ReviewNature reviews. Microbiology2012
Viroporins: structure and biological functions.
Review in Nature reviews. Microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 309 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.
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Who cites it
309 citing papers in PubMed.
- Enterovirus 2B protein: From viroporin to membrane stress sensor, mechanistic principles of multi-pathway regulation.Virulence · 2027Review
- Review
- Structural Bases for the Unconventional Activity of a Viroporin Channel.Biochemistry · 2026Article
- A WEEV 6K viroporin activates MLKL-dependent necroptosis to drive inflammatory injury.Cell death discovery · 2026Article
- Article
- Poliovirus 3Dpol polymerase region is essential for cleavage of poliovirus 3AB in vivo.PLoS pathogens · 2026Article
- Review
- Migrasome-driven mitocytosis relieves mitochondrial damage induced by chikungunya virus TF and 6K.hLife · 2026Article
- A recurrent adaptive mutation in the transmembrane 2B protein of an insect picorna-like virus in a nonnative host.Journal of virology · 2026Article
- Conserved Transmembrane Asparagine Is Essential for the Ion-Conducting Structure and Dynamics of the SARS-CoV-2 Envelope Protein.Journal of the American Chemical Society · 2026Article
- Comparative Genomics of Viral Genomes and Identification of Three Novel Viroporin-Like Superfamilies.Microbial physiology · 2026Article
- Targeting the US21 viroporin of human cytomegalovirus by calcium channel blockers as a new antiviral strategy.Current research in microbial sciences · 2026Article
- Lipid-driven alignment and binding of p7 dimers in early oligomer assembly.PLoS computational biology · 2025Article
- The B169L protein of African swine fever virus functions as a viroporin that activates the calcium-mediated inflammasome.PLoS pathogens · 2025Article
- The citrus tristeza virus p33 protein functions as a viroporin.PLoS pathogens · 2025Article
- Antiviral nanomedicine: Advantages, mechanisms and advanced therapies.Bioactive materials · 2025Review
- Ion-Channel-Targeting Drugs for Chikungunya Virus.Molecules (Basel, Switzerland) · 2025Article
- Viroporins: emerging viral infection mechanisms and therapeutic targets.Journal of virology · 2025Review
- The Small Cysteine-Rich Protein of Potato Mop-Top Virus Exhibits Viroporin Activity.Molecular plant pathology · 2025Article
- Review
249 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Viroporins are small, hydrophobic proteins that are encoded by a wide range of clinically relevant animal viruses. When these proteins oligomerize in host cell membranes, they form hydrophilic pores that disrupt a number of physiological properties of the cell. Viroporins are crucial for viral pathogenicity owing to their involvement in several diverse steps of the viral life cycle. Thus, these viral proteins, which include influenza A virus matrix protein 2 (M2), HIV-1 viral protein U (Vpu) and hepatitis C virus p7, represent ideal targets for therapeutic intervention, and several compounds that block their pore-forming activity have been identified. Here, we review recent studies in the field that have advanced our knowledge of the structure and function of this expanding family of viral proteins.
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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.