Evidence map›Paper›PMID 20219914›Full record

ArticleJournal of virology2010

Influenza virus m2 ion channel protein is necessary for filamentous virion formation.

Jeremy S Rossman, Xianghong Jing, George P Leser, Victoria Balannik, Lawrence H Pinto, Robert A Lamb

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 125 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
125citing papers in PubMed, 1 pooled it
12.0field-weighted citation impact, top 1% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

125 citing papers in PubMed, 1 synthesis or guideline pooled it, 197 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Review
  5. Molecular architecture of Influenza A virions.bioRxiv : the preprint server for biology · 2026
    Article
  6. Article
  7. Implications of morphological variation in influenza viruses.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  8. Article
  9. The Role of Cholesterol in M2 Clustering and Viral Budding Explained.Journal of chemical theory and computation · 2025
    Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Antiviral Approaches against Influenza Virus.Clinical microbiology reviews · 2023
    Review
  20. Article

65 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 2 countries.

Jeremy S RossmanDepartment of Biochemistry, Molecular Biology, and Cell Biology, and Howard Hughes Medical Institute, Northwestern University, Evanston, Illinois 60208-3500, USA.
Xianghong Jing
George P Leser
Victoria Balannik
Lawrence H Pinto
Robert A Lamb
Institute of Molecular and Cell Biology · RUNorthwestern University · USHoward Hughes Medical Institute · US

Funding

The Structure and Function of the Influenza Virus GenomeR01AI020201 · NIAID · NORTHWESTERN UNIVERSITY · PI LAMB, ROBERT A · 1985 to 2016
$2.8M
Howard Hughes Medical InstituteNIAID NIH HHS R01 AI020201NIAID NIH HHS R01 AI-20201
6 · The paper itself

Abstract

Influenza A virus buds from cells as spherical (approximately 100-nm diameter) and filamentous (approximately 100 nm x 2 to 20 microm) virions. Previous work has determined that the matrix protein (M1) confers the ability of the virus to form filaments; however, additional work has suggested that the influenza virus M2 integral membrane protein also plays a role in viral filament formation. In examining the role of the M2 protein in filament formation, we observed that the cytoplasmic tail of M2 contains several sites that are essential for filament formation. Additionally, whereas M2 is a nonraft protein, expression of other viral proteins in the context of influenza virus infection leads to the colocalization of M2 with sites of virus budding and lipid raft domains. We found that an amphipathic helix located within the M2 cytoplasmic tail is able to bind cholesterol, and we speculate that M2 cholesterol binding is essential for both filament formation and the stability of existing viral filaments.

Indexed as

Virus AssemblyAmino Acid SequenceAnimalsCell LineCholesterolDogsHumansInfluenza A virusMicroscopy, ElectronMicroscopy, FluorescenceMolecular Sequence DataProtein BindingViral Matrix ProteinsVirionViroporin ProteinsCholesterolM2 protein, Influenza A virusViral Matrix ProteinsViroporin Proteins

Identifiers

PMID20219914
PMCPMC2863831
OpenAlexW1989788129

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.