ArticleVirus genes2017
Cellular interactome analysis of vaccinia virus K7 protein identifies three transport machineries as binding partners for K7.
Article in Virus genes, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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.
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Who cites it
8 citing papers in PubMed, 11 citations in OpenAlex.
- The Viral Protein K7 Inhibits Biochemical Activities and Condensate Formation by the DEAD-box Helicase DDX3X.Journal of molecular biology · 2023Article
- Selective events at individual sites underlie the evolution of monkeypox virus clades.Virus evolution · 2023Article
- The emerging roles of retromer and sorting nexins in the life cycle of viruses.Virologica Sinica · 2022Review
- The actin nucleator Spir-1 is a virus restriction factor that promotes innate immune signalling.PLoS pathogens · 2022Article
- Toward Understanding the Molecular Role of SNX27/Retromer in Human Health and Disease.Frontiers in cell and developmental biology · 2021Review
- Intraviral interactome of Chikungunya virus reveals the homo-oligomerization and palmitoylation of structural protein TF.Biochemical and biophysical research communications · 2019Article
- Elucidating the Host Interactome of EV-A71 2C Reveals Viral Dependency Factors.Frontiers in microbiology · 2019Article
- Emerging Role of Retromer in Modulating Pathogen Growth.Trends in microbiology · 2018Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Identification of viral-host interacting proteins will contribute to understanding of how poxvirus exploits the host cellular machinery. The vaccinia virus gene K7R encodes a conserved protein K7 in most orthopoxviruses. To gain insight into the biology of K7, we investigated the cellular interactome of K7 by GST pulldown coupled with mass spectrometry. The top categories of identified proteins contained components of trafficking machineries. We selected key components of three transport machineries including coatomer, retromer, and CHEVI to further confirm their binding abilities to K7. Di-lysine motif of K7 is required for its interaction with coatomer, while C terminal leucines in K7 are critical for association of retromer. Our study uncovers the viral-host interactome of vaccinia K7 and reveals three host transport machineries as binding partners of K7, which might have important roles in poxvirus' life cycles.
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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.