Evidence map›Paper›PMID 37326386›Full record

ReviewThe Biochemical journal2023

Paradigms of receptor kinase signaling in plants.

Kyle W Bender, Cyril Zipfel

Open access · hybridAbstract readReview
In one paragraph

Review in The Biochemical journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
39.3field-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

39 citing papers in PubMed, 83 citations in OpenAlex.

  1. Review
  2. How SCREW finds its NUT.Nature plants · 2026
    Article
  3. Article
  4. The ubiquitin code of receptor kinases in plants.Journal of integrative plant biology · 2026
    Review
  5. Article
  6. Article
  7. Article
  8. Processing and release of endogenous immunogenic peptide signals.The Plant journal : for cell and molecular biology · 2026
    Review
  9. SPlant biotechnology journal · 2026
    Article
  10. Review
  11. Review
  12. Review
  13. ERECTA-family receptor kinases: versatile regulators of plant developmental signaling.The Plant journal : for cell and molecular biology · 2026
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article
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 2 institutions in 2 countries.

Kyle W BenderInstitute of Plant and Microbial Biology, Zürich-Basel Plant Science Center, University of Zürich, 8008 Zürich, Switzerland.
Cyril ZipfelInstitute of Plant and Microbial Biology, Zürich-Basel Plant Science Center, University of Zürich, 8008 Zürich, Switzerland.ORCID 0000-0003-4935-8583
University of East Anglia · GBUniversity of Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plant receptor kinases (RKs) function as key plasma-membrane localized receptors in the perception of molecular ligands regulating development and environmental response. Through the perception of diverse ligands, RKs regulate various aspects throughout the plant life cycle from fertilization to seed set. Thirty years of research on plant RKs has generated a wealth of knowledge on how RKs perceive ligands and activate downstream signaling. In the present review, we synthesize this body of knowledge into five central paradigms of plant RK signaling: (1) RKs are encoded by expanded gene families, largely conserved throughout land plant evolution; (2) RKs perceive many different kinds of ligands through a range of ectodomain architectures; (3) RK complexes are typically activated by co-receptor recruitment; (4) post-translational modifications fulfill central roles in both the activation and attenuation of RK-mediated signaling; and, (5) RKs activate a common set of downstream signaling processes through receptor-like cytoplasmic kinases (RLCKs). For each of these paradigms, we discuss key illustrative examples and also highlight known exceptions. We conclude by presenting five critical gaps in our understanding of RK function.

Indexed as

Arabidopsis ProteinsProtein KinasesCytoplasmLigandsPlantsSignal TransductionArabidopsis ProteinsLigandsProtein Kinasesreceptor kinasereceptor-like cytoplasmic kinasesignaling

Identifiers

PMID37326386
PMCPMC10317173
OpenAlexW4380870628

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.