Article

Development of covalent probes to capture <i>Legionella pneumophila</i> effector enzymes

2024-03-19

Abstract excerpt

Upon infection of host cells, Legionella pneumophila releases a multitude of effector enzymes into the cells cytoplasm that hijack a plethora of cellular activities, including the hosts ubiquitination pathways. Effectors belonging to the SidE-family are involved in non-canonical serine phosphoribosyl ubiquitination of host substrate proteins contributing to the formation of a Legionella-containing vacuole that is...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: 20bfcf43-3a77-5546-9e2f-4222a8345eed
DOI: 10.1101/2024.03.19.585531

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Development of covalent probes to capture <i>Legionella pneumophila</i> effector enzymesDOI 10.1101/2024.03.19.585531Read

Covalent Probes To Capture Legionella pneumophila Dup Effector EnzymesSemantic proximity Read

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

Ubiquitin and Legionella: From bench to bedsideSemantic proximity Read

Legionella pneumophila-mediated host posttranslational modificationsSemantic proximity Read

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

Diversity of bacterial manipulation of the host ubiquitin pathwaysSemantic proximity Read

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

The Molecular Basis for Ubiquitin and Ubiquitin-like Specificities in Bacterial Effector Proteases.Semantic proximity Read

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

Engineered Ubiquitin Variants Mitigate Pathogenic Bacterial Ubiquitin Ligase FunctionSemantic proximity Read

Controlled enzymatic synthesis of natural-linkage, defined-length polyubiquitin chains using lysines with removable protecting groups.Semantic proximity Read

Assessing the Suitability of Deubiquitylases As Substrates For Targeted Protein DegradationSemantic proximity Read