Alkylation of Estradiol 17beta-Dehydrogenase from Human Placenta with 3-Chloroacetylpyridine - Adenine Dinucleotide
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1976.tb10250.x/fullpdf
Reference13 articles.
1. Affinity labelling of the active site of the 17β-oestradiol dehydrogenase of human placental cytosol
2. (I) affinity labelling of an histidine of the active site of the human placental 17β-oestradiol dehydrogenase
3. NAD(P)+ Analogues: Tools for the Investigation of the Active Site of Oestradiol 17beta-Dehydrogenase from Human Placenta
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1. Design and validation of specific inhibitors of 17 -hydroxysteroid dehydrogenases for therapeutic application in breast and prostate cancer, and in endometriosis;Endocrine Related Cancer;2008-05-22
2. Estradiol−Adenosine Hybrid Compounds Designed to Inhibit Type 1 17β-Hydroxysteroid Dehydrogenase;Journal of Medicinal Chemistry;2005-11-18
3. Affinity Labeling of Arginyl Residues at the Catalytic Region of Estradiol 17β-Dehydrogenase from Human Placenta by 16-Oxoestrone;European Journal of Biochemistry;2005-03-03
4. Affinity Labeling of Glyceraldehyde-3-phosphate Dehydrogenase from Sturgeon and Bacillus stearothermophilus by 3-Chloroacetylpyridine-adenine Dinucleotide;European Journal of Biochemistry;2005-03-03
5. Inhibitors of 17β-Hydroxysteroid Dehydrogenases;Current Medicinal Chemistry;2003-03-01
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