Rotamers of tolrestat and their binding mode to aldose reductase

Advances in Experimental Medicine and Biology

Volumn 463, Issue , 1999, Pages 465-472

  Lee, Y S ^a   Sugiyama, K ^a   Kador, P F ^a  

^a NATIONAL EYE INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALDEHYDE REDUCTASE; TOLRESTAT;

COMPLEX FORMATION; CONFERENCE PAPER; DRUG PROTEIN BINDING; HUMAN; HUMAN TISSUE; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; PRIORITY JOURNAL;

EID: 0033282012     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4615-4735-8_58     Document Type: Conference Paper

References (15)

1. CHARMM: A program for macromolecular energy, minimizations, and molecular dynamics calculations
2. Studies on the inhibitor -binding site of porcine aldehyde reductase, crystal structure of the holoenzyme-inhibitor ternary complex
3. The role of aldose reductase in the development of diabetic complications
4. Aldose reductase in the diabetic eye
5. Kinetics and mechanism of thioamide rotational isomerism: N-thianaphthoyl-N-methyl glycine derivative
6. Chromatographic investigation of the slowly interconverting atropisomers of hindered naphthamides
7. Molecular dynamics simulations of the structure of aldose reductase complexed with the inhibitor tolrestat
8. Optimization of parameters for semiempirical methods
9. A specificity pocket inferred from the crystal structures of the complexes of aldose reductase with the pharmaceutically important inhibitors of tolrestat and sorbinil
10. Refined 1.8 Å structure of human aldose reductase complexed with the potent inhibitor zopolrestat
11. 1.7 Å structure of FR-1, a fibroblast growth factor induced member of the aldo-keto reductase family complexed with coenzyme and inhibitor