Evidence map›Paper›PMID 28808003›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Signaling from the plasma-membrane localized plant immune receptor RPM1 requires self-association of the full-length protein.

Farid El Kasmi, Eui-Hwan Chung, Ryan G Anderson, Jinyue Li, Li Wan, Timothy K Eitas, Zhiyong Gao, Jeffery L Dangl

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing 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

57 citing papers in PubMed.

  1. Article
  2. An Auto-Activated NLR-Protein OsRGA3Plant biotechnology journal · 2026
    Article
  3. The barley disease resistance proteinmicroPublication biology · 2026
    Article
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  14. Article
  15. Article
  16. Article
  17. Mutation of a highly conserved amino acid in RPM1 causes leaf yellowing and premature senescence in wheat.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2023
    Article
  18. Review
  19. Plasma membrane association and resistosome formation of plant helper immune receptors.Proceedings of the National Academy of Sciences of the United States of America · 2023
    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

8 authors.

Farid El KasmiDepartment of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-3280.ORCID 0000-0002-4634-7689
Eui-Hwan ChungDepartment of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-3280.
Ryan G AndersonDepartment of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-3280.
Jinyue LiState Key Laboratory of Hybrid Rice, College of Life Sciences, Wuhan University, Wuhan, Hubei Province, P. R. China 430072.
Li WanDepartment of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-3280.
Timothy K EitasCurriculum in Genetics and Molecular Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-3280.
Zhiyong GaoState Key Laboratory of Hybrid Rice, College of Life Sciences, Wuhan University, Wuhan, Hubei Province, P. R. China 430072; zygao@whu.edu.cn dangl@email.unc.edu.
Jeffery L DanglDepartment of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-3280; zygao@whu.edu.cn dangl@email.unc.edu.

Funding

Activation mechanism of a NLR protein innate immune receptorF32GM108226 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ANDERSON, RYAN G · 2014 to 2015
$109k
Howard Hughes Medical InstituteNIGMS NIH HHS F32 GM108226
6 · The paper itself

Abstract

Plants evolved intracellular immune receptors that belong to the NOD-like receptor (NLR) family to recognize the presence of pathogen-derived effector proteins. NLRs possess an N-terminal Toll-like/IL-1 receptor (TIR) or a non-TIR domain [some of which contain coiled coils (CCs)], a central nucleotide-binding (NB-ARC) domain, and a C-terminal leucine-rich repeat (LRR). Activation of NLR proteins results in a rapid and high-amplitude immune response, eventually leading to host cell death at the infection site, the so-called hypersensitive response. Despite their important contribution to immunity, the exact mechanisms of NLR activation and signaling remain unknown and are likely heterogenous. We undertook a detailed structure-function analysis of the plasma membrane (PM)-localized CC NLR Resistance to

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsBacterial ProteinsCarrier ProteinsCell MembraneImmunity, InnateIntracellular Signaling Peptides and ProteinsNicotianaNLR ProteinsPlant DiseasesPlant ImmunityProtein BindingPseudomonas syringaeReceptors, ImmunologicSignal TransductionArabidopsis ProteinsBacterial ProteinsCarrier ProteinsIntracellular Signaling Peptides and ProteinsNLR ProteinsReceptors, ImmunologicRIN4 protein, ArabidopsisRPM1 protein, ArabidopsisArabidopsis thalianaeffector-triggered immunityNLR receptoroligomerizationplant immunity

Identifiers

PMID28808003
PMCPMC5584451

What OpenQuestion holds

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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.