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

Restoration of replication-defective dengue type 1 virus bearing mutations in the N-terminal cytoplasmic portion of NS4A by additional mutations in NS4B.

Archives of virology - 1 Jan 2011

Tajima Shigeru, Takasaki Tomohiko, Kurane Ichiro

Abstract excerpt

Flavivirus NS4A has an N-terminal hydrophilic cytoplasmic portion; however, the role of this portion remains poorly understood. In this study, we show that a recombinant dengue type 1 virus (DENV-1) in which a subportion (amino acids 27-34) of the N-terminal portion of NS4A is replaced by the corresponding region from Japanese encephalitis virus (JEV) is defective in replication. Using the defective mutant clone...

Read the complete abstract on PubMed

Topics

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

Share to Chlorocebus aethiops
Share to Dengue Virus

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Gene Expression Regulation, Viral

Share to Mutagenesis, Site-Directed

Share to Vero Cells

Share to Viral Nonstructural Proteins

Share to Viral Proteins

Share to Virus Replication

Source

Identifiers

PMID: 20882304
DOI: 10.1007/s00705-010-0816-8

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

Restoration of replication-defective dengue type 1 virus bearing mutations in the N-terminal cytoplasmic portion of NS4A by additional mutations in NS4B.PMID 20882304Read ↗

Mutations in the cytoplasmic domain of dengue virus NS4A affect virus fitness and interactions with other non-structural proteins.Semantic proximity Read ↗

A non-structural protein 1 substitution of dengue virus enhances viral replication by interfering with the antiviral signaling pathwaySemantic proximity Read ↗

Recovery of a chemically synthesized Japanese encephalitis virus reveals two critical adaptive mutations in NS2B and NS4ASemantic proximity Read ↗

Mutagenesis of Dengue Virus Protein NS2A Revealed a Novel Domain Responsible for Virus-Induced Cytopathic Effect and Interactions between NS2A and NS2B Transmembrane Segments.Semantic proximity Read ↗

A Combined Genetic-Proteomic Approach Identifies Residues within Dengue Virus NS4B Critical for Interaction with NS3 and Viral ReplicationSemantic proximity Read ↗

Characterization of recombinant dengue-2 virus derived from a single nucleotide substitution in the 5' noncoding region.Semantic proximity Read ↗

Antibody-dependent enhancement (ADE) of dengue virus: Identification of the key amino acid that is vital in DENV vaccine research.Semantic proximity Read ↗

NS1 Protein N-Linked Glycosylation Site Affects the Virulence and Pathogenesis of Dengue VirusSemantic proximity Read ↗

Genetic Interaction of Flavivirus Nonstructural Proteins NS1 and NS4A as a Determinant of Replicase FunctionSemantic proximity Read ↗

Dengue type 4 virus mutants containing deletions in the 3' noncoding region of the RNA genome: analysis of growth restriction in cell culture and altered viremia pattern and immunogenicity in rhesus monkeys.Semantic proximity Read ↗

A Single Amino Acid in Nonstructural Protein NS4B Confers Virulence to Dengue Virus in AG129 Mice through Enhancement of Viral RNA SynthesisSemantic proximity Read ↗

Envelope Protein Mutations L107F and E138K Are Important for Neurovirulence Attenuation for Japanese Encephalitis Virus SA14-14-2 StrainSemantic proximity Read ↗

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