MEDI 73-Modeling, synthetic, crystallographic, and activity studies of novel bisphosphonates as inhibitors of farnesyl pyrophosphate synthase

Bibliográfalaš dieđut
Váldodahkkit:	Hogan, J, Deprele, S, Kashemirov, B, Barnett, B, Evdokimov, A, Dunford, J, Russell, R, Ebetino, F, McKenna, C
Materiálatiipa:	Journal article
Almmustuhtton:	2007

A mirror image pair of bisphosphonate analogs further demonstrates the mode of binding of the bisphosphonates in farnesyl pyrophosphate synthase
Dahkki: Ebetino, F, et al.
Almmustuhtton: (2008)

The mode of binding of nitrogen containing bisphosphonates in farnesyl pyrophosphate synthase
Dahkki: Ebetino, F, et al.
Almmustuhtton: (2007)

The Role of Active Site Threonine 201 in the Inhibition of Farnesyl Pyrophosphate Synthase by Nitrogen Containing Bisphosphonates
Dahkki: Dunford, J, et al.
Almmustuhtton: (2008)

Evidence for the involvement of the threonine 201 side-chain in the interaction of nitrogen-containing bisphosphonates with farnesyl pyrophosphate synthase
Dahkki: Kwassi, A, et al.
Almmustuhtton: (2009)

Analysis of the kinetic mechanism of inhibition of Farnesyl Pyrophosphate Synthase by nitrogen containing bisphosphonates.
Dahkki: Dunford, J, et al.
Almmustuhtton: (2006)

Kinetic analysis of conformational changes in farnesyl pyrophosphate synthase induced by nitrogen containing bisphosphonates
Dahkki: Dunford, J, et al.
Almmustuhtton: (2007)

The interaction of sidechain nitrogen with active site threonine is not essential for inhibition of farnesyl pyrophosphate synthase by nitrogen containing bisphosphonates
Dahkki: Dunford, J, et al.
Almmustuhtton: (2008)

Molecular interactions of nitrogen-containing bisphosphonates within farnesyl diphosphate synthase
Dahkki: Ebetino, F, et al.
Almmustuhtton: (2005)

Molecular modeling comparison of nitrogen-containing bisphosphonates of varying potency co-crystalized in farnesyl diphosphate synthase
Dahkki: Ebetino, F, et al.
Almmustuhtton: (2006)

Human farnesyl diphosphate synthase crystal structures with active and inactive bisphosphonates
Dahkki: Evdokimov, A, et al.
Almmustuhtton: (2006)

Structure activity relationships of nitrogen containing bisphosphonates which induce conformational changes in farnesyl pyrophosphate synthase
Dahkki: Dunford, J, et al.
Almmustuhtton: (2008)

Interaction of the active site threonine 201 sidechain with the nitrogen of nttrogen-containing bisphosphonates is not essential for slow tight inhibition to farnesyl pyrophosphate synthase
Dahkki: Dunford, J, et al.
Almmustuhtton: (2008)

Modeling of bisphosphonate binding to farnesyl diphosphate synthase
Dahkki: Ebetino, F, et al.
Almmustuhtton: (2002)

Refining structure activity relationships among nitrogen containing bisphosphonates: Dissociation of mineral binding affinity and inhibitory potency on farnesyl diphosphate synthase.
Dahkki: Xia, Z, et al.
Almmustuhtton: (2006)

Kinetic analysis of conformational changes in farnesyl pyrophosphate synthase induced by nitrogen containing bisphosphonates
Dahkki: Dunford, J, et al.
Almmustuhtton: (2007)

Stereochemical evidence of the mode of binding of nitrogen containing bisphosphonates in farnesyl diphosphate synthase
Dahkki: Ebetino, F, et al.
Almmustuhtton: (2007)

Structure-activity relationships among the nitrogen containing bisphosphonates in clinical use and other analogues: time-dependent inhibition of human farnesyl pyrophosphate synthase.
Dahkki: Dunford, J, et al.
Almmustuhtton: (2008)

Molecular modeling comparison of nitrogen-containing bisphosphonates of varying potency co-crystalized in farnesyl diphosphate synthase
Dahkki: Ebetino, F, et al.
Almmustuhtton: (2006)

Nitrogen-containing bisphosphonates of varying antiresorptive potency have been co-crystallized in farnesyl diphosphate synthase and modelled to understand the key structural features involved in enzyme inhibition.
Dahkki: Ebetino, F, et al.
Almmustuhtton: (2006)

Predicting the clinical potencies of bisphosphonates: Divergence of hydroxyapatite and farnesyl diphosphate synthase binding affinities
Dahkki: Xia, Z, et al.
Almmustuhtton: (2007)

Designed mutants of human farnesyl pyrophosphate synthase (FPPS) help to characterise the interactions of nitrogen-containing bisphosphonates with Tyrosine 204 and Phenylalanine 239 side-chain residues
Dahkki: Tsoumpra, M, et al.
Almmustuhtton: (2010)

The inhibition of human farnesyl pyrophosphate synthase by nitrogen-containing bisphosphonates. Elucidating the role of active site threonine 201 and tyrosine 204 residues using enzyme mutants.
Dahkki: Tsoumpra, M, et al.
Almmustuhtton: (2015)

Bisphosphonate affinity to hydroxyapatite and farnesyl pyrophosphate inhibitory potency, together, drive in vivo efficacy
Dahkki: Lundy, M, et al.
Almmustuhtton: (2007)

The inhibition of human farnesyl pyrophosphate synthase by nitrogen-containing bisphosphonates. Elucidating the role of active site threonine 201 and tyrosine 204 residues using enzyme mutants
Dahkki: Tsoumpra, MK, et al.
Almmustuhtton: (2015)

Investigations into the kinetic mechanism of inhibition of farnesyl diphosphate synthase by nitrogen containing bisphosphonates
Dahkki: Dunford, J, et al.
Almmustuhtton: (2006)

Phosphonate and Bisphosphonate Inhibitors of Farnesyl Pyrophosphate Synthases: A Structure-Guided Perspective
Dahkki: Jaeok Park, et al.
Almmustuhtton: (2021-01-01)

Molecular modeling of the bisphosphonates (BPs) in farnesyl diphosphate (FPP) synthase. Proposed new mechanism of inhibition by potent nitrogen containing bisphosphonates (NBPs).
Dahkki: Ebetino, F, et al.
Almmustuhtton: (2002)

Molecular modeling of the bisphosphonates in farnesyl diphosphate synthase. potential new details of the precise biochemical mechanism of action of potent nitrogen containing bisphosphonates
Dahkki: Ebetino, F, et al.
Almmustuhtton: (2002)

Human farnesyl diphosphate synthase (FDFS): Crystal structure and molecular interactions with Nnitrogen-containing bisphosphonates.
Dahkki: Kavanagh, K, et al.
Almmustuhtton: (2005)

New anti-candida active nitrogen-containing bisphosphonates as inhibitors of farnesyl pyrophosphate synthase Candida albicans
Dahkki: L. O. Metelytsia, et al.
Almmustuhtton: (2019-05-01)

Correlation between time-dependent inhibition of human farnesyl pyrophosphate synthase and blockade of mevalonate pathway by nitrogen-containing bisphosphonates in cultured cells
Dahkki: Räikkönen, J, et al.
Almmustuhtton: (2011)

Correlation between time-dependent inhibition of human farnesyl pyrophosphate synthase and blockade of mevalonate pathway by nitrogen-containing bisphosphonates in cultured cells.
Dahkki: Räikkönen, J, et al.
Almmustuhtton: (2011)

Inhibition of human mevalonate kinase by allosteric inhibitors of farnesyl pyrophosphate synthase
Dahkki: Saman Salari, et al.
Almmustuhtton: (2024-08-01)

Molecular Cloning and Characterisation of Farnesyl Pyrophosphate Synthase from Tripterygium wilfordii.
Dahkki: Yu-Jun Zhao, et al.
Almmustuhtton: (2015-01-01)

Human farnesyl pyrophosphate synthase is allosterically inhibited by its own product
Dahkki: Jaeok Park, et al.
Almmustuhtton: (2017-01-01)

Functional characterization of the Xanthophyllomyces dendrorhous farnesyl pyrophosphate synthase and geranylgeranyl pyrophosphate synthase encoding genes that are involved in the synthesis of isoprenoid precursors.
Dahkki: Jennifer Alcaíno, et al.
Almmustuhtton: (2014-01-01)

The relationship between the chemistry and biological activity of the bisphosphonates.
Dahkki: Ebetino, F, et al.
Almmustuhtton: (2011)

Crystal structures and molecular interactions of risedronate and zoledronate with human farnesyl diphosphate synthase
Dahkki: Kavanagh, K, et al.
Almmustuhtton: (2006)

Role of the geminal hydroxyl group in target enzyme inhibition by bisphosphonates and phosphonocarboxylates
Dahkki: Stewart, C, et al.
Almmustuhtton: (2007)

Differential effects of alpha-halogenation on the potency of bisphosphonates and phosphonocarboxylates for inhibition of their target enzymes
Dahkki: Stewart, C, et al.
Almmustuhtton: (2007)

MEDI 73-Modeling, synthetic, crystallographic, and activity studies of novel bisphosphonates as inhibitors of farnesyl pyrophosphate synthase

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