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

The TPR domain in the host Cyp40-like cyclophilin binds to the viral replication protein and inhibits the assembly of the tombusviral replicase.

PLoS pathogens - 1 Feb 2012

Lin Jing-Yi, Mendu Venugopal, Pogany Judit, Qin Jun, Nagy Peter D

Abstract excerpt

Replication of plus-stranded RNA viruses is greatly affected by numerous host-coded proteins acting either as susceptibility or resistance factors. Previous genome-wide screens and global proteomics approaches with Tomato bushy stunt tombusvirus (TBSV) in a yeast model host revealed the involvement of cyclophilins, which are a large family of host prolyl isomerases, in TBSV replication. In this paper, we...

Read the complete abstract on PubMed

Topics

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

Share to Cyclophilins
Share to Host-Pathogen Interactions

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Peptidylprolyl Isomerase

Share to RNA-Dependent RNA Polymerase

Share to Solanum lycopersicum

Share to Viral Proteins

Share to Virus Assembly

Share to Virus Replication

Source

Open in PubMed Open full text

Identifiers

PMID: 22346747
DOI: 10.1371/journal.ppat.1002491
PMCID: PMC3276564

Genes

TPR

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The TPR domain in the host Cyp40-like cyclophilin binds to the viral replication protein and inhibits the assembly of the tombusviral replicase.PMID 22346747Read ↗

Cyclophilin A Binds to the Viral RNA and Replication Proteins, Resulting in Inhibition of Tombusviral Replicase AssemblySemantic proximity Read ↗

Translation elongation factor 1A is a component of the tombusvirus replicase complex and affects the stability of the p33 replication co-factor.Semantic proximity Read ↗

Yeast screens for host factors in positive-strand RNA virus replication based on a library of temperature-sensitive mutants.Semantic proximity Read ↗

Translation elongation factor 1A facilitates the assembly of the tombusvirus replicase and stimulates minus-strand synthesis.Semantic proximity Read ↗

Synergistic roles of eukaryotic translation elongation factors 1Bγ and 1A in stimulation of tombusvirus minus-strand synthesis.Semantic proximity Read ↗

Transcriptome resequencing analysis of the responses of Ty-5-Mediated resistance to TYLCV via in resistant vs. susceptible tomato cultivarsSemantic proximity Read ↗

Subversion of selective autophagy for the biogenesis of tombusvirus replication organelles inhibits autophagySemantic proximity Read ↗

C2 from Beet curly top virus promotes a cell environment suitable for efficient replication of geminiviruses, providing a novel mechanism of viral synergism.Semantic proximity Read ↗

Host-dependent recombination of a Tomato bushy stunt virus coat protein mutant yields truncated capsid subunits that form virus-like complexes which benefit systemic spread.Semantic proximity Read ↗

Yeast as a model host to study replication and recombination of defective interfering RNA of Tomato bushy stunt virus.Semantic proximity Read ↗

Geminivirus βV1 protein activates bZIP17/28-mediated UPR signaling to facilitate viral pathogenicity but its activity is attenuated by autophagic degradation in plantsSemantic proximity Read ↗

Double-stranded RNA-binding protein 4 is required for resistance signaling against viral and bacterial pathogens.Semantic proximity Read ↗

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