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.

Cross Reference

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
Loading... please refresh the page if content is not showing up.

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
Loading... please refresh the page if content is not showing up.

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:

Location Cross reference Weighted score Related literatures
Loading... please refresh the page if content is not showing up.

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
Loading... please refresh the page if content is not showing up.

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

Download all related citations
Per page 10 20 50 100 | Total 614
Authors Title Published Journal PubMed Link
Tachibana A et al. Evidence for farnesol-mediated isoprenoid synthesis regulation in a halophilic archaeon, Haloferax volcanii. 1996 FEBS Lett. pmid:8566226
Keller RK Squalene synthase inhibition alters metabolism of nonsterols in rat liver. 1996 Biochim. Biophys. Acta pmid:8908150
Krisans SK Cell compartmentalization of cholesterol biosynthesis. 1996 Ann. N. Y. Acad. Sci. pmid:8993542
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
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
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
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
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
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
Soltis DA et al. Expression, purification, and characterization of the human squalene synthase: use of yeast and baculoviral systems. 1995 Arch. Biochem. Biophys. pmid:7864626
Cane DE et al. Trichodiene synthase. Substrate specificity and inhibition. 1995 Biochemistry pmid:7873526
Cane DE et al. Trichodiene synthase. Identification of active site residues by site-directed mutagenesis. 1995 Biochemistry pmid:7873527
Harwood HJ Protein farnesyltransferase: measurement of enzymatic activity in 96-well format using TopCount microplate scintillation counting technology. 1995 Anal. Biochem. pmid:7793628
Cohen LH et al. Different analogues of farnesyl pyrophosphate inhibit squalene synthase and protein:farnesyltransferase to different extents. 1995 Biochem. Pharmacol. pmid:7702642
Furfine ES et al. Protein farnesyltransferase: kinetics of farnesyl pyrophosphate binding and product release. 1995 Biochemistry pmid:7756316
Dolence JM and Poulter CD A mechanism for posttranslational modifications of proteins by yeast protein farnesyltransferase. 1995 Proc. Natl. Acad. Sci. U.S.A. pmid:7761439
Cox AD Mutation and analysis of prenylation signal sequences. 1995 Meth. Enzymol. pmid:7651143
Thissen JA et al. Prenylated peptides in identification of specific binding proteins. 1995 Meth. Enzymol. pmid:7651148
Reiss Y Substrate interactions of protein prenyltransferases. 1995 Meth. Enzymol. pmid:7651152
Caplin BE and Marshall MS Mutagenesis and biochemical analysis of recombinant yeast prenyltransferases. 1995 Meth. Enzymol. pmid:7651175
Chen XY et al. Cloning, expression, and characterization of (+)-delta-cadinene synthase: a catalyst for cotton phytoalexin biosynthesis. 1995 Arch. Biochem. Biophys. pmid:8554317
Wiedłocha A et al. Translocation of cytosol of exogenous, CAAX-tagged acidic fibroblast growth factor. 1995 J. Biol. Chem. pmid:8530506
Khan SG et al. A rapid and convenient filter-binding assay for ras p21 processing enzyme farnesyltransferase. 1995 J. Biochem. Biophys. Methods pmid:7494090
Patel DV et al. Farnesyl diphosphate-based inhibitors of Ras farnesyl protein transferase. 1995 J. Med. Chem. pmid:7636851
McGeady P et al. The farnesyl group of H-Ras facilitates the activation of a soluble upstream activator of mitogen-activated protein kinase. 1995 J. Biol. Chem. pmid:7592846
Runquist M et al. Distribution of branch point prenyltransferases in regions of bovine brain. 1995 J. Neurochem. pmid:7595519
Tanaka Y et al. Natural and synthetic non-peptide antigens recognized by human gamma delta T cells. 1995 Nature pmid:7753173
Vogt A et al. Burkitt lymphoma Daudi cells contain two distinct farnesyltransferases with different divalent cation requirements. 1995 Biochemistry pmid:7547984
Danesi R et al. Specific labeling of isoprenylated proteins: application to study inhibitors of the post-translational farnesylation and geranylgeranylation. 1995 Biochem. Biophys. Res. Commun. pmid:7826382
Epand RM et al. Lipid-mediated a-factor interactions with artificial membranes. 1995 Meth. Enzymol. pmid:7651149
Parmryd I et al. Identification of spinach farnesyl protein transferase. Dithiothreitol as an acceptor in vitro. 1995 Eur. J. Biochem. pmid:8575428
Thelin A et al. Effect of squalestatin 1 on the biosynthesis of the mevalonate pathway lipids. 1994 Biochim. Biophys. Acta pmid:7811707
Bansal VS and Vaidya S Characterization of two distinct allyl pyrophosphatase activities from rat liver microsomes. 1994 Arch. Biochem. Biophys. pmid:7986083
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. Novel isoprenoid modified proteins in Halobacteria. 1994 Biochem. Biophys. Res. Commun. pmid:8093082
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
Christensen DJ and Poulter CD Enzymatic synthesis of isotopically labeled isoprenoid diphosphates. 1994 Bioorg. Med. Chem. pmid:7858969
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
Zhao J et al. Farnesylation of p21 Ras proteins in Xenopus oocytes. 1994 Cell. Mol. Biol. Res. pmid:7866432
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
Ericsson J et al. Biosynthesis of dolichol and cholesterol in rat liver peroxisomes. 1993 Biochimie pmid:8507678
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
Cane DE et al. Overproduction of soluble trichodiene synthase from Fusarium sporotrichioides in Escherichia coli. 1993 Arch. Biochem. Biophys. pmid:8424673
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
Fenton RG et al. Regulation of intracellular actin polymerization by prenylated cellular proteins. 1992 J. Cell Biol. pmid:1560030