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?


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
Mookhtiar KA et al. Yeast squalene synthase. A mechanism for addition of substrates and activation by NADPH. 1994 J. Biol. Chem. pmid:8157649
Sagami H et al. Biosynthesis of prenyl diphosphates by cell-free extracts from mammalian tissues. 1993 J. Biochem. pmid:8407862
Sagami H et al. Geranylgeranyl diphosphate synthase catalyzing the single condensation between isopentenyl diphosphate and farnesyl diphosphate. 1993 J. Biochem. pmid:8407863
Cane DE et al. Overproduction of soluble trichodiene synthase from Fusarium sporotrichioides in Escherichia coli. 1993 Arch. Biochem. Biophys. pmid:8424673
Omer CA et al. Characterization of recombinant human farnesyl-protein transferase: cloning, expression, farnesyl diphosphate binding, and functional homology with yeast prenyl-protein transferases. 1993 Biochemistry pmid:8494894
Ericsson J et al. Biosynthesis of dolichol and cholesterol in rat liver peroxisomes. 1993 Biochimie pmid:8507678
Wiedłocha A et al. Translocation of cytosol of exogenous, CAAX-tagged acidic fibroblast growth factor. 1995 J. Biol. Chem. pmid:8530506
Chen XY et al. Cloning, expression, and characterization of (+)-delta-cadinene synthase: a catalyst for cotton phytoalexin biosynthesis. 1995 Arch. Biochem. Biophys. pmid:8554317
Tachibana A et al. Evidence for farnesol-mediated isoprenoid synthesis regulation in a halophilic archaeon, Haloferax volcanii. 1996 FEBS Lett. pmid:8566226
Parmryd I et al. Identification of spinach farnesyl protein transferase. Dithiothreitol as an acceptor in vitro. 1995 Eur. J. Biochem. pmid:8575428
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
Williams TM et al. 2-substituted piperazines as constrained amino acids. Application to the synthesis of potent, non carboxylic acid inhibitors of farnesyltransferase. 1996 J. Med. Chem. pmid:8691462
Cane DE et al. Trichodiene synthase. Probing the role of the highly conserved aspartate-rich region by site-directed mutagenesis. 1996 Biochemistry pmid:8823172
Goalstone ML et al. Characterization of Xenopus laevis oocyte farnesyl transferase. 1996 Biol. Reprod. pmid:8835391
Parmryd I and Dallner G Organization of isoprenoid biosynthesis. 1996 Biochem. Soc. Trans. pmid:8878825
Scholten JD et al. Inhibitors of farnesyl:protein transferase--a possible cancer chemotherapeutic. 1996 Bioorg. Med. Chem. pmid:8894110
Keller RK Squalene synthase inhibition alters metabolism of nonsterols in rat liver. 1996 Biochim. Biophys. Acta pmid:8908150
Dietrich A et al. Isoprenylation of the G protein gamma subunit is both necessary and sufficient for beta gamma dimer-mediated stimulation of phospholipase C. 1996 Biochemistry pmid:8952464
Gromov PS et al. Identification of isoprenyl modified proteins metabolically labeled with [3H]farnesyl- and [3H]geranylgeranyl-pyrophosphate. 1996 Electrophoresis pmid:8982605