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

An autoactive mutant of the M flax rust resistance protein has a preference for binding ATP, whereas wild-type M protein binds ADP.

Molecular plant-microbe interactions : MPMI - 1 Aug 2011

Williams Simon J, Sornaraj Pradeep, deCourcy-Ireland Emma, Menz R Ian, Kobe Bostjan, Ellis Jeffrey G, Dodds Peter N, Anderson Peter A

Abstract excerpt

Resistance (R) proteins are key regulators of the plant innate immune system and are capable of pathogen detection and activation of the hypersensitive cell death immune response. To understand the molecular mechanism of R protein activation, we undertook a phenotypic and biochemical study of the flax nucleotide binding (NB)-ARC leucine-rich repeat protein, M. Using Agrobacterium-mediated transient expression in...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Diphosphate
Share to Adenosine Triphosphate

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutagenesis, Site-Directed

Share to Plant Leaves

Share to Plant Proteins

Share to Recombinant Proteins

Share to Rhizobium

Source

Identifiers

PMID: 21539434
DOI: 10.1094/MPMI-03-11-0052

Genes

ARC

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

An autoactive mutant of the M flax rust resistance protein has a preference for binding ATP, whereas wild-type M protein binds ADP.PMID 21539434Read ↗

Structural basis of canonical TIR-NLR activation in plant innate immunitySemantic proximity Read ↗

AvrRpm1 Functions as an ADP-Ribosyl Transferase to Modify NOI Domain-Containing Proteins, Including Arabidopsis and Soybean RPM1-Interacting Protein4.Semantic proximity Read ↗

Structures of the flax-rust effector AvrM reveal insights into the molecular basis of plant-cell entry and effector-triggered immunity.Semantic proximity Read ↗

Direct protein interaction underlies gene-for-gene specificity and coevolution of the flax resistance genes and flax rust avirulence genes.Semantic proximity Read ↗

Comparative Analysis of the Flax Immune Receptors L6 and L7 Suggests an Equilibrium-Based Switch Activation Model.Semantic proximity Read ↗

The Tomato Nucleotide-binding Leucine-rich Repeat Immune Receptor I-2 Couples DNA-binding to Nucleotide-binding Domain Nucleotide Exchange.Semantic proximity Read ↗

A type III effector ADP-ribosylates RNA-binding proteins and quells plant immunity.Semantic proximity Read ↗

The receptor-like protein ReMAX of Arabidopsis detects the microbe-associated molecular pattern eMax from Xanthomonas.Semantic proximity Read ↗

Autoactive alleles of the flax L6 rust resistance gene induce non-race-specific rust resistance associated with the hypersensitive response.Semantic proximity Read ↗

A nucleotide phosphatase activity in the nucleotide binding domain of an orphan resistance protein from rice.Semantic proximity Read ↗

Large-scale structure-function analysis of the Arabidopsis RPM1 disease resistance protein.Semantic proximity Read ↗

Mutational analysis of the Arabidopsis nucleotide binding site-leucine-rich repeat resistance gene RPS2.Semantic proximity Read ↗

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