The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Chemical Compound Review

FPP003     (hydroxy-(3,7,11- trimethyldodeca-2,6,10...

Synonyms: CHEBI:50277, CTK4B6817, AC1L19U8, 13058-04-3, all-trans Farnesyl pyrophosphate
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Dehydrodolichyl diphosphate


High impact information on Dehydrodolichyl diphosphate


Chemical compound and disease context of Dehydrodolichyl diphosphate


Biological context of Dehydrodolichyl diphosphate


Anatomical context of Dehydrodolichyl diphosphate


Associations of Dehydrodolichyl diphosphate with other chemical compounds


Gene context of Dehydrodolichyl diphosphate


Analytical, diagnostic and therapeutic context of Dehydrodolichyl diphosphate


  1. Expression and mechanistic analysis of a germacradienol synthase from Streptomyces coelicolor implicated in geosmin biosynthesis. Cane, D.E., Watt, R.M. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  2. Conversion from farnesyl diphosphate synthase to geranylgeranyl diphosphate synthase by random chemical mutagenesis. Ohnuma, S., Nakazawa, T., Hemmi, H., Hallberg, A.M., Koyama, T., Ogura, K., Nishino, T. J. Biol. Chem. (1996) [Pubmed]
  3. Inhibition of protein prenylation by bisphosphonates causes sustained activation of Rac, Cdc42, and Rho GTPases. Dunford, J.E., Rogers, M.J., Ebetino, F.H., Phipps, R.J., Coxon, F.P. J. Bone Miner. Res. (2006) [Pubmed]
  4. Pentalenene synthase. Analysis of active site residues by site-directed mutagenesis. Seemann, M., Zhai, G., de Kraker, J.W., Paschall, C.M., Christianson, D.W., Cane, D.E. J. Am. Chem. Soc. (2002) [Pubmed]
  5. Molecular mechanisms of action of bisphosphonates: current status. Roelofs, A.J., Thompson, K., Gordon, S., Rogers, M.J. Clin. Cancer Res. (2006) [Pubmed]
  6. Inhibition of purified p21ras farnesyl:protein transferase by Cys-AAX tetrapeptides. Reiss, Y., Goldstein, J.L., Seabra, M.C., Casey, P.J., Brown, M.S. Cell (1990) [Pubmed]
  7. Bet2p and Mad2p are components of a prenyltransferase that adds geranylgeranyl onto Ypt1p and Sec4p. Jiang, Y., Rossi, G., Ferro-Novick, S. Nature (1993) [Pubmed]
  8. Crystal structure of pentalenene synthase: mechanistic insights on terpenoid cyclization reactions in biology. Lesburg, C.A., Zhai, G., Cane, D.E., Christianson, D.W. Science (1997) [Pubmed]
  9. Genetic and pharmacological suppression of oncogenic mutations in ras genes of yeast and humans. Schafer, W.R., Kim, R., Sterne, R., Thorner, J., Kim, S.H., Rine, J. Science (1989) [Pubmed]
  10. Elevated levels of SREBP-2 and cholesterol synthesis in livers of mice homozygous for a targeted disruption of the SREBP-1 gene. Shimano, H., Shimomura, I., Hammer, R.E., Herz, J., Goldstein, J.L., Brown, M.S., Horton, J.D. J. Clin. Invest. (1997) [Pubmed]
  11. Geosmin biosynthesis. Streptomyces coelicolor germacradienol/germacrene D synthase converts farnesyl diphosphate to geosmin. Jiang, J., He, X., Cane, D.E. J. Am. Chem. Soc. (2006) [Pubmed]
  12. Structural and functional roles of the cysteine residues of Bacillus stearothermophilus farnesyl diphosphate synthase. Koyama, T., Obata, S., Saito, K., Takeshita-Koike, A., Ogura, K. Biochemistry (1994) [Pubmed]
  13. Crystallization and preliminary X-ray diffraction study of the farnesyl diphosphate synthase from Trypanosoma brucei. Mao, J., Gao, Y.G., Odeh, S., Robinson, H., Montalvetti, A., Docampo, R., Oldfield, E. Acta Crystallogr. D Biol. Crystallogr. (2004) [Pubmed]
  14. The in vivo synthesis of plant sesquiterpenes by Escherichia coli. Martin, V.J., Yoshikuni, Y., Keasling, J.D. Biotechnol. Bioeng. (2001) [Pubmed]
  15. Partial purification and characterization of pentalenene synthase. Cane, D.E., Pargellis, C. Arch. Biochem. Biophys. (1987) [Pubmed]
  16. A mechanism for posttranslational modifications of proteins by yeast protein farnesyltransferase. Dolence, J.M., Poulter, C.D. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  17. Cloning and characterization of a gene from Escherichia coli encoding a transketolase-like enzyme that catalyzes the synthesis of D-1-deoxyxylulose 5-phosphate, a common precursor for isoprenoid, thiamin, and pyridoxol biosynthesis. Lois, L.M., Campos, N., Putra, S.R., Danielsen, K., Rohmer, M., Boronat, A. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  18. Lovastatin induces apoptosis in a metastatic ovarian tumour cell line. Han, Z., Wyche, J.H. Cell Death Differ. (1996) [Pubmed]
  19. Effects of site-directed mutagenesis of the highly conserved aspartate residues in domain II of farnesyl diphosphate synthase activity. Marrero, P.F., Poulter, C.D., Edwards, P.A. J. Biol. Chem. (1992) [Pubmed]
  20. Farnesyl-diphosphate synthase is localized in peroxisomes. Krisans, S.K., Ericsson, J., Edwards, P.A., Keller, G.A. J. Biol. Chem. (1994) [Pubmed]
  21. Biosynthesis of ubiquinone and plastoquinone in the endoplasmic reticulum-Golgi membranes of spinach leaves. Swiezewska, E., Dallner, G., Andersson, B., Ernster, L. J. Biol. Chem. (1993) [Pubmed]
  22. Nonparticipation of 105,000 x g liver supernatant or sterol carrier protein in the enzymatic conversion of farnesyl pyrophosphate to squalene by rat liver microsomes. Gavey, K.L., Scallen, T.J. J. Biol. Chem. (1978) [Pubmed]
  23. In vitro heme O synthesis by the cyoE gene product from Escherichia coli. Saiki, K., Mogi, T., Ogura, K., Anraku, Y. J. Biol. Chem. (1993) [Pubmed]
  24. Abnormal induction of 3-hydroxy-3-methylglutaryl coenzyme A reductase in leukocytes from subjects with heterozygous familial hypercholesterolemia. Fogelman, A.M., Edmond, J., Seager, J., Popják, G. J. Biol. Chem. (1975) [Pubmed]
  25. Zaragozic acids: a family of fungal metabolites that are picomolar competitive inhibitors of squalene synthase. Bergstrom, J.D., Kurtz, M.M., Rew, D.J., Amend, A.M., Karkas, J.D., Bostedor, R.G., Bansal, V.S., Dufresne, C., VanMiddlesworth, F.L., Hensens, O.D. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  26. Molecular cloning and characterization of the yeast gene for squalene synthetase. Jennings, S.M., Tsay, Y.H., Fisch, T.M., Robinson, G.W. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  27. The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics. Long, S.B., Hancock, P.J., Kral, A.M., Hellinga, H.W., Beese, L.S. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  28. Squalene synthase: structure and regulation. Tansey, T.R., Shechter, I. Prog. Nucleic Acid Res. Mol. Biol. (2001) [Pubmed]
  29. Compartmentalization of cholesterol biosynthesis. Conversion of mevalonate to farnesyl diphosphate occurs in the peroxisomes. Biardi, L., Krisans, S.K. J. Biol. Chem. (1996) [Pubmed]
  30. Mutants of Saccharomyces cerevisiae defective in the farnesylation of Ras proteins. Goodman, L.E., Judd, S.R., Farnsworth, C.C., Powers, S., Gelb, M.H., Glomset, J.A., Tamanoi, F. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  31. Regulation of macrophage cholesterol efflux through hydroxymethylglutaryl-CoA reductase inhibition: a role for RhoA in ABCA1-mediated cholesterol efflux. Argmann, C.A., Edwards, J.Y., Sawyez, C.G., O'Neil, C.H., Hegele, R.A., Pickering, J.G., Huff, M.W. J. Biol. Chem. (2005) [Pubmed]
  32. The Escherichia coli homologue of yeast RER2, a key enzyme of dolichol synthesis, is essential for carrier lipid formation in bacterial cell wall synthesis. Kato, J., Fujisaki, S., Nakajima, K., Nishimura, Y., Sato, M., Nakano, A. J. Bacteriol. (1999) [Pubmed]
  33. Geranylgeranyl pyrophosphate synthase encoded by the newly isolated gene GGPS6 from Arabidopsis thaliana is localized in mitochondria. Zhu, X.F., Suzuki, K., Saito, T., Okada, K., Tanaka, K., Nakagawa, T., Matsuda, H., Kawamukai, M. Plant Mol. Biol. (1997) [Pubmed]
  34. Inhibitors of prenylation of Ras and other G-proteins and their application as therapeutics. Cohen, L.H., Pieterman, E., van Leeuwen, R.E., Overhand, M., Burm, B.E., van der Marel, G.A., van Boom, J.H. Biochem. Pharmacol. (2000) [Pubmed]
  35. Regulation of intracellular actin polymerization by prenylated cellular proteins. Fenton, R.G., Kung, H.F., Longo, D.L., Smith, M.R. J. Cell Biol. (1992) [Pubmed]
  36. Yeast farnesyl-diphosphate synthase: site-directed mutagenesis of residues in highly conserved prenyltransferase domains I and II. Song, L., Poulter, C.D. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  37. Molecular cloning and promoter analysis of the rat liver farnesyl diphosphate synthase gene. Spear, D.H., Kutsunai, S.Y., Correll, C.C., Edwards, P.A. J. Biol. Chem. (1992) [Pubmed]
  38. Divalent cation and prenyl pyrophosphate specificities of the protein farnesyltransferase from rat brain, a zinc metalloenzyme. Reiss, Y., Brown, M.S., Goldstein, J.L. J. Biol. Chem. (1992) [Pubmed]
  39. Selection of potent inhibitors of farnesyl-protein transferase from a synthetic tetrapeptide combinatorial library. Wallace, A., Koblan, K.S., Hamilton, K., Marquis-Omer, D.J., Miller, P.J., Mosser, S.D., Omer, C.A., Schaber, M.D., Cortese, R., Oliff, A., Gibbs, J.B., Pessi, A. J. Biol. Chem. (1996) [Pubmed]
WikiGenes - Universities