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Articles, 2 records found
Articles 2 records found  
1.
15 p, 2.0 MB Identification of a novel polyfluorinated compound as a lead to inhibit human enzymes aldose reductase and AKR1B10 : structure determination of both ternary complexes and implications for drug design / Cousido-Siah, Alexandra (Institut de Génétique et de Biologie Moléculaire et Cellulaire (Illkirch, França)) ; Ruiz, Francesc X. (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Mitschler, André (Institut de Génétique et de Biologie Moléculaire et Cellulaire (Illkirch, França)) ; Porte Orduna, Sergio (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; de Lera Ángel R. (Universidade de Vigo. Departamento de Química Orgánica) ; Martín, María J. (Parque Tecnológico de León. Biomar Microbial Technologies S.A.) ; Manzanaro, Sonia (Parque Tecnológico de León. Biomar Microbial Technologies S.A.) ; de la Fuente, Jesús A. (Parque Tecnológico de León. Biomar Microbial Technologies S.A.) ; Terwesten, Felix (Universität Marburg. Department of Pharmaceutical Chemistry) ; Betz, Michael (Universität Marburg. Department of Pharmaceutical Chemistry) ; Klebe, Gerhard (Universität Marburg. Department of Pharmaceutical Chemistry) ; Farrés i Vicén, Jaume (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Parés i Casasampera, Xavier (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Podjarny, Alberto (Institut de Génétique et de Biologie Moléculaire et Cellulaire (Illkirch, França))
Aldo-keto reductases (AKRs) are mostly monomeric enzymes which fold into a highly conserved ([alpha]/[beta])8 barrel, while their substrate specificity and inhibitor selectivity are determined by interaction with residues located in three highly variable external loops. [...]
2014 - 10.1107/S1399004713033452
Acta crystallographica. Section D, Biological crystallography, Vol. 70 (December 2014) , p. 889-903  
2.
19 p, 2.5 MB Substrate Specificity, Inhibitor Selectivity and Structure-Function Relationships of Aldo-Keto Reductase 1B15 : a Novel Human Retinaldehyde Reductase / Giménez Dejoz, Joan (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Kolář, Michal H. (Academy of Sciences of the Czech Republic. Institute of Organic Chemistry and Biochemistry) ; Ruiz, Francesc X. (Centre de Biologie Intégrative (Illkirch-Graffenstaden, França)) ; Crespo García, Isidro (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Cousido-Siah, Alexandra (Centre de Biologie Intégrative (Illkirch-Graffenstaden, França)) ; Podjarny, Alberto (Centre de Biologie Intégrative (Illkirch-Graffenstaden, França)) ; Barski, Oleg A. (University of Louisville. School of Medicine) ; Fanfrlík, Jindřich (Academy of Sciences of the Czech Republic. Institute of Organic Chemistry and Biochemistry) ; Parés i Casasampera, Xavier (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Farrés i Vicén, Jaume (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Porté Orduna, Sergio (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Human aldo-keto reductase 1B15 (AKR1B15) is a newly discovered enzyme which shares 92% amino acid sequence identity with AKR1B10. While AKR1B10 is a well characterized enzyme with high retinaldehyde reductase activity, involved in the development of several cancer types, the enzymatic activity and physiological role of AKR1B15 are still poorly known. [...]
2015 - 10.1371/journal.pone.0134506
PloS one, Vol. 10 Núm. 7 (July 2015) , p. e0134506  

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