Structural basis for the exceptional in vivo efficacy of bisphosphonate drugs. - Wikidata - wikimedia - TriplyDB

Structural basis for the exceptional in vivo efficacy of bisphosphonate drugs.

Structural basis for the exceptional in vivo efficacy of bisphosphonate drugs.

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Structure of a heterotetrameric geranyl pyrophosphate synthase from mint (Mentha piperita) reveals intersubunit regulation Mechanism of action and inhibition of dehydrosqualene synthase Human isoprenoid synthase enzymes as therapeutic targets Bisphosphonates target multiple sites in both cis- and trans-prenyltransferases Structures of a potent phenylalkyl bisphosphonate inhibitor bound to farnesyl and geranylgeranyl diphosphate synthases Inhibition of Geranylgeranyl Diphosphate Synthase by Bisphosphonates: A Crystallographic and Computational Investigation †Lipophilic Bisphosphonates as Dual Farnesyl/Geranylgeranyl Diphosphate Synthase Inhibitors: An X-ray and NMR Investigation Binding of nitrogen-containing bisphosphonates (N-BPs) to the Trypanosoma cruzi farnesyl diphosphate synthase homodimer Crystal Structure of Heterodimeric Hexaprenyl Diphosphate Synthase from Micrococcus luteus B-P 26 Reveals That the Small Subunit Is Directly Involved in the Product Chain Length Regulation Molecular Characterization of a Novel Geranylgeranyl Pyrophosphate Synthase from Plasmodium Parasites Ternary complex structures of human farnesyl pyrophosphate synthase bound with a novel inhibitor and secondary ligands provide insights into the molecular details of the enzyme’s active site closure Chemo-Immunotherapeutic Antimalarials Targeting Isoprenoid Biosynthesis Lipophilic analogs of zoledronate and risedronate inhibit Plasmodium geranylgeranyl diphosphate synthase (GGPPS) and exhibit potent antimalarial activity Head-to-Head Prenyl Tranferases: Anti-Infective Drug Targets Design, Synthesis, Calorimetry, and Crystallographic Analysis of 2-Alkylaminoethyl-1,1-bisphosphonates as Inhibitors of Trypanosoma cruzi Farnesyl Diphosphate Synthase Structural and thermodynamic basis of the inhibition ofLeishmania majorfarnesyl diphosphate synthase by nitrogen-containing bisphosphonates Structure of human farnesyl pyrophosphate synthase in complex with an aminopyridine bisphosphonate and two molecules of inorganic phosphate Crystal structures of ligand-bound octaprenyl pyrophosphate synthase fromEscherichia colireveal the catalytic and chain-length determining mechanisms Taxodione and arenarone inhibit farnesyl diphosphate synthase by binding to the isopentenyl diphosphate site Discovery of Novel Allosteric Non-Bisphosphonate Inhibitors of Farnesyl Pyrophosphate Synthase by Integrated Lead Finding A General Strategy for Targeting Drugs to Bone The crystal structure of human geranylgeranyl pyrophosphate synthase reveals a novel hexameric arrangement and inhibitory product binding Moenomycin Biosynthesis: Structure and Mechanism of Action of the Prenyltransferase MoeN5.Mechanisms of action of bisphosphonates: similarities and differences and their potential influence on clinical efficacy.Adaptive evolution of the chrysanthemyl diphosphate synthase gene involved in irregular monoterpene metabolism.Characterization of Arabidopsis FPS isozymes and FPS gene expression analysis provide insight into the biosynthesis of isoprenoid precursors in seeds The molecular mechanism of nitrogen-containing bisphosphonates as antiosteoporosis drugs.Small interfering RNA knocks down the molecular target of alendronate, farnesyl pyrophosphate synthase, in osteoclast and osteoblast cultures.Non-bisphosphonate inhibitors of isoprenoid biosynthesis identified via computer-aided drug design.Farnesyl diphosphate synthase inhibitors with unique ligand-binding geometries Structural characterization of substrate and inhibitor binding to farnesyl pyrophosphate synthase from Pseudomonas aeruginosa.Isoprenoids and related pharmacological interventions: potential application in Alzheimer's disease.Phosphate: known and potential roles during development and regeneration of teeth and supporting structures.2-alkylaminoethyl-1,1-bisphosphonic acids are potent inhibitors of the enzymatic activity of Trypanosoma cruzi squalene synthase.Terpenoid synthase structures: a so far incomplete view of complex catalysis.1-(Fluoroalkylidene)-1,1-bisphosphonic acids are potent and selective inhibitors of the enzymatic activity of Toxoplasma gondii farnesyl pyrophosphate synthase Farnesyl diphosphate synthase inhibitors from in silico screening.A highly sensitive prenylation assay reveals in vivo effects of bisphosphonate drug on the Rab prenylome of macrophages outside the skeleton.Terpene biosynthesis: modularity rules Future of anticathepsin K drugs: dual therapy for skeletal disease and atherosclerosis?

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P2860

Structural basis for the exceptional in vivo efficacy of bisphosphonate drugs.

http://www.wikidata.org/entity/Q50720187

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2006 nî lūn-bûn

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2006年の論文

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2006年学术文章

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2006年学术文章

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2006年学术文章

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2006年學術文章

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2006年學術文章

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name

Structural basis for the exceptional in vivo efficacy of bisphosphonate drugs.

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Structural basis for the exceptional in vivo efficacy of bisphosphonate drugs.

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type

label

Structural basis for the exceptional in vivo efficacy of bisphosphonate drugs.

@en

Structural basis for the exceptional in vivo efficacy of bisphosphonate drugs.

@nl

prefLabel

Structural basis for the exceptional in vivo efficacy of bisphosphonate drugs.

@en

Structural basis for the exceptional in vivo efficacy of bisphosphonate drugs.

@nl

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Structural basis for the exceptional in vivo efficacy of bisphosphonate drugs.

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André Strauss

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Emmanuelle Bourgier

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Francis Bitsch

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Jean-Michel Rondeau

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Jonathan R Green

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Markus Kroemer

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Martin Geiser

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Rene Hemmig

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Sebastien Rieffel

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10.1002/CMDC.200500059

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