(Q45743706)

English

The C-terminal third of human respiratory syncytial virus attachment (G) protein is partially resistant to protease digestion and is glycosylated in a cell-type-specific manner

scientific article published in April 2000

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scholarly article

1 reference

Europe PubMed Central

15 December 2017

http://europepmc.org/abstract/MED/10725417

The C-terminal third of human respiratory syncytial virus attachment (G) protein is partially resistant to protease digestion and is glycosylated in a cell-type-specific manner (English)

1 reference

Europe PubMed Central

15 December 2017

http://europepmc.org/abstract/MED/10725417

1 reference

based on heuristic

inferred from title

respiratory syncytial virus

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RSV major surface glycoprotein G

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author name string

García-Beato R

1

1 reference

Europe PubMed Central

15 December 2017

http://europepmc.org/abstract/MED/10725417

Melero JA

2

1 reference

Europe PubMed Central

15 December 2017

http://europepmc.org/abstract/MED/10725417

language of work or name

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publication date

1 April 2000

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Europe PubMed Central

15 December 2017

http://europepmc.org/abstract/MED/10725417

Journal of General Virology

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Europe PubMed Central

15 December 2017

http://europepmc.org/abstract/MED/10725417

81

1 reference

Europe PubMed Central

15 December 2017

http://europepmc.org/abstract/MED/10725417

919-927

1 reference

Europe PubMed Central

15 December 2017

http://europepmc.org/abstract/MED/10725417

Pt 4

1 reference

Europe PubMed Central

15 December 2017

http://europepmc.org/abstract/MED/10725417

Antigenic structure, evolution and immunobiology of human respiratory syncytial virus attachment (G) protein

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The membrane-associated and secreted forms of the respiratory syncytial virus attachment glycoprotein G are synthesized from alternative initiation codons

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Nucleotide sequence of the G protein gene of human respiratory syncytial virus reveals an unusual type of viral membrane protein

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Host cell effect upon glycosylation and antigenicity of human respiratory syncytial virus G glycoprotein.

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The G protein of human respiratory syncytial virus: significance of carbohydrate side-chains and the C-terminal end to its antigenicity

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Respiratory syncytial virus

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Frame shift mutations as a novel mechanism for the generation of neutralization resistant mutants of human respiratory syncytial virus.

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10.1099/0022-1317-81-4-919

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1 reference

Europe PubMed Central

15 December 2017

http://europepmc.org/abstract/MED/10725417

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