Evidence map›Paper›PMID 31597700›Full record

ArticleThe Journal of biological chemistry2019

Impact of key residues within chloroplast thioredoxin-

Yuichi Yokochi, Kazunori Sugiura, Kazuhiro Takemura, Keisuke Yoshida, Satoshi Hara, Ken-Ichi Wakabayashi, Akio Kitao, Toru Hisabori

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

19 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Systematic determination of disulfide bond reduction potentials reveals a nonequilibrium redox hierarchy in cyanobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Article
  5. Functional recoding ofFrontiers in plant science · 2025
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. In vivo oxidation by thioredoxin regulates chloroplast enzyme activity.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  14. Article
  15. Oxidative regulation of chloroplast enzymes by thioredoxin and thioredoxin-like proteins inProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  16. Redox regulation of NADP-malate dehydrogenase is vital for land plants under fluctuating light environment.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  17. Article
  18. Article
  19. 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

8 authors at 1 institution in 2 countries.

Yuichi YokochiLaboratory for Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology, Nagatsuta-cho 4259-R1-8, Midori-ku, Yokohama 226-8503, Japan.
Kazunori SugiuraLaboratory for Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology, Nagatsuta-cho 4259-R1-8, Midori-ku, Yokohama 226-8503, Japan.
Kazuhiro TakemuraSchool of Life Science and Technology, Tokyo Institute of Technology, 2-12-1 Ookayama, Meguro, Tokyo 152-8550, Japan.
Keisuke YoshidaLaboratory for Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology, Nagatsuta-cho 4259-R1-8, Midori-ku, Yokohama 226-8503, Japan.ORCID 0000-0001-6542-6254
Satoshi HaraSchool of Life Science and Technology, Tokyo Institute of Technology, Nagatsuta-cho 4259-R1-8, Midori-ku, Yokohama 226-8503, Japan.
Ken-Ichi WakabayashiLaboratory for Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology, Nagatsuta-cho 4259-R1-8, Midori-ku, Yokohama 226-8503, Japan.
Akio KitaoSchool of Life Science and Technology, Tokyo Institute of Technology, 2-12-1 Ookayama, Meguro, Tokyo 152-8550, Japan.
Toru HisaboriLaboratory for Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology, Nagatsuta-cho 4259-R1-8, Midori-ku, Yokohama 226-8503, Japan thisabor@res.titech.ac.jp.ORCID 0000-0003-2046-0277
Tokyo Institute of Technology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Thioredoxin (Trx) is a redox-responsive protein that modulates the activities of its target proteins mostly by reducing their disulfide bonds. In chloroplasts, five Trx isoforms (Trx-

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsChloroplast ThioredoxinsConserved SequenceModels, MolecularOxidation-ReductionProtein IsoformsArabidopsis ProteinsChloroplast ThioredoxinsProtein Isoformsatypical Cys His-rich thioredoxinchloroplastdisulfide bondoxidation-reduction (redox)photosynthesisprotein–protein interactionredox regulationtarget selectivitythioredoxin

Identifiers

PMID31597700
PMCPMC6873186
OpenAlexW2979310388

What OpenQuestion holds

Textmetadata
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.