Evidence map›Paper›PMID 23299425›Full record

ArticlePlant signaling & behavior2013

Chaperonin 20 might be an iron chaperone for superoxide dismutase in activating iron superoxide dismutase (FeSOD).

Wen-Yu Kuo, Chien-Hsun Huang, Tsung-Luo Jinn

Open access · bronzeAbstract read
In one paragraph

Article in Plant signaling & behavior, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.7field-weighted citation impact, top 29% 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

8 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Stress resilience inFrontiers in plant science · 2025
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. 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

3 authors at 1 institution in 2 countries.

Wen-Yu KuoInstitute of Plant Biology and Department of Life Science; National Taiwan University; Taipei, Taiwan.
Chien-Hsun HuangInstitute of Plant Biology and Department of Life Science; National Taiwan University; Taipei, Taiwan.
Tsung-Luo JinnInstitute of Plant Biology and Department of Life Science; National Taiwan University; Taipei, Taiwan.
Institute of Plant Biology · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Activation of Cu/Zn superoxide dismutases (CuZnSODs) is aided by Cu incorporation and disulfide isomerization by Cu chaperone of SOD (CCS). As well, an Fe-S cluster scaffold protein, ISU, might alter the incorporation of Fe or Mn into yeast MnSOD (ySOD2), thus leading to active or inactive ySOD2. However, metallochaperones involved in the activation of FeSODs are unknown. Recently, we found that a chloroplastic chaperonin cofactor, CPN20, could mediate FeSOD activity. To investigate whether Fe incorporation in FeSOD is affected by CPN20, we used inductively coupled plasma mass spectrometry to analyze the ability of CPN20 to bind Fe. CPN20 could bind Fe, and the Fe binding to FeSOD was increased with CPN20 incubation. Thus, CPN20 might be an Fe chaperone for FeSOD activation, a role independent of its well-known co-chaperonin activity.

Indexed as

ArabidopsisArabidopsis ProteinsGroup I ChaperoninsIronSuperoxide DismutaseArabidopsis ProteinsCpn20 protein, ArabidopsisGroup I ChaperoninsIronSuperoxide DismutaseArabidopsischaperonin 20FeSODiron chaperoneiron homeostasisSOD activation

Identifiers

PMID23299425
PMCPMC3657002
OpenAlexW2043507033

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.