Artikel
Open Access
Human aldo-keto reductases: structure, substrate specificity and roles in tumorigenesis
-
Jun Ma
Veröffentlicht/Copyright:
17. März 2011
Published Online: 2011-03-17
Published in Print: 2011-04-01
©2011 by Walter de Gruyter Berlin New York
Artikel in diesem Heft
- Reviews
- Functional specificity of Akt isoforms in cancer progression
- Embryonic stem cells: protein interaction networks
- Antimicrobial peptides from amphibians
- MAPKs in development: insights from Dictyostelium signaling pathways
- The role of symmetry in the regulation of bacterial carboxyltransferase
- Solution NMR studies of periplasmic binding proteins and their interaction partners
- Calcineurin inhibitors: status quo and perspectives
- Interactions of natural polyamines with mammalian proteins
- Cystatins: a versatile family
- Aldose reductase: new insights for an old enzyme
- Human aldo-keto reductases: structure, substrate specificity and roles in tumorigenesis
Schlagwörter für diesen Artikel
aldo-keto reductases;
AKR1B1;
AKR1B10;
AKR1C;
anticancer agents;
carbonyls;
polycyclic aromatic hydrocarbons;
prostaglandins;
retinaldehyde;
tumorigenesis
Creative Commons
BY-NC-ND 3.0
Artikel in diesem Heft
- Reviews
- Functional specificity of Akt isoforms in cancer progression
- Embryonic stem cells: protein interaction networks
- Antimicrobial peptides from amphibians
- MAPKs in development: insights from Dictyostelium signaling pathways
- The role of symmetry in the regulation of bacterial carboxyltransferase
- Solution NMR studies of periplasmic binding proteins and their interaction partners
- Calcineurin inhibitors: status quo and perspectives
- Interactions of natural polyamines with mammalian proteins
- Cystatins: a versatile family
- Aldose reductase: new insights for an old enzyme
- Human aldo-keto reductases: structure, substrate specificity and roles in tumorigenesis
