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Jan-Olov Höög

Researcher at Karolinska Institutet

Publications -  94
Citations -  3586

Jan-Olov Höög is an academic researcher from Karolinska Institutet. The author has contributed to research in topics: Alcohol dehydrogenase & Complementary DNA. The author has an hindex of 37, co-authored 94 publications receiving 3513 citations. Previous affiliations of Jan-Olov Höög include Swedish University of Agricultural Sciences.

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Recommended nomenclature for the vertebrate alcohol dehydrogenase gene family.

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.
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SDR and MDR: completed genome sequences show these protein families to be large, of old origin, and of complex nature.

TL;DR: Repeated duplications can be traced for the alcohol dehydrogenases, with independent enzymogenesis of ethanol activity, showing a general importance of this enzyme activity.
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Alcohol dehydrogenase in human tissues: localisation of transcripts coding for five classes of the enzyme

TL;DR: Significantly higher levels of class V transcripts were present in fetal liver when compared with levels in adult liver, which suggests that human class V is a predominantly fetal alcohol dehydrogenase.
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Nomenclature of alcohol dehydrogenases

TL;DR: Six different classes of mammalian alcohol dehydrogenase have been characterized, most of which are common to humans, mammals and many vertebrates, which therefore share class distinctions in general.
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Comparison of three classes of human liver alcohol dehydrogenase. Emphasis on different substrate binding pockets.

TL;DR: Conformational models of the three characterized classes of mammalian liver alcohol dehydrogenase were constructed using computer graphics based on the known three-dimensional structure of the E subunit of the horse enzyme and the primary structures of the four human enzyme classes to correlate the substrate-binding pockets with those of the class II and III subunits for three enzymes that differ in substrate specificity, inhibition pattern and many other properties.