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Article

Myristoylation of the RING finger Z protein is essential for arenavirus budding.

Journal of virology - 1 Oct 2004

Perez Mar, Greenwald Dori L, de la Torre Juan Carlos

Abstract excerpt

The arenavirus small RING finger Z protein is the main driving force of arenavirus budding. The primary structure of Z is devoid of hydrophobic transmembrane domains, but both lymphocytic choriomeningitis virus (LCMV) and Lassa fever virus Z proteins accumulate near the inner surface of the plasma membrane and are strongly membrane associated. All known arenavirus Z proteins contain a glycine (G) at position 2,...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 15452271
DOI: 10.1128/JVI.78.20.11443-11448.2004
PMCID: PMC521847

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Myristoylation of the RING finger Z protein is essential for arenavirus budding.PMID 15452271Read ↗

The role of myristoylation in the membrane association of the Lassa virus matrix protein Z.Semantic proximity Read ↗

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Molecular Mechanism of Arenavirus Assembly and BuddingSemantic proximity Read ↗

The RING Domain and the L79 Residue of Z Protein Are Involved in both the Rescue of Nucleocapsids and the Incorporation of Glycoproteins into Infectious Chimeric Arenavirus-Like ParticlesSemantic proximity Read ↗

Arenavirus Budding: A Common Pathway with Mechanistic DifferencesSemantic proximity Read ↗

Myristoylation of the Arenavirus Envelope Glycoprotein Stable Signal Peptide Is Critical for Membrane Fusion but Dispensable for Virion MorphogenesisSemantic proximity Read ↗

Identification of Two Functional Domains within the Arenavirus NucleoproteinSemantic proximity Read ↗

Efficient Budding of the Tacaribe Virus Matrix Protein Z Requires the NucleoproteinSemantic proximity Read ↗

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