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

Characterization of Human Immunodeficiency Virus (HIV-1) Envelope Glycoprotein Variants Selected for Resistance to a CD4-Mimetic Compound.

Journal of virology - 14 Sept 2022

Anang Saumya, Richard Jonathan, Bourassa Catherine, Goyette Guillaume, Chiu Ta-Jung, Chen Hung-Ching, Smith Amos B, Madani Navid, Finzi Andrés, Sodroski Joseph

Abstract excerpt

Binding to the host cell receptors CD4 and CCR5/CXCR4 triggers conformational changes in the human immunodeficiency virus (HIV-1) envelope glycoprotein (Env) trimer that promote virus entry. CD4 binding allows the gp120 exterior Env to bind CCR5/CXCR4 and induces a short-lived prehairpin intermediate conformation in the gp41 transmembrane Env. Small-molecule CD4-mimetic compounds (CD4mcs) bind within the...

Read the complete abstract on PubMed

Topics

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

Share to CD4 Antigens
Share to env Gene Products, Human Immunodeficiency Virus

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

Share to Guanidines

Share to HIV Envelope Protein gp120

Share to HIV Envelope Protein gp41

Share to HIV Fusion Inhibitors

Share to Indenes

Share to Receptors, HIV

Source

Open in PubMed Open full text

Identifiers

PMID: 35980207
DOI: 10.1128/jvi.00636-22
PMCID: PMC9472635

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

Characterization of Human Immunodeficiency Virus (HIV-1) Envelope Glycoprotein Variants Selected for Resistance to a CD4-Mimetic Compound.PMID 35980207Read ↗

Characterization of human immunodeficiency virus (HIV-1) envelope glycoprotein variants selected for resistance to a CD4-mimetic compoundSemantic proximity Read ↗

V3 tip determinants of susceptibility to inhibition by CD4-mimetic compounds in natural clade A human immunodeficiency virus (HIV-1) envelope glycoproteinsSemantic proximity Read ↗

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

Localized Changes in the gp120 Envelope Glycoprotein Confer Resistance to Human Immunodeficiency Virus Entry Inhibitors BMS-806 and #155Semantic proximity Read ↗

Broadly resistant HIV-1 against CD4-binding site neutralizing antibodiesSemantic proximity Read ↗

Activation and Inactivation of Primary Human Immunodeficiency Virus Envelope Glycoprotein Trimers by CD4-Mimetic Compounds.Semantic proximity Read ↗

The HIV-1 Env gp120 Inner Domain Shapes the Phe43 Cavity and the CD4 Binding SiteSemantic proximity Read ↗

Structure-function analyses reveal key molecular determinants of HIV-1 CRF01_AE resistance to the entry inhibitor temsavirSemantic proximity Read ↗

A low-molecular-weight entry inhibitor of both CCR5- and CXCR4-tropic strains of human immunodeficiency virus type 1 targets a novel site on gp41.Semantic proximity Read ↗

Reduced Susceptibility to VIRIP-Based HIV-1 Entry Inhibitors Has a High Genetic Barrier and Severe Fitness Costs.Semantic proximity Read ↗

A small molecule HIV-1 inhibitor that targets the HIV-1 envelope and inhibits CD4 receptor bindingSemantic proximity Read ↗

A common mechanism of clinical HIV-1 resistance to the CCR5 antagonist maraviroc despite divergent resistance levels and lack of common gp120 resistance mutations.Semantic proximity Read ↗

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