Evidence map›Paper›PMID 21897129›Full record

ArticlePlant signaling & behavior2011

Effect of Cu content on the activity of Cu/ZnSOD1 in the Arabidopsis SUMO E3 ligase siz1 mutant.

Chyi-Chuann Chen, Yong-Yi Chen, Kuo-Chen Yeh

Abstract read
In one paragraph

Article in Plant signaling & behavior, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
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

6 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. 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.

Chyi-Chuann ChenAgricultural Biotechnology Research Center, Academia Sinica, Taipei, Taiwan.
Yong-Yi Chen
Kuo-Chen Yeh

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In a previous study, we found copper (Cu) accumulated to a higher level in the aerial parts of soil-grown plants of the SUMO E3 ligase siz1 mutant than in those of the wild type. Here, we found that all superoxide dismutase (SOD) isoforms, such as FeSOD, MnSOD and different types of Cu/ZnSOD, were more active in the siz1 mutant than in the wild type under normal growth conditions. We further examined the expression and enzymatic activity of Cu/ZnSOD1 (CSD1) in shoots of the siz1 mutant under excess Cu. Shoot CSD1 protein level and activity were reduced in siz1 with excess Cu but induced in the wild type. SIZ1-dependent SUMOylation may be involved in maintaining CSD1 protein stability or repelling a feedback regulation under Cu stress.

Indexed as

ArabidopsisArabidopsis ProteinsCopperLigasesMutationSmall Ubiquitin-Related Modifier ProteinsSuperoxide DismutaseUbiquitin-Protein LigasesArabidopsis ProteinsCopperLigasesSIZ1 protein, ArabidopsisSmall Ubiquitin-Related Modifier ProteinsSuperoxide DismutaseUbiquitin-Protein Ligases

Identifiers

PMID21897129
PMCPMC3256361

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.