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

Basic amino acid mutations in the nuclear localization signal of hibiscus chlorotic ringspot virus p23 inhibit virus long distance movement.

PloS one - 1 Jan 2013

Gao Ruimin, Wong Sek-Man

Abstract excerpt

The p23 is a unique protein in the Hibiscus chlorotic ringspot virus which belongs to Family Tombusviridae Genus Carmovirus. Our previous results showed that the p23 is indispensable for host-specific replication and is localized in the nucleus with a novel nuclear localization signal. To investigate additional function(s) of p23, mutations of basic amino acids lysine (K), arginine (R) and histidine (H) that...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Substitution
Share to Amino Acids
Share to Blotting, Western

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to In Situ Hybridization, Fluorescence

Share to MicroRNAs

Share to Nuclear Localization Signals

Share to Viral Proteins

Share to Virus Replication

Source

Open in PubMed Open full text

Identifiers

PMID: 24019944
DOI: 10.1371/journal.pone.0074000
PMCID: PMC3760818

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Basic amino acid mutations in the nuclear localization signal of hibiscus chlorotic ringspot virus p23 inhibit virus long distance movement.PMID 24019944Read ↗

Hibiscus chlorotic ringspot virus p27 and its isoforms affect symptom expression and potentiate virus movement in kenaf (Hibiscus cannabinus L.).Semantic proximity Read ↗

Efficient infection of Nicotiana benthamiana by Tomato bushy stunt virus is facilitated by the coat protein and maintained by p19 through suppression of gene silencing.Semantic proximity Read ↗

Molecular mechanism of RNA silencing suppression mediated by p19 protein of tombusviruses.Semantic proximity Read ↗

Host-induced avirulence of hibiscus chlorotic ringspot virus mutants correlates with reduced gene-silencing suppression activity.Semantic proximity Read ↗

An internal ribosome entry site directs translation of the 3'-gene from Pelargonium flower break virus genomic RNA: implications for infectivity.Semantic proximity Read ↗

A membrane-associated movement protein of Pelargonium flower break virus shows RNA-binding activity and contains a biologically relevant leucine zipper-like motif.Semantic proximity Read ↗

A Viral Noncoding RNA Complements a Weakened Viral RNA Silencing Suppressor and Promotes Efficient Systemic Host Infection.Semantic proximity Read ↗

The p23 of Citrus Tristeza Virus Interacts with Host FKBP-Type Peptidyl-Prolylcis-Trans Isomerase 17-2 and Is Involved in the Intracellular Movement of the Viral Coat Protein.Semantic proximity Read ↗

Involvement of C4 protein of beet severe curly top virus (family Geminiviridae) in virus movement.Semantic proximity Read ↗

First evidence showing that Pepper vein yellows virus P4 protein is a movement protein.Semantic proximity Read ↗

Functional analysis of V2 protein of Beet curly top Iran virusSemantic proximity Read ↗

Replication and movement of a coat protein mutant of cymbidium ringspot tombusvirus.Semantic proximity Read ↗

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