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

Characterization of a cyanobacterial RNase P ribozyme recognition motif in the IRES of foot-and-mouth disease virus reveals a unique structural element.

RNA (New York, N.Y.) - 1 Jun 2007

Serrano Paula, Gomez Jordi, Martínez-Salas Encarnación

Abstract excerpt

Translation initiation driven by internal ribosome entry site (IRES) elements is dependent on the structural organization of the IRES region. Picornavirus IRES are organized in structural domains, in which the terminal stem-loops participate in functional RNA-protein interactions. However, the me...

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 Foot-and-Mouth Disease Virus
Share to Nucleic Acid Conformation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Biosynthesis

Share to Ribonuclease P

Share to RNA, Viral

Share to Substrate Specificity

Share to Synechocystis

Source

Open in PubMed Open full text

Identifiers

PMID: 17449727
DOI: 10.1261/rna.506607
PMCID: PMC1869033

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-17449727-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Characterization of a cyanobacterial RNase P ribozyme recognition motif in the IRES of foot-and-mouth disease virus reveals a unique structural element.PMID 17449727Read ↗

Picornavirus IRES: Structure Function RelationshipSemantic proximity Read ↗

Identification and Characterization of a <i>cis</i> -Acting Replication Element ( <i>cre</i> ) Adjacent to the Internal Ribosome Entry Site of Foot-and-Mouth Disease VirusSemantic proximity Read ↗

Sequence and secondary structure requirements in a highly conserved element for foot-and-mouth disease virus internal ribosome entry site activity and eIF4G binding.Semantic proximity Read ↗

Relevance of RNA structure for the activity of picornavirus IRES elementsSemantic proximity Read ↗

Structural organization of a viral IRES depends on the integrity of the GNRA motifSemantic proximity Read ↗

Validating the EMCV IRES Secondary Structure with Structure–Function AnalysisSemantic proximity Read ↗

Evidence of reciprocal tertiary interactions between conserved motifs involved in organizing RNA structure essential for internal initiation of translation.Semantic proximity Read ↗

The RNA pseudoknots in foot-and-mouth disease virus are dispensable for genome replication but essential for the production of infectious virusSemantic proximity Read ↗

The 3′ end of the foot-and-mouth disease virus genome establishes two distinct long-range RNA–RNA interactions with the 5′ end regionSemantic proximity Read ↗

Common conformational changes induced in type 2 picornavirus IRESs by cognate trans-acting factors.Semantic proximity Read ↗

Glycyl-tRNA synthetase specifically binds to the poliovirus IRES to activate translation initiation.Semantic proximity Read ↗

Conserved Nucleotides within the J Domain of the Encephalomyocarditis Virus Internal Ribosome Entry Site Are Required for Activity and for Interaction with eIF4GSemantic proximity Read ↗

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