ArticleJournal of virology2006
Two domains that control prefusion stability and transport competence of the measles virus fusion protein.
Article in Journal of virology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
38 citing papers in PubMed, 51 citations in OpenAlex.
- Target-Based Antiviral Drug Development Against Human Respiratory Viruses.Pathogens (Basel, Switzerland) · 2026Review
- Structural basis of measles virus polymerase inhibition by nonnucleoside inhibitor ERDRP-0519.Nature communications · 2025Article
- Repurposing an In Vitro Measles Virus Dissemination Assay for Screening of Antiviral Compounds.Viruses · 2022Review
- Antivirals targeting paramyxovirus membrane fusion.Current opinion in virology · 2021Review
- M protein of subacute sclerosing panencephalitis virus, synergistically with the F protein, plays a crucial role in viral neuropathogenicity.The Journal of general virology · 2021Article
- Inhibition of Measles Viral Fusion Is Enhanced by Targeting Multiple Domains of the Fusion Protein.ACS nano · 2021Article
- Fitness selection of hyperfusogenic measles virus F proteins associated with neuropathogenic phenotypes.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Identification and Characterization of a Small-Molecule Rabies Virus Entry Inhibitor.Journal of virology · 2020Article
- Measles Resurgence and Drug Development.Current opinion in virology · 2020Review
- Review
- Measles Encephalitis: Towards New Therapeutics.Viruses · 2019Review
- Bipartite interface of the measles virus phosphoprotein X domain with the large polymerase protein regulates viral polymerase dynamics.PLoS pathogens · 2019Article
- Structures of the prefusion form of measles virus fusion protein in complex with inhibitors.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Mutations in the Fusion Protein of Measles Virus That Confer Resistance to the Membrane Fusion Inhibitors Carbobenzoxy-d-Phe-l-Phe-Gly and 4-Nitro-2-Phenylacetyl Amino-Benzamide.Journal of virology · 2017Article
- In Vivo Efficacy of Measles Virus Fusion Protein-Derived Peptides Is Modulated by the Properties of Self-Assembly and Membrane Residence.Journal of virology · 2017Article
- Review
- Blocking Respiratory Syncytial Virus Entry: A Story with Twists.DNA and cell biology · 2015Article
- Efficient replication of a paramyxovirus independent of full zippering of the fusion protein six-helix bundle domain.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Cross-resistance mechanism of respiratory syncytial virus against structurally diverse entry inhibitors.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Molecular determinants defining the triggering range of prefusion F complexes of canine distemper virus.Journal of virology · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Most viral glycoproteins mediating membrane fusion adopt a metastable native conformation and undergo major conformational changes during fusion. We previously described a panel of compounds that specifically prevent fusion induced by measles virus (MV), most likely by interfering with conformational rearrangements of the MV fusion (F) protein. To further elucidate the basis of inhibition and better understand the mechanism of MV glycoprotein-mediated fusion, we generated and characterized resistant MV variants. Spontaneous mutations conferring drug resistance were confirmed in transient assays and in the context of recombinant virions and were in all cases located in the fusion protein. Several mutations emerged independently at F position 462, which is located in the C-terminal heptad repeat (HR-B) domain. In peptide competition assays, all HR-B mutants at residue 462 revealed reduced affinity for binding to the HR-A core complex compared to unmodified HR-B. Combining mutations at residue 462 with mutations in the distal F head region, which we had previously identified as mediating drug resistance, causes intracellular retention of the mutant proteins. The transport competence and activity of the mutants can be restored, however, by incubation at reduced temperature or in the presence of the inhibitory compounds, indicating that the F escape mutants have a reduced conformational stability and that the inhibitors stabilize a transport-competent conformation of the F trimer. The data support the conclusion that residues located in the head domain of the F trimer and the HR-B region contribute jointly to controlling F conformational stability.
Indexed as
Identifiers
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.