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

The human respiratory syncytial virus matrix protein is required for maturation of viral filaments.

Journal of virology - 1 Apr 2012

Mitra Ruchira, Baviskar Pradyumna, Duncan-Decocq Rebecca R, Patel Darshna, Oomens Antonius G P

Abstract excerpt

An experimental system was developed to generate infectious human respiratory syncytial virus (HRSV) lacking matrix (M) protein expression (M-null virus) from cDNA. The role of the M protein in virus assembly was then examined by infecting HEp-2 and Vero cells with the M-null virus and assessing the impact on infectious virus production and viral protein trafficking. In the absence of M, the production of...

Read the complete abstract on PubMed

Topics

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

Share to Cell Surface Extensions
Share to Chlorocebus aethiops

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

Share to Gene Order

Share to Open Reading Frames

Share to Protein Transport

Share to Respiratory Syncytial Virus, Human

Share to Viral Matrix Proteins

Share to Virus Replication

Source

Open in PubMed Open full text

Identifiers

PMID: 22318136
DOI: 10.1128/JVI.06744-11
PMCID: PMC3318654

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

The human respiratory syncytial virus matrix protein is required for maturation of viral filaments.PMID 22318136Read ↗

The respiratory syncytial virus fusion protein targets to the perimeter of inclusion bodies and facilitates filament formation by a cytoplasmic tail-dependent mechanism.Semantic proximity Read ↗

Requirements for Human Respiratory Syncytial Virus Glycoproteins in Assembly and Egress from Infected CellsSemantic proximity Read ↗

Respiratory Syncytial Virus Matrix (M) Protein Interacts with Actin In Vitro and in Cell CultureSemantic proximity Read ↗

Association of respiratory syncytial virus M protein with viral nucleocapsids is mediated by the M2-1 protein.Semantic proximity Read ↗

Host cytoskeleton in respiratory syncytial virus assembly and buddingSemantic proximity Read ↗

Structural Analysis of Respiratory Syncytial Virus Reveals the Position of M2-1 between the Matrix Protein and the Ribonucleoprotein ComplexSemantic proximity Read ↗

Helical ordering of envelope‐associated proteins and glycoproteins in respiratory syncytial virusSemantic proximity Read ↗

Cryotomography of Budding Influenza A Virus Reveals Filaments with Diverse Morphologies that Mostly Do Not Bear a Genome at Their Distal EndSemantic proximity Read ↗

Imaging analysis reveals budding of filamentous human metapneumovirus virions and direct transfer of inclusion bodies through intercellular extensionsSemantic proximity Read ↗

Roles for the cytoplasmic tails of the fusion and hemagglutinin-neuraminidase proteins in budding of the paramyxovirus simian virus 5.Semantic proximity Read ↗

Dynamics of filamentous viral RNPs prior to egressSemantic proximity Read ↗

Structural landscape of the respiratory syncytial virus nucleocapsidsSemantic proximity Read ↗

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