
Thioredoxin (Trx) reduces disulfide bonds and play numerous important functions in plants. In cereal seeds, cytosolic h-type Trx facilitates the release of energy reserves during the germination process and is recycled by NADPH-dependent Trx reductase. This review presents a summary of the research conducted during the last 10 years to elucidate the structure and function of the barley seed Trx system at the molecular level combined with proteomic approaches to identify target proteins.
Disulfide bond, Plant culture, NADPH-dependent thioredoxin reductase, thioredoxin, Plant Science, Cereal Proteomics, [SDV.BBM.BM] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, SB1-1110, redox regulation, Redox regulation, Cereal proteomics, disulfide bond, Thioredoxin, cereal proteomics, thioredoxin disulfide bond redox regulation NADPH-dependent thioredoxin reductase cereal proteomics H-ISOFORMS PROTEIN RECOGNITION GERMINATING BARLEY STARCHY ENDOSPERM IDENTIFICATION REDUCTION SEEDS ALEURONE HVTRXH2 DISULFIDES
Disulfide bond, Plant culture, NADPH-dependent thioredoxin reductase, thioredoxin, Plant Science, Cereal Proteomics, [SDV.BBM.BM] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, SB1-1110, redox regulation, Redox regulation, Cereal proteomics, disulfide bond, Thioredoxin, cereal proteomics, thioredoxin disulfide bond redox regulation NADPH-dependent thioredoxin reductase cereal proteomics H-ISOFORMS PROTEIN RECOGNITION GERMINATING BARLEY STARCHY ENDOSPERM IDENTIFICATION REDUCTION SEEDS ALEURONE HVTRXH2 DISULFIDES
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