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

Journal of Biological Chemistry

Volumn 277, Issue 50, 2002, Pages 48295-48302

  Borges, Chad R ^a   Geddes, Timothy ^b,c   Watson, J Throck ^a   Kuhn, Donald M ^b,c  

^a Michigan State University   (United States)

^b WAYNE STATE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c VETERANS AFFAIRS MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOSYNTHESIS; CATALYST ACTIVITY; ENZYMES; IMMUNOLOGY; IONIZATION; LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; SULFUR COMPOUNDS; TOXICITY;

NEUROTRANSMITTERS;

BIOCHEMISTRY;

CYSTEINE; DIAMIDE; DITHIOTHREITOL; DOPAMINE; GLUTAREDOXIN; GLUTATHIONE; SULFUR 35; TYROSINE 3 MONOOXYGENASE;

ANIMAL CELL; ARTICLE; BIOSYNTHESIS; CELL STRAIN; CONTROLLED STUDY; DOPAMINERGIC NERVE CELL; DOPAMINERGIC SYSTEM; ENZYME ACTIVITY; NEUROTRANSMISSION; NONHUMAN; PRIORITY JOURNAL; REVERSED PHASE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; TANDEM MASS SPECTROMETRY;

AMINO ACID SEQUENCE; ANIMALS; DIAMIDE; DOPAMINE; GLUTATHIONE; MOLECULAR SEQUENCE DATA; OXIDATIVE STRESS; RATS; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; TYROSINE 3-MONOOXYGENASE;

ANIMALIA;

EID: 2242477521     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M209042200     Document Type: Article

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