ReviewNature reviews. Immunology2026
Ubiquitination and autophagy in host-pathogen interactions: from immune surveillance to therapeutic targeting.
Review in Nature reviews. Immunology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 5 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
5 citing papers in PubMed.
- ChemBioParis 2025: Approaching Biology Through Chemistry in the City of Light.Chembiochem : a European journal of chemical biology · 2026Article
- NRF2 controls a diverse network of antiviral effectors with p62 acting as a central restriction factor effective across virus families.Redox biology · 2026Article
- Interplay between proteostasis pathways and innate immune responses inInfection and immunity · 2026Review
- MCL1 promotes porcine epidemic diarrhea virus replication by modulating arachidonic acid metabolic pathway.PLoS pathogens · 2026Article
- Metagenomic next-generation sequencing reveals airway microbial dysbiosis and functional alterations inFrontiers in cellular and infection microbiology · 2026Article
Corrections and comments
- Erratum issued
Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ubiquitination, the covalent attachment of ubiquitin to proteins and other cellular substrates, is a dynamic post-translational modification that enables cells to rapidly respond to internal and external threats. Beyond its canonical role in targeting proteins for proteasomal degradation, ubiquitination orchestrates the assembly of signalling complexes that regulate innate and adaptive immune responses, modulates inflammatory pathways and directs selective autophagy to eliminate intracellular pathogens through lysosomal degradation. To persist and replicate within the host, viruses, bacteria and parasites have evolved diverse mechanisms to evade, manipulate or exploit the host's ubiquitin and autophagy machinery. Some pathogens subvert these systems to dampen immune surveillance, whereas others co-opt them to facilitate replication or dissemination. In this Review, we examine how ubiquitin and autophagy shape host-pathogen interactions, uncover common and pathogen-specific strategies of immune evasion, and discuss emerging therapeutic approaches that aim to leverage these interconnected pathways to enhance antimicrobial immunity.
Indexed as
Identifiers
41491841What Socratic holds
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 Socratic graph.