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Ida S. Owens

Researcher at National Institutes of Health

Publications -  74
Citations -  6331

Ida S. Owens is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Isozyme & Glucuronidation. The author has an hindex of 36, co-authored 74 publications receiving 6188 citations.

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Nomenclature update for the mammalian UDP glycosyltransferase (UGT) gene superfamily.

TL;DR: The UGT nomenclature is updated to include new genes identified in the human, mouse and rat genomes and in other mammalian species to prevent confusion when the same gene is given different names.
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A novel complex locus UGT1 encodes human bilirubin, phenol, and other UDP-glucuronosyltransferase isozymes with identical carboxyl termini.

TL;DR: It is reported that the two corresponding bilirubin transferases and the phenol transferase are encoded by a novel locus, UGT1, which is also predicted to encode three other bilirUBin transferase-like isozymes all having identical carboxyl termini.
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The phenobarbital response enhancer module in the human bilirubin UDP-glucuronosyltransferase UGT1A1 gene and regulation by the nuclear receptor CAR.

TL;DR: The UDP‐glucuronosyltransferase, UGT1A1, is the critical enzyme responsible for detoxification of the potentially neurotoxic bilirubin by conjugating it with glucuronic acid and was effectively activated in mouse primary hepatocytes in response to phenobarbital.
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Thirteen UDPglucuronosyltransferase genes are encoded at the human UGT1 gene complex locus.

TL;DR: This locus is indeed novel, indicating the least usage of exon sequences in specifying different transferase isozymes that have an expansive substrate range.