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
Adenocarcinoma D000230 166 associated lipids
Colonic Neoplasms D003110 161 associated lipids
Osteosarcoma D012516 50 associated lipids
Leukemia, Erythroblastic, Acute D004915 41 associated lipids
Hypercholesterolemia D006937 91 associated lipids
Liver Neoplasms, Experimental D008114 46 associated lipids
Endometriosis D004715 29 associated lipids
Leukemia, Myeloid D007951 52 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
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
Brown AJ Isoprenoid is a perfect fit for fat factor. 2011 Biochem. J. pmid:21793802
Cohen LH et al. Inhibition of human smooth muscle cell proliferation in culture by farnesyl pyrophosphate analogues, inhibitors of in vitro protein: farnesyl transferase. 1999 Biochem. Pharmacol. pmid:9933024
Sillero MA et al. Synthesis of ATP derivatives of compounds of the mevalonate pathway (isopentenyl di- and triphosphate; geranyl di- and triphosphate, farnesyl di- and triphosphate, and dimethylallyl diphosphate) catalyzed by T4 RNA ligase, T4 DNA ligase and other ligases Potential relationship with the effect of bisphosphonates on osteoclasts. 2009 Biochem. Pharmacol. pmid:19414000
Cohen LH et al. Different analogues of farnesyl pyrophosphate inhibit squalene synthase and protein:farnesyltransferase to different extents. 1995 Biochem. Pharmacol. pmid:7702642
Hartmann MA et al. Metabolism of farnesyl diphosphate in tobacco BY-2 cells treated with squalestatin. 2000 Biochem. Soc. Trans. pmid:11171211
Cane DE Cell-free studies of monoterpene and sesquiterpene biosynthesis. 1983 Biochem. Soc. Trans. pmid:6642060
Brindle PA and Threlfall DR The metabolism of phytoalexins. 1983 Biochem. Soc. Trans. pmid:6642061
Parmryd I and Dallner G Organization of isoprenoid biosynthesis. 1996 Biochem. Soc. Trans. pmid:8878825
Reigard SA et al. Interplay of isoprenoid and peptide substrate specificity in protein farnesyltransferase. 2005 Biochemistry pmid:16101305
Micali E et al. Protein farnesyltransferase isoprenoid substrate discrimination is dependent on isoprene double bonds and branched methyl groups. 2001 Biochemistry pmid:11591144
Dursina B et al. Interaction of yeast Rab geranylgeranyl transferase with its protein and lipid substrates. 2002 Biochemistry pmid:12022885
Holstein SA et al. Isoprenoids influence expression of Ras and Ras-related proteins. 2002 Biochemistry pmid:12427032
Kloer DP et al. Structure and reaction geometry of geranylgeranyl diphosphate synthase from Sinapis alba. 2006 Biochemistry pmid:17176041
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
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
Thomä NH et al. Phosphoisoprenoid binding specificity of geranylgeranyltransferase type II. 2000 Biochemistry pmid:11009619
Radisky ES and Poulter CD Squalene synthase: steady-state, pre-steady-state, and isotope-trapping studies. 2000 Biochemistry pmid:10677224
Huang C et al. Mechanistic studies of rat protein farnesyltransferase indicate an associative transition state. 2000 Biochemistry pmid:10704208
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
Chang SY et al. Identification of the active conformation and the importance of length of the flexible loop 72-83 in regulating the conformational change of undecaprenyl pyrophosphate synthase. 2003 Biochemistry pmid:14661956
Chen M et al. Mechanistic insights from the binding of substrate and carbocation intermediate analogues to aristolochene synthase. 2013 Biochemistry pmid:23905850
van der Kamp MW et al. Conformational change and ligand binding in the aristolochene synthase catalytic cycle. 2013 Biochemistry pmid:24106830
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
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
Cane DE et al. Trichodiene synthase. Probing the role of the highly conserved aspartate-rich region by site-directed mutagenesis. 1996 Biochemistry pmid:8823172
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
Vogt A et al. Burkitt lymphoma Daudi cells contain two distinct farnesyltransferases with different divalent cation requirements. 1995 Biochemistry pmid:7547984
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
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
Kurth DD et al. Functional consequence of mutating conserved residues of the yeast farnesyl-protein transferase beta-subunit Ram1(Dpr1). 1997 Biochemistry pmid:9398327
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
Dunten P et al. Protein farnesyltransferase: structure and implications for substrate binding. 1998 Biochemistry pmid:9609683
Fu Z et al. Biochemical and structural basis for feedback inhibition of mevalonate kinase and isoprenoid metabolism. 2008 Biochemistry pmid:18302342
Liliom K et al. Farnesyl phosphates are endogenous ligands of lysophosphatidic acid receptors: inhibition of LPA GPCR and activation of PPARs. 2006 Biochim. Biophys. Acta pmid:17092771
Raisig A and Sandmann G Functional properties of diapophytoene and related desaturases of C(30) and C(40) carotenoid biosynthetic pathways. 2001 Biochim. Biophys. Acta pmid:11566453
Koyama T et al. Substrate specificity of squalene synthetase. 1980 Biochim. Biophys. Acta pmid:7357018