredoxin; possible involvement of dithiol-reduction in the IL-2 receptor inductionBacillithiol is an antioxidant thiol produced in BacilliHow mitochondria produce reactive oxygen speciesT helper cell activation and human retroviral pathogenesisThe blind men 'see' the elephant-the many faces of fatty liver diseaseThe mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coliNuclear magnetic resonance characterization of the N-terminal thioredoxin-like domain of protein disulfide isomeraseThioredoxin and ventricular remodelingStructure and mechanism of mammalian thioredoxin reductase: the active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequenceChlorophyllase is a rate-limiting enzyme in chlorophyll catabolism and is posttranslationally regulatedGenomic organisation and alternative splicing of mouse and human thioredoxin reductase 1 genesRegulating the Intersection of Metabolism and Pathogenesis in Gram-positive BacteriaStaphylococcal response to oxidative stressThioredoxin/Txnip: redoxisome, as a redox switch for the pathogenesis of diseasesRegulation of cell survival and death by pyridine nucleotidesDevelopment of cysteine-free fluorescent proteins for the oxidative environmentAn African swine fever virus ERV1-ALR homologue, 9GL, affects virion maturation and viral growth in macrophages and viral virulence in swineThe high resolution crystal structure of recombinant Crithidia fasciculata tryparedoxin-ICrystal structure of reduced thioredoxin reductase from Escherichia coli: Structural flexibility in the isoalloxazine ring of the flavin adenine dinucleotide cofactorStructures of tryparedoxins revealing interaction with trypanothioneCrystal structure of the wild-type and D30A mutant thioredoxin h of Chlamydomonas reinhardtii and implications for the catalytic mechanismThe crystal structure of Mycobacterium tuberculosis alkylhydroperoxidase AhpD, a potential target for antitubercular drug designCrystal structure of the catalytic domain of a human thioredoxin-like proteinNMR structure of oxidized Escherichia coli glutaredoxin: Comparison with reduced E. coli glutaredoxin and functionally related proteins
P2860
Q22011055-B7DE21C1-CB9A-4021-B2E2-51D1B178154EQ22011094-E24A00E6-3569-40F3-B236-CE0230C53CE4Q23923916-F714B619-6348-44E2-A8A3-E04A76F01CC0Q24290725-B5DAF48E-FA26-46DB-A305-3F3E54581483Q24291314-59651DE1-9792-4C80-AC6D-BF517D55126FQ24297014-C4288382-5A02-4939-B80E-DD881330F0C9Q24299385-1296E170-F442-42C6-A05A-5998EB00897FQ24304387-26335957-F026-404F-BE40-29701D9B8838Q24313474-08934947-1EF8-4C13-AE32-FCCBB36C1E04Q24336442-AB14A65D-A903-41DC-9F36-7A7F315F8E80Q24516950-06305A7A-ED1A-41AF-AED7-1801FA5AACAEQ24527353-27193F80-8516-4E4F-83CC-1356CE0E46EEQ24533236-F3CC3C81-E08C-442B-95FA-3ACD75B971B0Q24548981-338216C9-4DDF-4ACC-A092-2232DB3BB4C7Q24555669-21247558-D79D-403A-8BB5-F7EFE265F90AQ24555780-58FBAAA8-3928-42BF-972E-D7D29D28A4AAQ24567518-22441088-55D1-410A-A615-0655404EEC4BQ24605652-B9A9AF7E-7517-4A2D-9265-7EF2EC5BD97DQ24643882-4C222DE9-F72D-4430-BDEB-CA1EFA5CA269Q24650854-B77E85BA-4955-49CB-B2C2-B3D1EA842DCBQ24654991-1DDC72EE-ACAA-4463-9227-843439E728F6Q24670171-D0E5C4A7-F2E3-4BCF-A429-49F9959CAA2DQ24675311-13214978-0C89-422C-82A9-02E1025F7FF2Q24683258-CA582664-0658-4D4C-B12D-8F6354B308B9Q24683648-2F9DD66D-691D-4EBA-95D1-F4DB59F14074Q24685972-D9B2E0CA-5EB9-4B65-8715-08948E13DC55Q24795742-BDDFC5AA-9F8A-411A-BF83-4CD1BB63F44EQ26799806-BA678C7B-5498-485B-9B47-8C0EAB95CF49Q26991866-637C4835-A225-4C7F-B9DA-7316DD77720AQ27003070-58D59A47-2DB8-4682-A8C4-11C710FDFE51Q27026075-093A84FD-A484-409B-93C4-E63D5379DFDFQ27302354-F21A092D-DF36-41ED-8149-EAB307B420ABQ27469614-3391CD8E-8020-42A3-B0BF-0B9255FDB468Q27619480-909662A7-31E4-460B-946A-95E9AD3D221CQ27620661-E8510194-F829-4FC8-A715-2A257F44D87EQ27631706-76FB6D46-73FB-46CF-BF94-456127C4BEFAQ27634914-740A6343-9007-4780-A836-024AF5A2B307Q27638528-062D7FFE-C02E-4214-A19E-73DA49604C92Q27638927-BA7557B4-90C5-4F05-893C-9ABF4889891EQ27642039-E935F661-3A87-48C5-859A-D2C1041D3782
P2860
description
1985 թուականին հրատարակուած գիտական յօդուած
@hyw
1985 թվականին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1985
@ast
im Januar 1985 veröffentlichter wissenschaftlicher Artikel
@de
scientific article (publication date: 1985)
@en
wetenschappelijk artikel (gepubliceerd in 1985)
@nl
наукова стаття, опублікована в 1985
@uk
مقالة علمية (نشرت عام 1985)
@ar
name
Thioredoxin
@ast
Thioredoxin
@en
type
label
Thioredoxin
@ast
Thioredoxin
@en
prefLabel
Thioredoxin
@ast
Thioredoxin
@en
P3181
P1476
Thioredoxin
@en
P2093
Holmgren A
P304
P3181
P356
10.1146/ANNUREV.BI.54.070185.001321
P407
P577
1985-01-01T00:00:00Z