ArticleArchives of Razi Institute2021
Investigation of Interferon Gamma Activity Using Bioinformatics Methods.
Article in Archives of Razi Institute, 2021. 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
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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
2 citing papers in PubMed, 2 citations in OpenAlex.
- Computational design of a novel multi-epitope vaccine candidate against group A rotavirus.Virology journal · 2026Article
- Genome-wide identification, molecular evolution and gene expression of P450 gene family in Cyrtotrachelus buqueti.BMC genomics · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Breast cancer grows from the breast tissue and is a severe health problem worldwide. Genetics is believed to be the primary cause of all cases of breast cancer via gene mutation. Bioinformatics methodology has been used to determine the sequences and structures of bioactive substances. This study aimed to analyze the function and structure of the Interferon Gamma (IFNγ) in healthy controls and patients with breast cancer using bioinformatics methods. Blood samples were collected from 75 patients with breast cancer and 25 healthy subjects as control samples. The results showed transition mutation (30%) and transversion mutation (70%) in patients with breast cancer. Moreover, missense mutations (84%) and silent mutations (16%) were detected by BLAST. In addition, the amino acid of the IFNγ protein consisting of alpha-helical, β-sheet, and coil of secondary structure was determined in this study using BioEdit. The results of the physicochemical properties of the IFNγ protein reflect the function, stability, molecular weight, isoelectric point, and instability index of the IFNγ protein using ProtParam. Moreover, the results of mutation affected the percentage of alpha-helix, β-turns, and coil in breast cancer patients compared to healthy groups with reference of NCBI using PSIpred program. Additionally, the PHYRE2 server and RasMol program showed a tertiary structure of the IFNγ protein in breast cancer patients. Furthermore, the STRING program revealed the poly IFNγ protein interacted with other proteins to perform its functions normally. From the recorded data in the current study, it was concluded that IFNγ is considered a marker for patients with breast cancer.
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Registered trials
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