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

Molecular Endocrinology

Volumn 14, Issue 1, 2000, Pages 52-65

  Clemm, David L ^a   Sherman, Lori ^c   Boonyaratanakornkit, Viroj ^c   Schrader, William T ^a   Weigel, Nancy L ^b   Edwards, Dean P ^c,d  

^a LIGAND PHARMACEUTICALS INC   (United States)

^b BAYLOR COLLEGE OF MEDICINE   (United States)

^c UNIVERSITY OF COLORADO SCHOOL OF MEDICINE   (United States)

^d UNIVERSITY OF COLORADO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

MONOCLONAL ANTIBODY; PHOSPHOSERINE; PROGESTERONE RECEPTOR;

ANIMAL CELL; ANIMAL EXPERIMENT; ARTICLE; BINDING SITE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DOWN REGULATION; ENZYME KINETICS; HUMAN; HUMAN CELL; MALE; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION;

ANIMALIA;

EID: 0034463134     PISSN: 08888809     EISSN: None     Source Type: Journal    
DOI: 10.1210/mend.14.1.0413     Document Type: Article

References (44)

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27. Antagonist-occupied human progesterone B-receptors activate transcription without binding to progesterone response elements and are dominantly inhibited by A-receptors
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41. Synthesis of O-phosphoserine and Ophosphothreonine containing peptides
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43. High-mobility group chromatin proteins 1 and 2 functionally interact with steroid hormone receptors to enhance their DNA binding in vitro and transcriptional activity in mammalian cells