Evidence map›Paper›PMID 31461469›Full record

ArticlePloS one2019

Structural and biochemical studies of an NB-ARC domain from a plant NLR immune receptor.

John F C Steele, Richard K Hughes, Mark J Banfield

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
6.1field-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

37 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
  2. Article
  3. An Auto-Activated NLR-Protein OsRGA3Plant biotechnology journal · 2026
    Article
  4. Precision Editing of NLRS Improves Effector Recognition for Enhanced Disease Resistance.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Advances in understanding the interaction betweenPlant signaling & behavior · 2024
    Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Genetic mapping of the powdery mildew resistance gene Pm7 on oat chromosome 5D.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2023
    Article
  19. NLRscape: an atlas of plant NLR proteins.Nucleic acids research · 2023
    Article
  20. Review
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 1 country.

John F C SteeleDepartment of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich, England, United Kingdom.ORCID 0000-0002-4388-4956
Richard K HughesDepartment of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich, England, United Kingdom.ORCID 0000-0001-9910-6566
Mark J BanfieldDepartment of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich, England, United Kingdom.ORCID 0000-0001-8921-3835
John Innes Centre · GB

Funding

Biotechnology and Biological Sciences Research Council BB/J004553Biotechnology and Biological Sciences Research Council BB/P012574
6 · The paper itself

Abstract

Plant NLRs are modular immune receptors that trigger rapid cell death in response to attempted infection by pathogens. A highly conserved nucleotide-binding domain shared with APAF-1, various R-proteins and CED-4 (NB-ARC domain) is proposed to act as a molecular switch, cycling between ADP (repressed) and ATP (active) bound forms. Studies of plant NLR NB-ARC domains have revealed functional similarities to mammalian homologues, and provided insight into potential mechanisms of regulation. However, further advances have been limited by difficulties in obtaining sufficient yields of protein suitable for structural and biochemical techniques. From protein expression screens in Escherichia coli and Sf9 insect cells, we defined suitable conditions to produce the NB-ARC domain from the tomato NLR NRC1. Biophysical analyses of this domain showed it is a folded, soluble protein. Structural studies revealed the NRC1 NB-ARC domain had co-purified with ADP, and confirmed predicted structural similarities between plant NLR NB-ARC domains and their mammalian homologues.

Indexed as

Adenosine TriphosphatasesAmino Acid SequenceAnimalsChromatography, GelDisease ResistanceEscherichia coliGene Expression Regulation, PlantInsectaModels, MolecularNucleotide MotifsPlant DiseasesPlant ImmunityPlant ProteinsProtein DomainsProtein FoldingSolanum lycopersicumAdenosine TriphosphatasesPlant Proteins

Identifiers

PMID31461469
PMCPMC6713354
OpenAlexW2970351044

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.