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Xavier Parés
Researcher at Autonomous University of Barcelona
Publications - 112
Citations - 5035
Xavier Parés is an academic researcher from Autonomous University of Barcelona. The author has contributed to research in topics: Alcohol dehydrogenase & Enzyme. The author has an hindex of 38, co-authored 109 publications receiving 4833 citations. Previous affiliations of Xavier Parés include Karolinska Institutet.
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Journal ArticleDOI
Recommended nomenclature for the vertebrate alcohol dehydrogenase gene family.
Gregg Duester,Jaume Farrés,Michael R. Felder,Roger S. Holmes,Jan-Olov Höög,Xavier Parés,Bryce V. Plapp,Shih-Jiun Yin,Hans Jörnvall +8 more
TL;DR: A nomenclature that uses the widely accepted vertebrate ADH class system as its basis and will accommodate newly discovered members of the vertebrates ADH family, and will facilitate functional and evolutionary studies.
Journal ArticleDOI
Genetic polymorphism of alcohol dehydrogenase in europeans: the ADH2*2 allele decreases the risk for alcoholism and is associated with ADH3*1.
Emma Borràs,Christiane Coutelle,Albert Rosell,Fina Fernández-Muixi,Montserrat Broch,Bernat Crosas,Lars Hjelmqvist,Alfons Lorenzo,Cristina Gutierrez,Mauro Santos,Małgorzata Szczepanek,Markus Heilig,Pierrette Quattrocchi,Jaume Farrés,Francesc Vidal,Cristóbal Richart,Tomasz Mach,Bogdał J,Hans Jörnvall,Helmut K. Seitz,Patrice Couzigou,Xavier Parés +21 more
TL;DR: The ADH 2*2 allele decreases the risk for alcoholism, whereas the ADH2*2 and ADH3*1 alleles are found to be associated in the European population.
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Physiological Substrates for Rat Alcohol Dehydrogenase Classes: Aldehydes of Lipid Peroxidation, ω-Hydroxyfatty Acids, and Retinoids
TL;DR: Alcohol dehydrogenase is an enzyme with multiple metabolic roles, and the different substrate specificity and tissue localization for each class provide organs and tissues with distinct physiological functions.
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Characterization of the Saccharomyces cerevisiae YMR318C (ADH6) gene product as a broad specificity NADPH-dependent alcohol dehydrogenase: relevance in aldehyde reduction.
TL;DR: The YMR318C gene product has been purified to homogeneity from overexpressing yeast cells, and found to be a homodimeric ADH, composed of 40 kDa subunits and with a pI of 5.0-5.4, to be the first NADPH-dependent medium-chain ADH to be characterized in S. cerevisiae.
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Characterization of three isoenzymes of rat alcohol dehydrogenase. Tissue distribution and physical and enzymatic properties
TL;DR: The specific localization and kinetic properties of rat ADH isoenzymes suggest that ADH-1 andADH-3 may act as metabolic barriers to external alcohols and aldehydes whereas ADh-2 may have a function in the metabolism of the endogenous long-chain alcohols