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:

Location Cross reference Weighted score Related literatures
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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
Sakoda K et al. Simvastatin decreases IL-6 and IL-8 production in epithelial cells. 2006 J. Dent. Res. pmid:16723648
Kim SH et al. Cyclization mechanism of amorpha-4,11-diene synthase, a key enzyme in artemisinin biosynthesis. 2006 J. Nat. Prod. pmid:16724836
Picaud S et al. Amorpha-4,11-diene synthase: mechanism and stereochemistry of the enzymatic cyclization of farnesyl diphosphate. 2006 Arch. Biochem. Biophys. pmid:16143293
Roberts MJ et al. Hydrophilic anilinogeranyl diphosphate prenyl analogues are Ras function inhibitors. 2006 Biochemistry pmid:17176109
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Camino-López S et al. Tissue factor induction by aggregated LDL depends on LDL receptor-related protein expression (LRP1) and Rho A translocation in human vascular smooth muscle cells. 2007 Cardiovasc. Res. pmid:17141748
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Guo RT et al. Bisphosphonates target multiple sites in both cis- and trans-prenyltransferases. 2007 Proc. Natl. Acad. Sci. U.S.A. pmid:17535895
Ling Y et al. The farnesyl-diphosphate/geranylgeranyl-diphosphate synthase of Toxoplasma gondii is a bifunctional enzyme and a molecular target of bisphosphonates. 2007 J. Biol. Chem. pmid:17724033
Saito K et al. Short-chain prenyl diphosphate synthase that condenses isopentenyl diphosphate with dimethylallyl diphosphate in ispA null Escherichia coli strain lacking farnesyl diphosphate synthase. 2007 J. Biosci. Bioeng. pmid:17630132
Miller DJ et al. Competitive inhibition of aristolochene synthase by phenyl-substituted farnesyl diphosphates: evidence of active site plasticity. 2007 Org. Biomol. Chem. pmid:17912381
Faraldos JA et al. Interception of the enzymatic conversion of farnesyl diphosphate to 5-epi-aristolochene by using a fluoro substrate analogue: 1-fluorogermacrene A from (2E,6Z)-6-fluorofarnesyl diphosphate. 2007 Chembiochem pmid:17886322
Oswald M et al. Monoterpenoid biosynthesis in Saccharomyces cerevisiae. 2007 FEMS Yeast Res. pmid:17096665
Miller DJ et al. Aristolochene synthase-catalyzed cyclization of 2-fluorofarnesyl-diphosphate to 2-fluorogermacrene A. 2007 Chembiochem pmid:17683054
Das S et al. Farnesyl pyrophosphate is a novel transcriptional activator for a subset of nuclear hormone receptors. 2007 Mol. Endocrinol. pmid:17666588
Qiu G and Hill JS Atorvastatin decreases lipoprotein lipase and endothelial lipase expression in human THP-1 macrophages. 2007 J. Lipid Res. pmid:17644777
Shishova EY et al. X-ray crystal structure of aristolochene synthase from Aspergillus terreus and evolution of templates for the cyclization of farnesyl diphosphate. 2007 Biochemistry pmid:17261032
Troutman JM et al. Protein farnesyl transferase target selectivity is dependent upon peptide stimulated product release. 2007 Biochemistry pmid:17877368
Troutman JM et al. Selective modification of CaaX peptides with ortho-substituted anilinogeranyl lipids by protein farnesyl transferase: competitive substrates and potent inhibitors from a library of farnesyl diphosphate analogues. 2007 Biochemistry pmid:17854205