Evidence map›Paper›PMID 28808108›Full record

ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2017

Chloroplast thioredoxin systems: prospects for improving photosynthesis.

Lauri Nikkanen, Jouni Toivola, Manuel Guinea Diaz, Eevi Rintamäki

Open access · hybridAbstract readReview
In one paragraph

Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

24 citing papers in PubMed, 54 citations in OpenAlex.

  1. Review
  2. Article
  3. Universal Stress Proteins: From Gene to Function.International journal of molecular sciences · 2023
    Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Crystal Structure of Chloroplastic Thioredoxin f2 fromAntioxidants (Basel, Switzerland) · 2018
    Article
  19. Article
  20. Review
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

4 authors at 1 institution in 2 countries.

Lauri NikkanenMolecular Plant Biology, Department of Biochemistry, University of Turku, 20014 Turku, Finland.
Jouni ToivolaMolecular Plant Biology, Department of Biochemistry, University of Turku, 20014 Turku, Finland.
Manuel Guinea DiazMolecular Plant Biology, Department of Biochemistry, University of Turku, 20014 Turku, Finland.
Eevi RintamäkiMolecular Plant Biology, Department of Biochemistry, University of Turku, 20014 Turku, Finland evirin@utu.fi.ORCID http://orcid.org/0000-0002-1353-3995
Google (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Thioredoxins (TRXs) are protein oxidoreductases that control the structure and function of cellular proteins by cleavage of a disulphide bond between the side chains of two cysteine residues. Oxidized thioredoxins are reactivated by thioredoxin reductases (TR) and a TR-dependent reduction of TRXs is called a thioredoxin system. Thiol-based redox regulation is an especially important mechanism to control chloroplast proteins involved in biogenesis, in regulation of light harvesting and distribution of light energy between photosystems, in photosynthetic carbon fixation and other biosynthetic pathways, and in stress responses of plants. Of the two plant plastid thioredoxin systems, the ferredoxin-dependent system relays reducing equivalents from photosystem I via ferredoxin and ferredoxin-thioredoxin reductase (FTR) to chloroplast proteins, while NADPH-dependent thioredoxin reductase (NTRC) forms a complete thioredoxin system including both reductase and thioredoxin domains in a single polypeptide. Chloroplast thioredoxins transmit environmental light signals to biochemical reactions, which allows fine tuning of photosynthetic processes in response to changing environmental conditions. In this paper we focus on the recent reports on specificity and networking of chloroplast thioredoxin systems and evaluate the prospect of improving photosynthetic performance by modifying the activity of thiol regulators in plants.This article is part of the themed issue 'Enhancing photosynthesis in crop plants: targets for improvement'.

Indexed as

ArabidopsisArabidopsis ProteinsChloroplast ThioredoxinsCrops, AgriculturalPhotosynthesisArabidopsis ProteinsChloroplast ThioredoxinsCalvin–Benson cycleFTRlight reactionsNTRCredox regulationthioredoxin reductase

Identifiers

PMID28808108
PMCPMC5566889
OpenAlexW2749172067

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.