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

Mutational Analysis of the Putative Fusion Domain of Ebola Virus Glycoprotein

1 Oct 1999

Abstract excerpt

Ebola viruses contain a single glycoprotein (GP) spike, which functions as a receptor binding and membrane fusion protein. It contains a highly conserved hydrophobic region (amino acids 524 to 539) located 24 amino acids downstream of the N terminus of the Ebola virus GP2 subunit. Comparison of this region with the structural features of the transmembrane subunit of avian retroviral GPs suggests that the...

Read the complete abstract on PubMed

Topics

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

Share to Viral Infections and Outbreaks Research
Share to Viral Infections and Vectors
Share to Virology and Viral Diseases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 10482652
DOI: 10.1128/jvi.73.10.8907-8912.1999

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutational Analysis of the Putative Fusion Domain of Ebola Virus GlycoproteinPMID 10482652Read ↗

Comprehensive Analysis of Ebola Virus GP1 in Viral EntrySemantic proximity Read ↗

A Polymorphism within the Internal Fusion Loop of the Ebola Virus Glycoprotein Modulates Host Cell Entry.Semantic proximity Read ↗

Functional importance of the coiled-coil of the Ebola virus glycoprotein.Semantic proximity Read ↗

Less Is More: Ebola Virus Surface Glycoprotein Expression Levels Regulate Virus Production and InfectivitySemantic proximity Read ↗

Growth-Adaptive Mutations in the Ebola Virus Makona Glycoprotein Alter Different Steps in the Virus Entry Pathway.Semantic proximity Read ↗

A Glycoprotein Mutation That Emerged during the 2013-2016 Ebola Virus Epidemic Alters Proteolysis and Accelerates Membrane Fusion.Semantic proximity Read ↗

A glycoprotein mutation that emerged during the 2013-2016 Ebola virus epidemic alters proteolysis and accelerates membrane fusionSemantic proximity Read ↗

Structural basis for membrane fusion by enveloped virusesSemantic proximity Read ↗

A system for functional analysis of Ebola virus glycoproteinSemantic proximity Read ↗

Ebolavirus Glycoprotein GP Masks both Its Own Epitopes and the Presence of Cellular Surface ProteinsSemantic proximity Read ↗

Identification of Ebola Virus Inhibitors Targeting GP2 Using Principles of Molecular MimicrySemantic proximity Read ↗

Reverse Genetics Demonstrates that Proteolytic Processing of the Ebola Virus Glycoprotein Is Not Essential for Replication in Cell CultureSemantic proximity Read ↗

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