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

Binding of the V proteins to the nucleocapsid proteins of human parainfluenza type 2 virus.

Medical microbiology and immunology - 1 Sept 1996

Watanabe N, Kawano M, Tsurudome M, Nishio M, Ito M, Ohgimoto S, Suga S, Komada H, Ito Y

Abstract excerpt

Interaction of the nucleocapsid (NP) and V proteins of human parainfluenza type 2 virus (HPIV-2) was investigated using a transient expression system. When the NP proteins were co-expressed with the V proteins, some of the NP proteins were translocated into the nuclei. These findings suggest that the NP protein interact with the V proteins. We examined the interaction of the NP proteins and the P, V proteins or...

Read the complete abstract on PubMed

Topics

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

Share to Binding Sites
Share to Biological Transport

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Protein Binding

Share to Recombinant Fusion Proteins

Share to Sequence Deletion

Share to Transfection

Share to Viral Proteins

Source

Identifiers

PMID: 8884740
DOI: 10.1007/s004300050019

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

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Binding of the V proteins to the nucleocapsid proteins of human parainfluenza type 2 virus.PMID 8884740Read ↗

Identification of the sequences responsible for nuclear targeting of the V protein of human parainfluenza virus type 2.Semantic proximity Read ↗

The conserved carboxyl terminus of human parainfluenza virus type 2 V protein plays an important role in virus growth.Semantic proximity Read ↗

Nucleocapsid Incorporation into Parainfluenza Virus Is Regulated by Specific Interaction with Matrix ProteinSemantic proximity Read ↗

Mapping of domains on the human parainfluenza virus type 2 nucleocapsid protein (NP) required for NP–phosphoprotein or NP–NP interactionSemantic proximity Read ↗

Regions on the hemagglutinin-neuraminidase proteins of human parainfluenza virus type-1 and Sendai virus important for membrane fusion.Semantic proximity Read ↗

Human parainfluenza virus type 2 V protein inhibits genome replication by binding to the L protein: possible role in promoting viral fitness.Semantic proximity Read ↗

In Vivo Interaction of Rabies Virus Phosphoprotein (P) and Nucleoprotein (N): Existence of Two N-binding Sites on P ProteinSemantic proximity Read ↗

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

Oligomerization, secretion, and biological function of an anchor-free parainfluenza virus type 2 (PI2) fusion protein.Semantic proximity Read ↗

Down-regulation of paramyxovirus hemagglutinin-neuraminidase glycoprotein surface expression by a mutant fusion protein containing a retention signal for the endoplasmic reticulum.Semantic proximity Read ↗

Regions on nucleocapsid protein of Newcastle disease virus that interact with its phosphoprotein.Semantic proximity Read ↗

Paramyxovirus-induced syncytium cell formation is suppressed by a dominant negative fusion regulatory protein-1 (FRP-1)/CD98 mutated construct: an important role of FRP-1 in virus-induced cell fusion.Semantic proximity Read ↗

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