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

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

The Journal of biological chemistry - 17 Aug 2018

Yu Danwei, Ding Xiaohui, Liu Zixuan, Wu Xiyuan, Zhu Yuanmei, Wei Huanmian, Chong Huihui, Cui Sheng, He Yuxian

Abstract excerpt

Host cell infection with HIV-1 requires fusion of viral and cell membranes. Sifuvirtide (SFT) is a peptide-based HIV-1 fusion inhibitor approved for phase III clinical trials in China. Here, we focused on characterizing HIV-1 variants highly resistant to SFT to gain insight into the molecular resistance mechanism. Three primary substitutions (V38A, A47I, and Q52R) located at the inhibitor-binding site of HIV-1's...

Read the complete abstract on PubMed

Topics

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

Share to Crystallography, X-Ray
Share to Drug Resistance, Viral

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HIV Envelope Protein gp41

Share to HIV Fusion Inhibitors

Share to Membrane Fusion

Share to Peptides

Share to Sequence Homology

Share to Structure-Activity Relationship

Source

Open in PubMed Open full text

Identifiers

PMID: 29929981
DOI: 10.1074/jbc.RA118.003538
PMCID: PMC6102148

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Molecular mechanism of HIV-1 resistance to sifuvirtide, a clinical trial-approved membrane fusion inhibitor.PMID 29929981Read ↗

Mechanism of HIV-1 Resistance to Short-Peptide Fusion Inhibitors Targeting the Gp41 Pocket.Semantic proximity Read ↗

Broad antiviral activity and crystal structure of HIV-1 fusion inhibitor sifuvirtide.Semantic proximity Read ↗

The M-T hook structure increases the potency of HIV-1 fusion inhibitor sifuvirtide and overcomes drug resistance.Semantic proximity Read ↗

Design and evaluation of sifuvirtide, a novel HIV-1 fusion inhibitor.Semantic proximity Read ↗

In vitro selection and characterization of HIV-1 variants with increased resistance to sifuvirtide, a novel HIV-1 fusion inhibitor.Semantic proximity Read ↗

Detailed mechanistic insights into HIV-1 sensitivity to three generations of fusion inhibitors.Semantic proximity Read ↗

Design of a highly potent HIV-1 fusion inhibitor targeting the gp41 pocket.Semantic proximity Read ↗

Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency VirusSemantic proximity Read ↗

Resistance of human immunodeficiency virus type 1 to a third-generation fusion inhibitor requires multiple mutations in gp41 and is accompanied by a dramatic loss of gp41 function.Semantic proximity Read ↗

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

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

Exceptional potency and structural basis of a T1249-derived lipopeptide fusion inhibitor against HIV-1, HIV-2, and simian immunodeficiency virusSemantic proximity Read ↗

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