Cargando…
Inhibition of cell adhesion by phosphorylated Ezrin/Radixin/Moesin
Altered phosphorylation status of the C-terminal Thr residues of Ezrin/Radixin/Moesin (ERM) is often linked to cell shape change. To determine the role of phophorylated ERM, we modified phosphorylation status of ERM and investigated changes in cell adhesion and morphology. Treatment with Calyculin-A...
Autores principales: | Tachibana, Kouichi, Haghparast, Seyed Mohammad Ali, Miyake, Jun |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Taylor & Francis
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4955964/ https://www.ncbi.nlm.nih.gov/pubmed/26555866 http://dx.doi.org/10.1080/19336918.2015.1113366 |
Ejemplares similares
-
Pharmacologic Inhibition of Ezrin-Radixin-Moesin Phosphorylation is a Novel Therapeutic Strategy in Rhabdomyosarcoma
por: Proudfit, Austin, et al.
Publicado: (2020) -
Ezrin/Radixin/Moesin Proteins and Flotillins Cooperate to Promote Uropod Formation in T Cells
por: Martinelli, Sibylla, et al.
Publicado: (2013) -
Immunohistochemical analysis of ezrin-radixin-moesin-binding phosphoprotein 50 in prostatic adenocarcinoma
por: Bartholow, Tanner L, et al.
Publicado: (2011) -
PKCθ Regulates T Cell Motility via Ezrin-Radixin-Moesin Localization to the Uropod
por: Cannon, Judy L., et al.
Publicado: (2013) -
CD43 interaction with ezrin-radixin-moesin (ERM) proteins regulates T-cell trafficking and CD43 phosphorylation
por: Cannon, J. L., et al.
Publicado: (2011)