Kristopher E. Kubow

TL;DR: It is concluded that the resting state of Fn fibrils does not contain Fn molecules with crossed-over arms, and that the several-fold extensibility of Fnfibrils involves the unfolding of type III modules, which could imply that Fn might play a significant role in mechanotransduction processes.

TL;DR: Fibre stretch-assay studies reveal that collagen I's Fn-binding domain is responsible for the mechano-regulated interaction and it is shown that Fn-collagen interactions are reciprocal: relaxed Fn fibrils act as multivalent templates for collagen assembly, but once assembled, collagen fibres shield Fn fibres from being stretched by cellular traction forces.

TL;DR: Fn fibers can be extended more than 8-fold (>700% strain) before 50% of the fibers break, and fiber extension steadily up-regulates fiber rigidity and cryptic epitope exposure, both of which are known to differentially alter cell behavior.

TL;DR: These studies demonstrate the versatility of SF as a biomaterial to engineer modified fibrous scaffolds and underscore the use of biofunctionally relevant analytical assays to optimize fibrous biomaterial scaffolds.

TL;DR: An EGFP (enhanced green fluorescent protein)–paxillin construct is used under the control of a truncated CMV (cytomegalovirus) promoter that was originally developed to express GFP–β-actin at very low levels and observed adhesions in cells at depths up to the limit of the working distance of the objective.