Evidence map›Paper›PMID 16829581›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

Plant cells recognize chitin fragments for defense signaling through a plasma membrane receptor.

Hanae Kaku, Yoko Nishizawa, Naoko Ishii-Minami, Chiharu Akimoto-Tomiyama, Naoshi Dohmae, Koji Takio, Eiichi Minami, Naoto Shibuya

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 415 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
415citing papers in PubMed, 1 pooled it
58.5field-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

415 citing papers in PubMed, 1 synthesis or guideline pooled it, 1,133 citations in OpenAlex.

  1. Pooled it
  2. Chitosan activates a sequential CaPlant signaling & behavior · 2026
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  5. Biological Control ofMicroorganisms · 2026
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  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Plant cell surface receptors.The Plant journal : for cell and molecular biology · 2026
    Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Grapevine LysM-containing receptor-like kinaseFrontiers in plant science · 2026
    Article
  18. Article
  19. Article
  20. Article

355 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 1 country.

Hanae KakuDepartment of Biochemistry, National Institute of Agrobiological Sciences, 2-1-2 Kannondai, Tsukuba, Ibaraki 305-8602, Japan. kaku@isc.meiji.ac.jp
Yoko Nishizawa
Naoko Ishii-Minami
Chiharu Akimoto-Tomiyama
Naoshi Dohmae
Koji Takio
Eiichi Minami
Naoto Shibuya
Institute of Agrobiological Sciences · JPRIKEN · JPMeiji University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chitin is a major component of fungal cell walls and serves as a molecular pattern for the recognition of potential pathogens in the innate immune systems of both plants and animals. In plants, chitin oligosaccharides have been known to induce various defense responses in a wide range of plant cells including both monocots and dicots. To clarify the molecular machinery involved in the perception and transduction of chitin oligosaccharide elicitor, a high-affinity binding protein for this elicitor was isolated from the plasma membrane of suspension-cultured rice cells. Characterization of the purified protein, CEBiP, as well as the cloning of the corresponding gene revealed that CEBiP is actually a glycoprotein consisting of 328 amino acid residues and glycan chains. CEBiP was predicted to have a short membrane spanning domain at the C terminus. Knockdown of CEBiP gene by RNA interference resulted in the suppression of the elicitor-induced oxidative burst as well as the gene responses, showing that CEBiP plays a key role in the perception and transduction of chitin oligosaccharide elicitor in the rice cells. Structural analysis of CEBiP also indicated the presence of two LysM motifs in the extracellular portion of CEBiP. As the LysM motif has been known to exist in the putative Nod-factor receptor kinases involved in the symbiotic signaling between leguminous plants and rhizobial bacteria, the result indicates the involvement of partially homologous plasma membrane proteins both in defense and symbiotic signaling in plant cells.

Indexed as

Amino Acid SequenceCell LineCell MembraneChitinCloning, MolecularConserved SequenceDNA, ComplementaryGene Expression Regulation, PlantMembrane ProteinsMolecular Sequence DataOligonucleotide Array Sequence AnalysisOryzaPlant ProteinsRNA InterferenceSequence AlignmentSignal TransductionChitinDNA, ComplementaryMembrane ProteinsPlant Proteins

Identifiers

PMID16829581
PMCPMC1636686
OpenAlexW2050607290

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.