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Article

Mutations in a conserved residue in the influenza virus neuraminidase active site decreases sensitivity to Neu5Ac2en-derived inhibitors.

Journal of virology - 1 Mar 1998

McKimm-Breschkin J L, Sahasrabudhe A, Blick T J, McDonald M, Colman P M, Hart G J, Bethell R C, Varghese J N

Abstract excerpt

The influenza virus neuraminidase (NA)-specific inhibitor zanamivir (4-guanidino-Neu5Ac2en) is effective in humans when administered topically within the respiratory tract. The search for compounds with altered pharmacological properties has led to the identification of a novel series of influenza virus NA inhibitors in which the triol group of zanamivir has been replaced by a hydrophobic group linked by a...

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Identifiers

PMID: 9499107
DOI: 10.1128/JVI.72.3.2456-2462.1998
PMCID: PMC109546

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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