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
Reigard SA et al. Interplay of isoprenoid and peptide substrate specificity in protein farnesyltransferase. 2005 Biochemistry pmid:16101305
Roberts MJ et al. Hydrophilic anilinogeranyl diphosphate prenyl analogues are Ras function inhibitors. 2006 Biochemistry pmid:17176109
Turek-Etienne TC et al. Biochemical and structural studies with prenyl diphosphate analogues provide insights into isoprenoid recognition by protein farnesyl transferase. 2003 Biochemistry pmid:12667062
Pan JJ et al. Product distribution and pre-steady-state kinetic analysis of Escherichia coli undecaprenyl pyrophosphate synthase reaction. 2000 Biochemistry pmid:10978182
Radisky ES and Poulter CD Squalene synthase: steady-state, pre-steady-state, and isotope-trapping studies. 2000 Biochemistry pmid:10677224
Long SB et al. Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate. 1998 Biochemistry pmid:9657673
Subramanian T et al. Farnesyl diphosphate analogues with aryl moieties are efficient alternate substrates for protein farnesyltransferase. 2012 Biochemistry pmid:22989235
Strickland CL et al. Crystal structure of farnesyl protein transferase complexed with a CaaX peptide and farnesyl diphosphate analogue. 1998 Biochemistry pmid:9843427
Pompliano DL et al. Steady-state kinetic mechanism of Ras farnesyl:protein transferase. 1992 Biochemistry pmid:1567835
Grundy DJ et al. Mechanism of Germacradien-4-ol Synthase-Controlled Water Capture. 2016 Biochemistry pmid:26998816
Harris GG et al. Structural Studies of Geosmin Synthase, a Bifunctional Sesquiterpene Synthase with αα Domain Architecture That Catalyzes a Unique Cyclization-Fragmentation Reaction Sequence. 2015 Biochemistry pmid:26598179
Furfine ES et al. Protein farnesyltransferase: kinetics of farnesyl pyrophosphate binding and product release. 1995 Biochemistry pmid:7756316
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
Cane DE et al. Pre-steady-state kinetic analysis of the trichodiene synthase reaction pathway. 1997 Biochemistry pmid:9204880
Mathis JR et al. Pre-steady-state study of recombinant sesquiterpene cyclases. 1997 Biochemistry pmid:9204881
Zhang YW et al. Chain length determination of prenyltransferases: both heteromeric subunits of medium-chain (E)-prenyl diphosphate synthase are involved in the product chain length determination. 2000 Biochemistry pmid:11027152
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
Thelin A et al. Effect of squalestatin 1 on the biosynthesis of the mevalonate pathway lipids. 1994 Biochim. Biophys. Acta pmid:7811707
Keller RK Squalene synthase inhibition alters metabolism of nonsterols in rat liver. 1996 Biochim. Biophys. Acta pmid:8908150
Exnowitz F et al. NMR for direct determination of K(m) and V(max) of enzyme reactions based on the Lambert W function-analysis of progress curves. 2012 Biochim. Biophys. Acta pmid:22079737