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

Legionella Manipulates Non-canonical SNARE Pairing Using a Bacterial Deubiquitinase

1 Sept 2020

Abstract excerpt

The intracellular bacterial pathogen Legionella pneumophila uses many effector proteins delivered by the bacterial type IV secretion system (T4SS) to hijack the early secretory pathway to establish its replicative niche, known as the Legionella-containing vacuole (LCV). On LCV biogenesis, the endoplasmic reticulum (ER) vesicular soluble N-ethylmaleimide-sensitive factor attachment protein receptors (v-SNARE)...

Read the complete abstract on PubMed

Topics

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

Share to Autophagy in Disease and Therapy
Share to Heme Oxygenase-1 and Carbon Monoxide
Share to Legionella and Acanthamoeba research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 32905772
DOI: 10.1016/j.celrep.2020.108107

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

Legionella Manipulates Non-canonical SNARE Pairing Using a Bacterial DeubiquitinasePMID 32905772Read ↗

Interplay between bacterial deubiquitinase and ubiquitin E3 ligase regulates ubiquitin dynamics on Legionella phagosomesSemantic proximity Read ↗

LotA, a Legionella deubiquitinase, has dual catalytic activity and contributes to intracellular growthSemantic proximity Read ↗

Phosphoribosyl ubiquitination of SNARE proteins regulates autophagy during Legionella infectionSemantic proximity Read ↗

Phosphoribosyl ubiquitination of SNARE proteins regulate autophagy in Legionella infectionSemantic proximity Read ↗

Cross-family small GTPase ubiquitination by the intracellular pathogen Legionella pneumophilaSemantic proximity Read ↗

Phosphoribosyl modification of poly-ubiquitin chains at the Legionella-containing vacuole prohibiting autophagy adaptor recognitionSemantic proximity Read ↗

Deubiquitination of phosphoribosyl-ubiquitin conjugates by PDE domain-containing <i>Legionella</i> effectorsSemantic proximity Read ↗

Bacterial ubiquitin ligases hijack the host deubiquitinase OTUB1 to inhibit MTORC1 signaling and promote autophagySemantic proximity Read ↗

E3 Ubiquitin Ligase Activity and Targeting of BAT3 by Multiple<i>Legionella pneumophila</i>Translocated SubstratesSemantic proximity Read ↗

The bacterial deubiquitinase Ceg23 regulates the association of Lys-63–linked polyubiquitin molecules on the Legionella phagosomeSemantic proximity Read ↗

Ubiquitin and Legionella: From bench to bedsideSemantic proximity Read ↗

Legionella pneumophila Excludes Autophagy Adaptors from the Ubiquitin-Labeled Vacuole in Which It ResidesSemantic proximity Read ↗

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