ReviewBiomolecules2014
Cullin E3 ligases and their rewiring by viral factors.
Review in Biomolecules, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 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
58 citing papers in PubMed, 105 citations in OpenAlex.
- The vesicular stomatitis virus matrix protein promotes FACT subunit depletion to suppress the FEAR pathway.PLoS pathogens · 2026Article
- The African swine fever virus MGF505-1R protein recruits the cullin-RING-ligase machinery to promote p300 degradation.Npj viruses · 2026Article
- BIK polymorphism and proteasome regulation unveil host risk factor for severe influenza.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Redox-driven regulation of UCHL3/Yuh1 influences mitochondrial health via the NEDD8/Rub1 pathway.Redox biology · 2025Article
- Activation and Evasion of the FEAR Pathway by RNA Viruses.bioRxiv : the preprint server for biology · 2025Article
- Profiling Cullin4-E3 Ligases Interactomes and Their Rewiring in Influenza A Virus Infection.Molecular & cellular proteomics : MCP · 2024Article
- Modelling protein complexes with crosslinking mass spectrometry and deep learning.Nature communications · 2024Article
- Targeted protein degradation: from mechanisms to clinic.Nature reviews. Molecular cell biology · 2024Review
- SARS-CoV-2 Protein Nsp9 Is Involved in Viral Evasion through Interactions with Innate Immune Pathways.ACS omega · 2024Article
- Exploiting the Cullin E3 Ligase Adaptor Protein SKP1 for Targeted Protein Degradation.ACS chemical biology · 2024Article
- B cell expression of E3 ubiquitin ligase Cul4b promotes chronic gammaherpesvirus infectionJournal of virology · 2023Article
- Exploiting the Cullin E3 Ligase Adaptor Protein SKP1 for Targeted Protein Degradation.bioRxiv : the preprint server for biology · 2023Article
- Recognition and reprogramming of E3 ubiquitin ligase surfaces by α-helical peptides.Nature communications · 2023Article
- Genetically Encoded Crosslinking Enables Identification of Multivalent Ubiquitin-Deubiquitylating Enzyme Interactions.Chembiochem : a European journal of chemical biology · 2023Article
- Article
- Targeted protein degradation as an antiviral approach.Antiviral research · 2023Article
- Structural modeling of protein ensembles between E3 RING ligases and SARS-CoV-2: The role of zinc binding domains.Journal of trace elements in medicine and biology : organ of the Society for Minerals and Trace Elements (GMS) · 2023Article
- The SARS-CoV-2 UTR's Intrudes Host RBP's and Modulates Cellular Splicing.Advances in virology · 2023Article
- Elevated ubiquitination contributes to protective immunity against severe SARS-CoV-2 infection.Clinical and translational medicine · 2022Article
- Spectral and theoretical study of SARS-CoV-2 ORF10 protein interaction with endogenous and exogenous macroheterocyclic compounds.Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
The ability of viruses to subvert host pathways is central in disease pathogenesis. Over the past decade, a critical role for the Ubiquitin Proteasome System (UPS) in counteracting host immune factors during viral infection has emerged. This counteraction is commonly achieved by the expression of viral proteins capable of sequestering host ubiquitin E3 ligases and their regulators. In particular, many viruses hijack members of the Cullin-RING E3 Ligase (CRL) family. Viruses interact in many ways with CRLs in order to impact their ligase activity; one key recurring interaction involves re-directing CRL complexes to degrade host targets that are otherwise not degraded within host cells. Removal of host immune factors by this mechanism creates a more amenable cellular environment for viral propagation. To date, a small number of target host factors have been identified, many of which are degraded via a CRL-proteasome pathway. Substantial effort within the field is ongoing to uncover the identities of further host proteins targeted in this fashion and the underlying mechanisms driving their turnover by the UPS. Elucidation of these targets and mechanisms will provide appealing anti-viral therapeutic opportunities. This review is focused on the many methods used by viruses to perturb host CRLs, focusing on substrate sequestration and viral regulation of E3 activity.
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What OpenQuestion 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 OpenQuestion graph.