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

Paramyxovirus fusion (F) protein: a conformational change on cleavage activation.

Virology - 1 Mar 2001

Dutch R E, Hagglund R N, Nagel M A, Paterson R G, Lamb R A

Abstract excerpt

The fusion (F) protein of the paramyxovirus SV5 promotes both virus-cell and cell-cell fusion. Recently, the atomic structure at 1.4 A of an extremely thermostable six-helix bundle core complex consisting of two heptad repeat regions of the F protein has been described (K. A. Baker, R. E. Dutch, R. A. Lamb, and T. S Jardetsky, Mol. Cell 3, 309-319, 1999). To analyze the conformations of the F protein at various...

Read the complete abstract on PubMed

Topics

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

Share to Immune Sera
Share to Membrane Fusion
Share to Papain

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

Share to Repetitive Sequences, Amino Acid

Share to Respirovirus

Share to Succinimides

Share to Trypsin

Share to Viral Fusion Proteins

Source

Identifiers

PMID: 11222104
DOI: 10.1006/viro.2000.0817

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

Paramyxovirus fusion (F) protein: a conformational change on cleavage activation.PMID 11222104Read ↗

The paramyxovirus fusion protein C-terminal region: mutagenesis indicates an indivisible protein unit.Semantic proximity Read ↗

Spring-loaded heptad repeat residues regulate the expression and activation of paramyxovirus fusion protein.Semantic proximity Read ↗

A conserved region in the F(2) subunit of paramyxovirus fusion proteins is involved in fusion regulation.Semantic proximity Read ↗

Fusion protein of the paramyxovirus SV5: destabilizing and stabilizing mutants of fusion activation.Semantic proximity Read ↗

Mutants of the paramyxovirus SV5 fusion protein: regulated and extensive syncytium formation.Semantic proximity Read ↗

Paramyxovirus fusion protein: characterization of the core trimer, a rod-shaped complex with helices in anti-parallel orientation.Semantic proximity Read ↗

Functional analysis of the transmembrane domain in paramyxovirus F protein-mediated membrane fusion.Semantic proximity Read ↗

Mutations in the fusion peptide and adjacent heptad repeat inhibit folding or activity of the Newcastle disease virus fusion protein.Semantic proximity Read ↗

A Quantitative and Kinetic Fusion Protein-Triggering Assay Can Discern Distinct Steps in the Nipah Virus Membrane Fusion CascadeSemantic proximity Read ↗

Reversible inhibition of fusion activity of a paramyxovirus fusion protein by an engineered disulfide bond in the membrane-proximal external region.Semantic proximity Read ↗

Functional interaction between paramyxovirus fusion and attachment proteins.Semantic proximity Read ↗

Reversible inhibition of the fusion activity of measles virus F protein by an engineered intersubunit disulfide bridge.Semantic proximity Read ↗

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