Ruben G. Vidal, PhD

Associate Professor
Department of Pathology & Laboratory Medicine
Indiana University School of Medicine
Telephone: 317-274-1729
FAX: 317-274-0504

Fibrillization and aggregation of proteins in the brain is a common theme in a diverse group of neurodegenerative disorders. Insight into the pathogenesis of any one of these disorders may have implications for understanding the mechanisms that underlie all these diseases as well as for the discovery of better strategies to treat them.

In our laboratories, we study the pathogenesis of Alzheimer disease (AD), familial British and Danish dementia (FBD and FDD) and other neurodegenerative disorders in which the main biochemical event leading to brain degeneration involves the deposition of a protein with an abnormal conformation. These are disorders of protein conformation leading to aggregation, in which a protein that is present in body fluids as a soluble precursor deposits, producing organ dysfunction and cell death. In most cases, such as in AD, amyloid fibrils are composed of self-assembled, low molecular weight mass peptides adopting beta-pleated sheet structure, the conformation responsible for their physicochemical properties and tinctoreal characteristics.

The association between protein aggregation and neurodegenerative diseases is an emerging field of study. We are investigating the genetic basis and the pathogenic mechanisms by which misfolded proteins cause neurodegeneration. To accomplish our goals we employ a multidisciplinary approach in which we use a variety of modern methodologies including molecular cloning, protein biochemistry, recombinant protein expression and cell transfection. In addition, we have developed transgenic animal models for some of these diseases, on which therapeutic approaches might be tested. As our understanding of the pathological mechanisms involved in neurodegenerative diseases increases, the hope for effective, novel therapeutic approaches is raised. Our research efforts are funded by grants from the National Institutes of Health, the American Federation for Aging Research and the Alzheimer’s Association.


  1. Miravalle L, Calero M, Takao M, Roher AE, Ghetti B, Vidal R; Amino-terminally truncated Ab peptide species are the main component of cotton wool plaques; Biochemistry 44:10810-10821; 2005
  2. Vidal R. Delisle MB. Ghetti B. Neurodegeneration caused by proteins with an aberrant carboxyl-terminus.  Journal of Neuropathology & Experimental Neurology. 63(8):787-800, 2004
  3. Vidal R. Ghetti B. Takao M. Brefel-Courbon C. Uro-Coste E. Glazier BS. Siani V. Benson MD. Calvas P. Miravalle L. Rascol O. Delisle MB. Intracellular ferritin accumulation in neural and extraneural tissue characterizes a neurodegenerative disease associated with a mutation in the ferritin light polypeptide gene.  Journal of Neuropathology & Experimental Neurology. 63(4):363-80, 2004
  4. Choi SI. Vidal R. Frangione B. Levy E. Axonal transport of British and Danish amyloid peptides via secretory vesicles.  FASEB Journal. 18(2):373-5, 2004
  5. Roher AE. Kokjohn TA. Esh C. Weiss N. Childress J. Kalback W. Luehrs DC. Lopez J. Brune D. Kuo YM. Farlow M. Murrell J. Vidal R. Ghetti B. The human amyloid-beta precursor protein770 mutation V717F generates peptides longer than amyloid-beta-(40-42) and flocculent amyloid aggregates. Journal of Biological Chemistry. 279(7):5829-36, 2004  

Dept. of Pathology & Laboratory Medicine Administration Office | Van Nuys Medical Science Building | 635 Barnhill Drive, room A-128 | Indianapolis, IN 46202 Indiana University Health Pathology Laboratory: 350 W. 11th Street, Indianapolis, Indiana 46202