Ergosterol

Ergosterol is a lipid of Sterol Lipids (ST) class. Ergosterol is associated with abnormalities such as Disintegration (morphologic abnormality), Consumption-archaic term for TB, Candidiasis, Mycoses and Iodotyrosyl coupling defect. The involved functions are known as Anabolism, sporulation, 5-(carboxyamino)imidazole ribonucleotide mutase activity, Subtraction process and Physiologic Organization. Ergosterol often locates in Pore, Membrane, Protoplasm, Plasma membrane and Endoplasmic Reticulum. The associated genes with Ergosterol are IMPACT gene, BLVRB gene, CYP51A1 gene, CDR1 wt Allele and HM13 gene. The related lipids are Sterols, Cardiolipins, Membrane Lipids, fecosterol and Phosphatidylserines. The related experimental models are Knock-out.

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Introduction

To understand associated biological information of Ergosterol, we collected biological information of abnormalities, associated pathways, cellular/molecular locations, biological functions, related genes/proteins, lipids and common seen animal/experimental models with organized paragraphs from literatures.

What diseases are associated with Ergosterol?

Ergosterol is suspected in Infection, Mycoses, Candidiasis, Chagas Disease, Cyst, Dermatophytosis and other diseases in descending order of the highest number of associated sentences.

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Disease Cross reference Weighted score Related literature
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Possible diseases from mapped MeSH terms on references

We collected disease MeSH terms mapped to the references associated with Ergosterol

PubChem Associated disorders and diseases

What pathways are associated with Ergosterol

Lipid pathways are not clear in current pathway databases. We organized associated pathways with Ergosterol through full-text articles, including metabolic pathways or pathways of biological mechanisms.

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Pathway name Related literatures
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PubChem Biomolecular Interactions and Pathways

Link to PubChem Biomolecular Interactions and Pathways

What cellular locations are associated with Ergosterol?

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What functions are associated with Ergosterol?


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Function Cross reference Weighted score Related literatures

What lipids are associated with Ergosterol?

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What genes are associated with Ergosterol?

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Gene Cross reference Weighted score Related literatures

What common seen animal models are associated with Ergosterol?

Knock-out

Knock-out are used in the study 'Multidrug transporters CaCdr1p and CaMdr1p of Candida albicans display different lipid specificities: both ergosterol and sphingolipids are essential for targeting of CaCdr1p to membrane rafts.' (Pasrija R et al., 2008) and Knock-out are used in the study 'UPC2A is required for high-level azole antifungal resistance in Candida glabrata.' (Whaley SG et al., 2014).

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Model Cross reference Weighted score Related literatures
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NCBI Entrez Crosslinks

All references with Ergosterol

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Authors Title Published Journal PubMed Link
Ohvo-Rekilä H et al. Cyclodextrin-catalyzed extraction of fluorescent sterols from monolayer membranes and small unilamellar vesicles. 2000 Chem. Phys. Lipids pmid:10823464
Ohnuma N et al. Sterol constituents from two edible mushrooms, Lentinula edodes and Tricholoma matsutake. 2000 Chem. Pharm. Bull. pmid:10823718
Barton DH and Patin H Chemistry of the tricarbonyliron complexes of calciferol and ergosterol. 1976 J. Chem. Soc. Perkin Trans. I pmid:1083856
Tsukida K et al. Simultaneous determination of eight vitamin D2 isomers by proton magnetic resonance spectroscopy. 1976 J. Nutr. Sci. Vitaminol. pmid:1085350
Múcková M et al. Synergy between 6-amino-2-n-pentylthiobenzothiazole and ergosterol biosynthesis-inhibiting antimycotics against Candida albicans in vitro. 2000 Int. J. Antimicrob. Agents pmid:10854813
Aceves MB Soil ergosterol, dimethyl sulphide reduction, and microbial biomass along a Zn concentrations gradient in soils from a mine spoil tip. 2000 Bull Environ Contam Toxicol pmid:10856334
Schoer JK et al. Lysosomal membrane cholesterol dynamics. 2000 Biochemistry pmid:10869172
Dales RE et al. Testing the association between residential fungus and health using ergosterol measures and cough recordings. 1999 Mycopathologia pmid:10872512
Chen TC et al. An evaluation of the biologic activity and vitamin D receptor binding affinity of the photoisomers of vitamin D3 and previtamin D3. 2000 J. Nutr. Biochem. pmid:10876100
Arthington-Skaggs BA et al. Quantitation of Candida albicans ergosterol content improves the correlation between in vitro antifungal susceptibility test results and in vivo outcome after fluconazole treatment in a murine model of invasive candidiasis. 2000 Antimicrob. Agents Chemother. pmid:10898679
Nurminen T et al. Neutral lipids in the cells and cell envelope fractions of aerobic baker's yeast and anaerobic brewer's yeast. 1975 Chem. Phys. Lipids pmid:1091369
Zeppa S et al. Estimation of fungal biomass and transcript levels in Tilia platyphyllos-Tuber borchii ectomycorrhizae. 2000 FEMS Microbiol. Lett. pmid:10913693
Bailey RB and Parks LW Potassium translocation in yeast mitochondria and its relationship to ergostrol biosynthesis. 1975 J. Bacteriol. pmid:1092661
Hughes TR et al. Functional discovery via a compendium of expression profiles. 2000 Cell pmid:10929718
Kontoyiannis DP Modulation of fluconazole sensitivity by the interaction of mitochondria and erg3p in Saccharomyces cerevisiae. 2000 J. Antimicrob. Chemother. pmid:10933640
Kontoyiannis DP Efflux-mediated resistance to fluconazole could be modulated by sterol homeostasis in Saccharomyces cerevisiae. 2000 J. Antimicrob. Chemother. pmid:10933641
Barton DH et al. Biosynthesis of terpenes and steroids. X. The sterols of some yeast mutants doubly defective in ergosterol biosynthesis. 1975 J. Chem. Soc. Perkin Trans. I pmid:1094026
Gale EF et al. Factors affecting the changes in amphotericin sensitivity of Candida albicans during growth. 1975 J. Gen. Microbiol. pmid:1094096
Pieringer J and Conner RL Positional distribution of fatty acids in the glycerophospholipids of Tetrahymena pyriformis. 1979 J. Lipid Res. pmid:109555
Avdulov NA et al. Cholesterol efflux to high-density lipoproteins and apolipoprotein A-I phosphatidylcholine complexes is inhibited by ethanol: role of apolipoprotein structure and cooperative interaction of phosphatidylcholine and cholesterol. 2000 Biochemistry pmid:10956052