@article {70313,
	title = {BPS2026 {\textendash} Real-time visualization and analysis of fibrin polymerization},
	journal = {Biophysical Journal},
	volume = {125},
	year = {2026},
	month = {Jan-02-2026},
	pages = {227a - 228a},
	abstract = {<p>To form a blood clot, fibrinogen is converted into fibrin through the action of the enzyme thrombin. Fibrin then polymerizes longitudinally and laterally as it matures into a fiber. Polymerization results in a dense, 3-dimensional branched network. Previous research has shown the relevance of these fibrin gel structures in hemostatic conditions; however, the mechanism by which they form has not been fully resolved. Using light sheet microscopy, 3-dimensional volumes of the fibrin polymerization process were captured. Manual annotation of these microscopy videos revealed that fiber branch points occur through the collision and the binding of diffusing fibers rather than through the splitting of growing fiber termini. However, the density of fibers and amount of data greatly slows manual annotation-based analysis and limits the ability to capture important data, such as growth rates and fiber stiffness. To more quickly process these data, a computational approach was utilized. A custom tracking pipeline, suited to the networks formed by cylindrical fibrin fibers, was developed, beginning with an AI-based classifier. This custom pipeline allowed for the tracking of uniquely labeled fibers over time. Automated merge detection between linking phases further improved accuracy. Additionally, network formation was analyzed through skeletonization techniques to measure the number of branches per junction over time. Combining the skeletonization and tracking methods, single fibers were identified by their lack of branch points and tracked. The addition of branch points to previously tracked objects served as a signal for merge detection. This approach yielded measurements of single fibrin fiber diffusion rates, as well as the first volumetric and length growth rates of fibers throughout polymerization. In addition, the gel point was quantified by analyzing the span of connected objects to characterize the network consolidation over time at the level of single fibers.</p>
},
	issn = {00063495},
	doi = {10.1016/j.bpj.2025.11.1510},
	url = {https://doi.org/10.1016/j.bpj.2025.11.1510},
	author = {Miller, Dylan M. and Elangovan, Aravind and Belcher, Heather A. and Lee, Rachel M. and Hobson, Chad M. and Crosley, Key and Hart, David M. and Laverty, Brittany Bannish E. and Guthold, Martin and Hudson, Nathan E.}
}
@article {70266,
	title = {Mechanically-induced Septin Networks protect nuclear integrity},
	journal = {bioRxiv},
	year = {2026},
	month = {2026 Jan 21},
	abstract = {<p>The cytoskeleton is a key mediator of mechanical interactions in cells, but specific contributions of septins remains unclear. Septins preferentially localize with a subset of actin stress fibers positioned under the nucleus, where they are situated between the membrane and stress fibers. Removing the nucleus from the cell results in the loss of these subnuclear septin-decorated stress fibers. Surprisingly, however, their formation can be rescued using a large glass bead in place of the nucleus. Similarly, applying a compressive force to the cell via confinement, whether externally or through internally generated actomyosin forces, results in increased septin accumulation in regions where the nucleus engages the cell cortex. Finally, loss of septin filaments via knockdown of SEPT7 increases the likelihood of nuclear membrane rupture during confinement. Together these data suggest that septins act as a dynamic mechanosensitive protective mechanism to buffer mechanical forces on the nucleus.</p>
},
	doi = {10.64898/2026.01.20.700414},
	url = {https://www.biorxiv.org/content/early/2026/01/21/2026.01.20.700414},
	author = {Utgaard, Margaret E. and Caillier, Alexia and Chandrasekar, Shreya and Tidei, Joseph J. and Balasubramanian, Harikrushnan and Lee, Rachel M. and Puls, Owen and Khuon, Satya and Aaron, Jesse and Chew, Teng-Leong and Beach, Jordan R. and Oakes, Patrick W.}
}
