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

Variable Surface Epitopes in the Crystal Structure of Dengue Virus Type 3 Envelope Glycoprotein

21 Dec 2004

Abstract excerpt

Dengue virus is an emerging global health threat. The major envelope glycoprotein, E, mediates viral attachment and entry by membrane fusion. Antibodies that bind but fail to neutralize noncognate serotypes enhance infection. We have determined the crystal structure of a soluble fragment of the envelope glycoprotein E from dengue virus type 3. The structure closely resembles those of E proteins from dengue type 2...

Read the complete abstract on PubMed

Topics

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

Share to Insect symbiosis and bacterial influences
Share to Mosquito-borne diseases and control
Share to Viral Infections and Vectors

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 15613349
DOI: 10.1128/jvi.79.2.1223-1231.2005

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Variable Surface Epitopes in the Crystal Structure of Dengue Virus Type 3 Envelope GlycoproteinPMID 15613349Read ↗

Characterization of Dengue Virus Complex-Specific Neutralizing Epitopes on Envelope Protein Domain III of Dengue 2 VirusSemantic proximity Read ↗

Recognition determinants of broadly neutralizing human antibodies against dengue viruses.Semantic proximity Read ↗

Natural strain variation and antibody neutralization of dengue serotype 3 viruses.Semantic proximity Read ↗

Genotype-specific neutralization and protection by antibodies against dengue virus type 3.Semantic proximity Read ↗

A highly potent human antibody neutralizes dengue virus serotype 3 by binding across three surface proteins.Semantic proximity Read ↗

Type- and Subcomplex-Specific Neutralizing Antibodies against Domain III of Dengue Virus Type 2 Envelope Protein Recognize Adjacent EpitopesSemantic proximity Read ↗

Genetic diversity of the E protein of dengue type 3 virus.Semantic proximity Read ↗

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

Mapping to completeness and transplantation of a group-specific, discontinuous, neutralizing epitope in the envelope protein of dengue virusSemantic proximity Read ↗

Characterization of dengue complex-reactive epitopes on dengue 3 virus envelope protein domain IIISemantic proximity Read ↗

Characterization of a dengue type-specific epitope on dengue 3 virus envelope protein domain IIISemantic proximity Read ↗

Antibody recognition and neutralization determinants on domains I and II of West Nile Virus envelope protein.Semantic proximity Read ↗

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