Progesterone and cAMP-dependent protein kinase regulate in vivo the level of phosphorylation of two proteins (Mr 20,000 and Mr 32,000) in Xenopus oocytes-Reference-Cited by-同舟云学术

Progesterone and cAMP-dependent protein kinase regulate in vivo the level of phosphorylation of two proteins (Mr 20,000 and Mr 32,000) in Xenopus oocytes

Published:1986-02 Issue:2 Volume:113 Page:420-428
ISSN:0012-1606
Container-title:Developmental Biology
language:en
Short-container-title:Developmental Biology

Author:

Boyer Jeanne,Asselin Joelle,Bellé Robert,Ozon René

Publisher

Elsevier BV

Subject

Cell Biology,Developmental Biology,Molecular Biology

Reference33 articles.

1. Endogenous phosphorylated proteins during maturation of Xenopus laevis oocytes;Bellé;Gamete Res,1979

2. ATP-γ-S (Adenosine 5′-0(3-thiotriphosphate)) blocks progesterone-induced maturation of the Xenopus oocyte;Bellé;J. Exp. Zool,1984

3. A film detection method for tritium labelled proteins and nucleic acids in polyacrylamide gels;Bonner;Eur. J. Biochem,1974

4. Early increase of a 105,000-dalton phosphoprotein during meiotic maturation of Xenopus laevis oocyte;Boyer;Biochimie,1983

5. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding;Bradford;Anal. Biochem,1976

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