Results overview: Found 5 records in 0.02 seconds.
Articles, 4 records found
Research literature, 1 records found
Articles 4 records found  
1.
26 p, 1.1 MB Structural and kinetic features of aldehyde dehydrogenase 1A (ALDH1A) subfamily members, cancer stem cell markers active in retinoic acid biosynthesis / Pequerul Pavon, Raquel (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Vera Lillo, Javier (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) ; Crespo, Isidro (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Coines, Joan (Universitat de Barcelona) ; Porté, Sergio (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Rovira, Carme (Universitat de Barcelona) ; 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)
Aldehyde dehydrogenases catalyze the NAD(P)+-dependent oxidation of aldehydes to their corresponding carboxylic acids. The three-dimensional structures of the human ALDH1A enzymes were recently obtained, while a complete kinetic characterization of them, under the same experimental conditions, is lacking. [...]
2020 - 10.1016/j.abb.2020.108256
Archives of biochemistry and biophysics, Vol. 681 (2020) , p. 108256  
2.
31 p, 986.9 KB Engineering aldo-keto reductase 1B10 to mimic the distinct 1B15 topology and specificity towards inhibitors and substrates, including retinoids and steroids / Giménez-Dejoz, Joan (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Weber, Susanne (Research Unit Molecular Endocrinology and Metabolism, Helmholtz Zentrum München) ; Fernández-Pardo, Álvaro (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Möller, Gabriele (Research Unit Molecular Endocrinology and Metabolism, Helmholtz Zentrum München) ; Adamski, Jerzy (Research Unit Molecular Endocrinology and Metabolism, Helmholtz Zentrum München) ; Porté, Sergio (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) ; Farrés, Jaume (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
The aldo-keto reductase (AKR)superfamily comprises NAD(P)H-dependent enzymes that catalyze the reduction of a variety of carbonyl compounds. AKRs are classified in families and subfamilies. Humans exhibit three members of the AKR1B subfamily: AKR1B1 (aldose reductase, participates in diabetes complications), AKR1B10 (overexpressed in several cancer types), and the recently described AKR1B15. [...]
2019 - 10.1016/j.cbi.2019.04.030
Chemico-Biological Interactions, Vol. 307 (2019) , p. 186-194  
3.
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  
4.
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  

Research literature 1 records found  
1.
181 p, 5.5 MB Functional and structural studies of AKR1B15 and AKR1B16: Two novel additions to human and mouse aldo-keto reductase superfamily / Giménez Dejoz, Joan ; Porté Orduna, Sergio, dir. ; Farrés, Jaume, dir. (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Parés i Casasampera, Xavier, dir. (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular
La superfamília de les aldo-ceto reductases (AKR) comprèn un gran nombre de proteïnes monomèriques de localització citosòlica d'un un pes molecular d'aproximadament 36 kDa. Les AKRs tenen un plegament proteic comú evolutivament conservat, que consisteix en un barril (α/β)8. [...]
The aldo-keto reductase (AKR) superfamily comprises a large number of monomeric proteins with cytosolic localization and a molecular weight of about 36 kDa. AKRs have a common evolutionarily conserved protein fold which consists of a (α/β)8 barrel. [...]

[Barcelona] : Universitat Autònoma de Barcelona, 2016  

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