desmosomal cadherins undergo a locking mechanism that creates a periodic arrangement, trapping Ca2+, and resulting in strong extracellular Ca2+-independent adhesive properties, or the desmosomal cadherins form a series of densely tangled knots with no regular structure. A crystal structure has not ye...
Corneodesmosin, also known as CDSN and the S gene product, is a highly polymorphic secreted glycoprotein that plays an important structural role in the skin (1). Mature mouse Corneodesmosin shares 62% and 82% amino acid sequence identity with human and rat Corneodesmosin, respectively. It is...
To address the functional significance of plakoglobin-desmoglein interaction, we have mapped the sequences of Dsg1 that are crucial for this association by using blot overlay techniques. By examining the binding of plakoglobin to a deletion series of the Dsg1 cytoplasmic domain expressed as fusion ...
Second, much evidence suggests that desmosomal cadherins interact at their tips or EC1 domains (14, 15, 16, 17, 26). Third, anti-adhesion peptides derived from the sequences of the so-called cell adhesion recognition sites in the EC1 domain block adhesion of both classical and desmosomal ...
The desmogleins have additional unique sequences with unknown functions, including a proline-rich linker region, a repeat unit domain, and a desmoglein terminal domain10 (Fig. 5.2). Each of the three desmocollin RNAs can be alternatively spliced to yield an “a” and a “b” isoform. In ...
Herein, a series of C-3 glycosyl monodesmosidic saponins was synthesized via the microfluidic glycosylation of triterpenoids or steroids at the C-3 position, without the formation of orthoester byproducts, and subsequent deprotection of the benzoyl (Bz) group. This microfluidic glycosylation/batch ...