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

Recognition of 5'-terminal TAR structure in human immunodeficiency virus-1 mRNA by eukaryotic translation initiation factor 2.

Nucleic acids research - 15 Feb 2000

Ben-Asouli Y, Banai Y, Hauser H, Kaempfer R

Abstract excerpt

TAR, a 59 nt 5'-terminal hairpin in human immuno-deficiency virus 1 (HIV-1) mRNA, binds viral Tat and several cellular proteins. We report that eukaryotic translation initiation factor 2 (eIF2) recognizes TAR. TAR and the AUG initiation codon domain, located well downstream from TAR, both contribute to the affinity of HIV-1 mRNA for eIF2. The affinity of TAR for eIF2 was insensitive to lower stem mutations that...

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 Codon
Share to Eukaryotic Initiation Factor-2

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

Share to Nucleic Acid Conformation

Share to Protein Biosynthesis

Share to RNA, Messenger

Share to RNA, Viral

Source

Open in PubMed Open full text

Identifiers

PMID: 10648795
DOI: 10.1093/nar/28.4.1011
PMCID: PMC102579

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

Recognition of 5'-terminal TAR structure in human immunodeficiency virus-1 mRNA by eukaryotic translation initiation factor 2.PMID 10648795Read ↗

Different effects of the TAR structure on HIV-1 and HIV-2 genomic RNA translationSemantic proximity Read ↗

The Structure of the Human Immunodeficiency Virus Type-1 TAR RNA Reveals Principles of RNA Recognition by Tat ProteinSemantic proximity Read ↗

The sequence and structure of the 3' arm of the first stem-loop of the human immunodeficiency virus type 2 trans-activation responsive region mediate Tat-2 transactivation.Semantic proximity Read ↗

Destabilization of the TAR hairpin leads to extension of the polyA hairpin and inhibition of HIV-1 polyadenylationSemantic proximity Read ↗

Tat functions to stimulate the elongation properties of transcription complexes paused by the duplicated TAR RNA element of human immunodeficiency virus 2.Semantic proximity Read ↗

Structures of complete HIV-1 TAR RNA portray a dynamic platform poised for protein binding and structural remodelingSemantic proximity Read ↗

The TAR RNA-binding protein, TRBP, stimulates the expression of TAR-containing RNAs in vitro and in vivo independently of its ability to inhibit the dsRNA-dependent kinase PKR.Semantic proximity Read ↗

The C-terminal domain of eukaryotic initiation factor 5 promotes start codon recognition by its dynamic interplay with eIF1 and eIF2β.Semantic proximity Read ↗

An Arg/Lys-rich core peptide mimics TRBP binding to the HIV-1 TAR RNA upper-stem/loop.Semantic proximity Read ↗

Anti-termination by SIV Tat requires flexibility of the nascent TAR structure.Semantic proximity Read ↗

The apical loop of the HIV-1 TAR RNA hairpin is stabilized by a cross-loop base pair.Semantic proximity Read ↗

Functional analysis of the complex trans-activating response element RNA structure in simian immunodeficiency virus.Semantic proximity Read ↗

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