Evidence map›Paper›PMID 23053766›Full record

ReviewProtoplasma2013

Mapping FLS2 function to structure: LRRs, kinase and its working bits.

Silke Robatzek, Lennart Wirthmueller

Erratum issuedAbstract readReview
PubMed Publisher
In one paragraph

Review in Protoplasma, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

  1. Review
  2. Article
  3. mamp-ml: A deep learning approach to epitope immunogenicity in plants.bioRxiv : the preprint server for biology · 2025
    Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Exogenous 1',4'-International journal of molecular sciences · 2021
    Article
  12. Review
  13. TALEN-BasedFrontiers in plant science · 2021
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

2 authors.

Silke RobatzekThe Sainsbury Laboratory, Norwich Research Park, Norwich, NR4 7UH, UK. robatzek@tsl.ac.uk
Lennart Wirthmueller

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The plasma membrane-localised FLAGELLIN SENSING 2 (FLS2) receptor is an important component of plant immunity against potentially pathogenic bacteria, acting to recognise the conserved flg22 peptide of flagellin. FLS2 shares the common structure of transmembrane receptor kinases with a receptor-like ectodomain composed of leucine-rich repeats (LRR) and an active intracellular kinase domain. Upon ligand binding, FLS2 dimerises with the regulatory LRR-receptor kinase BRI1-associated kinase 1, which in turn triggers downstream signalling cascades. Although lacking crystal structure data, recent advances have been made in our understanding of flg22 recognition based on structural and functional analyses of FLS2. These studies have revealed critical regions/residues of FLS2 and post-translational modifications that regulate the abundance and activity of this receptor. In this review, we present the current knowledge on the structural mechanism of the FLS2-flg22 interaction and subsequent receptor-mediated signalling.

Indexed as

Amino Acid SequenceAnimalsArabidopsisArabidopsis ProteinsCatalytic DomainFlagellinGlycosylationModels, MolecularMolecular Sequence DataPlant DiseasesPlant ImmunityProtein BindingProtein KinasesProtein Processing, Post-TranslationalProtein Structure, SecondaryReceptors, Pattern RecognitionArabidopsis ProteinsFlagellinFLS2 protein, ArabidopsisProtein KinasesReceptors, Pattern Recognition

Identifiers

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.