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

Pub. Date : 2000 Jan

PMID : 10628747






5 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 This was unexpected because Ser 294 and flanking sequences are identical on both proteins, suggesting that a distinct conformation of the N-terminal domain of PR-A inhibits phosphorylation of this site. Serine S100 calcium binding protein A6 Homo sapiens
2 That Ser 294 lies within an inhibitory domain that mediates the unique repressive functions of PR-A raises the possibility that differential phosphorylation of Ser 294 is involved in the distinct functional properties of PR-A and PR-B. Serine S100 calcium binding protein A6 Homo sapiens
3 That Ser 294 lies within an inhibitory domain that mediates the unique repressive functions of PR-A raises the possibility that differential phosphorylation of Ser 294 is involved in the distinct functional properties of PR-A and PR-B. Serine S100 calcium binding protein A6 Homo sapiens
4 That Ser 294 lies within an inhibitory domain that mediates the unique repressive functions of PR-A raises the possibility that differential phosphorylation of Ser 294 is involved in the distinct functional properties of PR-A and PR-B. Serine S100 calcium binding protein A6 Homo sapiens
5 That Ser 294 lies within an inhibitory domain that mediates the unique repressive functions of PR-A raises the possibility that differential phosphorylation of Ser 294 is involved in the distinct functional properties of PR-A and PR-B. Serine S100 calcium binding protein A6 Homo sapiens