ANGEL
RODRIGUEZ DE LERA
CATEDRATICO/A UNIVERSIDADE - TEMPO COMPLETO


Universitat Autònoma de Barcelona
Barcelona, EspañaPublicacións en colaboración con investigadores/as de Universitat Autònoma de Barcelona (17)
2020
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Synthesis of C11-to-C14 methyl-shifted all-: Trans -retinal analogues and their activities on human aldo-keto reductases
Organic and Biomolecular Chemistry, Vol. 18, Núm. 25, pp. 4788-4801
2018
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Synthesis of apocarotenoids by acyclic cross metathesis and characterization as substrates for human retinaldehyde dehydrogenases
Tetrahedron, Vol. 74, Núm. 21, pp. 2567-2574
2017
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Structural basis for the inhibition of AKR1B10 by the C3 brominated TTNPB derivative UVI2008
Chemico-Biological Interactions, Vol. 276, pp. 174-181
2015
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Structural Determinants of the Selectivity of 3-Benzyluracil-1-acetic Acids toward Human Enzymes Aldose Reductase and AKR1B10
ChemMedChem, Vol. 10, Núm. 12, pp. 1989-2003
2014
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Identification of a novel polyfluorinated compound as a lead to inhibit the human enzymes aldose reductase and AKR1B10: Structure determination of both ternary complexes and implications for drug design
Acta Crystallographica Section D: Biological Crystallography, Vol. 70, Núm. 3, pp. 889-903
2013
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Aldo-keto reductases in retinoid metabolism: Search for substrate specificity and inhibitor selectivity
Chemico-Biological Interactions
2012
2009
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Aldo-keto reductases from the AKR1B subfamily: Retinoid specificity and control of cellular retinoic acid levels
Chemico-Biological Interactions, Vol. 178, Núm. 1-3, pp. 171-177
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C-C reductive elimination in palladium complexes, and the role of coupling additives. A DFT study supported by experiment
Journal of the American Chemical Society, Vol. 131, Núm. 10, pp. 3650-3657
2007
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Structural basis for the high all-trans-retinaldehyde reductase activity of the tumor marker AKR1B10
Proceedings of the National Academy of Sciences of the United States of America, Vol. 104, Núm. 52, pp. 20764-20769
2006
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Synthesis of enantiopure C3- and C4-hydroxyretinals and their enzymatic reduction by ADH8 from Xenopus laevis
Organic and Biomolecular Chemistry, Vol. 4, Núm. 1, pp. 155-164
2005
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Synthesis of N-heteroaryl retinals and their artificial bacteriorhodopsins
ChemBioChem, Vol. 6, Núm. 11, pp. 2078-2087
2004
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Kinetics of human alcohol dehydrogenase with ring-oxidized retinoids: Effect of Tween 80
Archives of Biochemistry and Biophysics
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Synthesis of ring-oxidized retinoids as substrates of mouse class I alcohol dehydrogenase (ADH1)
Organic and Biomolecular Chemistry, Vol. 2, Núm. 22, pp. 3368-3373
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The specificity of alcohol dehydrogenase with cis-retinoids Activity with 11-cis-retinol and localization in retina
European Journal of Biochemistry, Vol. 271, Núm. 9, pp. 1660-1670
1995
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Experimental and Theoretical Analysis of the Steric Tolerance of the Binding Site of Bacterioopsin with the Use of Side-Chain Methyl-Shifted Retinal Analogs
Journal of the American Chemical Society, Vol. 117, Núm. 31, pp. 8220-8231
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Fourier transform infrared spectroscopy indicates a major conformational rearrangement in the activation of rhodopsin
Biophysical Journal, Vol. 69, Núm. 3, pp. 1077-1082