Mass-spectrometric identification of proteins detected in forskolin-stimulated Xenopus laevis oocytes using antibody against phospho-(Ser/Thr) cAMPdependent protein kinase substrate-Reference-Cited by-同舟云学术

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Mass-spectrometric identification of proteins detected in forskolin-stimulated Xenopus laevis oocytes using antibody against phospho-(Ser/Thr) cAMPdependent protein kinase substrate

Published:2007 Issue:5 Volume:28 Page:231-238
ISSN:1880-313X
Container-title:Biomedical Research
language:en
Short-container-title:Biomed. Res.

Author:

SUGIMOTO Isamu,LI Zhijun,SAKAMOTO Yoko,ITO Susumu,HASHIMOTO Eikichi

Publisher

Biomedical Research Press

Subject

General Biochemistry, Genetics and Molecular Biology,General Medicine

Reference31 articles.

1. Progesterone-inhibited phosphorylation of an unique Mr 48,000 protein in the plasma membrane of Xenopus laevis oocytes.

2. Changes in ribosome function by cAMP-dependent and cAMP-independent phosphorylation of ribosomal protein S6.

3. Phosphorylation of 40-S Ribosomal Subunits by cAMP-Dependent, cGMP-Dependent and Protease-Activated Protein Kinases

4. G2 arrest in Xenopus oocytes depends on phosphorylation of cdc25 by protein kinase A

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1. Effect of H89 on the meiotic resumption of pig oocytes;Reproductive Medicine and Biology;2011-01-20

2. Glucocorticoid- and Protein Kinase A–Dependent Transcriptome Regulation in Airway Smooth Muscle;American Journal of Respiratory Cell and Molecular Biology;2009-07

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