Ebselen: a substrate for human thioredoxin reductase strongly stimulating its hydroperoxide reductase activity and a superfast thioredoxin oxidant - Wikidata - awgldk - TriplyDB

Ebselen: a substrate for human thioredoxin reductase strongly stimulating its hydroperoxide reductase activity and a superfast thioredoxin oxidant

Ebselen: a substrate for human thioredoxin reductase strongly stimulating its hydroperoxide reductase activity and a superfast thioredoxin oxidant

http://www.wikidata.org/entity/Q34065084

about

The redox state of SECIS binding protein 2 controls its localization and selenocysteine incorporation function Pharmacology of iron transport Inhibitors of the Hydrolytic Enzyme Dimethylarginine Dimethylaminohydrolase (DDAH): Discovery, Synthesis and Development Oxidative stress in MeHg-induced neurotoxicity Improved tricyclic inhibitors of trypanothione reductase by screening and chemical synthesis.Developing selective histone deacetylases (HDACs) inhibitors through ebselen and analogs.The selenium-independent inherent pro-oxidant NADPH oxidase activity of mammalian thioredoxin reductase and its selenium-dependent direct peroxidase activities.Mitochondrial dysfunction induced by different organochalchogens is mediated by thiol oxidation and is not dependent of the classical mitochondrial permeability transition pore opening.Post-transcriptional defects of antioxidant selenoenzymes cause oxidative stress under methylmercury exposure.Enhancement of auranofin-induced apoptosis in MCF-7 human breast cells by selenocystine, a synergistic inhibitor of thioredoxin reductase.Screening for dimethylarginine dimethylaminohydrolase inhibitors reveals ebselen as a bioavailable inactivator Drosophila melanogaster - an embryonic model for studying behavioral and biochemical effects of manganese exposure.High-throughput screening using the differential radial capillary action of ligand assay identifies ebselen as an inhibitor of diguanylate cyclases.High-throughput screen identifies novel inhibitors of cancer biomarker α-methylacyl coenzyme A racemase (AMACR/P504S)Small-molecule screening identifies the selanazal drug ebselen as a potent inhibitor of DMT1-mediated iron uptake.Thioredoxin reductase-1 negatively regulates HIV-1 transactivating protein Tat-dependent transcription in human macrophages Apocynin and Nox2 regulate NF-κB by modifying thioredoxin-1 redox-state.Organochalcogens inhibit mitochondrial complexes I and II in rat brain: possible implications for neurotoxicity.Toxicology and pharmacology of selenium: emphasis on synthetic organoselenium compounds.Association of oxidative stress to the genesis of anxiety: implications for possible therapeutic interventions Ebselen, a promising antioxidant drug: mechanisms of action and targets of biological pathways.Thioredoxin reductase and its inhibitors.Nanomedicine in the ROS-mediated pathophysiology: Applications and clinical advances.Selected ebselen analogs reduce mechlorethamine toxicity in vitro.Challenges in searching for therapeutics against Botulinum Neurotoxins.Glutathione and glutaredoxin act as a backup of human thioredoxin reductase 1 to reduce thioredoxin 1 preventing cell death by aurothioglucose.Synchrotron radiation induced X-ray emission studies of the antioxidant mechanism of the organoselenium drug ebselen.Thioredoxin reductase 1 ablation sensitizes colon cancer cells to methylseleninate-mediated cytotoxicity.Endogenous and exogenous pathways maintain the reductive capacity of the phagosome.Ebselen induced C6 glioma cell death in oxygen and glucose deprivation.Redox Nanodomains Are Induced by and Control Calcium Signaling at the ER-Mitochondrial Interface.Convergent Synthesis of Two Fluorescent Ebselen-Coumarin Heterodimers Ebsulfur is a benzisothiazolone cytocidal inhibitor targeting the trypanothione reductase of Trypanosoma brucei.Anti-Inflammatory Thioredoxin Family Proteins for Medicare, Healthcare and Aging Care.Induction of apoptosis in human multiple myeloma cell lines by ebselen via enhancing the endogenous reactive oxygen species production.Catalytic oxidant scavenging by selenium-containing compounds: Reduction of selenoxides and N-chloramines by thiols and redox enzymes.Thioredoxin 1 is inactivated due to oxidation induced by peroxiredoxin under oxidative stress and reactivated by the glutaredoxin system.Influence of heme and heme oxygenase-1 transfection of pulmonary microvascular endothelium on oxidant generation and cGMP.2-Methoxyestradiol induces apoptosis in Ewing sarcoma cells through mitochondrial hydrogen peroxide production.Interactions of quinones with thioredoxin reductase: a challenge to the antioxidant role of the mammalian selenoprotein.

P2860

Q24548981-2D506A60-5318-4695-A07F-830438497066 Q27009387-0F5F6450-1274-4AEB-8D41-54D3E7ADD450 Q28070134-3752DD6C-FA76-42E7-972B-366CA5637768 Q28391544-967BDE2A-A060-49C1-A4E2-A23223E22178 Q33474992-7AA95301-FC3D-4219-BADD-61B1AC870FD0 Q33649853-22AA1983-DD3A-46E0-9CFF-3BAB99BAFC11 Q33967269-B1EFE3DD-7217-4956-A862-229970032ED0 Q34072010-FFEF584B-1FD6-4019-86C7-B309F07BA797 Q34151717-9240EDDF-CA6C-4E37-A0A4-88F990F2D6CB Q34558945-9DFFCD7B-B0BE-4030-A148-F4982DF9CC12 Q35209771-6236A077-0967-4DC3-8060-800FC0CE240F Q35728801-B5A8FFD5-E0E3-4D1A-AC46-5FACA49821CF Q35984313-99B07E9B-2179-4E91-B329-39B2893ADAEE Q36176367-78FB61E8-AE36-4F27-A2BD-BC15D953F737 Q36890133-38E4B70E-F8B0-438E-82E3-0A299BDDE402 Q36980967-B2FE493A-E1F5-4DD5-82D1-556E0827016F Q37307363-A3F47BD8-F51F-44BA-AE5F-A9CED4CD0041 Q37601925-0C339419-8FF5-45E5-9667-781107FE8F60 Q37896536-FA90B172-58B6-4798-AFBF-2F162CCCA5E9 Q38199486-BE31AF8B-0ABE-44A8-A6AD-B21C7816FA26 Q38215395-3EA7A29A-5212-4E7A-ADC8-FDB80042CC61 Q38215943-67C09A0A-4E4E-4596-9506-18ACE33D4309 Q38563026-34F05D71-95D2-4F0D-A7AF-41066031BF95 Q39144076-5046A3A2-536B-4A7F-9174-6FEF06B5508A Q39167871-F6410D49-38FD-4D88-AEC2-772F4B32C28C Q39278850-34C9691C-096F-406D-8419-965318FD2F32 Q39397685-5C03098A-6FEF-4834-A74A-D4BAAF63C2B8 Q39794894-74B21904-2D8A-46D8-BBFA-B0E673EF4AB4 Q40165086-11FCCF5F-5E38-4FDC-BAC0-EFFE80226462 Q40280651-2E0BD2AE-8328-4E7E-8C23-86F52B993E50 Q41140084-C0562113-467D-43DA-84D0-C0D7E7B06146 Q41202070-5C160BC4-8A18-48C0-8896-95633DC62A94 Q41813592-071FE470-2E9D-491E-AC14-781F05577FD3 Q41928061-DCA32767-EA4C-4866-AF3E-F9516DC709F7 Q41949390-BDEDFE15-B879-4304-A040-AF71965D7C72 Q41971945-FD38CF89-CA58-402B-9856-3A4F1DE31982 Q42917752-76B03BB8-665F-4913-97CE-E75B12DC30D5 Q44413017-E8C6BD96-95E5-41B7-AB28-EA0031779EEA Q44429627-8EAE6EC8-385E-4356-BCDC-2C59B8D8C9D3 Q44646961-9C979235-F704-40B6-8131-3FB9C5F827BB

P2860

Ebselen: a substrate for human thioredoxin reductase strongly stimulating its hydroperoxide reductase activity and a superfast thioredoxin oxidant

http://www.wikidata.org/entity/Q34065084

description

2002 nî lūn-bûn

@nan

2002 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի հունիսին 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

Ebselen: a substrate for human ...... superfast thioredoxin oxidant

@ast

Ebselen: a substrate for human ...... superfast thioredoxin oxidant

@en

Ebselen: a substrate for human ...... superfast thioredoxin oxidant

@nl

type

label

Ebselen: a substrate for human ...... superfast thioredoxin oxidant

@ast

Ebselen: a substrate for human ...... superfast thioredoxin oxidant

@en

Ebselen: a substrate for human ...... superfast thioredoxin oxidant

@nl

prefLabel

Ebselen: a substrate for human ...... superfast thioredoxin oxidant

@ast

Ebselen: a substrate for human ...... superfast thioredoxin oxidant

@en

Ebselen: a substrate for human ...... superfast thioredoxin oxidant

@nl

P1433

Q34065084-D7EA3EF2-B557-4300-960C-1E102F0E94A1

P1476

Q34065084-0B13A014-3C4D-44AC-A196-A0136F549896

P2093

Q34065084-0532CD7A-8CD6-4DCA-A344-75BA8166E24F

Q34065084-A86FE2E9-C565-44F0-BBA6-E0F5485A880E

P2860

Q34065084-09A647E8-341E-4F94-ACEE-973E8664CB5B

Q34065084-0FB837A2-2919-4435-839A-44DE21969BCD

Q34065084-1E8E330C-3B0D-44A4-A14E-0DED1D611E4E

Q34065084-1F655258-6A4F-40D4-BA6E-FB8C12EB9B5E

Q34065084-264CE536-06B4-45C3-BB55-05BF1CED00DA

Q34065084-4D05EA46-80AA-4BBB-BCC7-74C33784F9E1

Q34065084-53A3C043-8DC4-42D4-A9A7-FDF686393A27

Q34065084-5CEBDEA0-9E29-4AC2-BE38-CF19ABD470AF

Q34065084-5D213375-5D5A-49BA-B12B-7C970A148742

Q34065084-639CD089-42DB-4FB6-84A9-D1A7E6A7A020

P304

Q34065084-1D08229E-781D-4CB3-89B0-8A90B443C283

P31

Q34065084-4756B5A0-F8AA-4CDC-82FA-BA607990DA3B

P356

Q34065084-748033FC-892F-4B58-B7CF-1E3E65BE38A7

P407

Q34065084-3EC3B81F-DED2-4AA5-90D4-71A7ACD1640A

P433

Q34065084-FF8CB3B7-3048-445D-A132-56A7E8AF8382

P478

Q34065084-912AED57-55AD-4A29-8064-412C5F2DB35F

P50

Q34065084-1C839F79-396D-4EE0-8F67-D15537FAFD80

P577

Q34065084-889D35FD-5E7D-4D41-9B55-F9E8237E622E

P5875

Q34065084-32462D62-8D79-4818-BFF5-3C3E603E50F0

P698

Q34065084-710B5CDD-7EEC-488B-AFCA-2AB057D15977

P932

Q34065084-BFDCC43C-6106-4572-A9F3-0BA72441C923

P356

P1433

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

P1476

Ebselen: a substrate for human ...... superfast thioredoxin oxidant

@en

P2093

Hiroyuki Masayasu

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

Rong Zhao

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

P2860

Three-dimensional structure of a mammalian thioredoxin reductase: implications for mechanism and evolution of a selenocysteine-dependent enzyme

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

Ebselen in acute ischemic stroke: a placebo-controlled, double-blind clinical trial. Ebselen Study Group

Thioredoxin and glutaredoxin systems

Molecular actions of ebselen--an antiinflammatory antioxidant

Molecular cloning and characterization of a mitochondrial selenocysteine-containing thioredoxin reductase from rat liver

Cloning and expression of a novel mammalian thioredoxin

Essential role of selenium in the catalytic activities of mammalian thioredoxin reductase revealed by characterization of recombinant enzymes with selenocysteine mutations

Selenite is a substrate for calf thymus thioredoxin reductase and thioredoxin and elicits a large non-stoichiometric oxidation of NADPH in the presence of oxygen

Selenodiglutathione is a highly efficient oxidant of reduced thioredoxin and a substrate for mammalian thioredoxin reductase

P304

8579-8584

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

P31

scholarly article

P356

10.1073/PNAS.122061399

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

P407

P433

13

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

P478

99

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

P50

P577

2002-06-17T00:00:00Z

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

P5875

11305042

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

P698

12070343

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

P932

124318

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