Differential hormone-dependent phosphorylation of progesterone receptor A and B forms revealed by a phosphoserine site-specific monoclonal antibody

Human progesterone receptor (PR) is phosphorylated on multiple serine residues (at least seven sites) in a manner that involves distinct groups of sites coordinately regulated by hormone and different kinases. Progress on defining a functional role for PR phosphorylation has been hampered both by th...

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Veröffentlicht in:	Molecular endocrinology (Baltimore, Md.) Md.), 2000-01, Vol.14 (1), p.52-65
Hauptverfasser:	Clemm, D L, Sherman, L, Boonyaratanakornkit, V, Schrader, W T, Weigel, N L, Edwards, D P
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Antibodies, Monoclonal - biosynthesis Antibodies, Monoclonal - immunology Antibodies, Monoclonal - metabolism COS Cells Humans Kinetics Mice Mice, Inbred BALB C Molecular Sequence Data Phosphorylation Phosphoserine - metabolism Precipitin Tests Progesterone - antagonists & inhibitors Progesterone Congeners - pharmacology Promegestone - pharmacology Protein Binding Protein Conformation Receptors, Progesterone - chemistry Receptors, Progesterone - immunology Receptors, Progesterone - metabolism Serine - metabolism Tumor Cells, Cultured
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