Bachina, P. | Search bioRxiv

bioRxiv2025

Privacy-Preserving Generative AI Framework for Synthetic Multimodal Eye Movement Data

Eye movements, such as nystagmus, saccades, and smooth pursuit, provide valuable information about neurological function but have limited publicly accessible datasets due to patient privacy concerns. To address this, we leverage generative AI to create realistic videos of artificial eye movement, eliminating the need for real patient data. These synthetic datasets have shown performance comparable to actual patient data in clinical tasks. Our generated videos will be openly shared, facilitating broader research and advancement in neurologic and neuro-ophthalmic AI applications.

bioengineering↗

bioRxiv2020

Structure and mechanism of a primate ferroportin

Ferroportin is the only cellular iron exporter in human and essential for iron homoeostasis. Mutations in ferroportin are associated with hemochromatosis or ferroportin diseases characterized by a paradoxical combination of anemia and abnormal accumulation of iron in cells. Ferroportin is also the target of hepcidin, which is a hormone that downregulates ferroportin activity. However, due to a lack of three-dimensional structures, the mechanism of iron transport by ferroportin and its regulation by hepcidin remains unclear. Here we present the structure of a ferroportin from the primate Philippine tarsier (TsFpn) at 3.0 [A] resolution determined by cryo-electron microscopy. TsFpn has a structural fold common to major facilitator superfamily of transporters and the current structure is in an outward-open conformation. The structure identifies two potential ion binding sites with each site coordinated by two residues. Functional studies demonstrate that TsFpn is a H+/Fe2+ antiporter and that transport of one Fe2+ is coupled to the transport of two H+ in the opposite direction such that the transport cycle is electroneutral. Further studies show that the two ion binding sites affect transport of H+ and Fe2+ differently. The structure also provides mechanistic interpretation for mutations that cause ferroportin diseases.

biochemistry↗