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


Related references are published most in these journals:

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
Runquist M et al. Biosynthesis of trans,trans,trans-geranylgeranyl diphosphate by the cytosolic fraction from rat tissues. 1992 Biochem. Biophys. Res. Commun. pmid:1632765
Lutz RJ et al. Feedback inhibition of polyisoprenyl pyrophosphate synthesis from mevalonate in vitro. Implications for protein prenylation. 1992 J. Biol. Chem. pmid:1569056
Sinensky M and Lutz RJ The prenylation of proteins. 1992 Bioessays pmid:1546978
Sandmann G and Misawa N New functional assignment of the carotenogenic genes crtB and crtE with constructs of these genes from Erwinia species. 1992 FEMS Microbiol. Lett. pmid:1555761
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
Pompliano DL et al. Steady-state kinetic mechanism of Ras farnesyl:protein transferase. 1992 Biochemistry pmid:1567835
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
Butrynski JE et al. Differential isoprenylation of carboxy-terminal mutants of an inhibitory G-protein alpha-subunit: neither farnesylation nor geranylgeranylation is sufficient for membrane attachment. 1992 Biochemistry pmid:1510988
Inglese J et al. Isoprenylation in regulation of signal transduction by G-protein-coupled receptor kinases. 1992 Nature pmid:1522899
Tait RM Development of a radiometric spot-wash assay for squalene synthase. 1992 Anal. Biochem. pmid:1416027
Ericsson J et al. Characterization and distribution of cis-prenyl transferase participating in liver microsomal polyisoprenoid biosynthesis. 1991 Eur. J. Biochem. pmid:1765092
Das NP and Allen CM Inhibition of farnesyl transferases from malignant and non-malignant cultured human lymphocytes by prenyl substrate analogues. 1991 Biochem. Biophys. Res. Commun. pmid:1755854
Wolf MJ et al. Golgi-enriched membrane fractions from rat brain and liver contain long-chain polyisoprenyl pyrophosphate phosphatase activity. 1991 Glycobiology pmid:1668143
Newman P et al. Polyisoprenylation of the CAAX motif--an in vitro protein synthesis study. 1991 Biochim. Biophys. Acta pmid:1954230
Reiss Y et al. Nonidentical subunits of p21H-ras farnesyltransferase. Peptide binding and farnesyl pyrophosphate carrier functions. 1991 J. Biol. Chem. pmid:2037606
Kinsella BT et al. Posttranslational modification of Ha-ras p21 by farnesyl versus geranylgeranyl isoprenoids is determined by the COOH-terminal amino acid. 1991 Proc. Natl. Acad. Sci. U.S.A. pmid:1924354
Cane DE et al. Terpenoid biosynthesis and the stereochemistry of enzyme-catalysed allylic addition-elimination reactions. 1991 Philos. Trans. R. Soc. Lond., B, Biol. Sci. pmid:1678531
Biller SA et al. Isoprenyl phosphinylformates: new inhibitors of squalene synthetase. 1991 J. Med. Chem. pmid:2061928
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