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

Differential roles of two conserved glycine residues in the fusion peptide of Semliki Forest virus.

Virology - 5 Jan 2001

Shome S G, Kielian M

Abstract excerpt

Semliki Forest Virus (SFV) is an enveloped alphavirus that infects cells by a low-pH-dependent membrane fusion reaction. SFV fusion is catalyzed by the spike protein E1 subunit, which contains a putative fusion peptide between residues 79 and 97. Prior mutagenesis studies demonstrated that an E1 G91D mutation blocks both virus-membrane fusion and the formation of a highly stable E1 trimer believed to be a...

Read the complete abstract on PubMed

Topics

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

Share to Cricetinae
Share to Glycine
Share to Liposomes

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

Share to Membrane Fusion

Share to Peptides

Share to Transcription, Genetic

Share to Viral Fusion Proteins

Share to Virus Assembly

Source

Identifiers

PMID: 11145898
DOI: 10.1006/viro.2000.0688

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 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

Differential roles of two conserved glycine residues in the fusion peptide of Semliki Forest virus.PMID 11145898Read ↗

The conserved glycine residues in the transmembrane domain of the Semliki Forest virus fusion protein are not required for assembly and fusion.Semantic proximity Read ↗

Mechanisms of mutations inhibiting fusion and infection by Semliki Forest virus.Semantic proximity Read ↗

A conserved histidine in the ij loop of the Semliki Forest virus E1 protein plays an important role in membrane fusion.Semantic proximity Read ↗

Novel mutations that control the sphingolipid and cholesterol dependence of the Semliki Forest virus fusion protein.Semantic proximity Read ↗

fus-1, a pH shift mutant of Semliki Forest virus, acts by altering spike subunit interactions via a mutation in the E2 subunit.Semantic proximity Read ↗

Interactions between the transmembrane segments of the alphavirus E1 and E2 proteins play a role in virus budding and fusion.Semantic proximity Read ↗

A recombinant vesicular stomatitis virus bearing a lethal mutation in the glycoprotein gene uncovers a second site suppressor that restores fusion.Semantic proximity Read ↗

The domain I-domain III linker plays an important role in the fusogenic conformational change of the alphavirus membrane fusion protein.Semantic proximity Read ↗

Role of conserved histidine residues in the low-pH dependence of the Semliki Forest virus fusion protein.Semantic proximity Read ↗

Fusion function of the Semliki Forest virus spike is activated by proteolytic cleavage of the envelope glycoprotein precursor p62.Semantic proximity Read ↗

An interaction site of the envelope proteins of Semliki Forest virus that is preserved after proteolytic activation.Semantic proximity Read ↗

Structure and interactions at the viral surface of the envelope protein E1 of Semliki Forest virus.Semantic proximity Read ↗

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