Publications by authors named "Alaa Alshaer"
Extracellular matrix mechanics influence diverse cellular functions, yet surprisingly little is known about the mechanical properties of their constituent collagen proteins. In particular, network-forming collagen IV, an integral component of basement membranes, has been far less studied than fibril-forming collagens. A key feature of collagen IV is the presence of interruptions in the triple-helix-defining (Gly-X-Y) sequence along its collagenous domain.
View Article and Find Full Text PDFSingle-molecule imaging is widely used to determine statistical distributions of molecular properties. One such characteristic is the bending flexibility of biological filaments, which can be parameterized via the persistence length. Quantitative extraction of persistence length from images of individual filaments requires both the ability to trace the backbone of the chains in the images and sufficient chain statistics to accurately assess the persistence length.
View Article and Find Full Text PDFArticle Synopsis
- Collagen IV scaffold is a key component of the basement membrane that supports multicellularity and tissue evolution, beginning with the assembly of protochains inside cells and their subsequent secretion.
- The study focuses on how chloride ions facilitate the assembly of collagen IV protomers into stable hexamers through a noncollagenous domain (NC1), which is essential for structural integrity.
- Findings reveal that a specific chloride ring stabilizes the hexamer structure and is conserved throughout evolutionary history, providing insights for future research into collagen scaffolds and potential therapies for related diseases.