title: The barley grain thioredoxin system - an update.
abstract: 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.
authors.affiliation: Enzyme and Protein Chemistry, Department of Systems Biology, Technical University of Denmark Kongens Lyngby, Denmark.
authors.forename: Per
authors.initials: P
authors.lastname: Hägglund
authors.forename: Olof
authors.initials: O
authors.lastname: Björnberg
authors.forename: Nicolas
authors.initials: N
authors.lastname: Navrot
authors.forename: Johanne
authors.initials: J
authors.lastname: Mørch Jensen
authors.forename: Kenji
authors.initials: K
authors.lastname: Maeda
authors.forename: Kristine
authors.initials: K
authors.lastname: Kirkensgaard
authors.forename: Azar
authors.initials: A
authors.lastname: Shahpiri
authors.forename: Abida
authors.initials: A
authors.lastname: Sultan
authors.forename: Jakob
authors.initials: J
authors.lastname: Bunkenborg
authors.forename: Frank
authors.initials: F
authors.lastname: Gubler
authors.forename: José Maria
authors.initials: JM
authors.lastname: Barrero
authors.forename: Anette
authors.initials: A
authors.lastname: Henriksen
authors.forename: Christine
authors.initials: C
authors.lastname: Finnie
authors.forename: Birte
authors.initials: B
authors.lastname: Svensson
keywords: NADPH-dependent thioredoxin reductase; cereal proteomics; disulfide bond; redox regulation; thioredoxin