ArticleInternational journal of molecular sciences2025
Design, Co-Expression, and Evaluation for Assembly of the Structural Proteins from Thermophilic Bacteriophage ΦIN93.
Article in International journal of molecular sciences, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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
2 citing papers in PubMed.
- Multi-gene Co-expression systems inSynthetic and systems biotechnology · 2026Review
- The Structural Proteins of Thermophilic Bacteriophage P23-77: Expression and Characterization.International journal of molecular sciences · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Bacteriophage ΦIN93 has an icosahedral-like capsid that is believed to be composed of two putative capsid or coat proteins, namely open reading frame (ORF)13 and ORF14. In addition to the two capsid proteins, there are other proteins that may be associated with the structure of the virus. For example, five other proteins (ORF12, ORF16, ORF17, ORF19, and ORF20) in the virus have been identified as putative membrane-associated proteins. It is believed that membrane-associated proteins associate with coat proteins (serve as scaffolding proteins) to promote viral assembly. While the expression/co-expression of ORF13 and ORF14 have been done to assess if they can assemble to form virus-like particles (VLPs), the expression of any of the membrane-associated proteins and their contribution to assembly have never been attempted. In this study, we successfully co-expressed, for the first time, three membrane-associated proteins (ORF12, ORF16, ORF17) in addition to ORF13 and ORF14 in thermophilic bacteria (
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.