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mitochondrial targeting of FPS may be widespread among eukaryotes
Farnesyl diphosphate synthase (FPPS) of the dipteran Drosophila melanogaster has been cloned and its catalytic properties have been assessed.
Farnesyl pyrophosphate (FPP) allosterically regulated the activity of farnesyl pyrophosphate synthase.
FPPS mediates TGF-beta1-induced lung cancer cell invasion and epithelial-to-mesenchymal transition via the RhoA/Rock1 pathway.
Crystallographic and thermodynamic characterization of phenylaminopyridine bisphosphonates binding to human farnesyl pyrophosphate synthase
These results are consistent with the previously proposed hypothesis that the allosteric pocket of human FPPS, located near the active site, plays a feed-back regulatory role for this enzyme.
our study indicated that DR patients have higher VEGF levels than diabetic patients without retinopathy, and -2578A/C (rs699947) and +405C/G (rs2010963) may be important factors in determining serum VEGF levels.
Results suggest that polymorphisms of the FDPS gene may influence the bone response to drugs targeting the mevalonate pathway, like statins.
A co-crystal structure of human farnesyl pyrophosphate synthase in complex with a bisphosphonate and two molecules of inorganic phosphate.
The results identify new classes of FPPS inhibitors, diterpenoids and sesquiterpenoids, that bind to the IPP site and may be of interest as anticancer and antiinfective drug leads.
These observations suggest that an increase in the expression of endogenous FPPS could confer at least partial resistance to the pharmacological effect of N-BP drugs such as ZOL in vivo
LRP5 and FDPS loci age-specifically affect skeletal traits in healthy fertile women.
Data indicate compounds represent a new structural class of farnesyl pyrophosphate synthase (hFPPS) inhibitors and suggest a development of therapeutics.
The iPA-driven modulation of FDPS can cause an enhancement of post-translational prenylation essential for the biological activity of key proteins in NK signaling and effector functions, such as Ras.
FPPS was more highly expressed in prostate cancer vs. normal prostate tissue. The association of FPPS with established histopathological risk parameters and biochemical recurrence implicates a contribution of the mevalonate pathway to PC progression.
FPPS might play an important role in Ang II-induced cardiac hypertrophy and fibrosis in vivo, at least in part through RhoA, p-38 MAPK and TGF-beta1.
The crystal structure of human FPPS in complex with a novel bisphosphonate YS0470 and in the absence of a second substrate showed partial ordering of the tail in the closed conformation.
Common polymorphisms of the FDPS gene influence the response to bisphosphonates in osteoporotic women.
findings reveal a FDPS-dependent mechanism in the internalization and down-regulation of beta2AR, identify FDPS as a potential target for improving the therapeutic efficacy of beta-agonists
first study on the gene FDPS rs2297480 SNP in postmenopausal Thai women.The effect did not contribute to the baseline of bone mineral density nor bone turnover markers.
The A/C rs2297480 polymorphism of FDPS was highly differently distributed among osteonecrosis-of-the-jaw patients and controls, with a correlation between AA carrier status and occurrence of ONJ after 18-24 months of treatment with bisphosphonates.
characterized the sterol-response-element-binding protein 2 and nuclear factor Y-binding site in the farnesyl diphosphate synthase promoter
Overexpression of FPPS aggravates myocardial ischemia/reperfusion injury in mice.
Farnesyl pyrophosphate synthase (FPPS) may function as a potent regulator in myocardial remodelling. The FPPS-regulated signalling pathway is relevant to the pathological changes in cardiac hypertrophy and heart failure.
novel role in fibroblast growth factor-mediated signal transduction
identified a single putative direct repeat 4 (DR4) LXR response element in the FPS promoter isolated from immortalized murine astrocyte P11-5 cells
This gene encodes an enzyme that catalyzes the production of geranyl pyrophosphate and farnesyl pyrophosphate from isopentenyl pyrophosphate and dimethylallyl pyrophosphate. The resulting product, farnesyl pyrophosphate, is a key intermediate in cholesterol and sterol biosynthesis, a substrate for protein farnesylation and geranylgeranylation, and a ligand or agonist for certain hormone receptors and growth receptors. Drugs that inhibit this enzyme prevent the post-translational modifications of small GTPases and have been used to treat diseases related to bone resorption. Multiple pseudogenes have been found on chromosomes 1, 7, 14, 15, 21 and X. Multiple transcript variants encoding different isoforms have been found for this gene.
farnesyl pyrophosphate synthase
, farnesyl diphosphate synthase
, farnesyl diphosphate synthase (farnesyl pyrophosphate synthetase, dimethylallyltranstransferase, geranyltranstransferase)
, farnesyl pyrophosphate synthetase
, Farnesyl pyrophosphate synthetase
, (2E,6E)-farnesyl diphosphate synthase
, FPP synthase
, FPP synthetase
, farnesyl pyrophosphate synthetase, dimethylallyltranstransferase, geranyltranstransferase
, CR 39
, cholesterol-regulated 39 kDa protein
, farnesyl diphosphate synthetase
, testis-specific farnesyl pyrophosphate synthetase
, 6E)-farnesyl diphosphate synthase
, geranylgeranyl-diphosphate synthase