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

Lipid binding activities of flax rust AvrM and AvrL567 effectors.

Plant signaling & behavior - 1 Oct 2010

Gan Pamela H P, Rafiqi Maryam, Ellis Jeffrey G, Jones David A, Hardham Adrienne R, Dodds Peter N

Abstract excerpt

Effectors are pathogen-encoded proteins that are thought to facilitate infection by manipulation of host cells. Evidence showing that the effectors of some eukaryotic plant pathogens are able to interact directly with cytoplasmic host proteins indicates that translocation of these proteins into h...

Read the complete abstract on PubMed

Topics

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

Share to Basidiomycota
Share to Flax
Share to Fungal Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Lipid Metabolism

Share to Mutation

Share to Plant Diseases

Share to Protein Binding

Source

Open in PubMed Open full text

Identifiers

PMID: 20855950
DOI: 10.4161/psb.5.10.13013
PMCID: PMC3115366

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-20855950-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Lipid binding activities of flax rust AvrM and AvrL567 effectors.PMID 20855950Read ↗

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

A new family of structurally conserved fungal effectors displays epistatic interactions with plant resistance proteinsSemantic proximity Read ↗

Avirulence protein 3a (AVR3a) from the potato pathogen Phytophthora infestans forms homodimers through its predicted translocation region and does not specifically bind phospholipids.Semantic proximity Read ↗

Molecular and cellular analysis of the biotrophic interaction between rice and Magnaporthe oryzae – Exploring situations in which the blast fungus controls the infectionSemantic proximity Read ↗

Inorganic cations mediate plant PR5 protein antifungal activity through fungal Mnn1- and Mnn4-regulated cell surface glycans.Semantic proximity Read ↗

Structural basis for interactions of the Phytophthora sojae RxLR effector Avh5 with phosphatidylinositol 3-phosphate and for host cell entry.Semantic proximity Read ↗

N-terminal motifs in some plant disease resistance proteins function in membrane attachment and contribute to disease resistance.Semantic proximity Read ↗

Interaction of GAPR-1 with lipid bilayers is regulated by alternative homodimerization.Semantic proximity Read ↗

The pseudomonas AvrPto protein is differentially recognized by tomato and tobacco and is localized to the plant plasma membrane.Semantic proximity Read ↗

Pseudomonas syringae Effector AvrPphB Suppresses AvrB-Induced Activation of RPM1 but Not AvrRpm1-Induced Activation.Semantic proximity Read ↗

Physiological and proteomic approaches to evaluate the role of sterol binding in elicitin-induced resistance.Semantic proximity Read ↗

Permeabilization of fungal membranes by plant defensins inhibits fungal growth.Semantic proximity Read ↗

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