ReviewViruses2012
Envelope glycoprotein of arenaviruses.
Review in Viruses, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 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
69 citing papers in PubMed, 105 citations in OpenAlex.
- Immunogenicity of recombinant vesicular stomatitis virus-vectored vaccines expressing the Machupo virus glycoprotein in different genome positions.Journal of virology · 2026Article
- CD164 is an endolysomal host factor for entry of Clade A New World Arenaviruses.bioRxiv : the preprint server for biology · 2026Article
- Comparison of Vaccine Platforms for Machupo Virus.Vaccines · 2026Article
- Molecular organization of the New World arenavirus spike glycoprotein complex.Nature microbiology · 2025Article
- In situ insights into antibody-mediated neutralization of a pre-fusion Junin virus glycoprotein complex.Cell reports · 2025Article
- Article
- The Lassa Virus Stable Signal Peptide Undergoes a Conformational Change to Aid Viral Fusion.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Flunarizine as a Candidate for Drug Repurposing Against Human Pathogenic Mammarenaviruses.Viruses · 2025Article
- A Lassa virus live attenuated vaccine candidate that is safe and efficacious in guinea pigs.NPJ vaccines · 2024Article
- Glycoprotein-Specific Polyclonal Antibodies Targeting Machupo Virus Protect Guinea Pigs against Lethal Infection.Vaccines · 2024Article
- Treatment of highly virulent mammarenavirus infections-status quo and future directions.Expert opinion on drug discovery · 2024Review
- Entry inhibitors as arenavirus antivirals.Frontiers in microbiology · 2024Review
- Intrasegmental recombination as an evolutionary force of Lassa fever virus.Frontiers in microbiology · 2024Article
- The underlying mechanisms of arenaviral entry through matriglycan.Frontiers in molecular biosciences · 2024Review
- Article
- Fusogenic structural changes in arenavirus glycoproteins are associated with viroporin activity.PLoS pathogens · 2023Article
- Lassa Virus Genetics.Current topics in microbiology and immunology · 2023Article
- Glycosylation of viral proteins: Implication in virus-host interaction and virulence.Virulence · 2022Review
- Persistent Reptarenavirus and Hartmanivirus Infection in Cultured Boid Cells.Microbiology spectrum · 2022Article
- Article
9 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Arenaviruses include lethal human pathogens which pose serious public health threats. So far, no FDA approved vaccines are available against arenavirus infections, and therapeutic options are limited, making the identification of novel drug targets for the development of efficacious therapeutics an urgent need. Arenaviruses are comprised of two RNA genome segments and four proteins, the polymerase L, the envelope glycoprotein GP, the matrix protein Z, and the nucleoprotein NP. A crucial step in the arenavirus life-cycle is the biosynthesis and maturation of the GP precursor (GPC) by cellular signal peptidases and the cellular enzyme Subtilisin Kexin Isozyme-1 (SKI-1)/Site-1 Protease (S1P) yielding a tripartite mature GP complex formed by GP1/GP2 and a stable signal peptide (SSP). GPC cleavage by SKI-1/S1P is crucial for fusion competence and incorporation of mature GP into nascent budding virion particles. In a first part of our review, we cover basic aspects and newer developments in the biosynthesis of arenavirus GP and its molecular interaction with SKI-1/S1P. A second part will then highlight the potential of SKI-1/S1P-mediated processing of arenavirus GPC as a novel target for therapeutic intervention to combat human pathogenic arenaviruses.
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.