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

An Intrabody Based on a Llama Single-domain Antibody Targeting the N-terminal α-Helical Multimerization Domain of HIV-1 Rev Prevents Viral Production

21 Apr 2010

Abstract excerpt

The human immunodeficiency virus, type 1 (HIV-1)-encoded Rev protein is essential for the expression of late viral mRNAs. Rev forms a large organized multimeric protein-protein complex on the Rev response element of these viral mRNA species and transports them from the nucleus to the cytoplasm, exploiting the CRM1-mediated cellular machinery. Here we report the selection of a nanobody, derived from a llama...

Read the complete abstract on PubMed

Topics

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

Share to Glycosylation and Glycoproteins Research
Share to HIV Research and Treatment
Share to Monoclonal and Polyclonal Antibodies Research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 20406803
DOI: 10.1074/jbc.m110.112490

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

An Intrabody Based on a Llama Single-domain Antibody Targeting the N-terminal α-Helical Multimerization Domain of HIV-1 Rev Prevents Viral ProductionPMID 20406803Read ↗

A stably expressed llama single-domain intrabody targeting Rev displays broad-spectrum anti-HIV activity.Semantic proximity Read ↗

Mapping the binding interface between an HIV-1 inhibiting intrabody and the viral protein Rev.Semantic proximity Read ↗

Protease-Containing Nanobodies for Detecting and Manipulating Intracellular Antigens Using Antiviral DrugsSemantic proximity Read ↗

HIV Rev Assembly on the Rev Response Element (RRE): A Structural PerspectiveSemantic proximity Read ↗

Generation and validation of a highly sensitive bioluminescent HIV-1 reporter vector that simplifies measurement of virus release.Semantic proximity Read ↗

Novel Lentivirus-Based Method for Rapid Selection of Inhibitory Nanobody against PRRSVSemantic proximity Read ↗

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

Interaction between HIV-1 Rev and Integrase ProteinsSemantic proximity Read ↗

A solution to limited genomic capacity: using adaptable binding surfaces to assemble the functional HIV Rev oligomer on RNA.Semantic proximity Read ↗

Identification of a homogenous structural basis for oligomerization by retroviral Rev-like proteins.Semantic proximity Read ↗

Ultrasensitive quantification of HIV-1 cell-to-cell transmission in primary human CD4 <sup>+</sup> T cells measures viral sensitivity to broadly neutralizing antibodiesSemantic proximity Read ↗

Interactions between HIV Rev and nuclear import and export factors: the Rev nuclear localisation signal mediates specific binding to human importin-beta.Semantic proximity Read ↗

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