Evidence map›Paper›PMID 20693412›Full record

ArticleJournal of experimental botany2010

Functional analysis of the structural domain of ARF proteins in rice (Oryza sativa L.).

ChenJia Shen, SuiKang Wang, YouHuang Bai, YunRong Wu, SaiNa Zhang, Ming Chen, Tom J Guilfoyle, Ping Wu, YanHua Qi

Open access · hybridAbstract read
In one paragraph

Article in Journal of experimental botany, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
7.5field-weighted citation impact, top 3% 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

78 citing papers in PubMed, 173 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. The Auxin Response FactorPlants (Basel, Switzerland) · 2025
    Article
  5. Bioinformatics Analysis Reveals the Evolutionary Characteristics of theInternational journal of molecular sciences · 2025
    Article
  6. A conserved ARF-DNA interface underlies auxin-triggered transcriptional response.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Functional Divergence of the Closely Related Genes PhARF5 and PhARF19a inInternational journal of molecular sciences · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Analysis of Auxin-Encoding Gene Family inPlants (Basel, Switzerland) · 2023
    Article
  16. Article
  17. Review
  18. Article
  19. Cooperative action of separate interaction domains promotes high-affinity DNA binding ofProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  20. Article

18 more citing papers are in PubMed but not listed here.

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

9 authors at 3 institutions in 2 countries.

ChenJia ShenState Key Laboratory of Plant Physiology and Biochemistry, Zhejiang University, Hangzhou 310058, China.
SuiKang Wang
YouHuang Bai
YunRong Wu
SaiNa Zhang
Ming Chen
Tom J Guilfoyle
Ping Wu
YanHua Qi
Zhejiang University · CNState Key Laboratory of Plant Physiology and BiochemistryUniversity of Missouri · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Auxin response factors (ARFs) are key regulators of plant growth and development. Through interaction with auxin/indole acetic acid (Aux/IAA) proteins, they influence the expression of auxin response genes. An ARF gene family has been predicted in rice, but the functions of the individual structural domains of the OsARFs remain obscure. Bioinformatics was used to analyse the position of the DNA-binding domain (DBD), middle region (MR), and C-terminal dimerization domain (CTD) of OsARFs, and experimentally confirmed the presence of a classical monopartite nuclear localization signal (NLS) in the DBD. The DBD was shown to contribute to nuclear localization of OsARF proteins in addition to its known DNA-binding function. Interactions between 14 integrated OsARFs and 15 OsIAA proteins were tested using yeast two-hybrid assays. It was found that eight OsARF activators interacted with the 15 OsIAA proteins, while six OsARF repressors did not. The interactions between the MR+CTD or CTD of 10 OsARFs and 15 OsIAA proteins were also tested and the results were consistent with those of each intact OsARF, although some slight differences in interaction intensity were observed by α-galactosidase quantitative assays. The truncated CTD of OsARF11 did not interact with any OsIAA, implying that the CTD is required for ARF-IAA dimerization, and that the MR influences the interaction intensity in yeast. A subset of the interactions in yeast were also observed in tobacco plants using firefly luciferase complementation imaging assays, indicating that these interactions are specific in plants, and might have a special role in the auxin signalling response. This study provides new insight into the structure of OsARF proteins and ARF-Aux/IAA interactions.

Indexed as

alpha-GalactosidaseNuclear ProteinsOryzaPlant ProteinsProtein Structure, TertiaryRepressor ProteinsTrans-ActivatorsTwo-Hybrid System Techniquesalpha-GalactosidaseNuclear ProteinsPlant ProteinsRepressor ProteinsTrans-Activators

Identifiers

PMID20693412
PMCPMC2935870
OpenAlexW2136343511

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.