PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 24598749-1 2014 Farnesyl diphosphate synthase (FPPS) is an essential enzyme involved in the biosynthesis of sterols (cholesterol in humans and ergosterol in yeasts, fungi and trypanosomatid parasites) as well as in protein prenylation. Sterols 92-99 farnesyl diphosphate synthase Homo sapiens 0-29 24598749-1 2014 Farnesyl diphosphate synthase (FPPS) is an essential enzyme involved in the biosynthesis of sterols (cholesterol in humans and ergosterol in yeasts, fungi and trypanosomatid parasites) as well as in protein prenylation. Sterols 92-99 farnesyl diphosphate synthase Homo sapiens 31-35 10620343-9 2000 These findings (i) identify farnesyl diphosphate synthase as the selective target of alendronate in the mevalonate pathway, (ii) show that this enzyme is inhibited by other N-containing bisphosphonates, such as risendronate, but not by clodronate, supporting a different mechanism of action for different bisphosphonates, and (iii) document in purified osteoclasts alendronate inhibition of prenylation and sterol biosynthesis. Sterols 407-413 farnesyl diphosphate synthase Homo sapiens 28-57 21497677-8 2011 FPPS generates isoprenoid lipids utilized in sterol synthesis and for the post-translational modification of small GTP-binding proteins essential for osteoclast function. Sterols 45-51 farnesyl diphosphate synthase Homo sapiens 0-4 20450493-3 2010 In the present study, we characterized the sterol-response element and NF-Y (nuclear factor Y)-binding site in the human FDPS promoter. Sterols 43-49 farnesyl diphosphate synthase Homo sapiens 121-125 20450493-5 2010 We also investigated whether sterol-mediated FDPS expression is involved in the cell proliferation induced by zoledronic acid, an FDPS inhibitor. Sterols 29-35 farnesyl diphosphate synthase Homo sapiens 45-49 20450493-5 2010 We also investigated whether sterol-mediated FDPS expression is involved in the cell proliferation induced by zoledronic acid, an FDPS inhibitor. Sterols 29-35 farnesyl diphosphate synthase Homo sapiens 130-134 22842101-2 2013 A key enzyme in this pathway is farnesyl pyrophosphate (EC 2.5.1.10) synthase (FPPS) which supplies precursors for the biosynthesis of essential isoprenoids like carotenoids, withanolides, ubiquinones, dolichols, sterols, among others and also helps in farnesylation and geranylation of proteins. Sterols 213-220 farnesyl diphosphate synthase Homo sapiens 79-83 16475941-9 2006 There are many enzymes involved in this biosynthetic pathway such us squalene synthase, farnesylpyrophosphate synthase, and other enzymes that are able to deplete endogenous sterols will be treated in this article. Sterols 174-181 farnesyl diphosphate synthase Homo sapiens 88-118 15827605-1 2005 Farnesyl diphosphate synthase (FPPS) is a key enzyme in isoprenoid biosynthesis which supplies sesquiterpene precursors for several classes of essential metabolites including sterols, dolichols, ubiquinones and carotenoids as well as substrates for farnesylation and geranylgeranylation of proteins. Sterols 175-182 farnesyl diphosphate synthase Homo sapiens 0-29 15827605-1 2005 Farnesyl diphosphate synthase (FPPS) is a key enzyme in isoprenoid biosynthesis which supplies sesquiterpene precursors for several classes of essential metabolites including sterols, dolichols, ubiquinones and carotenoids as well as substrates for farnesylation and geranylgeranylation of proteins. Sterols 175-182 farnesyl diphosphate synthase Homo sapiens 31-35 15713990-1 2004 OBJECTIVE: Farnesyl diphosphate synthase (FPPs) produces FPP which is considered a branch-point intermediate in the synthesis of sterols and isoprenylated cellular metabolites. Sterols 129-136 farnesyl diphosphate synthase Homo sapiens 11-40 15713990-1 2004 OBJECTIVE: Farnesyl diphosphate synthase (FPPs) produces FPP which is considered a branch-point intermediate in the synthesis of sterols and isoprenylated cellular metabolites. Sterols 129-136 farnesyl diphosphate synthase Homo sapiens 42-46 7665553-3 1995 Co-transfection of cells with NF-YA29, a dominant negative form of NF-Y, and various promoter-reporter genes specifically inhibits the sterol-dependent regulation of FPP synthase and 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) synthase. Sterols 135-141 farnesyl diphosphate synthase Homo sapiens 166-178 9651391-8 1998 We conclude that when cells are incubated in the absence of sterols, the transcriptional activation of the HMG-CoA synthase, HMG-CoA reductase, FPP synthase, and low density lipoprotein receptor genes is dependent on a specific interaction between SREBP, which is bound to the promoter DNA, and the amino-terminal domain (amino acids 1-451) of CBP. Sterols 60-67 farnesyl diphosphate synthase Homo sapiens 144-156 1346397-1 1992 We report that the sterol-mediated suppression of the mRNA levels of three cholesterogenic enzymes, 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase, HMG-CoA synthase, and farnesyl diphosphate (FPP) synthetase is partially overcome by the calcium ionophore A23187. Sterols 19-25 farnesyl diphosphate synthase Homo sapiens 181-218 2613235-2 1989 Somatic cell hybrid studies and in situ hybridization show that the human genome contains five distinct loci that hybridize to the cDNA for the enzyme farnesyl pyrophosphate synthetase (FPS), a prenyltransferase that catalyzes the synthesis of an intermediate common to both the sterol and the nonsterol branches of the isoprene biosynthetic pathway. Sterols 279-285 farnesyl diphosphate synthase Homo sapiens 151-184 2613235-2 1989 Somatic cell hybrid studies and in situ hybridization show that the human genome contains five distinct loci that hybridize to the cDNA for the enzyme farnesyl pyrophosphate synthetase (FPS), a prenyltransferase that catalyzes the synthesis of an intermediate common to both the sterol and the nonsterol branches of the isoprene biosynthetic pathway. Sterols 279-285 farnesyl diphosphate synthase Homo sapiens 186-189