ArticleFEMS yeast research2018
Reconstitution of human peroxisomal β-oxidation in yeast.
Article in FEMS yeast research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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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.
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Who cites it
5 citing papers in PubMed, 3 citations in OpenAlex.
- HOM2 and TPK1 are associated with Kluyveromyces marxianus growth under high-temperature and reduced-aeration conditions.World journal of microbiology & biotechnology · 2026Article
- Engineering de novo formatotrophy in the non-model yeastNature synthesis · 2026Article
- Acyl CoA oxidase: from its expression, structure, folding, and import to its role in human health and disease.Molecular genetics and genomics : MGG · 2023Review
- Key enzymes involved in the utilization of fatty acids byFrontiers in microbiology · 2023Review
- Application of Metabolomics in the Study of Starvation-Induced Autophagy inJournal of fungi (Basel, Switzerland) · 2021Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
We report the permanent introduction of the human peroxisomal β-oxidation enzymatic machinery required for straight chain degradation of fatty acids into the yeast, Saccharomyces cerevisiae. Peroxisomal β-oxidation encompasses four sequential reactions that are confined to three enzymes. The genes encoding human acyl-CoA oxidase 1, peroxisomal multifunctional enzyme type 2 and 3-ketoacyl-CoA thiolase were introduced into the genomic loci of their yeast gene equivalents. The human β-oxidation genes were individually tagged with sequence coding for GFP and expression of the protein chimeras as well as their targeting to peroxisomes was confirmed. Functional complementation of the β-oxidation pathway was assessed by growth on media containing fatty acids of different chain lengths. Yeast cells exhibited distinctive substrate specificities depending on whether they expressed the human or their endogenous β-oxidation machinery. The genetic engineering of yeast to contain a 'humanized' organelle is a first step for the in vivo study of human peroxisome disorders in a model organism.
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Registered trials
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