ReviewMicrobiological research2020
Modification of the host ubiquitome by bacterial enzymes.
Review in Microbiological research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
15 citing papers in PubMed, 20 citations in OpenAlex.
- Proteasome-dependent cytoskeleton disruption during Leptospira interrogans infection induces aberrant collective cell migration.PLoS pathogens · 2026Article
- Mapping of Phenotype Specific Host-Microbiome Protein-Protein Interaction Networks in Colorectal Cancer Using Deep Learning.International journal of molecular sciences · 2026Article
- Mechanistic basis for protein conjugation in a diverged bacterial ubiquitination pathway.Nature structural & molecular biology · 2026Article
- The ubiquitin system targets translocated EspH to proteasomal degradation.Gut microbes · 2025Article
- Article
- Structural diversity and oligomerization of bacterial ubiquitin-like proteins.Structure (London, England : 1993) · 2025Article
- Article
- Review
- Legionella pneumophila-mediated host posttranslational modifications.Journal of molecular cell biology · 2023Review
- Genetically Encoded Crosslinking Enables Identification of Multivalent Ubiquitin-Deubiquitylating Enzyme Interactions.Chembiochem : a European journal of chemical biology · 2023Article
- The Attenuation Mechanism and Live Vaccine Potential of a Low-VirulenceJournal of microbiology and biotechnology · 2023Article
- Structural Basis of Ubiquitin Recognition by a Bacterial Ovarian Tumor Deubiquitinase LotA.Journal of bacteriology · 2022Article
- Non-lysine ubiquitylation: Doing things differently.Frontiers in molecular biosciences · 2022Review
- A Brief Introduction to Effector-Triggered Immunity.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Diverse ubiquitin codes in the regulation of inflammatory signaling.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2020Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Attachment of ubiquitin molecules to protein substrates is a reversible post-translational modification (PTM), which occurs ubiquitously in eukaryotic cells and controls most cellular processes. As a consequence, ubiquitination is an attractive target of pathogen-encoded virulence factors. Pathogenic bacteria have evolved multiple mechanisms to hijack the host's ubiquitin system to their advantage. In this review, we discuss the bacteria-encoded E3 ligases and deubiquitinases translocated to the host for an addition or removal of eukaryotic ubiquitin modification, effectively hijacking the host's ubiquitination processes. We review bacterial enzymes homologous to host proteins in sequence and functions, as well as enzymes with novel mechanisms in ubiquitination, which have significant structural differences in comparison to the mammalian E3 ligases. Finally, we will also discuss examples of molecular "counter-weapons" - eukaryotic proteins, which counteract pathogen-encoded E3 ligases. The many examples of the pathogen effector molecules that catalyze eukaryotic ubiquitin modification bring to light the intricate pathways involved in the pathogenesis of some of the most virulent bacterial infections with human pathogens. The role of these effector molecules remains an essential determinant of bacterial virulence in terms of infection, invasion, and replication. A comprehensive understanding of the mechanisms dictating the mimicry employed by bacterial pathogens is of vital importance in developing new strategies for therapeutic approaches.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.