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

E3 Ubiquitin Ligase Activity and Targeting of BAT3 by Multiple<i>Legionella pneumophila</i>Translocated Substrates

15 Jun 2010

Abstract excerpt

The intracellular bacterial pathogen Legionella pneumophila modulates a number of host processes during intracellular growth, including the eukaryotic ubiquitination machinery, which dictates the stability, activity, and/or localization of a large number of proteins. A number of L. pneumophila proteins contain eukaryotic-like motifs typically associated with ubiquitination. Central among these is a family of five...

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 Legionella and Acanthamoeba research
Share to Toxoplasma gondii Research Studies

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 20547746
DOI: 10.1128/iai.00344-10

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

E3 Ubiquitin Ligase Activity and Targeting of BAT3 by Multiple<i>Legionella pneumophila</i>Translocated SubstratesPMID 20547746Read ↗

<i>Legionella</i> translocates an E3 ubiquitin ligase that has multiple U‐boxes with distinct functionsSemantic proximity Read ↗

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

Evolution and Adaptation of Legionella pneumophila to Manipulate the Ubiquitination Machinery of Its Amoebae and Mammalian HostsSemantic proximity Read ↗

Legionella Manipulates Non-canonical SNARE Pairing Using a Bacterial DeubiquitinaseSemantic proximity Read ↗

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

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

The Legionella pneumophila F-box protein Lpp2082 (AnkB) modulates ubiquitination of the host protein parvin B and promotes intracellular replicationSemantic proximity Read ↗

Discovery of Ubiquitin Deamidases in the Pathogenic Arsenal of Legionella pneumophilaSemantic proximity Read ↗

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

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

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

Effector-mediated subversion of proteasome activator (PA)28αβ enhances host defense against <i>Legionella pneumophila</i> under inflammatory and oxidative stress conditionsSemantic proximity Read ↗

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