Evidence map›Paper›PMID 28137883›Full record

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

TIR-only protein RBA1 recognizes a pathogen effector to regulate cell death in

Marc T Nishimura, Ryan G Anderson, Karen A Cherkis, Terry F Law, Qingli L Liu, Mischa Machius, Zachary L Nimchuk, Li Yang, Eui-Hwan Chung, Farid El Kasmi and 4 more

Open access · bronzeAbstract 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 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
30.9field-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

73 citing papers in PubMed, 165 citations in OpenAlex.

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  10. TheProceedings of the National Academy of Sciences of the United States of America · 2025
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  11. Current issues in molecular biology · 2025
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13 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

14 authors at 1 institution in 1 country.

Marc T NishimuraDepartment of Biology, University of North Carolina, Chapel Hill, NC 27599; marcusn@colostate.edu dangl@email.unc.edu.ORCID 0000-0003-4666-6900
Ryan G AndersonDepartment of Biology, University of North Carolina, Chapel Hill, NC 27599.
Karen A CherkisCurriculum in Genetics and Molecular Biology, University of North Carolina, Chapel Hill, NC 27599.
Terry F LawDepartment of Biology, University of North Carolina, Chapel Hill, NC 27599.
Qingli L LiuDepartment of Biology, University of North Carolina, Chapel Hill, NC 27599.
Mischa MachiusDepartment of Pharmacology, University of North Carolina, Chapel Hill, NC 27599.
Zachary L NimchukDepartment of Biology, University of North Carolina, Chapel Hill, NC 27599.
Li YangDepartment of Biology, University of North Carolina, Chapel Hill, NC 27599.
Eui-Hwan ChungDepartment of Biology, University of North Carolina, Chapel Hill, NC 27599.
Farid El KasmiDepartment of Biology, University of North Carolina, Chapel Hill, NC 27599.
Michael HyunhDepartment of Biology, University of North Carolina, Chapel Hill, NC 27599.
Erin Osborne NishimuraLineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, NC 27599.ORCID 0000-0002-4313-4573
John E SondekDepartment of Pharmacology, University of North Carolina, Chapel Hill, NC 27599.
Jeffery L DanglDepartment of Biology, University of North Carolina, Chapel Hill, NC 27599; marcusn@colostate.edu dangl@email.unc.edu.
University of North Carolina at Chapel Hill · US

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

Detection of pathogens by plants is mediated by intracellular nucleotide-binding site leucine-rich repeat (NLR) receptor proteins. NLR proteins are defined by their stereotypical multidomain structure: an N-terminal Toll-interleukin receptor (TIR) or coiled-coil (CC) domain, a central nucleotide-binding (NB) domain, and a C-terminal leucine-rich repeat (LRR). The plant innate immune system contains a limited NLR repertoire that functions to recognize all potential pathogens. We isolated Response to the bacterial type III effector protein HopBA1 (

Indexed as

Gene Expression Regulation, PlantArabidopsisArabidopsis ProteinsBinding SitesCell DeathCrystallography, X-RayErwiniaHost-Pathogen InteractionsModels, MolecularMutationNicotianaPlant DiseasesPlant ImmunityPlant ProteinsProtein BindingProtein Interaction Domains and MotifsArabidopsis ProteinsPlant ProteinsRecombinant Proteinsrps4 protein, plantType III Secretion SystemsNLRoligomerizationplant immunityToll–interleukin-1 receptor homology domaintype III secretion

Identifiers

PMID28137883
PMCPMC5347586
OpenAlexW2580724658

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.