Phosphorylation of serine 208 in the human vitamin D receptor. The predominant amino acid phosphorylated by casein kinase II, in vitro, and identification as a significant phosphorylation site in intact cells.-Reference-Cited by-同舟云学术

Phosphorylation of serine 208 in the human vitamin D receptor. The predominant amino acid phosphorylated by casein kinase II, in vitro, and identification as a significant phosphorylation site in intact cells.

Published:1993-03 Issue:9 Volume:268 Page:6791-6799
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Jurutka P.W.,Hsieh J.C.,MacDonald P.N.,Terpening C.M.,Haussler C.A.,Haussler M.R.,Whitfield G.K.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference55 articles.

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2. Gene regulation by steroid hormones

3. Regulation of Progesterone Receptor-Mediated Transcription by Phosphorylation

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