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Structure-activity relationships of human AKR-type oxidoreductases involved in bile acid synthesis: AKR1D1 and AKR1C4.

  • Read more about Structure-activity relationships of human AKR-type oxidoreductases involved in bile acid synthesis: AKR1D1 and AKR1C4.

The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative.

  • Read more about The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative.

Structural insights into the inhibited states of the Mer receptor tyrosine kinase.

  • Read more about Structural insights into the inhibited states of the Mer receptor tyrosine kinase.

Extremely tight binding of a ruthenium complex to glycogen synthase kinase 3.

  • Read more about Extremely tight binding of a ruthenium complex to glycogen synthase kinase 3.

The human short-chain dehydrogenase/reductase (SDR) superfamily: a bioinformatics summary.

  • Read more about The human short-chain dehydrogenase/reductase (SDR) superfamily: a bioinformatics summary.

Analysis of the substrate-binding site of human carbonyl reductases CBR1 and CBR3 by site-directed mutagenesis.

  • Read more about Analysis of the substrate-binding site of human carbonyl reductases CBR1 and CBR3 by site-directed mutagenesis.

An intact SAM-dependent methyltransferase fold is encoded by the human endothelin-converting enzyme-2 gene.

  • Read more about An intact SAM-dependent methyltransferase fold is encoded by the human endothelin-converting enzyme-2 gene.

Discovery of a potent and selective inhibitor for human carbonyl reductase 1 from propionate scanning applied to the macrolide zearalenone.

  • Read more about Discovery of a potent and selective inhibitor for human carbonyl reductase 1 from propionate scanning applied to the macrolide zearalenone.

Targeting a uniquely nonspecific prenyl synthase with bisphosphonates to combat cryptosporidiosis.

  • Read more about Targeting a uniquely nonspecific prenyl synthase with bisphosphonates to combat cryptosporidiosis.

Structure of the pseudokinase VRK3 reveals a degraded catalytic site, a highly conserved kinase fold, and a putative regulatory binding site.

  • Read more about Structure of the pseudokinase VRK3 reveals a degraded catalytic site, a highly conserved kinase fold, and a putative regulatory binding site.

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