Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Comparative Analysis of the Glycosylation Profiles of Membrane-Anchored HIV-1 Envelope Glycoprotein Trimers and Soluble gp140

28 May 2015

Abstract excerpt

UNLABELLED: The human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein (Env) trimer, which consists of the gp120 and gp41 subunits, is the focus of multiple strategies for vaccine development. Extensive Env glycosylation provides HIV-1 with protection from the immune system, yet the glycans are also essential components of binding epitopes for numerous broadly neutralizing antibodies. Recent studies...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Glycosylation and Glycoproteins Research
Share to HIV Research and Treatment
Share to Monoclonal and Polyclonal Antibodies Research

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Source

Identifiers

PMID: 26018173
DOI: 10.1128/jvi.00628-15

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 25 Oct 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Comparative Analysis of the Glycosylation Profiles of Membrane-Anchored HIV-1 Envelope Glycoprotein Trimers and Soluble gp140PMID 26018173Read ↗

Exploitation of glycosylation in enveloped virus pathobiologySemantic proximity Read ↗

Structure and Role of O-Linked Glycans in Viral Envelope ProteinsSemantic proximity Read ↗

HIV-1 gp120 N-linked glycosylation differs between plasma and leukocyte compartments.Semantic proximity Read ↗

Hyperglycosylated Stable Core Immunogens Designed To Present the CD4 Binding Site Are Preferentially Recognized by Broadly Neutralizing AntibodiesSemantic proximity Read ↗

Engineering, Expression, Purification, and Characterization of Stable Clade A/B Recombinant Soluble Heterotrimeric gp140 ProteinsSemantic proximity Read ↗

Vulnerabilities in coronavirus glycan shields despite extensive glycosylationSemantic proximity Read ↗

Global Mapping of O-Glycosylation of Varicella Zoster Virus, Human Cytomegalovirus, and Epstein-Barr VirusSemantic proximity Read ↗

Dengue Virus Glycosylation: What Do We Know?Semantic proximity Read ↗

Germline VRC01 antibody recognition of a modified clade C HIV-1 envelope trimer and a glycosylated HIV-1 gp120 coreSemantic proximity Read ↗

Evolving roles of glycosylation in the tug-of-war between virus and hostSemantic proximity Read ↗

Structural insights into key sites of vulnerability on <scp>HIV</scp>‐1 Env and influenza <scp>HA</scp>Semantic proximity Read ↗

Conservation, Compensation, and Evolution of N-Linked Glycans in the HIV-1 Group M Subtypes and Circulating Recombinant FormsSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.