Cargando…
Phosphorylation of conserved serine residues does not regulate the ability of mosxe protein kinase to induce oocyte maturation or function as cytostatic factor
Expression of the mosxe protein kinase is required for the normal meiotic maturation of Xenopus oocytes and overexpression induces maturation in the absence of other stimuli. In addition, mosxe functions as a component of cytostatic factor (CSF), an activity responsible for arrest of the mature egg...
Formato: | Texto |
---|---|
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1992
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2289311/ https://www.ncbi.nlm.nih.gov/pubmed/1530949 |
Ejemplares similares
-
Cross-phosphorylation of bacterial serine/threonine and tyrosine protein kinases on key regulatory residues
por: Shi, Lei, et al.
Publicado: (2014) -
At least two kinases phosphorylate the MPM-2 epitope during Xenopus oocyte maturation
Publicado: (1993) -
Regulation of Greatwall kinase during Xenopus oocyte maturation
por: Yamamoto, Tomomi M., et al.
Publicado: (2011) -
p90Rsk is not involved in cytostatic factor arrest in mouse oocytes
por: Dumont, Julien, et al.
Publicado: (2005) -
Protein Kinase D Interacts with Neuronal Nitric Oxide Synthase and Phosphorylates the Activatory Residue Serine(1412)
por: Sánchez-Ruiloba, Lucía, et al.
Publicado: (2014)