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

Human Parainfluenza Virus Type 3 Matrix Protein Reduces Viral RNA Synthesis of HPIV3 by Regulating Inclusion Body Formation.

Viruses - 11 Mar 2018

Zhang Shengwei, Cheng Qi, Luo Chenxi, Qin Yali, Chen Mingzhou

Abstract excerpt

Human parainfluenza virus type 3 is one of the main causes of lower respiratory illness in newborns and infants. The role of the matrix protein (M) in viral budding is extensively studied, but the effect of M on viral replication remains to be determined. Using an HPIV3 minigenome assay, we found that M reduced HPIV3 mingenome-encoded reporter activity even though it had an unspecific effect on the expression of...

Read the complete abstract on PubMed

Topics

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

Share to Gene Expression Regulation, Viral
Share to Genes, Reporter

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HeLa Cells

Share to Viral Matrix Proteins

Share to Viral Proteins

Share to Virus Assembly

Share to Virus Release

Share to Virus Replication

Source

Open in PubMed Open full text

Identifiers

PMID: 29534486
DOI: 10.3390/v10030125
PMCID: PMC5869518

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Human Parainfluenza Virus Type 3 Matrix Protein Reduces Viral RNA Synthesis of HPIV3 by Regulating Inclusion Body Formation.PMID 29534486Read ↗

Human metapneumovirus nucleoprotein and phosphoprotein interact and provide the minimal requirements for inclusion body formationSemantic proximity Read ↗

Minimal Elements Required for the Formation of Respiratory Syncytial Virus Cytoplasmic Inclusion Bodies In Vivo and In VitroSemantic proximity Read ↗

Inclusion bodies of human parainfluenza virus type 3 inhibit antiviral stress granule formation by shielding viral RNAsSemantic proximity Read ↗

Human Metapneumovirus Induces Formation of Inclusion Bodies for Efficient Genome Replication and TranscriptionSemantic proximity Read ↗

Specific Residues in the C-Terminal Domain of the Human Metapneumovirus Phosphoprotein Are Indispensable for Formation of Viral Replication Centers and Regulation of the Function of the Viral Polymerase ComplexSemantic proximity Read ↗

Structural Basis of Human Parainfluenza Virus 3 Unassembled Nucleoprotein in Complex with Its Viral Chaperone.Semantic proximity Read ↗

Characterization of the Interaction Domains between the Phosphoprotein and the Nucleoprotein of Human Metapneumovirus.Semantic proximity Read ↗

Structural and molecular properties of mumps virus inclusion bodiesSemantic proximity Read ↗

Tetramerization of Phosphoprotein Is Essential for Respiratory Syncytial Virus Budding while Its N-Terminal Region Mediates Direct Interactions with the Matrix ProteinSemantic proximity Read ↗

VP40 octamers are essential for Ebola virus replication.Semantic proximity Read ↗

Mutations in the FPIV motif of Newcastle disease virus matrix protein attenuate virus replication and reduce virus budding.Semantic proximity Read ↗

The C-terminal end of parainfluenza virus 5 NP protein is important for virus-like particle production and M-NP protein interaction.Semantic proximity Read ↗

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