MeSH term | MeSH ID | Detail |
---|---|---|
Cattle Diseases | D002418 | 24 associated lipids |
Body Weight | D001835 | 333 associated lipids |
Adenoma | D000236 | 40 associated lipids |
Adenocarcinoma | D000230 | 166 associated lipids |
STERIGMATOCYSTIN is a lipid of Polyketides (PK) class. Sterigmatocystin is associated with abnormalities such as CLEFT LIP, CONGENITAL HEALED, Exanthema and Lung diseases. The involved functions are known as sterigmatocystin biosynthetic process, Signal, secondary metabolic process, Biosynthetic Pathways and Anabolism. Sterigmatocystin often locates in Genital system, SAGA complex, Chromosomes, germ tube and Extracellular. The associated genes with STERIGMATOCYSTIN are Genome, Genes, vif, Homologous Gene, Genes, Regulator and Gene Clusters. The related lipids are hexanoic acid, Fatty Acids and Fatty Acids, Unsaturated.
To understand associated biological information of STERIGMATOCYSTIN, 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.
STERIGMATOCYSTIN is suspected in CLEFT LIP, CONGENITAL HEALED, Exanthema, Lung diseases and other diseases in descending order of the highest number of associated sentences.
Disease | Cross reference | Weighted score | Related literature |
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We collected disease MeSH terms mapped to the references associated with STERIGMATOCYSTIN
MeSH term | MeSH ID | Detail |
---|---|---|
Cattle Diseases | D002418 | 24 associated lipids |
Body Weight | D001835 | 333 associated lipids |
Adenoma | D000236 | 40 associated lipids |
Adenocarcinoma | D000230 | 166 associated lipids |
There are no associated biomedical information in the current reference collection.
Associated locations are in red color. Not associated locations are in black.
Location | Cross reference | Weighted score | Related literatures |
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Function | Cross reference | Weighted score | Related literatures |
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Lipid concept | Cross reference | Weighted score | Related literatures |
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Gene | Cross reference | Weighted score | Related literatures |
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There are no associated biomedical information in the current reference collection.
Authors | Title | Published | Journal | PubMed Link |
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Leitao J et al. | Action of phosphine (PH3) on production of sterigmatocystin by various fungal strains isolated from foodstuffs. | 1990 | Food Addit Contam | pmid:2262035 |
Anderson JA et al. | Versicolorin A hemiacetal, hydroxydihydrosterigmatocystin, and aflatoxin G2 alpha reductase activity in extracts from Aspergillus parasiticus. | 1990 | Mycopathologia | pmid:2233978 |
Cleveland TE | Conversion of dihydro-O-methylsterigmatocystin to aflatoxin B2 by Aspergillus parasiticus. | 1989 May-Jun | Arch. Environ. Contam. Toxicol. | pmid:2730159 |
Baertschi SW et al. | Comparison of rates of enzymatic oxidation of aflatoxin B1, aflatoxin G1, and sterigmatocystin and activities of the epoxides in forming guanyl-N7 adducts and inducing different genetic responses. | 1989 Mar-Apr | Chem. Res. Toxicol. | pmid:2519710 |
Shimada T et al. | Human liver microsomal cytochrome P-450 enzymes involved in the bioactivation of procarcinogens detected by umu gene response in Salmonella typhimurium TA 1535/pSK1002. | 1989 | Cancer Res. | pmid:2655891 |
Adamson RH | Induction of hepatocellular carcinoma in nonhuman primates by chemical carcinogens. | 1989 | Cancer Detect. Prev. | pmid:2559797 |
Lee LS | Metabolic precursor regulation of aflatoxin formation in toxigenic and non-toxigenic strains of Aspergillus flavus. | 1989 | Mycopathologia | pmid:2515437 |
Chung DH et al. | Immunochemical assay applied to mycotoxin biosynthesis: ELISA comparison of sterigmatocystin production by Aspergillus versicolor and Aspergillus nidulans. | 1989 | Mycopathologia | pmid:2693965 |
Shahin MM | The importance of analyzing structure-activity relationships in mutagenicity studies. | 1989 | Mutat. Res. | pmid:2682227 |
Shimada T and Guengerich FP | Evidence for cytochrome P-450NF, the nifedipine oxidase, being the principal enzyme involved in the bioactivation of aflatoxins in human liver. | 1989 | Proc. Natl. Acad. Sci. U.S.A. | pmid:2492107 |