Amino acid mutations in the env gp90 protein that modify N-linked glycosylation of the Chinese EIAV vaccine strain enhance resistance to neutralizing antibodies.

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Amino acid mutations in the env gp90 protein that modify N-linked glycosylation of the Chinese EIAV vaccine strain enhance resistance to neutralizing antibodies.

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http://www.wikidata.org/entity/Q38735230

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2016 nî lūn-bûn

@nan

2016年の論文

@ja

2016年論文

@yue

2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

@wuu

2016年论文

@zh

2016年论文

@zh-cn

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Amino acid mutations in the en ...... ce to neutralizing antibodies.

@en

type

Item

label

Amino acid mutations in the en ...... ce to neutralizing antibodies.

@en

prefLabel

Amino acid mutations in the en ...... ce to neutralizing antibodies.

@en

P1476

Amino acid mutations in the en ...... ce to neutralizing antibodies.

@en

P2093

Ping Zhang

http://www.w3.org/2001/XMLSchema#string

Wei Yu

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Wenhua Xiang

http://www.w3.org/2001/XMLSchema#string

Xiaodong Li

http://www.w3.org/2001/XMLSchema#string

Xiue Han

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P2860

Antibody neutralization and escape by HIV-1

Tissue sites of persistent infection and active replication of equine infectious anemia virus during acute disease and asymptomatic infection in experimentally infected equids

Equine infectious anemia virus genomic evolution in progressor and nonprogressor ponies.

Equine infectious anemia virus envelope evolution in vivo during persistent infection progressively increases resistance to in vitro serum antibody neutralization as a dominant phenotype.

Glycosylation of the ENV spike of primate immunodeficiency viruses and antibody neutralization.

Envelope variation as a primary determinant of lentiviral vaccine efficacy.

Genetic Evolution during the development of an attenuated EIAV vaccine

Immune responses and viral replication in long-term inapparent carrier ponies inoculated with equine infectious anemia virus.

Assorted mutations in the envelope gene of simian immunodeficiency virus lead to loss of neutralization resistance against antibodies representing a broad spectrum of specificities.

Combined amino acid mutations occurring in the envelope closely correlate with pathogenicity of EIAV.

P2888

s11262-016-1382-2

P304

814-822

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P31

scholarly article

P356

10.1007/S11262-016-1382-2

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P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P577

2016-08-29T00:00:00Z

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P6179

1045059288

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P698

27572122

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P921

glycosylation