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

Influenza virus hemagglutinin and neuraminidase glycoproteins stimulate the membrane association of the matrix protein.

Journal of virology - 1 Oct 1996

Enami M, Enami K

Abstract excerpt

We have analyzed the mechanism by which the matrix (M1) protein associates with cellular membranes during influenza A virus assembly. Interaction of the M1 protein with the viral hemagglutinin (HA) or neuraminidase (NA) glycoprotein was extensively analyzed by using wild-type and transfectant inf...

Topics

Hemagglutinins, Viral
Mutation
Neuraminidase
Orthomyxoviridae
Transfection
Viral Matrix Proteins
Virus Assembly

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 8794300
DOI: 10.1128/JVI.70.10.6653-6657.1996
PMCID: PMC190706

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8794300-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Influenza virus hemagglutinin and neuraminidase glycoproteins stimulate the membrane association of the matrix protein.PMID 8794300Read ↗

Matrix proteins of enveloped viruses: a case study of Influenza A virus M1 proteinSemantic 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 ↗

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 ↗

Entry of influenza A virus into host cells — recent progress and remaining challengesSemantic proximity Read ↗

Measles virus nucleocapsid transport to the plasma membrane requires stable expression and surface accumulation of the viral matrix protein.Semantic proximity Read ↗

Sendai virus M protein binds independently to either the F or the HN glycoprotein in vivoSemantic proximity Read ↗

Structural Determinants of the Interactions Between Influenza A Virus Matrix Protein M1 and Lipid MembranesSemantic proximity Read ↗

Altered Interaction of the Matrix Protein with the Cytoplasmic Tail of Hemagglutinin Modulates Measles Virus Growth by Affecting Virus Assembly and Cell-Cell FusionSemantic proximity Read ↗

Interactions of normal and mutant vesicular stomatitis virus matrix proteins with the plasma membrane and nucleocapsids.Semantic proximity Read ↗

Transmembrane Domain Length of Influenza a Virus M2 Does Not Determine Its Non-Lipid Raft Localization.Semantic proximity Read ↗

Specific Nucleoprotein Residues Affect Influenza Virus MorphologySemantic proximity Read ↗

Rescue of human immunodeficiency virus type 1 matrix protein mutants by envelope glycoproteins with short cytoplasmic domains.Semantic proximity Read ↗

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