MeSH term | MeSH ID | Detail |
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Melanoma | D008545 | 69 associated lipids |
Dimethylallyl pyrophosphate is a lipid of Prenol Lipids (PR) class. Dimethylallyl pyrophosphate is associated with abnormalities such as Consumption-archaic term for TB and Wiskott-Aldrich Syndrome. The involved functions are known as Anabolism, Biochemical Pathway, Oxidation, Process and Chelating Activity [MoA]. Dimethylallyl pyrophosphate often locates in Chloroplasts, Plastids, chloroplast stroma, Cytosol and Cell membrane. The associated genes with Dimethylallyl pyrophosphate are IRF6 wt Allele and ADRBK1 gene. The related lipids are Sterols.
To understand associated biological information of Dimethylallyl pyrophosphate, 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.
Dimethylallyl pyrophosphate is suspected in 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 Dimethylallyl pyrophosphate
MeSH term | MeSH ID | Detail |
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Melanoma | D008545 | 69 associated lipids |
Lipid pathways are not clear in current pathway databases. We organized associated pathways with Dimethylallyl pyrophosphate through full-text articles, including metabolic pathways or pathways of biological mechanisms.
Pathway name | Related literatures |
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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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Kumano T et al. | Functional characterization of the promiscuous prenyltransferase responsible for furaquinocin biosynthesis: identification of a physiological polyketide substrate and its prenylated reaction products. | 2010 | J. Biol. Chem. | pmid:20937800 |