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

Conserved Rotavirus NSP5 and VP2 Domains Interact and Affect Viroplasm.

Journal of virology - 17 Mar 2020

Buttafuoco Antonino, Michaelsen Kevin, Tobler Kurt, Ackermann Mathias, Fraefel Cornel, Eichwald Catherine

Abstract excerpt

One step of the life cycle common to all rotaviruses (RV) studied so far is the formation of viroplasms, membrane-less cytosolic inclusions providing a microenvironment for early morphogenesis and RNA replication. Viroplasm-like structures (VLS) are simplified viroplasm models consisting of complexes of nonstructural protein 5 (NSP5) with the RV core shell VP2 or NSP2. We identified and characterized the domains...

Read the complete abstract on PubMed

Topics

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

Share to Capsid Proteins
Share to Chlorocebus aethiops

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cytosol

Share to Guinea Pigs

Share to Macaca mulatta

Share to Protein Domains

Share to Rotavirus

Share to Viral Nonstructural Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 31915278
DOI: 10.1128/JVI.01965-19
PMCID: PMC7081909

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Conserved Rotavirus NSP5 and VP2 Domains Interact and Affect Viroplasm.PMID 31915278Read ↗

Comparative analysis of NSP5/VP2-induced viroplasm-like structures in rotavirus species A to JSemantic proximity Read ↗

Rotavirus NSP2: A Master Orchestrator of Early Viral Particle AssemblySemantic proximity Read ↗

Two non-structural rotavirus proteins, NSP2 and NSP5, form viroplasm-like structures in vivo.Semantic proximity Read ↗

Rotavirus Spike Protein VP4 Mediates Viroplasm Assembly by Association to Actin FilamentsSemantic proximity Read ↗

Recent Advances From Studies on the Role of Structural Proteins in Enterovirus InfectionSemantic proximity Read ↗

The SARS-CoV-2 NSP4 T492I mutation promotes double-membrane vesicle formation to facilitate transmission.Semantic proximity Read ↗

The PRRSV replicase: Exploring the multifunctionality of an intriguing set of nonstructural proteinsSemantic proximity Read ↗

A RNA Dodecahedral Cage Inside a Human Virus Plays a Dual Biological Role in Virion Assembly and Genome Release ControlSemantic proximity Read ↗

A Novel Protein NLRP12‐119aa that Prevents Rhabdovirus Replication by Disrupting the RNP Complex FormationSemantic proximity Read ↗

Group B rotavirus encodes a functional fusion-associated small transmembrane (FAST) proteinSemantic proximity Read ↗

Two conserved oligomer interfaces of NSP7 and NSP8 underpin the dynamic assembly of SARS-CoV-2 RdRP.Semantic proximity Read ↗

Function, Architecture, and Biogenesis of Reovirus Replication NeoorganellesSemantic proximity Read ↗

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