Author pages are created from data sourced from our academic publisher partnerships and public sources.
Share This Author
Cadherin‐catenin complex: Protein interactions and their implications for cadherin function
In the light of a fundamental role of the CCC during mammalian development and tissue morphogenesis, the phenotypes of embryos lacking E‐cadherin or β‐catenin are discussed and a structural basis for understanding the homophilic interaction mechanism and the calcium requirement of cadherins is provided.
Single amino acid substitutions in proteins of the armadillo gene family abolish their binding to alpha-catenin.
The results indicate that single amino acid mutations in the alpha-catenin binding site of homologs of Armadillo could prevent a stable association with alpha- catenin, thus affecting cadherin-mediated adhesion.
Single Amino Acid Substitutions in Proteins of the armadillo Gene Family Abolish Their Binding to -Catenin (*)
- H. Aberle, H. Schwartz, H. Hoschuetzky, R. Kemler
- BiologyThe Journal of Biological Chemistry
- 19 January 1996
The results indicate that single amino acid mutations in the α- catenin binding site of homologs of Armadillo could prevent a stable association with α-catenin, thus affecting cadherin-mediated adhesion.