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

Molecular dissection of Flock house virus protein B2 reveals that electrostatic interactions between N-terminal domains of B2 monomers are critical for dimerization.

Virology - 25 Oct 2012

Seo Jang-Kyun, Kwon Sun-Jung, Rao A L N

Abstract excerpt

Flock house virus (FHV) encodes a suppressor protein B2 to overcome antiviral RNA silencing during infection. Biochemical analyses have shown that a homodimer of B2 binds to double-stranded RNA to inhibit dicer-mediated cleavage of dsRNA and incorporation of small interfering RNAs into the RNA-induced silencing complex. In this study, using FHV-Nicotiana benthamiana system, we identified that the charged amino...

Read the complete abstract on PubMed

Topics

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

Share to Protein Conformation
Share to Protein Multimerization

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to RNA, Double-Stranded

Share to RNA Interference

Share to RNA, Small Interfering

Share to RNA, Viral

Share to Static Electricity

Share to Viral Proteins

Source

Identifiers

PMID: 22721960
DOI: 10.1016/j.virol.2012.05.023

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

Molecular dissection of Flock house virus protein B2 reveals that electrostatic interactions between N-terminal domains of B2 monomers are critical for dimerization.PMID 22721960Read ↗

Suppression of RNA silencing by Flock house virus B2 protein is mediated through its interaction with the PAZ domain of DicerSemantic proximity Read ↗

RNA Binding by a Novel Helical Fold of B2 Protein from Wuhan Nodavirus Mediates the Suppression of RNA Interference and Promotes B2 DimerizationSemantic proximity Read ↗

The structure of the flock house virus B2 protein, a viral suppressor of RNA interference, shows a novel mode of double‐stranded RNA recognitionSemantic proximity Read ↗

Sequestration and protection of double-stranded RNA by the betanodavirus b2 protein.Semantic proximity Read ↗

Targeting of Dicer-2 and RNA by a Viral RNA Silencing Suppressor in Drosophila CellsSemantic proximity Read ↗

Dual modes of RNA-silencing suppression by Flock House virus protein B2Semantic proximity Read ↗

Nodamura virus nonstructural protein B2 can enhance viral RNA accumulation in both mammalian and insect cells.Semantic proximity Read ↗

Structure of the RNA-Binding Domain of Nodamura Virus Protein B2, a Suppressor of RNA Interference,Semantic proximity Read ↗

Functional modulation of the geminivirus AL2 transcription factor and silencing suppressor by self-interaction.Semantic proximity Read ↗

Bipartite viral RNA genome heterodimerization influences genome packaging and virion thermostability.Semantic proximity Read ↗

Dicer-2 Processes Diverse Viral RNA SpeciesSemantic proximity Read ↗

Essential function in vivo for Dicer-2 in host defense against RNA viruses in drosophila.Semantic proximity Read ↗

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