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1.
Structure/function of human type 1 3beta-hydroxysteroid dehydrogenase: An intrasubunit disulfide bond in the Rossmann-fold domain and a Cys residue in the active site are critical for substrate and coenzyme utilization.
J Steroid Biochem Mol Biol
; 107(1-2): 80-7, 2007 Oct.
Artículo
en Inglés
| MEDLINE | ID: mdl-17624763
2.
Rational proteomics V: structure-based mutagenesis has revealed key residues responsible for substrate recognition and catalysis by the dehydrogenase and isomerase activities in human 3beta-hydroxysteroid dehydrogenase/isomerase type 1.
J Steroid Biochem Mol Biol
; 101(1): 50-60, 2006 Sep.
Artículo
en Inglés
| MEDLINE | ID: mdl-16889958
3.
Identification of key amino acids responsible for the substantially higher affinities of human type 1 3beta-hydroxysteroid dehydrogenase/isomerase (3beta-HSD1) for substrates, coenzymes, and inhibitors relative to human 3beta-HSD2.
J Biol Chem
; 280(22): 21321-8, 2005 Jun 03.
Artículo
en Inglés
| MEDLINE | ID: mdl-15797861
4.
The higher affinity of human type 1 3beta-hydroxysteroid dehydrogenase (3beta-HSD1) for substrate and inhibitor steroids relative to human 3beta-HSD2 is validated in MCF-7 tumor cells and related to subunit interactions.
Endocr Res
; 30(4): 935-41, 2004 Nov.
Artículo
en Inglés
| MEDLINE | ID: mdl-15666848
5.
Agonist-induced endocytosis of lysophosphatidic acid-coupled LPA1/EDG-2 receptors via a dynamin2- and Rab5-dependent pathway.
J Cell Sci
; 116(Pt 10): 1969-80, 2003 May 15.
Artículo
en Inglés
| MEDLINE | ID: mdl-12668728
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