The barley grain thioredoxin system – an update

The barley grain thioredoxin system – an update

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...

Full description

Bibliographic Details
Main Authors: Hägglund, Per, Björnberg, Olof, Navrot, Nicolas, Mørch Jensen, Johanne, Maeda, Kenji, Kirkensgaard, Kristine, Shahpiri, Azar, Sultan, Abida, Bunkenborg, Jakob, Gubler, Frank, Barrero, José Maria, Henriksen, Anette, Finnie, Christine, Svensson, Birte
Format: Online
Language:English
Published: Frontiers Media S.A. 2013
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3659290/
id pubmed-3659290
recordtype oai_dc
spelling pubmed-36592902013-06-03 The barley grain thioredoxin system – an update Hägglund, Per Björnberg, Olof Navrot, Nicolas Mørch Jensen, Johanne Maeda, Kenji Kirkensgaard, Kristine Shahpiri, Azar Sultan, Abida Bunkenborg, Jakob Gubler, Frank Barrero, José Maria Henriksen, Anette Finnie, Christine Svensson, Birte Plant Science 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. Frontiers Media S.A. 2013-05-21 /pmc/articles/PMC3659290/ /pubmed/23734159 http://dx.doi.org/10.3389/fpls.2013.00151 Text en Copyright © Hägglund, Björnberg, Navrot, Mørch Jensen, Maeda, Kirkensgaard, Shahpiri, Sultan, Bunkenborg, Gubler, Barrero, Henriksen, Finnie and Svensson. http://creativecommons.org/licenses/by/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in other forums, provided the original authors and source are credited and subject to any copyright notices concerning any third-party graphics etc.
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Hägglund, Per
Björnberg, Olof
Navrot, Nicolas
Mørch Jensen, Johanne
Maeda, Kenji
Kirkensgaard, Kristine
Shahpiri, Azar
Sultan, Abida
Bunkenborg, Jakob
Gubler, Frank
Barrero, José Maria
Henriksen, Anette
Finnie, Christine
Svensson, Birte
spellingShingle Hägglund, Per
Björnberg, Olof
Navrot, Nicolas
Mørch Jensen, Johanne
Maeda, Kenji
Kirkensgaard, Kristine
Shahpiri, Azar
Sultan, Abida
Bunkenborg, Jakob
Gubler, Frank
Barrero, José Maria
Henriksen, Anette
Finnie, Christine
Svensson, Birte
The barley grain thioredoxin system – an update
author_facet Hägglund, Per
Björnberg, Olof
Navrot, Nicolas
Mørch Jensen, Johanne
Maeda, Kenji
Kirkensgaard, Kristine
Shahpiri, Azar
Sultan, Abida
Bunkenborg, Jakob
Gubler, Frank
Barrero, José Maria
Henriksen, Anette
Finnie, Christine
Svensson, Birte
author_sort Hägglund, Per
title The barley grain thioredoxin system – an update
title_short The barley grain thioredoxin system – an update
title_full The barley grain thioredoxin system – an update
title_fullStr The barley grain thioredoxin system – an update
title_full_unstemmed The barley grain thioredoxin system – an update
title_sort barley grain thioredoxin system – an update
description 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.
publisher Frontiers Media S.A.
publishDate 2013
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3659290/
_version_ 1611979549842604032

Similar Items