Farnesyl diphosphate

Farnesyl diphosphate is a lipid of Prenol Lipids (PR) class. Farnesyl diphosphate is associated with abnormalities such as Dental caries and Hyperostosis, Diffuse Idiopathic Skeletal. The involved functions are known as Regulation, Process, Signal, Anabolism and inhibitors. Farnesyl diphosphate often locates in peroxisome, Cytoplasmic matrix, Plasma membrane, soluble and Mitochondria. The associated genes with Farnesyl diphosphate are HSD3B1 gene, ABRA gene, MATN1 gene, SEPSECS gene and MBD2 gene. The related lipids are Sterols, 22-hydroxycholesterol, dehydrosqualene, SK&F 104976 and 25-hydroxycholesterol.

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Introduction

To understand associated biological information of Farnesyl diphosphate, 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 Farnesyl diphosphate?

Farnesyl diphosphate is suspected in and other diseases in descending order of the highest number of associated sentences.

Related references are mostly published in these journals:

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 Farnesyl diphosphate

MeSH term MeSH ID Detail
Protozoan Infections D011528 6 associated lipids
Leukemia-Lymphoma, Adult T-Cell D015459 25 associated lipids
Endometriosis D004715 29 associated lipids
Leukemia, Erythroblastic, Acute D004915 41 associated lipids
Liver Neoplasms, Experimental D008114 46 associated lipids
Osteosarcoma D012516 50 associated lipids
Leukemia, Myeloid D007951 52 associated lipids
Hypercholesterolemia D006937 91 associated lipids
Colonic Neoplasms D003110 161 associated lipids
Adenocarcinoma D000230 166 associated lipids
Total 10

PubChem Associated disorders and diseases

What pathways are associated with Farnesyl diphosphate

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

Related references are published most in these journals:

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 Farnesyl diphosphate?

Related references are published most in these journals:

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What functions are associated with Farnesyl diphosphate?


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Function Cross reference Weighted score Related literatures

What lipids are associated with Farnesyl diphosphate?

Related references are published most in these journals:

Lipid concept Cross reference Weighted score Related literatures
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What genes are associated with Farnesyl diphosphate?

Related references are published most in these journals:


Gene Cross reference Weighted score Related literatures

What common seen animal models are associated with Farnesyl diphosphate?

There are no associated biomedical information in the current reference collection.

NCBI Entrez Crosslinks

All references with Farnesyl diphosphate

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Authors Title Published Journal PubMed Link
Lindsey S and Harwood HJ Inhibition of mammalian squalene synthetase activity by zaragozic acid A is a result of competitive inhibition followed by mechanism-based irreversible inactivation. 1995 J. Biol. Chem. pmid:7721822
Vukelic S et al. Farnesyl pyrophosphate inhibits epithelialization and wound healing through the glucocorticoid receptor. 2010 J. Biol. Chem. pmid:19903814
Lutz RJ et al. Feedback inhibition of polyisoprenyl pyrophosphate synthesis from mevalonate in vitro. Implications for protein prenylation. 1992 J. Biol. Chem. pmid:1569056
Faulkner A et al. The LPP1 and DPP1 gene products account for most of the isoprenoid phosphate phosphatase activities in Saccharomyces cerevisiae. 1999 J. Biol. Chem. pmid:10329682
Mookhtiar KA et al. Yeast squalene synthase. A mechanism for addition of substrates and activation by NADPH. 1994 J. Biol. Chem. pmid:8157649
Reiss Y et al. Divalent cation and prenyl pyrophosphate specificities of the protein farnesyltransferase from rat brain, a zinc metalloenzyme. 1992 J. Biol. Chem. pmid:1556143
Shechter I et al. Solubilization, purification, and characterization of a truncated form of rat hepatic squalene synthetase. 1992 J. Biol. Chem. pmid:1569107
Ericsson J et al. Isoprenoid biosynthesis in rat liver peroxisomes. Characterization of cis-prenyltransferase and squalene synthetase. 1992 J. Biol. Chem. pmid:1527001
Schaber MD et al. Polyisoprenylation of Ras in vitro by a farnesyl-protein transferase. 1990 J. Biol. Chem. pmid:2203759
Reiss Y et al. Nonidentical subunits of p21H-ras farnesyltransferase. Peptide binding and farnesyl pyrophosphate carrier functions. 1991 J. Biol. Chem. pmid:2037606
Bradfute DL and Simoni RD Non-sterol compounds that regulate cholesterogenesis. Analogues of farnesyl pyrophosphate reduce 3-hydroxy-3-methylglutaryl-coenzyme A reductase levels. 1994 J. Biol. Chem. pmid:8120018
Oh DY et al. Identification of farnesyl pyrophosphate and N-arachidonylglycine as endogenous ligands for GPR92. 2008 J. Biol. Chem. pmid:18499677
Biardi L and Krisans SK Compartmentalization of cholesterol biosynthesis. Conversion of mevalonate to farnesyl diphosphate occurs in the peroxisomes. 1996 J. Biol. Chem. pmid:8576183
Otto JC and Casey PJ The hepatitis delta virus large antigen is farnesylated both in vitro and in animal cells. 1996 J. Biol. Chem. pmid:8617711
Light DR and Dennis MS Purification of a prenyltransferase that elongates cis-polyisoprene rubber from the latex of Hevea brasiliensis. 1989 J. Biol. Chem. pmid:2808388
Light DR et al. Rubber elongation by farnesyl pyrophosphate synthases involves a novel switch in enzyme stereospecificity. 1989 J. Biol. Chem. pmid:2808389
Miriyala S et al. Functional characterization of the atypical integral membrane lipid phosphatase PDP1/PPAPDC2 identifies a pathway for interconversion of isoprenols and isoprenoid phosphates in mammalian cells. 2010 J. Biol. Chem. pmid:20110354
Scholten JD et al. Synergy between anions and farnesyldiphosphate competitive inhibitors of farnesyl:protein transferase. 1997 J. Biol. Chem. pmid:9218438
Correll CC et al. Identification of farnesol as the non-sterol derivative of mevalonic acid required for the accelerated degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase. 1994 J. Biol. Chem. pmid:8021239
Tschantz WR et al. Substrate binding is required for release of product from mammalian protein farnesyltransferase. 1997 J. Biol. Chem. pmid:9092540