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

Targeting of the Small GTPase Rab6A′ by the Legionella pneumophila Effector LidA

9 Apr 2013

Abstract excerpt

When the bacterium Legionella pneumophila, the causative agent of Legionnaires' disease, is phagocytosed by alveolar macrophages, it delivers a large number of effector proteins through its Dot/Icm type IV secretion system into the host cell cytosol. Among those proteins is LidA, an effector that interacts with several host GTPases of the Rab family, including Rab6A', a regulator of retrograde vesicle trafficking...

Read the complete abstract on PubMed

Topics

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

Share to Biomedical Research and Pathophysiology
Share to Erythrocyte Function and Pathophysiology
Share to Legionella and Acanthamoeba research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 23569112
DOI: 10.1128/iai.00157-13

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Targeting of the Small GTPase Rab6A′ by the Legionella pneumophila Effector LidAPMID 23569112Read ↗

Legionella pneumophila LidA Affects Nucleotide Binding and Activity of the Host GTPase Rab1Semantic proximity Read ↗

Targeting of host Rab GTPase function by the intravacuolar pathogen Legionella pneumophila.Semantic proximity Read ↗

Protein LidA from Legionella is a Rab GTPase supereffectorSemantic proximity Read ↗

The Legionella pneumophila effector protein DrrA is a Rab1 guanine nucleotide-exchange factor.Semantic proximity Read ↗

Structural mechanism of host Rab1 activation by the bifunctional Legionella type IV effector SidM/DrrA.Semantic proximity Read ↗

Activation of Ran GTPase by a Legionella effector promotes microtubule polymerization, pathogen vacuole motility and infection.Semantic proximity Read ↗

Legionella pneumophila SidD is a deAMPylase that modifies Rab1.Semantic proximity Read ↗

Taking control: Hijacking of Rab GTPases by intracellular bacterial pathogensSemantic proximity Read ↗

De-AMPylation of the Small GTPase Rab1 by the Pathogen <i>Legionella pneumophila</i>Semantic proximity Read ↗

Rab1 guanine nucleotide exchange factor SidM is a major phosphatidylinositol 4-phosphate-binding effector protein of Legionella pneumophila.Semantic proximity Read ↗

Atypical Legionella GTPase effector hijacks host vesicular transport factor p115 to regulate host lipid dropletSemantic proximity Read ↗

Anchors for Effectors: Subversion of Phosphoinositide Lipids by LegionellaSemantic proximity Read ↗

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