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:

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
Micali E et al. Protein farnesyltransferase isoprenoid substrate discrimination is dependent on isoprene double bonds and branched methyl groups. 2001 Biochemistry pmid:11591144
Holstein SA et al. Isoprenoids influence expression of Ras and Ras-related proteins. 2002 Biochemistry pmid:12427032
Deligeorgopoulou A and Allemann RK Evidence for differential folding of farnesyl pyrophosphate in the active site of aristolochene synthase: a single-point mutation converts aristolochene synthase into an (E)-beta-farnesene synthase. 2003 Biochemistry pmid:12820883
Thomä NH et al. Phosphoisoprenoid binding specificity of geranylgeranyltransferase type II. 2000 Biochemistry pmid:11009619
Huang C et al. Mechanistic studies of rat protein farnesyltransferase indicate an associative transition state. 2000 Biochemistry pmid:10704208
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
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
Cui G and Merz KM Computational studies of the farnesyltransferase ternary complex part II: the conformational activation of farnesyldiphosphate. 2007 Biochemistry pmid:17918965
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