Cargando…
The interaction of the retina cell surface N- acetylgalactosaminylphosphotransferase with an endogenous proteoglycan ligand results in inhibition of cadherin-mediated adhesion
We have previously shown that the binding to cells of a monoclonal antibody directed against the chick neural retina N- acetylgalactosaminylphosphotransferase (GalNAcPTase) results in inhibition of cadherin-mediated adhesion and neurite outgrowth. We hypothesized that the antibody mimics the action...
Formato: | Texto |
---|---|
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1995
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2120464/ https://www.ncbi.nlm.nih.gov/pubmed/7775582 |
Ejemplares similares
-
Antibodies to the retina N-acetylgalactosaminylphosphotransferase modulate N-cadherin-mediated adhesion and uncouple the N-cadherin transferase complex from the actin-containing cytoskeleton
Publicado: (1991) -
Small Leucine-Rich Proteoglycans (SLRPs) in the Retina
por: Low, Shermaine W. Y., et al.
Publicado: (2021) -
E-cadherin cytoplasmic domain inhibits cell surface localization of endogenous cadherins and fusion of C2C12 myoblasts
por: Ozawa, Masayuki
Publicado: (2015) -
Coordinate Regulation of Cadherin and Integrin Function by the Chondroitin Sulfate Proteoglycan Neurocan
por: Li, Hedong, et al.
Publicado: (2000) -
Cadherin Cytoplasmic Domains Inhibit the Cell Surface Localization of Endogenous E-Cadherin, Blocking Desmosome and Tight Junction Formation and Inducing Cell Dissociation
por: Ozawa, Masayuki, et al.
Publicado: (2014)