Dopamine biosynthesis is regulated by S-glutathionylation. Potential mechanism of tyrosine hydroxylast inhibition during oxidative stress. - Wikidata - awgldk - TriplyDB

Dopamine biosynthesis is regulated by S-glutathionylation. Potential mechanism of tyrosine hydroxylast inhibition during oxidative stress.

Dopamine biosynthesis is regulated by S-glutathionylation. Potential mechanism of tyrosine hydroxylast inhibition during oxidative stress.

http://www.wikidata.org/entity/Q30862475

about

Tyrosine hydroxylase and regulation of dopamine synthesis The role of glutathione S-transferase P in signaling pathways and S-glutathionylation in cancer Mechanisms of altered redox regulation in neurodegenerative diseases--focus on S--glutathionylation The role of free radicals in the aging brain and Parkinson's Disease: convergence and parallelism Vinpocetine and α-tocopherol prevent the increase in DA and oxidative stress induced by 3-NPA in striatum isolated nerve endings Redox regulation of 3'-phosphoadenylylsulfate reductase from Escherichia coli by glutathione and glutaredoxins.Inhibition of caspase-3 activity and activation by protein glutathionylation.Identification of liver proteins and their roles associated with carbon tetrachloride-induced hepatotoxicity.Techniques for the analysis of cysteine sulfhydryls and oxidative protein folding.Why are neurotransmitters neurotoxic? An evolutionary perspective Nitrotyrosine as a marker for peroxynitrite-induced neurotoxicity: the beginning or the end of the end of dopamine neurons?Comparative Proteomic Analysis of Carbonylated Proteins from the Striatum and Cortex of Pesticide-Treated Mice.Acute actions and novel targets of matrix metalloproteinases in the heart and vasculature Redox proteomics: identification and functional role of glutathionylated proteins.Human p53 is inhibited by glutathionylation of cysteines present in the proximal DNA-binding domain during oxidative stress.S-Glutathionylation and Redox Protein Signaling in Drug Addiction.Molecular mechanisms and clinical implications of reversible protein S-glutathionylation.S-glutathionylation of ion channels: insights into the regulation of channel functions, thiol modification crosstalk, and mechanosensing Analytical approaches to the diagnosis and treatment of aging and aging-related disease: redox status and proteomics.Redox Signaling in Neurotransmission and Cognition During Aging.Leaf extract of Rhus verniciflua Stokes protects dopaminergic neuronal cells in a rotenone model of Parkinson's disease.Astaxanthin protects against MPTP/MPP+-induced mitochondrial dysfunction and ROS production in vivo and in vitro.Glutathionylation regulates cytosolic NADP+-dependent isocitrate dehydrogenase activity.Free aminothiols, glutathione redox state and protein mixed disulphides in aging Drosophila melanogaster.Determination of reactive oxygen species associated with the degeneration of dopaminergic neurons during dopamine metabolism.Glutathione s-transferase omega 1-1 is a target of cytokine release inhibitory drugs and may be responsible for their effect on interleukin-1beta posttranslational processing.The sugar-metabolic enzymes aldolase and triose-phosphate isomerase are targets of glutathionylation in Arabidopsis thaliana: detection using biotinylated glutathione.S-glutathionylation decreases Mg2+ inhibition and S-nitrosylation enhances Ca2+ activation of RyR1 channels.A major fraction of endoplasmic reticulum-located glutathione is present as mixed disulfides with protein.Lack of congruence between cysteine dioxygenase activity and S-carboxymethyl-L-cysteine S-oxidation activity in rat cytosol.Dicyclohexylphthalate causes hyperactivity in the rat concomitantly with impairment of tyrosine hydroxylase immunoreactivity.Fetal exposure to 2,3,7,8-tetrachlorodibenzo-p-dioxin transactivates aryl hydrocarbon receptor-responsive element III in the tyrosine hydroxylase immunoreactive neurons of the mouse midbrain.Cardiac sympathetic neuroprotective effect of desipramine in tachycardia-induced cardiomyopathy.Agaricus blazei extract abrogates rotenone-induced dopamine depletion and motor deficits by its anti-oxidative and anti-inflammatory properties in Parkinsonic mice.Melatonin inhibits maneb-induced aggregation of alpha-synuclein in rat pheochromocytoma cells.

P2860

Q21710723-B8895641-C830-4D70-9AA1-0259997CB1F3 Q24603861-297A641B-F2F0-482C-84D6-D8A4F6FDDBE5 Q26830954-7B429D43-2F64-44EA-922C-8E2BD150D65A Q26852148-758186C1-9012-4135-89BA-C2321053659B Q28278543-7B61F937-BC89-40B4-A0F6-9A419B51D3E5 Q31137779-BBD6C928-5EDA-412F-B911-34E8F6B308A0 Q33327210-A0D551C0-C36E-4D82-96EA-F202542BD6D8 Q33765395-83C9C711-163F-41A6-8560-369336EEA7AF Q33828281-307BF395-86C8-4F9B-BF46-61B227720BDE Q34885948-0264D330-6F4E-431D-B99F-EA3C40F40856 Q35746663-5B56A102-75AA-4B41-BCDD-34A30CD2FFFA Q35988085-6A9874C7-7826-4BD7-89F2-717C64DB5A3E Q35995215-D89CBC5D-8A29-46E2-83F2-B5689C01F3D4 Q36168403-8EAF311F-A665-4973-919D-A742C7DFC280 Q36841921-F301449D-E1DD-4673-A799-65F0566790C0 Q36938969-4D871583-9126-4F50-8295-BB5AF7BCE464 Q37262124-E55E9823-55FA-470B-904B-4D356DF0DF3B Q38120049-4961262B-F8E9-4D10-82B1-C4E95554A436 Q38396814-14B467BA-A15B-43E8-B3DF-F5580EF2D218 Q38688126-D4735C83-8061-42C1-AEBF-A344792953E0 Q39478039-193D6D55-263E-4F2F-AD57-414806D8055D Q39634949-E32E9BA5-F2AE-4A40-A449-7073DFBF6C22 Q39871966-A4CD698E-869A-4385-8105-0E676278B7B8 Q41858245-5AE16FE0-AED6-4A1A-BC07-BA76E4505A2E Q43218756-0A0065B1-2FA1-4A11-B742-45ECA250215F Q44353882-AE8CB1D0-8844-456B-ACA9-B200401A159C Q44526033-F76CB08D-8493-4BA9-847F-ECEEACA2D795 Q44550513-B71DA352-5D86-412A-BFC6-851CEA4E32EF Q44664093-EA6669A6-5118-4708-B4B9-259BE1EABD2A Q45001391-3791F113-C443-4183-BDD0-643281D7E9FA Q45067542-86A5C002-21B5-476B-B881-A01872BD44C9 Q45746580-404A3A14-BD0C-445D-92AD-2A3D043A289E Q46743951-4D06659A-A782-4FC8-85B3-F5E33618CC0C Q48257347-E5D1CEEE-2479-44FF-B315-E7594AAF827F Q52576880-22412D3D-B40A-4698-8926-29A60BF81C45

P2860

Dopamine biosynthesis is regulated by S-glutathionylation. Potential mechanism of tyrosine hydroxylast inhibition during oxidative stress.

http://www.wikidata.org/entity/Q30862475

description

2002 nî lūn-bûn

@nan

2002 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի հոտեմբերին 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

Dopamine biosynthesis is regul ...... ition during oxidative stress.

@ast

Dopamine biosynthesis is regul ...... ition during oxidative stress.

@en

type

label

Dopamine biosynthesis is regul ...... ition during oxidative stress.

@ast

Dopamine biosynthesis is regul ...... ition during oxidative stress.

@en

prefLabel

Dopamine biosynthesis is regul ...... ition during oxidative stress.

@ast

Dopamine biosynthesis is regul ...... ition during oxidative stress.

@en

P1433

Q30862475-4932BB20-5829-4C18-865A-3D2861DB5E14

P1476

Q30862475-CE50C643-DA30-4B0E-959B-A9F328AAFC37

P2093

Q30862475-6DCB9D5C-B9C5-48A0-9CB8-75A6DF61B920

Q30862475-6F8C041D-D77C-4D4A-AE7B-C022928A8066

Q30862475-760E2460-5963-4419-BCF4-A8329773336B

Q30862475-CB79DB06-7402-4CE4-9C5F-4005C9C5187C

P2860

Q30862475-0796DE39-23CC-49CE-8C4F-890BD9033452

Q30862475-0A74BFAB-4913-4763-914B-767717E802A4

Q30862475-15026396-468B-4725-B357-B3E9697F90A5

Q30862475-2610FE11-D187-4864-8794-F6B5B88672E4

Q30862475-3B1DA2DB-FC28-4F74-B0D1-5E53598B5788

Q30862475-3F313E42-1079-4E08-BABA-E80B2762481E

Q30862475-47EC14FC-EF82-48DB-AC52-5F7C0093590A

Q30862475-4AB25678-5F96-447F-8E43-20EDDFB258D3

Q30862475-5CD38C3F-6321-46D9-BA91-5BF4332E0A8F

Q30862475-5EB7F25C-BC03-4243-BDEB-179254028986

P304

Q30862475-6E354D89-02DA-4479-A089-A2BCE0F82FD9

P31

Q30862475-3C2FCD4C-0BC0-4FEE-AE61-65174F3B574D

P356

Q30862475-242F8616-CA8C-436A-9413-8A1C0F2D4D3A

P407

Q30862475-B317974E-239A-4BB7-BDEF-43EAF579DCC4

P433

Q30862475-BCF78AB6-AE11-4FC1-B3DA-F45159954EDE

P478

Q30862475-0B86F0C5-BD0A-4F92-8BCE-073C73BE5EE9

P577

Q30862475-42E798E0-E99D-4721-A371-FA9CBD7E8CAE

P5875

Q30862475-60553C12-23F8-4A6D-95D1-C6C2B3D13FAA

P698

Q30862475-F850B7BE-81F5-4FCE-A1E1-5A51B9D67C3B

P921

Q30862475-38f6caf6-b14b-44ee-8f91-0bdd48fecd94

P356

P1433

Journal of Biological Chemistry

P1476

Dopamine biosynthesis is regul ...... ition during oxidative stress.

@en

P2093

Chad R Borges

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

Donald M Kuhn

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

J Throck Watson

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

Timothy Geddes

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

P2860

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Crystal structure of tyrosine hydroxylase at 2.3 A and its implications for inherited neurodegenerative diseases

Rat brain thioltransferase: regional distribution, immunological characterization, and localization by fluorescent in situ hybridization

Regulation of PTP1B via glutathionylation of the active site cysteine 215

The phosphatase activity of carbonic anhydrase III is reversibly regulated by glutathiolation

Activation of matrix metalloproteinases by peroxynitrite-induced protein S-glutathiolation via disulfide S-oxide formation.

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

Dopamine beta-hydroxylase inactivation generates a protein-bound quinone derivative.

Etiology and pathogenesis of Parkinson's disease.

P304

48295-48302

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

P31

scholarly article

P356

10.1074/JBC.M209042200

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

P407

P433

50

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

P478

277

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

P577

2002-10-09T00:00:00Z

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

P5875

11082725

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

P698

12376535

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

P921