Evidence map›Paper›PMID 23279894›Full record

ReviewInfluenza and other respiratory viruses2013

Influenza neuraminidase inhibitors: antiviral action and mechanisms of resistance.

Jennifer L McKimm-Breschkin

Abstract readReview
In one paragraph

Review in Influenza and other respiratory viruses, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 184 papers.

0numbers the graph read from it
0cells of the map it votes in
184citing papers in PubMed
–field-weighted citation impact
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

184 citing papers in PubMed.

  1. Trial
  2. Effect of Oral Oseltamivir on Virological Outcomes in Low-risk Adults With Influenza: A Randomized Clinical Trial.Clinical infectious diseases : an official publication of the Infectious Diseases Society of America · 2020
    Trial
  3. Trial
  4. Article
  5. Article
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  8. Review
  9. Article
  10. Review
  11. Fluorescence Imaging of Viral Sialidase Activity Using a Fluorogenic Probe.Advances in experimental medicine and biology · 2026
    Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Anti-Viral Activity of Conessine Against Influenza A Virus.International journal of molecular sciences · 2025
    Article

124 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

1 author.

Jennifer L McKimm-BreschkinCSIRO Materials Science and Engineering, Parkville, Victoria, Australia. mck245@csiro.au

Funding

Mechanisms of influenza NA drug resistanceR01AI062721 · NIAID · COMMONWEALTH SCIENTIFIC & INDUST RES ORG · PI MCKIMM-BRESCHKIN, JENNIFER L · 2006 to 2010
$1.3M
Medical Research CouncilNIAID NIH HHS R01 AI062721PHS HHS R01A1062721
6 · The paper itself

Abstract

There are two major classes of antivirals available for the treatment and prevention of influenza, the M2 inhibitors and the neuraminidase inhibitors (NAIs). The M2 inhibitors are cheap, but they are only effective against influenza A viruses, and resistance arises rapidly. The current influenza A H3N2 and pandemic A(H1N1)pdm09 viruses are already resistant to the M2 inhibitors as are many H5N1 viruses. There are four NAIs licensed in some parts of the world, zanamivir, oseltamivir, peramivir, and a long-acting NAI, laninamivir. This review focuses on resistance to the NAIs. Because of differences in their chemistry and subtle differences in NA structures, resistance can be both NAI- and subtype specific. This results in different drug resistance profiles, for example, the H274Y mutation confers resistance to oseltamivir and peramivir, but not to zanamivir, and only in N1 NAs. Mutations at E119, D198, I222, R292, and N294 can also reduce NAI sensitivity. In the winter of 2007-2008, an oseltamivir-resistant seasonal influenza A(H1N1) strain with an H274Y mutation emerged in the northern hemisphere and spread rapidly around the world. In contrast to earlier evidence of such resistant viruses being unfit, this mutant virus remained fully transmissible and pathogenic and became the major seasonal A(H1N1) virus globally within a year. This resistant A(H1N1) virus was displaced by the sensitive A(H1N1)pdm09 virus. Approximately 0.5-1.0% of community A(H1N1)pdm09 isolates are currently resistant to oseltamivir. It is now apparent that variation in non-active site amino acids can affect the fitness of the enzyme and compensate for mutations that confer high-level oseltamivir resistance resulting in minimal impact on enzyme function.

Indexed as

Drug Resistance, ViralAntiviral AgentsEnzyme InhibitorsHumansInfluenza A Virus, H1N1 SubtypeInfluenza A Virus, H3N2 SubtypeInfluenza A Virus, H5N1 SubtypeInfluenza B virusInfluenza, HumanNeuraminidaseAntiviral AgentsEnzyme InhibitorsNeuraminidase

Identifiers

PMID23279894
PMCPMC4942987

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.