(Q27739575)

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A 'specificity' pocket inferred from the crystal structures of the complexes of aldose reductase with the pharmaceutically important inhibitors tolrestat and sorbinil

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A 'specificity' pocket inferred from the crystal structures of the complexes of aldose reductase with the pharmaceutically important inhibitors tolrestat and sorbinil (English)

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crystal structure

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1 reference

ChEBI release 2020-05-28

author name string

A Urzhumtsev

1

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F Tête-Favier

2

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A Mitschler

3

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J Barbanton

4

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P Barth

5

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L Urzhumtseva

6

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J F Biellmann

7

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A Podjarny

8

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D Moras

9

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publication date

15 May 1997

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5

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5

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601-12

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Medicinal chemistry of aldose reductase inhibitors

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Purification and characterization of human-brain aldose reductase.

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Molecular cloning of testicular 20 alpha-hydroxysteroid dehydrogenase: identity with aldose reductase.

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Properties of an aldose reductase from pig lens. Comparative studies of an aldehyde reductase from pig lens

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Human brain aldehyde reductases: relationship to succinic semialdehyde reductase and aldose reductase

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Novel NADPH-binding domain revealed by the crystal structure of aldose reductase

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An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications

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Diabetic Cataracts and Flavonoids

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Synthesis, absolute configuration, and conformation of the aldose reductase inhibitor sorbinil

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Polyol accumulation in galactosemic and diabetic rats: control by an aldose reductase inhibitor

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N-[5-(trifluoromethyl)-6-methoxy-1-naphthalenyl]thioxomethyl]- N-methylglycine (Tolrestat), a potent, orally active aldose reductase inhibitor

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Properties of ICI 128,436, a novel aldose reductase inhibitor, and its effects on diabetic complications in the rat

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Current progress in clinical trials of aldose reductase inhibitors in Japan

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(2,6-Dimethylphenylsulphonyl)nitromethane: a new structural type of aldose reductase inhibitor which follows biphasic kinetics and uses an allosteric binding site

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Kinetic characteristics of ZENECA ZD5522, a potent inhibitor of human and bovine lens aldose reductase

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Refined 1.8 A structure of human aldose reductase complexed with the potent inhibitor zopolrestat

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An anion binding site in human aldose reductase: mechanistic implications for the binding of citrate, cacodylate, and glucose 6-phosphate

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Kinetic and spectroscopic evidence for active site inhibition of human aldose reductase

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Mechanistic basis for nonlinear kinetics of aldehyde reduction catalyzed by aldose reductase

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Aldose reductase as a target for drug design: molecular modeling calculations on the binding of acyclic sugar substrates to the enzyme

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A fast flexible docking method using an incremental construction algorithm.

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Mechanism of aldose reductase inhibition: binding of NADP+/NADPH and alrestatin-like inhibitors

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Mechanism of human aldehyde reductase: characterization of the active site pocket

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10.1016/S0969-2126(97)00216-5

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