ReviewJournal of cell science2017
Exploitation of the host cell ubiquitin machinery by microbial effector proteins.
Review in Journal of cell science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
50 citing papers in PubMed.
- Histone modification cross talk between a host and pathogen.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- The ubiquitin system targets translocated EspH to proteasomal degradation.Gut microbes · 2025Article
- A microsporidial deubiquitinase blocks ubiquitin transfer from adenylated E1 to human UBE2K ubiquitin conjugating enzyme.bioRxiv : the preprint server for biology · 2025Article
- Fumarylacetoacetate hydrolase targeted by a Fusarium graminearum effector positively regulates wheat FHB resistance.Nature communications · 2025Article
- Phosphoribosyl modification of poly-ubiquitin chains at the Legionella-containing vacuole prohibiting autophagy adaptor recognition.Nature communications · 2024Article
- Bacterial usurpation of the OTU deubiquitinase fold.The FEBS journal · 2024Review
- Multi-tiered actions ofeLife · 2024Article
- Article
- Target degradation specificity of phytoplasma effector phyllogen is regulated by the recruitment of host proteasome shuttle protein.Molecular plant pathology · 2024Article
- 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
- Structural insights into ubiquitin chain cleavage byLife science alliance · 2023Article
- The emerging role and therapeutic implications of bacterial and parasitic deubiquitinating enzymes.Frontiers in immunology · 2023Review
- The exploitation of host autophagy and ubiquitin machinery byAutophagy · 2023Review
- A phytoplasma effector acts as a ubiquitin-like mediator between floral MADS-box proteins and proteasome shuttle proteins.The Plant cell · 2022Article
- Article
- Structural Basis of Ubiquitin Recognition by a Bacterial Ovarian Tumor Deubiquitinase LotA.Journal of bacteriology · 2022Article
- The unity of opposites: Strategic interplay between bacterial effectors to regulate cellular homeostasis.The Journal of biological chemistry · 2021Review
- Innate control of adaptive immunity and adaptive instruction of innate immunity: bi-directional flow of information.Current opinion in immunology · 2021Review
- Bacterial effectors mimicking ubiquitin-proteasome pathway tweak plant immunity.Microbiological research · 2021Review
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Pathogenic bacteria are in a constant battle for survival with their host. In order to gain a competitive edge, they employ a variety of sophisticated strategies that allow them to modify conserved host cell processes in ways that favor bacterial survival and growth. Ubiquitylation, the covalent attachment of the small modifier ubiquitin to target proteins, is such a pathway. Ubiquitylation profoundly alters the fate of a myriad of cellular proteins by inducing changes in their stability or function, subcellular localization or interaction with other proteins. Given the importance of ubiquitylation in cell development, protein homeostasis and innate immunity, it is not surprising that this post-translational modification is exploited by a variety of effector proteins from microbial pathogens. Here, we highlight recent advances in our understanding of the many ways microbes take advantage of host ubiquitylation, along with some surprising deviations from the canonical theme. The lessons learned from the in-depth analyses of these host-pathogen interactions provide a fresh perspective on an ancient post-translational modification that we thought was well understood.This article is part of a Minifocus on Ubiquitin Regulation and Function. For further reading, please see related articles: 'Mechanisms of regulation and diversification of deubiquitylating enzyme function' by Pawel Leznicki and Yogesh Kulathu (
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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.