Hemagglutinin variants of influenza A(H1N1)pdm09 virus with reduced affinity for sialic acid receptors.

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Hemagglutinin variants of influenza A(H1N1)pdm09 virus with reduced affinity for sialic acid receptors.

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http://www.wikidata.org/entity/Q42251539

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2013 nî lūn-bûn

@nan

2013年の論文

@ja

2013年論文

@yue

2013年論文

@zh-hant

2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

2013年论文

@zh

2013年论文

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name

Hemagglutinin variants of influenza A

@nl

Hemagglutinin variants of infl ...... ity for sialic acid receptors.

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type

Item

label

Hemagglutinin variants of influenza A

@nl

Hemagglutinin variants of infl ...... ity for sialic acid receptors.

@en

prefLabel

Hemagglutinin variants of influenza A

@nl

Hemagglutinin variants of infl ...... ity for sialic acid receptors.

@en

P1476

Hemagglutinin variants of infl ...... ity for sialic acid receptors.

@en

P2093

A Matos-Patrón

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G Ayora-Talavera

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L Cetina-Montejo

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L Romero-Beltrán

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P2860

Structural Characterization of the Hemagglutinin Receptor Specificity from the 2009 H1N1 Influenza Pandemic

Functional balance of the hemagglutinin and neuraminidase activities accompanies the emergence of the 2009 H1N1 influenza pandemic

A two-amino acid change in the hemagglutinin of the 1918 influenza virus abolishes transmission

Early alterations of the receptor-binding properties of H1, H2, and H3 avian influenza virus hemagglutinins after their introduction into mammals

A single amino acid substitution in 1918 influenza virus hemagglutinin changes receptor binding specificity.

Glycan microarray analysis of the hemagglutinins from modern and pandemic influenza viruses reveals different receptor specificities.

Mutations in H5N1 influenza virus hemagglutinin that confer binding to human tracheal airway epithelium.

Altered receptor specificity and cell tropism of D222G hemagglutinin mutants isolated from fatal cases of pandemic A(H1N1) 2009 influenza virus.

Virulence-associated substitution D222G in the hemagglutinin of 2009 pandemic influenza A(H1N1) virus affects receptor binding.

H7N9 influenza viruses interact preferentially with α2,3-linked sialic acids and bind weakly to α2,6-linked sialic acids.

P2888

s00705-013-1934-x

P304

1207-1211

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scholarly article

P356

10.1007/S00705-013-1934-X

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P433

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P478

159

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P577

2013-12-03T00:00:00Z

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P5875

259114606

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P6179

1013124408

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24297491

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