Evidence map›Paper›PMID 23734159›Full record

ArticleFrontiers in plant science2013

The barley grain thioredoxin system - an update.

Per Hägglund, Olof Björnberg, Nicolas Navrot, Johanne Mørch Jensen, Kenji Maeda, Kristine Kirkensgaard, Azar Shahpiri, Abida Sultan, Jakob Bunkenborg, Frank Gubler and 4 more

Open access · goldAbstract read
In one paragraph

Article in Frontiers in plant science, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.3field-weighted citation impact, top 37% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed, 9 citations in OpenAlex.

  1. Redox-dependent interaction between thaumatin-like protein and β-glucan influences malting quality of barley.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  2. Article
  3. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

14 authors at 7 institutions in 4 countries.

Per HägglundEnzyme and Protein Chemistry, Department of Systems Biology, Technical University of Denmark Kongens Lyngby, Denmark.
Olof Björnberg
Nicolas Navrot
Johanne Mørch Jensen
Kenji Maeda
Kristine Kirkensgaard
Azar Shahpiri
Abida Sultan
Jakob Bunkenborg
Frank Gubler
José Maria Barrero
Anette Henriksen
Christine Finnie
Birte Svensson
Technical University of Denmark · DKCarlsberg Laboratory · DKCommonwealth Scientific and Industrial Research Organisation · AUInstitut de Biologie Moléculaire des Plantes · FRIsfahan University of Technology · IRPlant Industry · AUUniversity of Southern Denmark · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

cereal proteomicsdisulfide bondNADPH-dependent thioredoxin reductaseredox regulationthioredoxin

Identifiers

PMID23734159
PMCPMC3659290
OpenAlexW2152074773

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.