1.
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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
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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
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2.
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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
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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
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3.
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34 p, 1.3 MB |
Inhibitors of aldehyde dehydrogenases of the 1A subfamily as putative anticancer agents : Kinetic characterization and effect on human cancer cells
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Jiménez, Rafael (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Pequerul, Raquel (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Amor Minguez, Adrián (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Lorenzo Rivera, Julia (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Metwally, Kamel (Zagazig University. Department of Medicinal Chemistry) ;
Avilés, Francesc X (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
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 (ALDHs) are enzymes catalyzing the NAD(P)+-dependent oxidation of aldehydes to their corresponding carboxylic acids. High ALDH activity has been related to some important features of cancer stem cells. [...]
2019 - 10.1016/j.cbi.2019.04.004
Chemico-Biological Interactions, Vol. 306 (2019) , p. 123-130
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4.
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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
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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
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5.
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12 p, 3.2 MB |
Structural and biochemical evidence that ATP inhibits the cancer biomarker human aldehyde dehydrogenase 1A3
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Castellví Toledo, Albert (ALBA Laboratori de Llum de Sincrotró) ;
Pequerul, Raquel (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Barracco, Vito (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Juanhuix, Judith (ALBA Laboratori de Llum de Sincrotró) ;
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)
Human aldehyde dehydrogenase (ALDH) participates in the oxidative stress response and retinoid metabolism, being involved in several diseases, including cancer, diabetes and obesity. The ALDH1A3 isoform has recently elicited wide interest because of its potential use as a cancer stem cell biomarker and drug target. [...]
2022 - 10.1038/s42003-022-03311-1
Communications Biology, Vol. 5 (April 2022) , art. 354
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6.
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16 p, 4.0 MB |
Expansion of the 4-(Diethylamino)benzaldehyde Scaffold to Explore the Impact on Aldehyde Dehydrogenase Activity and Antiproliferative Activity in Prostate Cancer
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Ibrahim, Ali I. M. (Al-Zaytoonah University of Jordan) ;
Batlle, Elisabet (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Sneha, Smarakan (University of Bradford) ;
Jiménez, Rafael (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Pequerul, Raquel (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) ;
Rüngeler, Till (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Jha, Vibhu (University of Pisa. Department of Pharmacy) ;
Tuccinardi, Tiziano (University of Pisa. Department of Pharmacy) ;
Sadiq, Maria (University of York. Department of Biology) ;
Frame, Fiona (University of York. Department of Biology) ;
Maitland, Norman J. (University of York. Department of Biology) ;
Farrés, Jaume (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Pors, Klaus (University of Bradford)
Aldehyde dehydrogenases (ALDHs) are overexpressed in various tumor types including prostate cancer and considered a potential target for therapeutic intervention. 4-(Diethylamino)benzaldehyde (DEAB) has been extensively reported as a pan-inhibitor of ALDH isoforms, and here, we report on the synthesis, ALDH isoform selectivity, and cellular potencies in prostate cancer cells of 40 DEAB analogues; three analogues (14, 15, and 16) showed potent inhibitory activity against ALDH1A3, and two analogues (18 and 19) showed potent inhibitory activity against ALDH3A1. [...]
2022 - 10.1021/acs.jmedchem.1c01367
Journal of Medicinal Chemistry, Vol. 65, Issue 5 (February 2022) , p. 3833-3848
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7.
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8.
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23 p, 5.4 MB |
Design, synthesis, biological evaluation and in silico study of benzyloxybenzaldehyde derivatives as selective aldh1a3 inhibitors
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Ibrahim, Ali I. M. (Al-Zaytoonah University of Jordan. Faculty of Pharmacy) ;
Ikhmais, Balqis (Al-Zaytoonah University of Jordan. Faculty of Pharmacy) ;
Batlle, Elisabet (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Abuharb, Waed K. (Al-Zaytoonah University of Jordan. Faculty of Pharmacy) ;
Jha, Vibhu (University of Pisa. Department of Pharmacy) ;
Jaradat, Khaled T. (American University of the Middle East. College of Engineering and Technology) ;
Jiménez, Rafael (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Pequerul, Raquel (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) ;
Pors, Klaus (University of Bradford. Faculty of Life Sciences)
Aldehyde dehydrogenase 1A3 (ALDH1A3) has recently gained attention from researchers in the cancer field. Several studies have reported ALDH1A3 overexpression in different cancer types, which has been found to correlate with poor treatment recovery. [...]
2021 - 10.3390/molecules26195770
Molecules, Vol. 26 Núm. 19 (september 2021) , p. 5770
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9.
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13 p, 2.9 MB |
Efficacy of aldose reductase inhibitors is affected by oxidative stress induced under X-ray irradiation
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Castellví Toledo, Albert (ALBA Laboratori de Llum de Sincrotró) ;
Crespo, Isidro (ALBA Laboratori de Llum de Sincrotró) ;
Crosas, Eva (ALBA Laboratori de Llum de Sincrotró) ;
Cámara-Artigas, Ana (Universidad de Almería) ;
Gavira, José A. (Universidad de Granada) ;
Aranda, Miguel A. G. (ALBA Laboratori de Llum de Sincrotró) ;
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) ;
Juanhuix, Judith (ALBA Laboratori de Llum de Sincrotró)
Human aldose reductase (hAR, AKR1B1) has been explored as drug target since the 1980s for its implication in diabetic complications. An activated form of hAR was found in cells from diabetic patients, showing a reduced sensitivity to inhibitors in clinical trials, which may prevent its pharmacological use. [...]
2019 - 10.1038/s41598-019-39722-0
Scientific reports, Vol. 9 (February 2019) , art. 3177
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10.
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18 p, 1.2 MB |
The Xenopus alcohol dehydrogenase gene family : characterization and comparative analysis incorporating amphibian and reptilian genomes
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Borràs, Emma (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Albalat, Ricard (Universitat de Barcelona. Departament de Genètica) ;
Duester, Gregg (Sanford-Burnham Medical Research Institute. Development, Aging and Regeneration Program (USA)) ;
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 alcohol dehydrogenase (ADH) gene family uniquely illustrates the concept of enzymogenesis. In vertebrates, tandem duplications gave rise to a multiplicity of forms that have been classified in eight enzyme classes, according to primary structure and function. [...]
2014 - 10.1186/1471-2164-15-216
BMC genomics, Vol. 15 (March 2014) , art. 216
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