Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Effect of an Asparagine-to-Serine Mutation at Position 294 in Neuraminidase on the Pathogenicity of Highly Pathogenic H5N1 Influenza A Virus

4 Mar 2011

Abstract excerpt

Like the histidine-to-tyrosine substitution at position 274 in neuraminidase (NA H274Y), an asparagine-to-serine mutation at position 294 in this protein (NA N294S) confers oseltamivir resistance to highly pathogenic H5N1 influenza A viruses. However, unlike viruses with the NA H274Y mutation, the properties of viruses possessing NA N294S are not well understood. Here, we assessed the effect of the NA N294S...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Immune Response and Inflammation
Share to Influenza Virus Research Studies
Share to Respiratory viral infections research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 21367898
DOI: 10.1128/jvi.00047-11

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Effect of an Asparagine-to-Serine Mutation at Position 294 in Neuraminidase on the Pathogenicity of Highly Pathogenic H5N1 Influenza A VirusPMID 21367898Read ↗

Oseltamivir-Resistant Pandemic A/H1N1 Virus Is as Virulent as Its Wild-Type Counterpart in Mice and FerretsSemantic proximity Read ↗

Amino Acid Mutations A286V and T437M in the Nucleoprotein Attenuate H7N9 Viruses in MiceSemantic proximity Read ↗

The R292K Mutation That Confers Resistance to Neuraminidase Inhibitors Leads to Competitive Fitness Loss of A/Shanghai/1/2013 (H7N9) Influenza Virus in FerretsSemantic proximity Read ↗

Influenza virus carrying neuraminidase with reduced sensitivity to oseltamivir carboxylate has altered properties in vitro and is compromised for infectivity and replicative ability in vivo.Semantic proximity Read ↗

Characterization of highly pathogenic avian influenza H5Nx viruses in the ferret model.Semantic proximity Read ↗

Neuraminidase Mutations Conferring Resistance to Oseltamivir in Influenza A(H7N9) Viruses.Semantic proximity Read ↗

Avian Influenza (H5N1) Viruses Isolated from Humans in Asia in 2004 Exhibit Increased Virulence in MammalsSemantic proximity Read ↗

Characterization of oseltamivir-resistant 2009 H1N1 pandemic influenza A viruses.Semantic proximity Read ↗

Novel Avian-Origin Human Influenza A(H7N9) Can Be Transmitted Between Ferrets via Respiratory DropletsSemantic proximity Read ↗

Adaptive amino acid substitutions enhance the virulence of a novel human H7N9 influenza virus in mice.Semantic proximity Read ↗

PA-X I94V mutation modulates the pathogenicity of the highly pathogenic H7N9 influenza A virus in mice and chickens.Semantic proximity Read ↗

Effect of Neuraminidase Inhibitor–Resistant Mutations on Pathogenicity of Clade 2.2 A/Turkey/15/06 (H5N1) Influenza Virus in FerretsSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.