Replacement of water molecules in a phosphate binding site by furanoside-appended lin-benzoguanine ligands of tRNA-guanine transglycosylase (TGT) (Q27696473)

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English	Replacement of water molecules in a phosphate binding site by furanoside-appended lin-benzoguanine ligands of tRNA-guanine transglycosylase (TGT)	scientific article

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Replacement of water molecules in a phosphate binding site by furanoside-appended lin-benzoguanine ligands of tRNA-guanine transglycosylase (TGT) (English)

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11

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François Diederich

12

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Bernd Schweizer

7

object named as

W Bernd Schweizer

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author name string

Luzi J Barandun

1

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Frederik R Ehrmann

2

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Daniel Zimmerli

3

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Florian Immekus

4

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Maude Giroud

5

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Claudio Grünenfelder

6

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Bruno Bernet

8

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Michael Betz

9

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Andreas Heine

10

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language of work or name

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publication date

2 January 2015

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Chemistry—A European Journal

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21

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1

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126-35

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A medicinal chemist's guide to molecular interactions

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Substrate specificity and affinity of a protein modulated by bound water molecules

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Classification of water molecules in protein binding sites.

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Water as an active constituent in cell biology

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Energetics of displacing water molecules from protein binding sites: consequences for ligand optimization

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Water networks contribute to enthalpy/entropy compensation in protein-ligand binding

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Crystal structure analysis and in silico pKa calculations suggest strong pKa shifts of ligands as driving force for high-affinity binding to TGT

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High-affinity inhibitors of tRNA-guanine transglycosylase replacing the function of a structural water cluster

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10.1002/CHEM.201405764

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