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

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

The Journal of biological chemistry - 3 Feb 2012

Fenyk Stepan, Campillo Alba de San Eustaquio, Pohl Ehmke, Hussey Patrick J, Cann Martin J

Abstract excerpt

Plant resistance proteins (R-proteins) are key components of the plant immune system activated in response to a plethora of different pathogens. R-proteins are P-loop NTPase superfamily members, and current models describe their main function as ATPases in defense signaling pathways. Here we show that a subset of R-proteins have evolved a new function to combat pathogen infection. This subset of R-proteins...

Read the complete abstract on PubMed

Topics

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

Share to Disease Resistance
Share to Kinetics

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Nucleotides

Share to Plant Diseases

Share to Plant Proteins

Share to Zea mays

Source

Open in PubMed Open full text

Identifiers

PMID: 22157756
DOI: 10.1074/jbc.M111.314450
PMCID: PMC3281693

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A nucleotide phosphatase activity in the nucleotide binding domain of an orphan resistance protein from rice.PMID 22157756Read ↗

A comprehensive analysis of protein phosphatases in rice and ArabidopsisSemantic proximity Read ↗

<i>In silico</i> characterization of five novel disease-resistance proteins in <i>Oryza sativa sp. japonica</i> against bacterial leaf blight and rice blast diseasesSemantic proximity Read ↗

Plant pathogenic fungi hijack phosphate starvation signaling with conserved enzymatic effectorsSemantic proximity Read ↗

MoPtc6, a Type 2C Protein Phosphatase Plays Critical Roles in the Development and Virulence of <i>Magnaporthe oryzae</i>Semantic proximity Read ↗

Structural basis for the preference of the Arabidopsis thaliana phosphatase RLPH2 for tyrosine-phosphorylated substrates.Semantic proximity Read ↗

Multiple variants of the fungal effector AVR-Pik bind the HMA domain of the rice protein OsHIPP19, providing a foundation to engineer plant defense.Semantic proximity Read ↗

Pathogen effector forms a hexameric phosphatase holoenzyme with host core enzyme to promote diseaseSemantic proximity Read ↗

Multiple variants of the blast fungus effector AVR-Pik bind the HMA domain of the rice protein OsHIPP19 with high affinitySemantic proximity Read ↗

The blast pathogen effector AVR-Pik binds and stabilizes rice heavy metal-associated (HMA) proteins to co-opt their function in immunitySemantic proximity Read ↗

Functional assignment to positively selected sites in the core type III effector RipG7 from Ralstonia solanacearum.Semantic proximity Read ↗

Mapping ortholog-restricted ligandable cysteines in the wheat pathogen <i>Zymoseptoria tritici</i>Semantic proximity Read ↗

A New ‘Comprehensive’ Annotation of Leucine-Rich Repeat-Containing Receptors in RiceSemantic proximity Read ↗

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