A Train-the-Trainer Simulation Program Implemented Between Two International Partners.

With the expansion of global health initiatives focused on healthcare professional training, it is important to ensure that such training is scalable and sustainable. Simulation-based education (SBE) is a highly effective means to achieve these goals. Although SBE is widely used in the United States, its integration globally is limited, which can impact the potential of SBE in many countries.

Sea Anemones, Actinoporins, and Cholesterol.

Spanish or Spanish-speaking scientists represent a remarkably populated group within the scientific community studying pore-forming proteins. Some of these scientists, ourselves included, focus on the study of actinoporins, a fascinating group of metamorphic pore-forming proteins produced within the venom of several sea anemones. These toxic proteins can spontaneously transit from a water-soluble fold to an integral membrane ensemble because they specifically recognize sphingomyelin in the membrane.

Sticholysin I-II oligomerization in the absence of membranes.

Sticholysins are pore-forming toxins produced by the sea anemone Stichodactyla helianthus. When they encounter a sphingomyelin-containing membrane, these proteins bind to it and oligomerize, a process that ends in pore formation. Mounting evidence indicates that StnII can favour the activity of StnI.

Disseminated Tele-OSCE During a Pandemic: One University's Experience.

Background: Due to coronavirus disease 2019 (COVID-19), in-person educational activities were suspended across the globe throughout 2020. In health care education, this required a swift, creative response to maintain the flow of trained clinicians into the workforce without compromising the integrity of core learning outcomes. Early during the pandemic, remote synchronous simulation emerged as a compelling focus of the overall strategy.

Structural foundations of sticholysin functionality.

Actinoporins constitute a family of α pore-forming toxins produced by sea anemones. The soluble fold of these proteins consists of a β-sandwich flanked by two α-helices. Actinoporins exert their activity by specifically recognizing sphingomyelin at their target membranes.