Unusual Binding Mode of the 2S4R Stereoisomer of the Potent Aldose Reductase Cyclic Imide Inhibitor Fidarestat (2S4S) in the 15 K Crystal Structure of the Ternary Complex Refined at 0.78 Å Resolution: Implications for the Inhibition Mechanism-Reference-Cited by-同舟云学术

Unusual Binding Mode of the 2S4R Stereoisomer of the Potent Aldose Reductase Cyclic Imide Inhibitor Fidarestat (2S4S) in the 15 K Crystal Structure of the Ternary Complex Refined at 0.78 Å Resolution: Implications for the Inhibition Mechanism

Published:2008-02-20 Issue:5 Volume:51 Page:1478-1481
ISSN:0022-2623
Container-title:Journal of Medicinal Chemistry
language:en
Short-container-title:J. Med. Chem.

Author:

Zhao Hai-Tao¹,Hazemann Isabelle¹,Mitschler Andre¹,Carbone Vincenzo¹,Joachimiak Andrzej¹,Ginell Steve¹,Podjarny Alberto¹,El-Kabbani Ossama¹

Affiliation:

1. Department of Medicinal Chemistry, Victorian College of Pharmacy, Monash University (Parkville Campus), 381 Royal Parade, Vic 3052, Australia, Departement de Biologie et Genomique Structurale, IGBMC, CNRS INSERM ULP, 1 rue Laurent Fries, B.P. 163, 67404 Illkirch, France, and Structural Biology Center, Biosciences Division, Argonne National Laboratory, Argonne, Illinois

Publisher

American Chemical Society (ACS)

Subject

Drug Discovery,Molecular Medicine

Link

https://pubs.acs.org/doi/pdf/10.1021/jm701514k

Reference31 articles.

1. Comparative anatomy of the aldo–keto reductase superfamily

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

3. Interactions between essential fatty acid, prostanoid, polyol pathway and nitric oxide mechanisms in the neurovascular deficit of diabetic rats

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