The influenza A virus hemagglutinin glycosylation state affects receptor-binding specificity (Q39707715)

14 September 2017

title

The influenza A virus hemagglutinin glycosylation state affects receptor-binding specificity (English)

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14 September 2017

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influenza A virus

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5

Peter J M Rottier

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14 September 2017

3

Berend Jan Bosch

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14 September 2017

1

Robert P de Vries

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14 September 2017

Cornelis A. M. de Haan

series ordinal

6

object named as

Cornelis A M de Haan

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14 September 2017

2

Erik de Vries

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14 September 2017

Raoul J de Groot

4

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14 September 2017

language of work or name

English

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publication date

2 May 2010

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14 September 2017

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14 September 2017

volume

403

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14 September 2017

issue

1

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14 September 2017

page(s)

17-25

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Printed covalent glycan array for ligand profiling of diverse glycan binding proteins

14 September 2017

cites work

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Neuraminidase Is Essential for Fowl Plague Virus Hemagglutinin to Show Hemagglutinating Activity

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Structure and function in rhodopsin: high-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line

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

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

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N-linked glycosylation attenuates H3N2 influenza viruses

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Glycans on influenza hemagglutinin affect receptor binding and immune response

7 January 2021

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7 January 2021

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Oligosaccharides in the stem region maintain the influenza virus hemagglutinin in the metastable form required for fusion activity.

7 January 2021

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Regulation of receptor binding affinity of influenza virus hemagglutinin by its carbohydrate moiety

7 January 2021

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inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1016/J.VIROL.2010.03.047

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14 September 2017

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