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

Mutations in the Influenza A Virus M1 Protein Enhance Virus Budding To Complement Lethal Mutations in the M2 Cytoplasmic Tail.

Journal of virology - 1 Jan 2018

Liu Hsuan, Grantham Michael L, Pekosz Andrew

Abstract excerpt

The influenza A virus M1 and M2 proteins play important roles in virus assembly and in the morphology of virus particles. Mutations in the distal cytoplasmic tail region of M2, and in particular a tyrosine-to-alanine mutation at residue 76 (Y76A), were essential for infectious virus production and filament formation while having limited effects on total virus particle budding. Using a novel selection method,...

Read the complete abstract on PubMed

Topics

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

Share to Cytoplasm
Share to Dogs
Share to Influenza A virus

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

Share to Madin Darby Canine Kidney Cells

Share to Suppression, Genetic

Share to Viral Matrix Proteins

Share to Virus Assembly

Share to Virus Release

Source

Open in PubMed Open full text

Identifiers

PMID: 29046451
DOI: 10.1128/JVI.00858-17
PMCID: PMC5730759

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

Mutations in the Influenza A Virus M1 Protein Enhance Virus Budding To Complement Lethal Mutations in the M2 Cytoplasmic Tail.PMID 29046451Read ↗

Tyrosines in the influenza A virus M2 protein cytoplasmic tail are critical for production of infectious virus particles.Semantic proximity Read ↗

A Glu-Glu-Tyr sequence in the cytoplasmic tail of the M2 protein renders IAV susceptible to restriction of HA-M2 association in primary human macrophagesSemantic proximity Read ↗

The highly conserved arginine residues at positions 76 through 78 of influenza A virus matrix protein M1 play an important role in viral replication by affecting the intracellular localization of M1.Semantic proximity Read ↗

SUMOylation of Matrix Protein M1 and Filamentous Morphology Collectively Contribute to the Replication and Virulence of Highly Pathogenic H5N1 Avian Influenza Viruses in Mammals.Semantic proximity Read ↗

Palmitoylation of the Influenza A Virus M2 Protein Is Not Required for Virus Replication In Vitro but Contributes to Virus VirulenceSemantic proximity Read ↗

The M1 and M2 proteins of influenza A virus are important determinants in filamentous particle formation.Semantic proximity Read ↗

Virus subtype-specific suppression of MAVS aggregation and activation by PB1-F2 protein of influenza A (H7N9) virusSemantic proximity Read ↗

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 ↗

Influenza B virus M2 protein can functionally replace its influenza A virus counterpart in promoting virus replication.Semantic proximity Read ↗

Involvement of an Arginine Triplet in M1 Matrix Protein Interaction with Membranes and in M1 Recruitment into Virus-Like Particles of the Influenza A(H1N1)pdm09 Virus.Semantic proximity Read ↗

Filamentous Influenza VirusesSemantic proximity Read ↗

Identification of a Novel Splice Variant Form of the Influenza A Virus M2 Ion Channel with an Antigenically Distinct EctodomainSemantic proximity Read ↗

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