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
Endometriosis D004715 29 associated lipids
Leukemia, Erythroblastic, Acute D004915 41 associated lipids
Hypercholesterolemia D006937 91 associated lipids
Leukemia, Myeloid D007951 52 associated lipids
Liver Neoplasms, Experimental D008114 46 associated lipids
Protozoan Infections D011528 6 associated lipids
Osteosarcoma D012516 50 associated lipids
Leukemia-Lymphoma, Adult T-Cell D015459 25 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
Shishova EY et al. X-ray crystallographic studies of substrate binding to aristolochene synthase suggest a metal ion binding sequence for catalysis. 2008 J. Biol. Chem. pmid:18385128
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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
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Garza RM et al. Geranylgeranyl pyrophosphate is a potent regulator of HRD-dependent 3-Hydroxy-3-methylglutaryl-CoA reductase degradation in yeast. 2009 J. Biol. Chem. pmid:19776008
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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
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
Leichner GS et al. Metabolically regulated endoplasmic reticulum-associated degradation of 3-hydroxy-3-methylglutaryl-CoA reductase: evidence for requirement of a geranylgeranylated protein. 2011 J. Biol. Chem. pmid:21778231
Kavanagh KL et al. The crystal structure of human geranylgeranyl pyrophosphate synthase reveals a novel hexameric arrangement and inhibitory product binding. 2006 J. Biol. Chem. pmid:16698791
Tschantz WR et al. Substrate binding is required for release of product from mammalian protein farnesyltransferase. 1997 J. Biol. Chem. pmid:9092540
Laufs U and Liao JK Post-transcriptional regulation of endothelial nitric oxide synthase mRNA stability by Rho GTPase. 1998 J. Biol. Chem. pmid:9727051