Glycosylation focuses sequence variation in the influenza A virus H1 hemagglutinin globular domain. (Q33760809)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21124818%20AND%20SRC:MED&resulttype=core&format=json

17 January 2020

title

Glycosylation focuses sequence variation in the influenza A virus H1 hemagglutinin globular domain (English)

1 reference

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17 January 2020

1 reference

influenza A virus

1 reference

2

1 reference

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17 January 2020

6

Jonathan W Yewdell

1 reference

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17 January 2020

1

Suman R Das

1 reference

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17 January 2020

author name string

Scott E Hensley

series ordinal

3

1 reference

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17 January 2020

Darrell E Hurt

series ordinal

4

1 reference

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17 January 2020

Jack R Bennink

series ordinal

5

1 reference

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17 January 2020

publication date

24 November 2010

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17 January 2020

1 reference

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17 January 2020

volume

6

1 reference

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17 January 2020

issue

11

1 reference

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17 January 2020

page(s)

e1001211

1 reference

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Creative Commons CC0 License

17 January 2020

copyright license

start time

24 November 2010

1 reference

April 2022 Public Data File from Crossref

copyright status

copyrighted, dedicated to the public domain by copyright holder

0 references

cites work

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Evolutionary dynamics of N-glycosylation sites of influenza virus hemagglutinin.

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Glycans on influenza hemagglutinin affect receptor binding and immune response

14 July 2018

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Structure and receptor specificity of the hemagglutinin from an H5N1 influenza virus

14 July 2018

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Tracking global patterns of N-linked glycosylation site variation in highly variable viral glycoproteins: HIV, SIV, and HCV envelopes and influenza hemagglutinin

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N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin.

14 July 2018

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Effect of addition of new oligosaccharide chains to the globular head of influenza A/H2N2 virus haemagglutinin on the intracellular transport and biological activities of the molecule

14 July 2018

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Importance of hemagglutinin glycosylation for the biological functions of influenza virus

14 July 2018

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N-Glycans attached to the stem domain of haemagglutinin efficiently regulate influenza A virus replication

14 July 2018

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Oligosaccharyltransferase is highly specific for the hydroxy amino acid in Asn-Xaa-Thr/Ser

14 July 2018

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Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin

14 July 2018

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Effects of egg-adaptation on the receptor-binding properties of human influenza A and B viruses

14 July 2018

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Effects of glycosylation on the properties and functions of influenza virus hemagglutinin

14 July 2018

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

14 July 2018

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14 July 2018

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Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes.

14 July 2018

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The hydroxy amino acid in an Asn-X-Ser/Thr sequon can influence N-linked core glycosylation efficiency and the level of expression of a cell surface glycoprotein

14 July 2018

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14 July 2018

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14 July 2018

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14 July 2018

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14 July 2018

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14 July 2018

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14 July 2018

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14 July 2018

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14 July 2018

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14 July 2018

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14 July 2018

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Monoclonal antibodies localize events in the folding, assembly, and intracellular transport of the influenza virus hemagglutinin glycoprotein

14 July 2018

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Biases and complex patterns in the residues flanking protein N-glycosylation sites

21 January 2018

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Statistical analysis of the protein environment of N-glycosylation sites: implications for occupancy, structure, and folding.

21 January 2018

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Apparent serological variation within a strain of influenza virus.

21 January 2018

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30 October 2018

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Experience with Vaccination Against Influenza in the Spring of 1947: A Preliminary Report

21 January 2018

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PubMed

https://pubmed.ncbi.nlm.nih.gov/21124818

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1371/JOURNAL.PPAT.1001211

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21124818%20AND%20SRC:MED&resulttype=core&format=json

17 January 2020

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21124818%20AND%20SRC:MED&resulttype=core&format=json

17 January 2020

1 reference