Ruben
Vidal

Ruben Vidal is the Luella McWhirter Martin Professor in Alzheimer’s Disease Research at Indiana University School of Medicine and a Chancellor’s Professor at Indiana University-Indianapolis. Dr. Vidal’s specific research focus has been investigating the pathogenesis of neurodegenerative diseases. Dr. Vidal was the first to characterize the genetic defect and the deposition of TTR amyloid in leptomeningeal vessels, leading to memory and psychomotor dysfunction in Familial meningocerebrovascular amyloidosis. He also described the disease hereditary ferritinopathy (HF), which has led to a comprehensive research program aimed at characterizing the clinical, pathologic, genetic, and biochemical basis of HF and developing the first animal model for HF. Dr. Vidal identified mutations in the gene BRI2 associated with dementia in the diseases familial British dementia (FBD) and familial Danish dementia (FDD), and developed the first animal model for FDD and an animal model for FDD with Danish amyloid and Tau co-deposition. He also carried out experimental studies of amyloid deposition in sporadic and familial forms of Alzheimer’s disease (AD), including the first biochemical characterization of cotton wool plaques (CWP) in a subset of individuals with Presenilin 1 mutations, and generated novel animal models for AD. Lately, Dr. Vidal has further developed his interest in the study of the structure of proteins in neurodegeneration using cryogenic electron microscopy (cryo-EM). A major advantage of cryo-EM over X-ray crystallography is that the molecule of interest does not have to be crystallized. His laboratory has played a major role in the structural characterization of protein aggregates in neurodegenerative diseases using cryo-EM, in particular Tau deposits in tauopathies, Aß in AD and Down syndrome, and Tau and APrP in Prion diseases. Ongoing projects in his lab explore the structure of Aß in different amyloid plaques in AD, understanding neurodegenerative diseases associated with BRI2 mutations and the interaction and synergy between extracellular amyloids (like Aß) and tau development, and the identification of specific structures important for binding of ligands designed for in vivo imaging and potential therapeutic approaches.