Active sites of thioredoxin reductases: Why selenoproteins?

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

Volumn 100, Issue 22, 2003, Pages 12618-12623

  Gromer, Stephan ^a   Johansson, Linda ^b   Bauer, Holger ^a   Arscott, L David ^c   Rauch, Susanne ^a   Ballou, David P ^c   Williams Jr , Charles H ^c   Schirmer, R Heiner ^a   Arnér, Elias S J ^b  

^a UNIVERSITY OF HEIDELBERG   (Germany)

^b KAROLINSKA INSTITUTE   (Sweden)

^c UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; GLYCINE; GLYCYLCYSTEINYLSERYLGLYCINE CARBOXYLIC ACID; ISOENZYME; SELENIUM; SELENOAMINO ACID; SELENOCYSTEINE; SELENOENZYME; SELENOPROTEIN; SERINE; SERYLCYSTEINYLCYSTEINYLSERINE CARBOXYLIC ACID; THIOREDOXIN REDUCTASE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; CARBOXY TERMINAL SEQUENCE; DNA FLANKING REGION; DROSOPHILA MELANOGASTER; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME KINETICS; ENZYMOLOGY; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CLONING, MOLECULAR; DROSOPHILA MELANOGASTER; DROSOPHILA PROTEINS; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEIN SUBUNITS; PROTEINS; RECOMBINANT PROTEINS; SELENIUM; SELENOPROTEINS; THIOREDOXIN REDUCTASE (NADPH);

DROSOPHILA MELANOGASTER; MAMMALIA; MELANOGASTER;

EID: 0242300123     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.2134510100     Document Type: Article

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