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 resistance to a potent D-peptide HIV entry inhibitor.

Retrovirology - 22 Oct 2019

Smith Amanda R, Weinstock Matthew T, Siglin Amanda E, Whitby Frank G, Francis J Nicholas, Hill Christopher P, Eckert Debra M, Root Michael J, Kay Michael S

Abstract excerpt

BACKGROUND: PIE12-trimer is a highly potent D-peptide HIV-1 entry inhibitor that broadly targets group M isolates. It specifically binds the three identical conserved hydrophobic pockets at the base of the gp41 N-trimer with sub-femtomolar affinity. This extremely high affinity for the transiently exposed gp41 trimer provides a reserve of binding energy (resistance capacitor) to prevent the viral resistance...

Read the complete abstract on PubMed

Topics

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

Share to Anti-HIV Agents
Share to Cell Line

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

Share to Drug Resistance, Viral

Share to HIV Infections

Share to Mutation

Share to Peptides

Share to Virus Internalization

Source

Open in PubMed Open full text

Identifiers

PMID: 31640718
DOI: 10.1186/s12977-019-0489-7
PMCID: PMC6805555

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Characterization of resistance to a potent D-peptide HIV entry inhibitor.PMID 31640718Read ↗

Altered Env conformational dynamics as a mechanism of resistance to peptide-triazole HIV-1 inactivators.Semantic proximity Read ↗

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

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

HIV-1 Env gp120 structural determinants for peptide triazole dual receptor site antagonism.Semantic proximity Read ↗

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

Progressive emergence of an S153F plus R263K combination of integrase mutations in the proviral DNA of one individual successfully treated with dolutegravir.Semantic 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 ↗

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

Escape from Human Immunodeficiency Virus Type 1 (HIV-1) Entry InhibitorsSemantic proximity Read ↗

Selective resistance profiles emerging in patient-derived clinical isolates with cabotegravir, bictegravir, dolutegravir, and elvitegravir.Semantic proximity Read ↗

Highly drug-resistant HIV-1 protease reveals decreased intra-subunit interactions due to clusters of mutations.Semantic proximity Read ↗

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