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

Structural and Functional Characterization of the Secondary Mutation N126K Selected by Various HIV-1 Fusion Inhibitors.

Viruses - 18 Mar 2020

Yu Danwei, Su Yang, Ding Xiaohui, Zhu Yuanmei, Qin Bo, Chong Huihui, Cui Sheng, He Yuxian

Abstract excerpt

Peptides derived from the C-terminal heptad repeat (CHR) region of HIV-1 gp41 is potent viral membrane fusion inhibitors, such as the first clinically approved peptide drug T20 and a group of newly-designed peptides. The resistance profiles of various HIV-1 fusion inhibitors were previously characterized, and the secondary mutation N126K in the gp41 CHR was routinely identified during the in vitro and in vivo...

Read the complete abstract on PubMed

Topics

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

Share to env Gene Products, Human Immunodeficiency Virus
Share to HIV Envelope Protein gp41

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HIV Fusion Inhibitors

Share to Molecular Conformation

Share to Molecular Docking Simulation

Share to Molecular Dynamics Simulation

Share to Protein Stability

Share to Virus Internalization

Source

Open in PubMed Open full text

Identifiers

PMID: 32197300
DOI: 10.3390/v12030326
PMCID: PMC7150849

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural and Functional Characterization of the Secondary Mutation N126K Selected by Various HIV-1 Fusion Inhibitors.PMID 32197300Read ↗

Identification of a Critical Motif for the Human Immunodeficiency Virus Type 1 (HIV-1) gp41 Core Structure: Implications for Designing Novel Anti-HIV Fusion InhibitorsSemantic proximity Read ↗

ADS-J1 inhibits HIV-1 infection and membrane fusion by targeting the highly conserved pocket in the gp41 NHR-trimer.Semantic proximity Read ↗

A novel HIV-1 gp41 tripartite model for rational design of HIV-1 fusion inhibitors with improved antiviral activitySemantic proximity Read ↗

Mutations of Glu560 within HIV-1 Envelope Glycoprotein N-terminal heptad repeat region contribute to resistance to peptide inhibitors of virus entry.Semantic proximity Read ↗

Identification of critical antibody-binding sites in the HIV-1 gp41 six-helix bundle core as potential targets for HIV-1 fusion inhibitors.Semantic proximity Read ↗

HIV-1 variants with a single-point mutation in the gp41 pocket region exhibiting different susceptibility to HIV fusion inhibitors with pocket- or membrane-binding domain.Semantic proximity Read ↗

Resistance profiles of novel electrostatically constrained HIV-1 fusion inhibitors.Semantic proximity Read ↗

Molecular mechanism of HIV-1 resistance to sifuvirtide, a clinical trial-approved membrane fusion inhibitor.Semantic proximity Read ↗

Mutations conferring resistance to human immunodeficiency virus type 1 fusion inhibitors are restricted by gp41 and Rev-responsive element functions.Semantic proximity Read ↗

Conserved Salt Bridge between the N- and C-Terminal Heptad Repeat Regions of the Human Immunodeficiency Virus Type 1 gp41 Core Structure Is Critical for Virus Entry and InhibitionSemantic proximity Read ↗

Conserved Residue Lys574 in the Cavity of HIV-1 Gp41 Coiled-coil Domain Is Critical for Six-helix Bundle Stability and Virus EntrySemantic proximity Read ↗

Human immunodeficiency virus (HIV) gp41 escape mutants: cross-resistance to peptide inhibitors of HIV fusion and altered receptor activation of gp120.Semantic proximity Read ↗

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