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

Sequential conformational changes in the morbillivirus attachment protein initiate the membrane fusion process.

PLoS pathogens - 1 May 2015

Ader-Ebert Nadine, Khosravi Mojtaba, Herren Michael, Avila Mislay, Alves Lisa, Bringolf Fanny, Örvell Claes, Langedijk Johannes P, Zurbriggen Andreas, Plemper Richard K, Plattet Philippe

Abstract excerpt

Despite large vaccination campaigns, measles virus (MeV) and canine distemper virus (CDV) cause major morbidity and mortality in humans and animals, respectively. The MeV and CDV cell entry system relies on two interacting envelope glycoproteins: the attachment protein (H), consisting of stalk and head domains, co-operates with the fusion protein (F) to mediate membrane fusion. However, how receptor-binding by...

Read the complete abstract on PubMed

Topics

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

Share to Cell Adhesion Molecules
Share to Chlorocebus aethiops

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Membrane Fusion

Share to Protein Interaction Domains and Motifs

Share to Protein Stability

Share to Vero Cells

Share to Virus Attachment

Share to Virus Internalization

Source

Open in PubMed Open full text

Identifiers

PMID: 25946112
DOI: 10.1371/journal.ppat.1004880
PMCID: PMC4422687

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Sequential conformational changes in the morbillivirus attachment protein initiate the membrane fusion process.PMID 25946112Read ↗

Regulatory Role of the Morbillivirus Attachment Protein Head-to-Stalk Linker Module in Membrane Fusion Triggering.Semantic proximity Read ↗

Canine Distemper Virus Infects Canine Keratinocytes and Immune Cells by Using Overlapping and Distinct Regions Located on One Side of the Attachment ProteinSemantic proximity Read ↗

Nearby Clusters of Hemagglutinin Residues Sustain SLAM-Dependent Canine Distemper Virus Entry in Peripheral Blood Mononuclear CellsSemantic proximity Read ↗

Molecular determinants defining the triggering range of prefusion F complexes of canine distemper virus.Semantic proximity Read ↗

Membrane fusion triggering: three modules with different structure and function in the upper half of the measles virus attachment protein stalk.Semantic proximity Read ↗

Measles Virus Fusion Protein: Structure, Function and InhibitionSemantic proximity Read ↗

Antiviral Screen against Canine Distemper Virus-Induced Membrane Fusion ActivitySemantic proximity Read ↗

A Stabilized Headless Measles Virus Attachment Protein Stalk Efficiently Triggers Membrane FusionSemantic proximity Read ↗

Structural and Mechanistic Studies of Measles Virus Illuminate Paramyxovirus EntrySemantic proximity Read ↗

Fusion Activation through Attachment Protein Stalk Domains Indicates a Conserved Core Mechanism of Paramyxovirus Entry into CellsSemantic proximity Read ↗

The heads of the measles virus attachment protein move to transmit the fusion-triggering signal.Semantic proximity Read ↗

The Viral Class II Membrane Fusion Machinery: Divergent Evolution from an Ancestral HeterodimerSemantic proximity Read ↗

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