ArticleJournal of the American Chemical Society2019
Dual Inhibition of Human Parainfluenza Type 3 and Respiratory Syncytial Virus Infectivity with a Single Agent.
Article in Journal of the American Chemical Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
20 citing papers in PubMed, 17 citations in OpenAlex.
- Hyperfusogenic Mutations Destabilize the Postfusion Six-Helix Bundle of the Measles Virus Fusion Glycoprotein.Biochemistry · 2026Article
- Identification and structure-activity relationship analysis of minimal fusion inhibitors targeting measles virus F protein.RSC medicinal chemistry · 2026Article
- Double-Stapled Peptide Scan Yields Potent Fusion Inhibitors of Respiratory Syncytial Virus.Journal of medicinal chemistry · 2026Article
- Article
- Enhancing the solubility of SARS-CoV-2 inhibitors to increase future prospects for clinical development.Journal of virology · 2025Article
- Development of nebulized inhalation delivery for fusion-inhibitory lipopeptides to protect non-human primates against Nipah-Bangladesh infection.Antiviral research · 2025Article
- Helical peptides with disordered regions for measles viruses provide new generalized insights into fusion inhibitors.iScience · 2024Article
- Article
- A pan-coronavirus peptide inhibitor prevents SARS-CoV-2 infection in mice by intranasal delivery.Science China. Life sciences · 2023Article
- Antivirals targeting paramyxovirus membrane fusion.Current opinion in virology · 2021Review
- Engineering Protease-Resistant Peptides to Inhibit Human Parainfluenza Viral Respiratory Infection.Journal of the American Chemical Society · 2021Article
- Invited review: human air-liquid-interface organotypic airway tissue models derived from primary tracheobronchial epithelial cells-overview and perspectives.In vitro cellular & developmental biology. Animal · 2021Review
- Parainfluenza virus entry at the onset of infection.Advances in virus research · 2021Article
- Intranasal fusion inhibitory lipopeptide prevents direct contact SARS-CoV-2 transmission in ferrets.bioRxiv : the preprint server for biology · 2020Article
- Inhibition of Coronavirus EntrymBio · 2020Article
- Effects of Single α-to-β Residue Replacements on Recognition of an Extended Segment in a Viral Fusion Protein.ACS infectious diseases · 2020Article
- Review
- Article
- Structure-Guided Improvement of a Dual HPIV3/RSV Fusion Inhibitor.Journal of the American Chemical Society · 2020Article
- Identification of the Functional Domain of HPIV3 Matrix Protein Interacting with Nucleocapsid Protein.BioMed research international · 2020Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Human parainfluenza virus 3 (HPIV3) and respiratory syncytial virus (RSV) cause lower respiratory infection in infants and young children. There are no vaccines for these pathogens, and existing treatments have limited or questionable efficacy. Infection by HPIV3 or RSV requires fusion of the viral and cell membranes, a process mediated by a trimeric fusion glycoprotein (F) displayed on the viral envelope. Once triggered, the pre-fusion form of F undergoes a series of conformational changes that first extend the molecule to allow for insertion of the hydrophobic fusion peptide into the target cell membrane and then refold the trimeric assembly into an energetically stable post-fusion state, a process that drives the merger of the viral and host cell membranes. Peptides derived from defined regions of HPIV3 F inhibit infection by HPIV3 by interfering with the structural transitions of the trimeric F assembly. Here we describe lipopeptides derived from the C-terminal heptad repeat (HRC) domain of HPIV3 F that potently inhibit infection by both HPIV3 and RSV. The lead peptide inhibits RSV infection as effectively as does a peptide corresponding to the RSV HRC domain itself. We show that the inhibitors bind to the N-terminal heptad repeat (HRN) domains of both HPIV3 and RSV F with high affinity. Co-crystal structures of inhibitors bound to the HRN domains of HPIV3 or RSV F reveal remarkably different modes of binding in the N-terminal segment of the inhibitor.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.