Evidence map›Paper›PMID 24970139›Full record

ArticleBiomolecules2012

Leucine-Rich Repeat (LRR) Domains Containing Intervening Motifs in Plants.

Norio Matsushima, Hiroki Miyashita

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
4.8field-weighted citation impact, top 6% 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

42 citing papers in PubMed, 98 citations in OpenAlex.

  1. FcLRR1 Regulates Hyphal Growth and Plant Infection inJournal of fungi (Basel, Switzerland) · 2026
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  3. Review
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  8. Review
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  10. NLRscape: an atlas of plant NLR proteins.Nucleic acids research · 2023
    Article
  11. Article
  12. Article
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  15. A new comprehensive annotation of leucine-rich repeat-containing receptors in rice.The Plant journal : for cell and molecular biology · 2021
    Article
  16. Article
  17. Article
  18. A receptor-like protein mediates plant immune responses to herbivore-associated molecular patterns.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  19. Crystal structure of the extracellular domain of the receptor-like kinase TMK3 from Arabidopsis thaliana.Acta crystallographica. Section F, Structural biology communications · 2020
    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 1 institution in 1 country.

Norio MatsushimaDivision of Biophysics, Center for Medical Education, Sapporo Medical University, Sapporo 060-8556, Japan. matusima@sapmed.ac.jp.
Hiroki MiyashitaDepartment of Biochemistry, School of Medicine, Sapporo Medical University, Sapporo 060-8556, Japan. h-miyashita@sapmed.ac.jp.
Sapporo Medical University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

LRRs (leucine rich repeats) are present in over 14,000 proteins. Non-LRR, island regions (IRs) interrupting LRRs are widely distributed. The present article reviews 19 families of LRR proteins having non-LRR IRs (LRR@IR proteins) from various plant species. The LRR@IR proteins are LRR-containing receptor-like kinases (LRR-RLKs), LRR-containing receptor-like proteins (LRR-RLPs), TONSOKU/BRUSHY1, and MJK13.7; the LRR-RLKs are homologs of TMK1/Rhg4, BRI1, PSKR, PSYR1, Arabidopsis At1g74360, and RPK2, while the LRR-RLPs are those of Cf-9/Cf-4, Cf-2/Cf-5, Ve, HcrVf, RPP27, EIX1, clavata 2, fascinated ear2, RLP2, rice Os10g0479700, and putative soybean disease resistance protein. The LRRs are intersected by single, non-LRR IRs; only the RPK2 homologs have two IRs. In most of the LRR-RLKs and LRR-RLPs, the number of repeat units in the preceding LRR block (N1) is greater than the number of the following block (N2); N1 » N2 in which N1 is variable in the homologs of individual families, while N2 is highly conserved. The five families of the LRR-RLKs except for the RPK2 family show N1 = 8 - 18 and N2 = 3 - 5. The nine families of the LRR-RLPs show N1 = 12 - 33 and N2 = 4; while N1 = 6 and N2 = 4 for the rice Os10g0479700 family and the N1 = 4 - 28 and N2 = 4 for the soybean protein family. The rule of N1 » N2 might play a common, significant role in ligand interaction, dimerization, and/or signal transduction of the LRR-RLKs and the LRR-RLPs. The structure and evolution of the LRR domains with non-LRR IRs and their proteins are also discussed.

Identifiers

PMID24970139
PMCPMC4030839
OpenAlexW1977563493

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.