Evidence map›Paper›PMID 41776336›Full record

ReviewNature genetics2026

The emerging role of kinase fusion proteins in cereal immunity.

Oliver R Powell, Francisco J Guzmán-Vega, Daniel S Yu, Yan L Wang, Ping Lu, Stefan T Arold, Zhiyong Liu, Mark J Banfield, Brande B H Wulff, Renjie Chen

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature genetics, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

10 authors.

Oliver R Powell *Plant Science Program, Biological and Environmental Science and Engineering Division (BESE), King Abdullah University of Science and Technology (KAUST), Thuwal, Saudi Arabia.
Francisco J Guzmán-VegaPlant Science Program, Biological and Environmental Science and Engineering Division (BESE), King Abdullah University of Science and Technology (KAUST), Thuwal, Saudi Arabia.ORCID http://orcid.org/0000-0002-6116-9534
Daniel S YuDepartment of Biochemistry and Metabolism, John Innes Centre, Norwich Research Park, Norwich, UK.ORCID http://orcid.org/0000-0003-0454-7989
Yan L WangPlant Science Program, Biological and Environmental Science and Engineering Division (BESE), King Abdullah University of Science and Technology (KAUST), Thuwal, Saudi Arabia.
Ping LuState Key Laboratory of Seed Innovation, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, China.ORCID http://orcid.org/0000-0002-5923-152X
Stefan T AroldKAUST Center of Excellence for Smart Health, Biological and Environmental Science and Engineering Division, King Abdullah University of Science and Technology (KAUST), Thuwal, Saudi Arabia.ORCID http://orcid.org/0000-0001-5278-0668
Zhiyong LiuState Key Laboratory of Seed Innovation, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, China.ORCID http://orcid.org/0000-0002-6958-5233
Mark J BanfieldDepartment of Biochemistry and Metabolism, John Innes Centre, Norwich Research Park, Norwich, UK.ORCID http://orcid.org/0000-0001-8921-3835
Brande B H WulffPlant Science Program, Biological and Environmental Science and Engineering Division (BESE), King Abdullah University of Science and Technology (KAUST), Thuwal, Saudi Arabia. brande.wulff@kaust.edu.sa.ORCID http://orcid.org/0000-0003-4044-4346
Renjie Chen *Plant Science Program, Biological and Environmental Science and Engineering Division (BESE), King Abdullah University of Science and Technology (KAUST), Thuwal, Saudi Arabia. renjie.chen@kaust.edu.sa.ORCID http://orcid.org/0009-0007-7858-1828

Funding

King Abdullah University of Science and Technology (KAUST) CRG11-2022-5087RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/X010996/1, UKRI1913
6 · The paper itself

Abstract

Kinase fusion proteins (KFPs) are an emerging class of diverse intracellular plant immune receptors with critical roles in immunity in wheat (Triticum aestivum) and other members of the Triticeae. These proteins contain at least one kinase domain fused to one or more additional domains, possibly including another kinase domain. Many KFP kinase domains are predicted to possess an atypical structural motif, the extended β-finger, indicating that KFPs may operate through shared mechanisms in plant immunity despite their structural diversity. Recent research has demonstrated that KFP SR62

Indexed as

Edible GrainPlant ImmunityPlant ProteinsProtein KinasesTriticumDisease ResistancePlant DiseasesPlant ProteinsProtein Kinases

Identifiers

PMID41776336

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.