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

farnesyl-PP     [hydroxy-[(2E,6E)-3,7,11- trimethyldodeca-2...

Synonyms: CHEMBL69330, CHEBI:17407, F6892_SIGMA, HMDB00961, DNC000637, ...
 
 
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 farnesyl pyrophosphate

 

High impact information on farnesyl pyrophosphate

 

Biological context of farnesyl pyrophosphate

 

Anatomical context of farnesyl pyrophosphate

 

Associations of farnesyl pyrophosphate with other chemical compounds

 

Gene context of farnesyl pyrophosphate

  • Suppression was reversed by downstream intermediates of HMG-CoA reductase, mevalonate, and geranylgeranylpyrophosphate, but not farnesylpyrophosphate [22].
  • Simple n-alkyl-1-hydroxy-1,1-bisphosphonates, known inhibitors of the enzyme farnesylpyrophosphate (FPP) synthase, were also active, with optimal activity being found with C9-C10 side chains [23].
  • Rab11 associates in vitro geranylgeranylpyrophosphate and farnesylpyrophosphate [24].
  • It could act by inhibiting the synthesis of isoprenoids (farnesylpyrophosphate (FPP) and geranylgeranylpyrophosphate (GGPP)), which are respectively essential for membrane attachment and biological activity of GTPases Ras and RhoA [25].
  • FTase catalyzes the transfer of a farnesyl group from farnesylpyrophosphate (FPP) to cysteine 185/186 at the carboxyl terminal end of ras proteins (ras p21), a reaction essential for the localization of ras p21 to the plasma membrane for their cellular functions including cell transformation in case of oncogenic ras p21 [26].
 

Analytical, diagnostic and therapeutic context of farnesyl pyrophosphate

References

  1. Molecular cloning and characterization of a protein farnesyltransferase from the enteric protozoan parasite Entamoeba histolytica. Kumagai, M., Makioka, A., Takeuchi, T., Nozaki, T. J. Biol. Chem. (2004) [Pubmed]
  2. Protein geranylgeranylation is critical for the regulation of survival and proliferation of lymphoma tumor cells. van de Donk, N.W., Schotte, D., Kamphuis, M.M., van Marion, A.M., van Kessel, B., Bloem, A.C., Lokhorst, H.M. Clin. Cancer Res. (2003) [Pubmed]
  3. Regulation of enzymes involved in the biosynthesis of the sesquiterpene antibiotic pentalenolactone in Streptomyces arenae. Maurer, K.H., Mecke, D. J. Antibiot. (1986) [Pubmed]
  4. Biochemical changes of mevalonate pathway in human colorectal cancer. Caruso, M.G., Notarnicola, M. Anticancer Res. (2005) [Pubmed]
  5. Lovastatin augments sulindac-induced apoptosis in colon cancer cells and potentiates chemopreventive effects of sulindac. Agarwal, B., Rao, C.V., Bhendwal, S., Ramey, W.R., Shirin, H., Reddy, B.S., Holt, P.R. Gastroenterology (1999) [Pubmed]
  6. Inhibition of systemic sclerosis dermal fibroblast type I collagen production and gene expression by simvastatin. Louneva, N., Huaman, G., Fertala, J., Jiménez, S.A. Arthritis Rheum. (2006) [Pubmed]
  7. 3-Hydroxy-3-methylglutaryl-CoA reductase inhibitors attenuate vascular smooth muscle proliferation by preventing rho GTPase-induced down-regulation of p27(Kip1). Laufs, U., Marra, D., Node, K., Liao, J.K. J. Biol. Chem. (1999) [Pubmed]
  8. Potent inhibition of human tumor p21ras farnesyltransferase by A1A2-lacking p21ras CA1A2X peptidomimetics. Nigam, M., Seong, C.M., Qian, Y., Hamilton, A.D., Sebti, S.M. J. Biol. Chem. (1993) [Pubmed]
  9. Statins activate the mitochondrial pathway of apoptosis in human lymphoblasts and myeloma cells. Cafforio, P., Dammacco, F., Gernone, A., Silvestris, F. Carcinogenesis (2005) [Pubmed]
  10. Protein farnesyltransferase isoprenoid substrate discrimination is dependent on isoprene double bonds and branched methyl groups. Micali, E., Chehade, K.A., Isaacs, R.J., Andres, D.A., Spielmann, H.P. Biochemistry (2001) [Pubmed]
  11. Simvastatin inhibits the migration and adhesion of monocytic cells and disorganizes the cytoskeleton of activated endothelial cells. Pozo, M., de Nicolás, R., Egido, J., González-Cabrero, J. Eur. J. Pharmacol. (2006) [Pubmed]
  12. Pitavastatin inhibits vascular smooth muscle cell proliferation by inactivating extracellular signal-regulated kinases 1/2. Yamakawa, T., Tanaka, S., Kamei, J., Kadonosono, K., Okuda, K. J. Atheroscler. Thromb. (2003) [Pubmed]
  13. Effect of lovastatin on small GTP binding proteins and on TGF-beta1 and fibronectin expression. Kim, S.I., Kim, H.J., Han, D.C., Lee, H.B. Kidney Int. Suppl. (2000) [Pubmed]
  14. HMG-CoA reductase inhibition causes neurite loss by interfering with geranylgeranylpyrophosphate synthesis. Schulz, J.G., Bösel, J., Stoeckel, M., Megow, D., Dirnagl, U., Endres, M. J. Neurochem. (2004) [Pubmed]
  15. Simvastatin suppresses coronary artery endothelial tube formation by disrupting Ras/Raf/ERK signaling. Miura, S., Matsuo, Y., Saku, K. Atherosclerosis (2004) [Pubmed]
  16. Connective tissue growth factor expression and induction by transforming growth factor-beta is abrogated by simvastatin via a Rho signaling mechanism. Watts, K.L., Spiteri, M.A. Am. J. Physiol. Lung Cell Mol. Physiol. (2004) [Pubmed]
  17. Geranylgeraniol potentiates lovastatin inhibition of oncogenic H-Ras processing and signaling while preventing cytotoxicity. McGuire, T.F., Sebti, S.M. Oncogene (1997) [Pubmed]
  18. Discordant regulation of proteins of cholesterol metabolism during the acute phase response. Feingold, K.R., Pollock, A.S., Moser, A.H., Shigenaga, J.K., Grunfeld, C. J. Lipid Res. (1995) [Pubmed]
  19. Stabilisation of transition states prior to and following eudesmane cation in aristolochene synthase. Forcat, S., Allemann, R.K. Org. Biomol. Chem. (2006) [Pubmed]
  20. 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitors decrease Fas ligand expression and cytotoxicity in activated human T lymphocytes. Blanco-Colio, L.M., Muñoz-García, B., Martín-Ventura, J.L., Lorz, C., Díaz, C., Hernández, G., Egido, J. Circulation (2003) [Pubmed]
  21. Glucose-potentiated chemotaxis in human vascular smooth muscle is dependent on cross-talk between the PI3K and MAPK signaling pathways. Campbell, M., Allen, W.E., Sawyer, C., Vanhaesebroeck, B., Trimble, E.R. Circ. Res. (2004) [Pubmed]
  22. Statins downregulate myeloperoxidase gene expression in macrophages. Kumar, A.P., Reynolds, W.F. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  23. Effects of bisphosphonates on the growth of Entamoeba histolytica and Plasmodium species in vitro and in vivo. Ghosh, S., Chan, J.M., Lea, C.R., Meints, G.A., Lewis, J.C., Tovian, Z.S., Flessner, R.M., Loftus, T.C., Bruchhaus, I., Kendrick, H., Croft, S.L., Kemp, R.G., Kobayashi, S., Nozaki, T., Oldfield, E. J. Med. Chem. (2004) [Pubmed]
  24. Isoprenylation of Rab proteins possessing a C-terminal CaaX motif. Joberty, G., Tavitian, A., Zahraoui, A. FEBS Lett. (1993) [Pubmed]
  25. Inhibition of endothelial cell migration by cerivastatin, an HMG-CoA reductase inhibitor: contribution to its anti-angiogenic effect. Vincent, L., Chen, W., Hong, L., Mirshahi, F., Mishal, Z., Mirshahi-Khorassani, T., Vannier, J.P., Soria, J., Soria, C. FEBS Lett. (2001) [Pubmed]
  26. A rapid and convenient filter-binding assay for ras p21 processing enzyme farnesyltransferase. Khan, S.G., Mukhtar, H., Agarwal, R. J. Biochem. Biophys. Methods (1995) [Pubmed]
  27. Internal mammary artery smooth muscle cells resist migration and possess high antioxidant capacity. Mahadevan, V.S., Campbell, M., McKeown, P.P., Bayraktutan, U. Cardiovasc. Res. (2006) [Pubmed]
  28. Purification of farnesylpyrophosphate synthetase by affinity chromatography. Bartlett, D.L., King, C.H., Poulter, C.D. Meth. Enzymol. (1985) [Pubmed]
 
WikiGenes - Universities