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Mapping the complete glycoproteome of virion-derived HIV-1 gp120 provides insights into broadly neut...

Mapping the complete glycoproteome of virion-derived HIV-1 gp120 provides insights into broadly neut...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5015092

Mapping the complete glycoproteome of virion-derived HIV-1 gp120 provides insights into broadly neutralizing antibody binding

About this item

Full title

Mapping the complete glycoproteome of virion-derived HIV-1 gp120 provides insights into broadly neutralizing antibody binding

Publisher

London: Nature Publishing Group UK

Journal title

Scientific reports, 2016-09, Vol.6 (1), p.32956, Article 32956

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

The surface envelope glycoprotein (SU) of Human immunodeficiency virus type 1 (HIV-1), gp120
SU
plays an essential role in virus binding to target CD4+ T-cells and is a major vaccine target. Gp120 has remarkably high levels of N-linked glycosylation and there is considerable evidence that this “glycan shield” can help protect the virus from a...

Alternative Titles

Full title

Mapping the complete glycoproteome of virion-derived HIV-1 gp120 provides insights into broadly neutralizing antibody binding

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5015092

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5015092

Other Identifiers

ISSN

2045-2322

E-ISSN

2045-2322

DOI

10.1038/srep32956

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