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

High-resolution mapping of the human T-cell leukemia virus type 1 Rex-binding element by in vitro selection.

Journal of virology - 1 Dec 1995

Baskerville S, Zapp M, Ellington A D

Abstract excerpt

Interactions between the Rex protein of HTLV-1 and the genomic Rex-binding element (XBE) mediate the cytoplasmic transport of viral mRNAs. However, it is uncertain which RNA sequences and structures contribute to Rex recognition. A portion of the viral genome that spanned the XBE was partially randomized, and functional Rex-binding variants were selected. Alignment of selected Rex-binding sequences revealed...

Read the complete abstract on PubMed

Topics

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

Share to Base Sequence
Share to Binding Sites
Share to Cloning, Molecular

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

Share to Genetic Variation

Share to Molecular Sequence Data

Share to Mutagenesis, Site-Directed

Share to Recombinant Fusion Proteins

Share to RNA, Messenger

Source

Open in PubMed Open full text

Identifiers

PMID: 7494262
DOI: 10.1128/JVI.69.12.7559-7569.1995
PMCID: PMC189694

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

High-resolution mapping of the human T-cell leukemia virus type 1 Rex-binding element by in vitro selection.PMID 7494262Read ↗

Multiple arginine residues within the basic domain of HTLV-I Rex are required for specific RNA binding and function.Semantic proximity Read ↗

The type I human T-cell leukemia virus (HTLV-I) Rex trans-activator binds directly to the HTLV-I Rex and the type 1 human immunodeficiency virus Rev RNA response elements.Semantic proximity Read ↗

HIV-1 structural gene expression requires binding of the Rev trans-activator to its RNA target sequence.Semantic proximity Read ↗

Dominant-negative mutants are clustered in a domain of the human T-cell leukemia virus type I Rex protein: implications for trans dominance.Semantic proximity Read ↗

Regulation of the nucleocytoplasmic transport of HTLV-1 RNASemantic proximity Read ↗

Transdominant repressors for human T-cell leukemia virus type I rex and human immunodeficiency virus type 1 rev function.Semantic proximity Read ↗

Mutational analysis of bovine leukemia virus Rex: identification of a dominant-negative inhibitor.Semantic proximity Read ↗

Multimer formation is not essential for nuclear export of human T-cell leukemia virus type 1 Rex trans-activator protein.Semantic proximity Read ↗

Heterologous basic domain substitutions in the HIV-1 Tat protein reveal an arginine-rich motif required for transactivation.Semantic proximity Read ↗

Functional domain structure of human T-cell leukemia virus type 2 rex.Semantic proximity Read ↗

Functional analyses reveal extensive RRE plasticity in primary HIV-1 sequences selected under selective pressure.Semantic proximity Read ↗

Identification of a novel cellular cofactor for the Rev/Rex class of retroviral regulatory proteins.Semantic proximity Read ↗

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