Evidence map›Paper›PMID 25604444›Full record

ReviewThe Plant cell2015

The PB1 domain in auxin response factor and Aux/IAA proteins: a versatile protein interaction module in the auxin response.

Tom J Guilfoyle

Open access · greenAbstract readReview
In one paragraph

Review in The Plant cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 119 papers.

0numbers the graph read from it
0cells of the map it votes in
119citing papers in PubMed
35.7field-weighted citation impact, top 1% 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

119 citing papers in PubMed, 231 citations in OpenAlex.

  1. Article
  2. Plants (Basel, Switzerland) · 2026
    Article
  3. Review
  4. Article
  5. Characterisation of theInternational journal of molecular sciences · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Mechanisms of auxin action in plant growth and development.Nature reviews. Molecular cell biology · 2025
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

59 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

1 author at 1 institution in 1 country.

Tom J GuilfoyleDepartment of Biochemistry, University of Missouri, Columbia, Missouri 65211 guilfoylet@missouri.edu.ORCID http://orcid.org/0000-0001-7863-0510
University of Missouri · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

An integral part of auxin-regulated gene expression involves the interplay of two types of transcription factors, the DNA binding auxin response factor (ARF) activators and the interacting auxin/indole acetic acid (Aux/IAA) repressors. Insight into the mechanism of how these transcription factors interact with one another has recently been revealed from crystallographic information on ARF5 and ARF7 C-terminal domains (i.e., a protein-protein interaction domain referred to as domain III/IV that is related to domain III/IV in Aux/IAA proteins). Three-dimensional structures showed that this domain in ARF5 and ARF7 conforms to a well-known PB1 (Phox and Bem1) domain that confers protein-protein interactions with other PB1 domain proteins through electrostatic contacts. Experiments verifying the importance of charged amino acids in conferring ARF and Aux/IAA interactions have confirmed the PB1 domain structure. Some in planta experiments designed to test the validity of PB1 interactions in the auxin response have led to updated models for auxin-regulated gene expression and raised many questions that will require further investigation. In addition to the PB1 domain, a second protein interaction module that functions in ARF-ARF dimerization and facilitates DNA binding has recently been revealed from crystallography studies on the ARF1 and ARF5 DNA binding domains.

Indexed as

Gene Expression Regulation, PlantIndoleacetic AcidsPlant ProteinsProtein BindingProtein Interaction Domains and MotifsSignal TransductionTranscription Factorsindoleacetic acidIndoleacetic AcidsPlant ProteinsTranscription Factors

Identifiers

PMID25604444
PMCPMC4330575
OpenAlexW2156970744

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.