(Q27675453)

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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

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scholarly article

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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 (English)

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structural biology

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Albert M Berghuis

object named as

Albert M Berghuis

5

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author name string

Jaeok Park

1

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Yih-Shyan Lin

2

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Joris W De Schutter

3

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Youla S Tsantrizos

4

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publication date

12 December 2012

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BMC Structural Biology

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12

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1

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32

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1 reference

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1 reference

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1 reference

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1 reference

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Regulation of product chain length by isoprenyl diphosphate synthases

1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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Nonpeptide antigens, presentation mechanisms, and immunological memory of human Vgamma2Vdelta2 T cells: discriminating friend from foe through the recognition of prenyl pyrophosphate antigens

1 reference

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1 reference

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Isoprenylated proteins

1 reference

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1 reference

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

1 reference

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21 January 2018

Differences between bisphosphonates in binding affinities for hydroxyapatite.

1 reference

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Investigation of the catalytic mechanism of farnesyl pyrophosphate synthase by computer simulation

1 reference

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27 November 2018

Design of potent bisphosphonate inhibitors of the human farnesyl pyrophosphate synthase via targeted interactions with the active site 'capping' phenyls

1 reference

https://pubmed.ncbi.nlm.nih.gov/23234314

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Processing of X-ray diffraction data collected in oscillation mode

1 reference

https://pubmed.ncbi.nlm.nih.gov/23234314

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1186/1472-6807-12-32

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