The MAM (Meprin/A5-protein/PTPmu) Domain Is a Homophilic Binding Site Promoting the Lateral Dimerization of Receptor-like Protein-tyrosine Phosphatase μ

This publication has 45 references indexed in Scilit:

• Expression of the Receptor Protein-tyrosine Phosphatase, PTPμ, Restores E-cadherin-dependent Adhesion in Human Prostate Carcinoma Cells
  Published by Elsevier ,2002
• Protein Kinase C δ (PKCδ) Is Required for Protein Tyrosine Phosphatase μ (PTPμ)-Dependent Neurite Outgrowth
  Molecular and Cellular Neuroscience, 2002
• Structural and Evolutionary Relationships among Protein Tyrosine Phosphatase Domains
  Molecular and Cellular Biology, 2001
• Receptor-Type Protein-Tyrosine Phosphatase μ Is Expressed in Specific Vascular Endothelial Bedsin Vivo
  Experimental Cell Research, 1999
• PTPμ Regulates N-Cadherin–dependent Neurite Outgrowth
  The Journal of cell biology, 1999
• Differential expression of MAM-subfamily protein tyrosine phosphatases during mouse development
  Mechanisms of Development, 1998
• Protein tyrosine phosphatases in signal transduction
  Current Opinion in Cell Biology, 1997
• Homophilic binding of PTP mu, a receptor-type protein tyrosine phosphatase, can mediate cell-cell aggregation
  The Journal of cell biology, 1993
• An adhesive domain detected in functionally diverse receptors
  Trends in Biochemical Sciences, 1993
• Cloning, expression and chromosomal localization of a new putative receptor‐like protein tyrosine phosphatase
  FEBS Letters, 1991