Glutathionylation of human thioredoxin: a possible crosstalk between the glutathione and thioredoxin systems - Wikidata - wikimedia - TriplyDB

Glutathionylation of human thioredoxin: a possible crosstalk between the glutathione and thioredoxin systems

Glutathionylation of human thioredoxin: a possible crosstalk between the glutathione and thioredoxin systems

http://www.wikidata.org/entity/Q31096762

about

Reactivation of oxidized PTP1B and PTEN by thioredoxin 1 Thioredoxin and ventricular remodeling Mechanisms of altered redox regulation in neurodegenerative diseases--focus on S--glutathionylation Glutathione and mitochondria Mitochondrial glutathione: features, regulation and role in disease Mitochondria: Much ado about nothing? How dangerous is reactive oxygen species production?Gene expression changes for antioxidants pathways in the mouse cochlea: relations to age-related hearing deficits.Thioredoxin-dependent enzymatic activation of mercaptopyruvate sulfurtransferase. An intersubunit disulfide bond serves as a redox switch for activation Glutaredoxin modulates platelet-derived growth factor-dependent cell signaling by regulating the redox status of low molecular weight protein-tyrosine phosphatase From structure to redox: The diverse functional roles of disulfides and implications in disease.S-glutathionylation: from molecular mechanisms to health outcomes Redox proteomics in selected neurodegenerative disorders: from its infancy to future applications.Dopamine biosynthesis is regulated by S-glutathionylation. Potential mechanism of tyrosine hydroxylast inhibition during oxidative stress.Redox regulation of 3'-phosphoadenylylsulfate reductase from Escherichia coli by glutathione and glutaredoxins.Protein disulfide bond formation in the cytoplasm during oxidative stress.The thioredoxin-independent isoform of chloroplastic glyceraldehyde-3-phosphate dehydrogenase is selectively regulated by glutathionylation.Glutathionylation of trypanosomal thiol redox proteins.The redox sensor TXNL1 plays a regulatory role in fluid phase endocytosis.Inhibition of caspase-3 activity and activation by protein glutathionylation.Identification of human thioredoxin as a novel IFN-gamma-induced factor: mechanism of induction and its role in cytokine production.Thiol-metabolizing proteins and endothelial redox state: differential modulation of eNOS and biopterin pathways.Effects of age and caloric restriction on glutathione redox state in mice.Redox-regulated chaperones.Pulmonary endothelial cell NOX Distinction of thioredoxin transnitrosylation and denitrosylation target proteins by the ICAT quantitative approach.Methodological aspects of ELISA analysis of thioredoxin 1 in human plasma and cerebrospinal fluid.Thioredoxin glycation: A novel posttranslational modification that inhibits its antioxidant and organ protective actions Redox systems of the cell: possible links and implications.Methylglyoxal increases cardiomyocyte ischemia-reperfusion injury via glycative inhibition of thioredoxin activity.Glutathionylation of chloroplast thioredoxin f is a redox signaling mechanism in plants.Thioredoxin regulates multiple hydrogen peroxide-induced signaling pathways in Candida albicans.Glutathione--functions and metabolism in the malarial parasite Plasmodium falciparum.Glutathione-dependent reductive stress triggers mitochondrial oxidation and cytotoxicity Inhibition of endogenous thioredoxin in the heart increases oxidative stress and cardiac hypertrophy.Lymphocyte surface thiol levels.S-glutathionylation enhances human cystathionine β-synthase activity under oxidative stress conditions.Thiol/disulfide redox states in signaling and sensing Sidechain biology and the immunogenicity of PDC-E2, the major autoantigen of primary biliary cirrhosis.Thioredoxin 1-mediated post-translational modifications: reduction, transnitrosylation, denitrosylation, and related proteomics methodologies.GSHSite: exploiting an iteratively statistical method to identify s-glutathionylation sites with substrate specificity

P2860

Q24300000-7477FE41-8372-491E-9855-0312BA7581C6 Q24683258-BF6768AF-CE58-4037-B87A-2672C95185F1 Q26830954-DB2EB6CB-F1B9-4B6B-88E9-FCC875BD0030 Q26865589-F0048958-D1C6-4505-8277-F98AD61EB871 Q27026521-4A381707-6D8C-4325-B0D2-DDB964443D0E Q28084963-2612252F-B40C-4ED8-B297-B5FBC165C056 Q28396740-B4A640AD-408C-4681-953F-BEF2E3270AFF Q28567305-AB396C71-2A8B-48D6-B4BB-2BD6A57BEC46 Q28580369-0876F150-DC8A-4634-8A2B-800707F987E1 Q30397007-A35B4116-96B1-4FC9-B6D7-58295DD5B507 Q30398587-CD7DA7CA-8144-4460-B041-DCE3828A1090 Q30446460-6F468972-EAFB-451A-B4C7-E34D8A5A26CA Q30862475-752E5E50-17A7-4AD0-86CC-809F93F754B8 Q31137779-303F01BC-550B-460A-ABEB-E45C7C2D3D10 Q33199830-5D127C5C-1F1E-49C7-BC41-264B0D43889F Q33265224-528283A4-2D35-42DB-A836-242724ADE0B8 Q33270008-8C415D4A-1508-4DDB-994D-71D17D1DEF52 Q33305213-374EE462-E306-4BFF-A0FB-B49B68AB733E Q33327210-8D6999D2-3A64-4A78-A61B-02B3BB6046C4 Q33382549-9275985A-E515-4280-8A11-B63C0A8A563B Q33589215-7514D7B1-81C3-4A39-823C-A3ABF5F51A43 Q33721622-E094B5F6-9FE4-4804-A5B7-926A5F182FFF Q33766707-B5B5E340-4168-4DE6-A128-068664467FD4 Q33769358-D11572CF-4B11-4134-9C35-E8C061CA2210 Q33942934-061CF150-7911-4C05-ACBF-CFFA322AC5CF Q33975493-990098CC-B714-4B41-9AA8-2219D5CABCDF Q33976920-08F5F41B-6C10-4CE1-8C2A-90186637EA12 Q34074762-9214CECD-C1C3-4BEC-B2BF-D351284A1174 Q34085212-C5E494BE-3858-4994-AB53-8356C4CD12B0 Q34132326-DF583511-E411-4746-8138-2418AF0A9FFA Q34178020-40F7A4C9-5F37-44BD-8D22-139D2D207693 Q34197581-0C38CFE5-765D-4DAA-BE38-BEF529F28F4B Q34243279-48900B5F-E26C-4184-9C74-1BBB94F5E5E9 Q34274405-6B51DC59-3E6E-44F7-BEE1-F30A31AB5C6A Q34920137-914A82AF-1F01-4CA0-B6C8-8ACE5DB24459 Q35015674-00C9E92D-EDB1-4593-8431-C2F88DF542E9 Q35069234-B06911DB-596A-4B27-9346-26BA045DA00C Q35119479-06FCFBD3-08CF-4577-9BF6-0E93C9CC803F Q35222209-30EFDA9D-B4FB-492E-930D-84C86C083FDD Q35304226-A50BAB09-A3EF-4A89-8F34-E9C03042CE14

P2860

Glutathionylation of human thioredoxin: a possible crosstalk between the glutathione and thioredoxin systems

http://www.wikidata.org/entity/Q31096762

description

2002 nî lūn-bûn

@nan

2002 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2002年の論文

@ja

2002年論文

@yue

2002年論文

@zh-hant

2002年論文

@zh-hk

2002年論文

@zh-mo

2002年論文

@zh-tw

2002年论文

@wuu

name

Glutathionylation of human thi ...... thione and thioredoxin systems

@ast

Glutathionylation of human thi ...... thione and thioredoxin systems

@en

type

label

Glutathionylation of human thi ...... thione and thioredoxin systems

@ast

Glutathionylation of human thi ...... thione and thioredoxin systems

@en

prefLabel

Glutathionylation of human thi ...... thione and thioredoxin systems

@ast

Glutathionylation of human thi ...... thione and thioredoxin systems

@en

P1433

Q31096762-0E433D68-76DA-4015-8B99-85CB85735FCE

P1476

Q31096762-9ECC21ED-5C9B-4D91-A339-4B4D478A070C

P2093

Q31096762-827F805E-2A64-48C4-B43F-F109F8C8EEF2

Q31096762-CC72809D-7D9F-463B-9609-8405597CDA89

Q31096762-D0ED0FF1-FACC-4095-8484-D0DB04B1A278

Q31096762-D7996743-E63E-4563-940A-483E123F4073

Q31096762-DFBDAC5A-D178-43FE-A72A-8C4A70C4DA31

P2860

Q31096762-010D9A69-51D6-4FFA-BDCE-316D811F8B5F

Q31096762-02C898CC-BFF9-482E-95DC-9EDB5F9863BB

Q31096762-0F65F309-6A31-442C-977A-9315804C15B2

Q31096762-1875AB1A-17A0-4448-95A5-61287AA0AA0B

Q31096762-1D628BF9-AEBF-494D-B722-AC05854B988D

Q31096762-2371187C-106F-4FE7-B609-EFB0E2CCED0C

Q31096762-445F08EA-86A0-43F9-A7D6-6A5C6F92F8C7

Q31096762-4893A0F9-BD44-45FA-99AF-C4A8CC51451A

Q31096762-50565AF9-6605-485D-ADF9-0F4B9AFDC163

Q31096762-58448613-F344-4EC7-ABE0-5EFD066F2E43

P304

Q31096762-644E3B95-D487-4AB3-BDAB-96FCAC02CEDA

P31

Q31096762-8BF516F7-29C6-4C32-A90E-B4C660C9D3AF

P356

Q31096762-D8A33E86-7389-4A05-863D-4557AB4B0818

P407

Q31096762-A07B73EA-C7B4-4713-A160-DE38EF8AE51A

P433

Q31096762-AAEFBCDF-52F5-43B4-9977-F39E21CCF377

P478

Q31096762-645C3CE2-1A30-42F5-BAFD-C0FE12E0DA69

P50

Q31096762-2395EF11-01CD-4B87-9063-CF5A935328A1

Q31096762-3B86E85E-CB01-496F-9668-DADAD7C4BA13

Q31096762-B8F058E9-531A-4596-8729-C8D40B2D9F1D

Q31096762-DDFC6ADD-F1B3-42AF-B15B-C54A4A62D1F5

Q31096762-F3FEEDA9-AF35-4EC1-AB38-251497B46F1B

P577

Q31096762-BB37F5D9-EBA7-4EAE-BEA1-587EAFC5D8BD

P5875

Q31096762-53394934-88DC-4728-83A4-3C3CF8B43C47

P698

Q31096762-A990A15D-A640-41F9-9075-A2E163E7C415

P932

Q31096762-42757620-1F78-44E8-8ED7-EBAE1C398F58

P356

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Glutathionylation of human thi ...... thione and thioredoxin systems

@en

P2093

Elisabetta Gianazza

http://www.w3.org/2001/XMLSchema#string

Geng Chang

http://www.w3.org/2001/XMLSchema#string

Ivano Eberini

http://www.w3.org/2001/XMLSchema#string

Simona Casagrande

http://www.w3.org/2001/XMLSchema#string

Tania Massignan

http://www.w3.org/2001/XMLSchema#string

P2860

Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1.

Structure and mechanism of mammalian thioredoxin reductase: the active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Crystal structure of S-glutathiolated carbonic anhydrase III

Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer

Thioredoxin and glutaredoxin systems

Physiological functions of thioredoxin and thioredoxin reductase

Oxidized redox state of glutathione in the endoplasmic reticulum

Glutathiolation of proteins by glutathione disulfide S-oxide derived from S-nitrosoglutathione. Modifications of rat brain neurogranin/RC3 and neuromodulin/GAP-43.

P304

9745-9749

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1073/PNAS.152168599

http://www.w3.org/2001/XMLSchema#string

P407

P433

15

http://www.w3.org/2001/XMLSchema#string

P478

99

http://www.w3.org/2001/XMLSchema#string

P50

Valentina Bonetto

Maddalena Fratelli

P577

2002-07-15T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

11260247

http://www.w3.org/2001/XMLSchema#string

P698

12119401

http://www.w3.org/2001/XMLSchema#string

P932

125000

http://www.w3.org/2001/XMLSchema#string