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.

ग्रंथसूची विवरण
मुख्य लेखकों:	Ebetino, F, Barnett, B, Roze, C, Kashemirov, B, McKenna, C, Evdokimov, A, Pokross, M, Dunford, J, Opermann, U, Kavanagh, K, Rogers, M, Russell, R
स्वरूप:	Conference item
प्रकाशित:	2006

Molecular modeling comparison of nitrogen-containing bisphosphonates of varying potency co-crystalized in farnesyl diphosphate synthase
द्वारा: Ebetino, F, और अन्य
प्रकाशित: (2006)

Human farnesyl diphosphate synthase crystal structures with active and inactive bisphosphonates
द्वारा: Evdokimov, A, और अन्य
प्रकाशित: (2006)

Molecular modeling comparison of nitrogen-containing bisphosphonates of varying potency co-crystalized in farnesyl diphosphate synthase
द्वारा: Ebetino, F, और अन्य
प्रकाशित: (2006)

Refining structure activity relationships among nitrogen containing bisphosphonates: Dissociation of mineral binding affinity and inhibitory potency on farnesyl diphosphate synthase.
द्वारा: Xia, Z, और अन्य
प्रकाशित: (2006)

Molecular interactions of nitrogen-containing bisphosphonates within farnesyl diphosphate synthase
द्वारा: Ebetino, F, और अन्य
प्रकाशित: (2005)

Stereochemical evidence of the mode of binding of nitrogen containing bisphosphonates in farnesyl diphosphate synthase
द्वारा: Ebetino, F, और अन्य
प्रकाशित: (2007)

Predicting the clinical potencies of bisphosphonates: Divergence of hydroxyapatite and farnesyl diphosphate synthase binding affinities
द्वारा: Xia, Z, और अन्य
प्रकाशित: (2007)

Modeling of bisphosphonate binding to farnesyl diphosphate synthase
द्वारा: Ebetino, F, और अन्य
प्रकाशित: (2002)

Investigations into the kinetic mechanism of inhibition of farnesyl diphosphate synthase by nitrogen containing bisphosphonates
द्वारा: Dunford, J, और अन्य
प्रकाशित: (2006)

MEDI 73-Modeling, synthetic, crystallographic, and activity studies of novel bisphosphonates as inhibitors of farnesyl pyrophosphate synthase
द्वारा: Hogan, J, और अन्य
प्रकाशित: (2007)

Human farnesyl diphosphate synthase (FDFS): Crystal structure and molecular interactions with Nnitrogen-containing bisphosphonates.
द्वारा: Kavanagh, K, और अन्य
प्रकाशित: (2005)

Molecular modeling of the bisphosphonates (BPs) in farnesyl diphosphate (FPP) synthase. Proposed new mechanism of inhibition by potent nitrogen containing bisphosphonates (NBPs).
द्वारा: Ebetino, F, और अन्य
प्रकाशित: (2002)

A mirror image pair of bisphosphonate analogs further demonstrates the mode of binding of the bisphosphonates in farnesyl pyrophosphate synthase
द्वारा: Ebetino, F, और अन्य
प्रकाशित: (2008)

Molecular modeling of the bisphosphonates in farnesyl diphosphate synthase. potential new details of the precise biochemical mechanism of action of potent nitrogen containing bisphosphonates
द्वारा: Ebetino, F, और अन्य
प्रकाशित: (2002)

The Role of Active Site Threonine 201 in the Inhibition of Farnesyl Pyrophosphate Synthase by Nitrogen Containing Bisphosphonates
द्वारा: Dunford, J, और अन्य
प्रकाशित: (2008)

Evidence for the involvement of the threonine 201 side-chain in the interaction of nitrogen-containing bisphosphonates with farnesyl pyrophosphate synthase
द्वारा: Kwassi, A, और अन्य
प्रकाशित: (2009)

Crystal structures and molecular interactions of risedronate and zoledronate with human farnesyl diphosphate synthase
द्वारा: Kavanagh, K, और अन्य
प्रकाशित: (2006)

Predicting pharmacological potencies of nitrogen-containing bisphosphonates; novel methods dissociate enzyme- and hydroxyapatite-binding affinities
द्वारा: Xia, Z, और अन्य
प्रकाशित: (2007)

Analysis of the kinetic mechanism of inhibition of Farnesyl Pyrophosphate Synthase by nitrogen containing bisphosphonates.
द्वारा: Dunford, J, और अन्य
प्रकाशित: (2006)

The interaction of sidechain nitrogen with active site threonine is not essential for inhibition of farnesyl pyrophosphate synthase by nitrogen containing bisphosphonates
द्वारा: Dunford, J, और अन्य
प्रकाशित: (2008)

Kinetic analysis of conformational changes in farnesyl pyrophosphate synthase induced by nitrogen containing bisphosphonates
द्वारा: Dunford, J, और अन्य
प्रकाशित: (2007)

The mode of binding of nitrogen containing bisphosphonates in farnesyl pyrophosphate synthase
द्वारा: Ebetino, F, और अन्य
प्रकाशित: (2007)

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
द्वारा: Dunford, J, और अन्य
प्रकाशित: (2008)

Structure activity relationships of nitrogen containing bisphosphonates which induce conformational changes in farnesyl pyrophosphate synthase
द्वारा: Dunford, J, और अन्य
प्रकाशित: (2008)

Bisphosphonate affinity to hydroxyapatite and farnesyl pyrophosphate inhibitory potency, together, drive in vivo efficacy
द्वारा: Lundy, M, और अन्य
प्रकाशित: (2007)

Differential effects of alpha-halogenation on the potency of bisphosphonates and phosphonocarboxylates for inhibition of their target enzymes
द्वारा: Stewart, C, और अन्य
प्रकाशित: (2007)

Structure-activity relationships among the nitrogen containing bisphosphonates in clinical use and other analogues: time-dependent inhibition of human farnesyl pyrophosphate synthase.
द्वारा: Dunford, J, और अन्य
प्रकाशित: (2008)

Insights about the structure of farnesyl diphosphate synthase (FPPS) and the activity of bisphosphonates on the proliferation and ultrastructure of Leishmania and Giardia
द्वारा: Ana Paula R. Gadelha, और अन्य
प्रकाशित: (2020-04-01)

Kinetic analysis of conformational changes in farnesyl pyrophosphate synthase induced by nitrogen containing bisphosphonates
द्वारा: Dunford, J, और अन्य
प्रकाशित: (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.
द्वारा: Tsoumpra, M, और अन्य
प्रकाशित: (2015)

Farnesyl diphosphate synthase is important for the maintenance of glioblastoma stemness
द्वारा: Hee Yeon Kim, और अन्य
प्रकाशित: (2018-10-01)

Plasmodium falciparum parasites overexpressing farnesyl diphosphate synthase/geranylgeranyl diphosphate synthase are more resistant to risedronate
द्वारा: Heloisa B Gabriel, और अन्य
प्रकाशित: (2018-08-01)

FARNESYL DIPHOSPHATE SYNTHASE (FDRS) AND GERANYLGERANYL DIPHOSPHATE SYNTHASE (GGSP1) GENE POLYMORPHISMS AND EFFICIENCY OF THERAPY WITH BISPHOSPHONATES IN RUSSIAN WOMEN WITH POSTMENOPAUSAL OSTEOPOROSIS: A PILOT STUDY
द्वारा: M. Yu. Krylov, और अन्य
प्रकाशित: (2016-03-01)

Bisphosphonate affects the behavioral responses to HCl by disrupting farnesyl diphosphate synthase in mouse taste bud and tongue epithelial cells
द्वारा: Asami Oike, और अन्य
प्रकाशित: (2022-12-01)

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
द्वारा: Tsoumpra, MK, और अन्य
प्रकाशित: (2015)

Nitrogen-containing bisphosphonates and prediction of their clinical potencies: Dissociation of target enzyme- and hydroxyapatite-binding affinities
द्वारा: Xia, Z, और अन्य
प्रकाशित: (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
द्वारा: Tsoumpra, M, और अन्य
प्रकाशित: (2010)

Role of the geminal hydroxyl group in target enzyme inhibition by bisphosphonates and phosphonocarboxylates
द्वारा: Stewart, C, और अन्य
प्रकाशित: (2007)

Functional characterization of a farnesyl diphosphate synthase from Dendrobium nobile Lindl
द्वारा: Daoyong Gong, और अन्य
प्रकाशित: (2022-10-01)

Polyprenol formation in the yeast Saccharomyces cerevisiae: effect of farnesyl diphosphate synthase overexpression
द्वारा: A Szkopińska, और अन्य
प्रकाशित: (1997-05-01)

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.

समान संसाधन

समान संसाधन