Evidence map›Paper›PMID 23743537›Full record

ReviewPlanta2013

Interactions between Arabidopsis acyl-CoA-binding proteins and their protein partners.

Zhi-Yan Du, Mee-Len Chye

Open access · bronzeAbstract readReview
PubMed Publisher
In one paragraph

Review in Planta, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

9 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Low-oxygen response is triggered by an ATP-dependent shift in oleoyl-CoA inProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
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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

2 authors at 1 institution in 1 country.

Zhi-Yan DuSchool of Biological Sciences, The University of Hong Kong, Pokfulam, Hong Kong, China.
Mee-Len Chye
University of Hong Kong · HK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein-protein interactions are at the core of cellular interactomics and are essential for various biological functions. Since proteins commonly function as macromolecular complexes, it is important to identify their interacting partners to better understand their function and the significance in these interactions. The acyl-CoA-binding proteins (ACBPs) of eukaryotes show conservation in the presence of a lipid-binding acyl-CoA-binding domain. In Arabidopsis thaliana, four of six members from the AtACBP family possess ankyrin repeats (AtACBP1 and AtACBP2) or kelch motifs (AtACBP4 and AtACBP5), which can potentially mediate protein-protein interactions. Through yeast two-hybrid screens, a dozen putative protein partners interacting with AtACBPs have been isolated from an Arabidopsis cDNA library. Investigations in the past decade on the interaction between AtACBPs and their protein partners have revealed novel roles for AtACBPs, including functions in mediating oxidative stress responses, heavy metal tolerance and oxygen sensing. Recent progress and current questions on AtACBPs and their interactors are discussed in this review.

Indexed as

Gene Expression Regulation, PlantAcyl Coenzyme AAnkyrin RepeatArabidopsisArabidopsis ProteinsDiazepam Binding InhibitorGene LibraryLipid MetabolismModels, MolecularOxidative StressOxygenProtein BindingStress, PhysiologicalTranscription FactorsTwo-Hybrid System TechniquesAcyl Coenzyme AArabidopsis ProteinsDiazepam Binding InhibitorOxygenTranscription Factors

Identifiers

PMID23743537
OpenAlexW2053415461

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.