ArticleJournal of virology2008
Ectromelia virus encodes a novel family of F-box proteins that interact with the SCF complex.
Article in Journal of virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 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
26 citing papers in PubMed, 43 citations in OpenAlex.
- Poxviral ANKR/F-box Proteins: Substrate Adapters for Ubiquitylation and More.Pathogens (Basel, Switzerland) · 2022Review
- Poxvirus Interactions with the Host Ubiquitin System.Pathogens (Basel, Switzerland) · 2021Review
- Progress on Poxvirus E3 Ubiquitin Ligases and Adaptor Proteins.Frontiers in immunology · 2021Review
- Novel Class of Viral Ankyrin Proteins Targeting the Host E3 Ubiquitin Ligase Cullin-2.Journal of virology · 2018Article
- Orientia tsutsugamushi Strain Ikeda Ankyrin Repeat-Containing Proteins Recruit SCF1 Ubiquitin Ligase Machinery via Poxvirus-Like F-Box Motifs.Journal of bacteriology · 2015Article
- Poxviral ankyrin proteins.Viruses · 2015Review
- Chlorovirus Skp1-binding ankyrin repeat protein interplay and mimicry of cellular ubiquitin ligase machinery.Journal of virology · 2014Article
- Vaccinia virus virulence factor N1 can be ubiquitylated on multiple lysine residues.The Journal of general virology · 2014Article
- EVM005: an ectromelia-encoded protein with dual roles in NF-κB inhibition and virulence.PLoS pathogens · 2014Article
- Poxviruses and the evolution of host range and virulence.Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases · 2014Review
- Genetic screen of a mutant poxvirus library identifies an ankyrin repeat protein involved in blocking induction of avian type I interferon.Journal of virology · 2013Article
- Genetic screen of a library of chimeric poxviruses identifies an ankyrin repeat protein involved in resistance to the avian type I interferon response.Journal of virology · 2013Article
- Orthopoxvirus genes that mediate disease virulence and host tropism.Advances in virology · 2012Article
- Regulation of vaccinia virus E3 protein by small ubiquitin-like modifier proteins.Journal of virology · 2011Article
- Viral takeover of the host ubiquitin system.Frontiers in microbiology · 2011Article
- A vaccinia virus deletion mutant reveals the presence of additional inhibitors of NF-kappaB.Journal of virology · 2011Article
- Review
- Article
- Structure function studies of vaccinia virus host range protein k1 reveal a novel functional surface for ankyrin repeat proteins.Journal of virology · 2010Article
- MNF, an ankyrin repeat protein of myxoma virus, is part of a native cellular SCF complex during viral infection.Virology journal · 2010Article
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
Poxviruses are notorious for encoding multiple proteins that regulate cellular signaling pathways, including the ubiquitin-proteasome system. Bioinformatics indicated that ectromelia virus, the causative agent of lethal mousepox, encoded four proteins, EVM002, EVM005, EVM154, and EVM165, containing putative F-box domains. In contrast to cellular F-box proteins, the ectromelia virus proteins contain C-terminal F-box domains in conjunction with N-terminal ankyrin repeats, a combination that has not been previously reported for cellular proteins. These observations suggested that the ectromelia virus F-box proteins interact with SCF (Skp1, cullin-1, and F-box) ubiquitin ligases. We focused our studies on EVM005, since this protein had only one ortholog in cowpox virus. Using mass spectrometry, we identified cullin-1 as a binding partner for EVM005, and this interaction was confirmed by overexpression of hemagglutinin (HA)-cullin-1. During infection, Flag-EVM005 and HA-cullin-1 colocalized to distinct cellular bodies. Significantly, EVM005 coprecipitated with endogenous Skp1, cullin-1, and Roc1 and associated with conjugated ubiquitin, suggesting that EVM005 interacted with the components of a functional ubiquitin ligase. Interaction of EVM005 with cullin-1 and Skp1 was abolished upon deletion of the F-box, indicating that the F-box played a crucial role in interaction with the SCF complex. Additionally, EVM002 and EVM154 interacted with Skp1 and conjugated ubiquitin, suggesting that ectromelia virus encodes multiple F-box-containing proteins that regulate the SCF complex. Our results indicate that ectromelia virus has evolved multiple proteins that interact with the SCF complex.
Indexed as
Identifiers
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.