Financial impact of incorporating deep learning reconstruction into magnetic resonance imaging routine.

Purpose: Artificial intelligence and deep learning solutions are increasingly utilized in healthcare and radiology. The number of studies addressing their enhancement of productivity and monetary impact is, however, still limited. Our hospital has faced a need to enhance MRI scanner throughput, and we investigate the utility of new commercial deep learning reconstruction (DLR) algorithm for this purpose.

Critical evaluation of deep neural networks for wrist fracture detection.

Wrist Fracture is the most common type of fracture with a high incidence rate. Conventional radiography (i.e.

Discrepancies in interpretation of night-time emergency computed tomography scans by radiology residents.

Background: In many emergency radiology units, most of the night-time work is performed by radiology residents. Residents' preliminary reports are typically reviewed by an attending radiologist. Accordingly, it is known that discrepancies in these preliminary reports exist.

Direct interaction of actin filaments with F-BAR protein pacsin2.

Two mechanisms have emerged as major regulators of membrane shape: BAR domain-containing proteins, which induce invaginations and protrusions, and nuclear promoting factors, which cause generation of branched actin filaments that exert mechanical forces on membranes. While a large body of information exists on interactions of BAR proteins with membranes and regulatory proteins of the cytoskeleton, little is known about connections between these two processes. Here, we show that the F-BAR domain protein pacsin2 is able to associate with actin filaments using the same concave surface employed to bind to membranes, while some other tested N-BAR and F-BAR proteins (endophilin, CIP4 and FCHO2) do not associate with actin.

Crystallization and phasing of focal adhesion protein 52 from Gallus gallus.

Focal adhesion protein 52 (FAP52) is a multidomain adaptor protein of 448 amino acids characterized as an abundant component of focal adhesions. FAP52 binds to filamin via its N-terminal alpha-helical domain, suggesting a role in linking focal adhesions to the actin-based cytoskeleton. The recombinant protein was crystallized using the hanging-drop vapour-diffusion method, which yielded two crystal forms.

Focal adhesion protein FAP52 self-associates through a sequence conserved among the members of the PCH family proteins.

FAP52 is a recently described focal adhesion-associated protein. It is a member of an emerging PCH (pombe Cdc15 homology) family of proteins characterized by a common domain organization and involvement in actin cytoskeleton organization, cytokinesis, and vesicular trafficking. Using gel filtration, surface plasmon resonance, and native polyacrylamide gel electrophoresis analysis, combined with chemical cross-linking of both native and recombinant protein, we show that FAP52 self-associates in vitro and suggest that it occurs predominantly as a trimer also in vivo.

FAP52 regulates actin organization via binding to filamin.

FAP52, a focal adhesion-associated phosphoprotein, is a member of a FAP52/PACSIN/syndapin family of proteins. They share a multidomain structure and are implicated in actin-based and endocytotic functions. We show, by using both native and recombinant proteins, that FAP52 selectively binds to the actin cross-linking protein filamin (ABP-280).