Home > Search Results: Cousido-Siah, Alexandra
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Articles, 3 records found
Articles 3 records found  
1.
52 p, 1.9 MB Design, synthesis, structure-activity relationships and X-ray structural studies of novel 1-oxopyrimido[4,5-c]quinoline-2-acetic acid derivatives as selective and potent inhibitors of human aldose reductase / Crespo, Isidro (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Giménez-Dejoz, Joan (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Porté, Sergio (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Cousido-Siah, Alexandra (Institut de Génétique et de Biologie Moléculaire et Cellulaire, France) ; Mitschler, André (Institut de Génétique et de Biologie Moléculaire et Cellulaire, France) ; Podjarny, Alberto (Institut de Génétique et de Biologie Moléculaire et Cellulaire, France) ; Pratsinis, Harris (Institute of Biosciences and Applications, National Centre of Scientific Research "Demokritos", Athens, Greece) ; Kletsas, Dimitris (Institute of Biosciences and Applications, National Centre of Scientific Research "Demokritos", Athens, Greece) ; Parés i Casasampera, Xavier (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Ruiz, Francesc Xavier (Institut de Génétique et de Biologie Moléculaire et Cellulaire, France) ; Metwally, Kamel (Zagazig University, Egypt) ; Farrés, Jaume (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Human aldose reductase (AKR1B1, AR) is a key enzyme of the polyol pathway, catalyzing the reduction of glucose to sorbitol at high glucose concentrations, as those found in diabetic condition. Indeed, AKR1B1 overexpression is related to diabetes secondary complications and, in some cases, with cancer. [...]
2018 - 10.1016/j.ejmech.2018.04.015
European Journal of Medicinal Chemistry, Vol. 152 (2018) , p. 160-174  
Detailed record -
2.
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 Quimica 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, Jaume (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Parés i Casasampera, Xavier (Universitat Autònoma de Barcelona. Departament de Bioquímica i de 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  
Detailed record -
3.
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, 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 de Biologia Molecular) ; Farrés, Jaume (Universitat Autònoma de Barcelona. Departament de Bioquímica i de 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  
Detailed record - Creative Commons

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