ArticleFrontiers in pharmacology2017
Evaluation of Selected CYP51A1 Polymorphisms in View of Interactions with Substrate and Redox Partner.
Article in Frontiers in pharmacology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 10 citations in OpenAlex.
- Deciphering cytochrome P450 reductase role in MASLD: molecular mechanisms and pathophysiological implications.Nature reviews. Gastroenterology & hepatology · 2026Review
- Knockouts ofiScience · 2024Article
- Visfatin impact on the proteome of porcine luteal cells during implantation.Scientific reports · 2024Article
- Proteomic analysis of small extracellular vesicles unique to cervical cancer.Translational cancer research · 2023Article
- Transcriptomic Modulation Reveals the Specific Cellular Response in Chinese Sea Bass (International journal of molecular sciences · 2023Article
- Transcriptome Analysis of Effects of Folic Acid Supplement on Gene Expression in Liver of Broiler Chickens.Frontiers in veterinary science · 2021Article
- Chronic Disruption of the Late Cholesterol Synthesis Leads to Female-Prevalent Liver Cancer.Cancers · 2020Article
- ITRAQ-Based Quantitative Proteomics Reveals the Proteome Profiles of Primary Duck Embryo Fibroblast Cells Infected with Duck Tembusu Virus.BioMed research international · 2019Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cholesterol is essential for development, growth, and maintenance of organisms. Mutations in cholesterol biosynthetic genes are embryonic lethal and few polymorphisms have been so far associated with pathologies in humans. Previous analyses show that lanosterol 14α-demethylase (CYP51A1) from the late part of cholesterol biosynthesis has only a few missense mutations with low minor allele frequencies and low association with pathologies in humans. The aim of this study is to evaluate the role of amino acid changes in the natural missense mutations of the hCYP51A1 protein. We searched SNP databases for existing polymorphisms of
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