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
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
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
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
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
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
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
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
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. 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