Glutathionylation of chloroplast thioredoxin f is a redox signaling mechanism in plants

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

Volumn 102, Issue 45, 2005, Pages 16478-16483

  Michelet, Laure ^a   Zaffagnini, Mirko ^a,b   Marchand, Christophe ^a   Collin, Valérie ^a   Decottignies, Paulette ^a   Tsan, Pascale ^c   Lancelin, Jean Marc ^c   Trost, Paolo ^b   Miginiac Maslow, Myroslawa ^a   Noctor, Graham ^a   Lemaire, Stéphane D ^a  

^a CNRS   (France)

^b UNIVERSITY OF BOLOGNA   (Italy)

^c UNIVERSITÉ LYON 1   (France)

Author keywords

Arabidopsis; Calvin cycle; Chlamydomonas; Enzyme light activation; Thiol

Indexed keywords

BUFFER; CYSTEINE; FERREDOXIN; THIOL DERIVATIVE; THIOREDOXIN F; THIOREDOXIN REDUCTASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARABIDOPSIS; ARTICLE; CARBON FIXATION; CHLAMYDOMONAS; CHLOROPLAST; ENZYME ACTIVATION; ENZYME ACTIVE SITE; GLUTATHIONYLATION; LIGHT EXPOSURE; NONHUMAN; OXIDATION REDUCTION REACTION; PLANT; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN MODIFICATION; PROTEIN PROCESSING; STRESS; THYLAKOID;

ANIMALS; ARABIDOPSIS; CHLAMYDOMONAS; CHLOROPLASTS; GLUTATHIONE; MALATE DEHYDROGENASE; MODELS, MOLECULAR; NADP; OXIDATION-REDUCTION; PLANTS; SIGNAL TRANSDUCTION; THIOREDOXIN;

ARABIDOPSIS; CHLAMYDOMONAS; MAMMALIA;

EID: 28044438233     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0507498102     Document Type: Article

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