Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structural basis of salicylic acid perception by Arabidopsis NPR proteins.

Nature - 1 Oct 2020

Wang Wei, Withers John, Li Heng, Zwack Paul J, Rusnac Domnița-Valeria, Shi Hui, Liu Lijing, Yan Shunping, Hinds Thomas R, Guttman Mikelos, Dong Xinnian, Zheng Ning

Abstract excerpt

Salicylic acid (SA) is a plant hormone that is critical for resistance to pathogens1-3. The NPR proteins have previously been identified as SA receptors4-10, although how they perceive SA and coordinate hormonal signalling remain unknown. Here we report the mapping of the SA-binding core of Arabidopsis thaliana NPR4 and its ligand-bound crystal structure. The SA-binding core domain of NPR4 refolded with SA adopts...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Crystallography, X-Ray
Share to Deuterium Exchange Measurement

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ligands

Share to Mass Spectrometry

Share to Plant Growth Regulators

Share to Plant Immunity

Share to Protein Domains

Share to Salicylic Acid

Source

Open in PubMed Open full text

Identifiers

PMID: 32788727
DOI: 10.1038/s41586-020-2596-y
PMCID: PMC7554156

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural basis of salicylic acid perception by Arabidopsis NPR proteins.PMID 32788727Read ↗

Salicylic acid binds NPR3 and NPR4 to regulate NPR1-dependent defense responses.Semantic proximity Read ↗

NPR3 and NPR4 are receptors for the immune signal salicylic acid in plants.Semantic proximity Read ↗

Diverse Roles of the Salicylic Acid Receptors NPR1 and NPR3/NPR4 in Plant Immunity.Semantic proximity Read ↗

Opposite Roles of Salicylic Acid Receptors NPR1 and NPR3/NPR4 in Transcriptional Regulation of Plant Immunity.Semantic proximity Read ↗

Contrasting and conserved roles of NPR pathways in diverged land plant lineages.Semantic proximity Read ↗

Structure-function analysis of npr1 alleles in Arabidopsis reveals a role for its paralogs in the perception of salicylic acid.Semantic proximity Read ↗

A prominent role of the circadian proteins PRR5 and PRR7 in governing Arabidopsis immunity.Semantic proximity Read ↗

Inducers of plant systemic acquired resistance regulate NPR1 function through redox changes.Semantic proximity Read ↗

High air humidity dampens salicylic acid pathway and plant resistance via targeting of NPR1Semantic proximity Read ↗

Role for novel family of pathogen-induced cysteine-rich transmembrane proteins in disease resistanceSemantic proximity Read ↗

Non-recognition-of-BTH4, an Arabidopsis mediator subunit homolog, is necessary for development and response to salicylic acid.Semantic proximity Read ↗

A gain-of-function mutation in an Arabidopsis Toll Interleukin1 receptor-nucleotide binding site-leucine-rich repeat type R gene triggers defense responses and results in enhanced disease resistance.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.