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

Engineered Single Human CD4 Domains as Potent HIV-1 Inhibitors and Components of Vaccine Immunogens

30 Jun 2011

Abstract excerpt

Soluble forms of the HIV-1 receptor CD4 (sCD4) have been extensively characterized for more than 2 decades as promising inhibitors and components of vaccine immunogens. However, they were mostly based on the first two CD4 domains (D1D2), and numerous attempts to develop functional, high-affinity, stable soluble one-domain sCD4 (D1) have not been successful because of the strong interactions between the two...

Read the complete abstract on PubMed

Topics

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

Share to HIV Research and Treatment
Share to Monoclonal and Polyclonal Antibodies Research
Share to vaccines and immunoinformatics approaches

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

Source

Identifiers

PMID: 21715496
DOI: 10.1128/jvi.05119-11

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 24 Oct 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

Engineered Single Human CD4 Domains as Potent HIV-1 Inhibitors and Components of Vaccine ImmunogensPMID 21715496Read ↗

Design and characterization of stabilized derivatives of human CD4D12 and CD4D1.Semantic proximity Read ↗

Rational Design of Envelope Identifies Broadly Neutralizing Human Monoclonal Antibodies to HIV-1Semantic proximity Read ↗

Stabilized gp120-specific CD4 for next-generation HIV-1 inhibitorsSemantic proximity Read ↗

A Novel Human Antibody against Human Immunodeficiency Virus Type 1 gp120 Is V1, V2, and V3 Loop Dependent and Helps Delimit the Epitope of the Broadly Neutralizing Antibody Immunoglobulin G1 b12Semantic proximity Read ↗

Indoline CD4-mimetic Compounds Mediate Potent and Broad HIV-1 Inhibition and Sensitization to Antibody-dependent Cellular CytotoxicitySemantic proximity Read ↗

Unique binding modes for the broad neutralizing activity of single-chain variable fragments (scFv) targeting CD4-induced epitopesSemantic proximity Read ↗

Neutralization of Human Immunodeficiency Virus Type 1 by sCD4-17b, a Single-Chain Chimeric Protein, Based on Sequential Interaction of gp120 with CD4 and CoreceptorSemantic proximity Read ↗

Recombinant CD4-selected human immunodeficiency virus type 1 variants with reduced gp120 affinity for CD4 and increased cell fusion capacity.Semantic proximity Read ↗

Improving the Expression and Purification of Soluble, Recombinant Native-Like HIV-1 Envelope Glycoprotein Trimers by Targeted Sequence Changes.Semantic proximity Read ↗

Structure- and sequence-based design of synthetic single-domain antibody librariesSemantic proximity Read ↗

Changes at V2 apex of HIV-1 Clade C trimer enhance elicitation of autologous neutralizing and broad V1V2-scaffold antibodiesSemantic proximity Read ↗

Mutational analysis of domain antibodies reveals aggregation hotspots within and near the complementarity determining regions.Semantic proximity Read ↗

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