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

Sequence requirements for Rev multimerization in vivo.

Virology - 1 Jul 1994

Madore S J, Tiley L S, Malim M H, Cullen B R

Abstract excerpt

Multimerization of the human immunodeficiency virus type 1 (HIV-1) Rev protein is believed to be critical to its biological activity. However, the precise protein sequence requirements for Rev multimerization in vivo, and whether multimerization is facilitated by specific RNA binding or vice versa, has remained controversial. In this report, we describe a sensitive in vivo assay for the multimerization of HIV-1...

Read the complete abstract on PubMed

Topics

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

Share to Cloning, Molecular
Share to HeLa Cells
Share to HIV-1

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

Share to Mutation

Share to Phenotype

Share to Binding Sites

Share to Amino Acid Sequence

Source

Identifiers

PMID: 7516596
DOI: 10.1006/viro.1994.1334

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

Sequence requirements for Rev multimerization in vivo.PMID 7516596Read ↗

Interaction of the human immunodeficiency virus type 1 Rev protein with a structured region in env mRNA is dependent on multimer formation mediated through a basic stretch of amino acids.Semantic proximity Read ↗

Measuring cooperative Rev protein-protein interactions on Rev responsive RNA by fluorescence resonance energy transfer.Semantic proximity Read ↗

Sequence specificity in the higher-order interaction of the Rev protein of HIV-1 with its target sequence, the RRE.Semantic proximity Read ↗

Structural model for the cooperative assembly of HIV-1 Rev multimers on the RRE as deduced from analysis of assembly-defective mutants.Semantic proximity Read ↗

Phenotypic analysis of human immunodeficiency virus type 1 Rev trimerization-interface mutants in human cells.Semantic proximity Read ↗

Dominant negative mutants of human T-cell leukemia virus type I Rex and human immunodeficiency virus type 1 Rev fail to multimerize in vivo.Semantic proximity Read ↗

Perturbation of the carboxy terminus of HIV-1 Rev affects multimerization on the Rev responsive element.Semantic proximity Read ↗

Limited nucleotide changes in the Rev response element (RRE) during HIV-1 infection alter overall Rev-RRE activity and Rev multimerization.Semantic proximity Read ↗

Real-time kinetics of HIV-1 Rev-Rev response element interactions. Definition of minimal binding sites on RNA and protein and stoichiometric analysis.Semantic proximity Read ↗

Rev-RRE Functional Activity Differs Substantially Among Primary HIV-1 Isolates.Semantic proximity Read ↗

Minimal Rev-response element for type 1 human immunodeficiency virus.Semantic proximity Read ↗

Formation of trans-activation competent HIV-1 Rev:RRE complexes requires the recruitment of multiple protein activation domains.Semantic proximity Read ↗

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