Structure of a glutathione conjugate bound to the active site of aldose reductase

Medicine & Life Sciences

• Aldehyde Reductase 92%
• Aldehydes 33%
• Anions 7%
• Binding Sites 5%
• Catalytic Domain 62%
• Diabetes Complications 6%
• Glucose 4%
• Glutathione 62%
• Glutathione Reductase 8%
• Glycine 6%
• Holoenzymes 9%
• Hydrogen Bonding 8%
• Ketones 8%
• Lipoproteins 6%
• Membranes 4%
• Molecular Dynamics Simulation 7%
• Molecular Models 8%
• NADP 7%
• Oxidoreductases 6%
• Phospholipids 6%
• propionaldehyde 12%
• S-(1,2-dicarboxyethyl)glutathione 15%
• Signal Transduction 5%
• Wounds and Injuries 3%
• X-Rays 5%

Chemical Compounds

• Aldehyde 19%
• Aldose 89%
• Anion 4%
• Binding Site 4%
• Flexibility 5%
• Glucose 5%
• Glutathione 49%
• Glutathione Conjugate 100%
• Glycine 6%
• Hydrogen Bond 4%
• Hyperglycemic 10%
• Lipoprotein 7%
• Molecular Dynamics 5%
• Phospholipid 5%
• Reduction 9%
• X-Ray 4%