Anil Prakasam

TL;DR: Force measurements quantified both kinetic and strength differences between different classical cadherins that may underlie cell sorting behavior and showed that differential cadherin-mediated adhesion, rather than exclusive homophilic binding between identical caderins, direct cell segregation and the organization of tissue interfaces during morphogenesis is shown.

TL;DR: The results suggest that the basis for cell segregation during morphogenesis does not map exclusively to protein-level differences in cadherin adhesion.

TL;DR: The histidine tag results in the site-selective immobilization of the protein A receptor and the preservation of its high ligand affinity when immobilized on solid supports, demonstrating a homogeneous, high affinity population at densities where steric crowding between large ligands does not affect the apparent receptor affinity.

TL;DR: This long-range effect suggests that the presence or absence of tryptophan-2 docking allosterically alters the adhesive function of distal sites on the protein, and appears to reconcile the multidomain binding mechanism with mutagenesis studies, which suggested that W2 is the sole binding interface.

TL;DR: It is shown at the single molecule level that homotypic C‐cadherin association involves transient intermediates lasting less than a few tens of milliseconds, which enable cells to detect ligands or measure surrounding mechanical behaviour within a fraction of a second, much more rapidly than was previously thought.