(Q27679987)

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A Unique and Conserved Neutralization Epitope in H5N1 Influenza Viruses Identified by an Antibody against the A/Goose/Guangdong/1/96 Hemagglutinin

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A Unique and Conserved Neutralization Epitope in H5N1 Influenza Viruses Identified by an Antibody against the A/Goose/Guangdong/1/96 Hemagglutinin (English)

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1 reference

based on heuristic

inferred from title

5

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10

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ORCID Public Data File 2021

11

object named as

Cheng-Feng Qin

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6

object named as

Xiao-Feng Li

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Ian Andrew Wilson

13

object named as

Ian A Wilson

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2

object named as

Yong-Hui Guo

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12

object named as

Xiao-Yan Che

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author name string

Xueyong Zhu

1

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Tao Jiang

3

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Ya-Di Wang

4

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Wenli Yu

7

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Ryan McBride

8

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James C Paulson

9

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publication date

December 2013

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Journal of Virology

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87

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23

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12619-35

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Hemagglutinin homologue from H17N10 bat influenza virus exhibits divergent receptor-binding and pH-dependent fusion activities

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Antibody recognition of a highly conserved influenza virus epitope

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Structural evidence for recognition of a single epitope by two distinct antibodies

1 reference

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Antigen distortion allows influenza virus to escape neutralization

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1 reference

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H5N1 receptor specificity as a factor in pandemic risk

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Unraveling of a neutralization mechanism by two human antibodies against conserved epitopes in the globular head of H5 hemagglutinin

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Recent advances in neuraminidase inhibitor development as anti-influenza drugs

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Two glycosylation sites in H5N1 influenza virus hemagglutinin that affect binding preference by computer-based analysis

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A human antibody recognizing a conserved epitope of H5 hemagglutinin broadly neutralizes highly pathogenic avian influenza H5N1 viruses.

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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10.1128/JVI.01577-13

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