Charles Glabe, Ph.D.
Professor, Molecular Biology and Biochemistry, School of Biological Sciences, University of California at Irvine
Dr. Glabe's research program is focused on amyloid structure and aggregation, in particular beta-amyloid, which is the key pathogenic hallmark of Alzheimer's disease. Dr. Glabe made the seminal discovery that protein components of amyloid share a common structure that is recognized by a conformation-specific antibody. This discovery indicates that amyloids likely share a common primary mechanism of pathogenesis in disease.
Funded Research
Project Description Researchers Funding Cellular and Animal Models of Amyloid Pathology in Early Alzheimer's Disease The goal of this project is to evaluate the pathological significance of a new type of Abeta deposits in the brain (at the onset of Alzheimer’s disease) in order to develop a novel mechanism for amyloid pathogenesis to help convince the FDA to approve and support early clinical trials.
Charles Glabe, Ph.D. 2011
$100,000Potential for Host Cytotoxicity from Microbially-derived Abeta Oligomers Alzheimer’s disease (AD) is the most common form of dementia in the elderly afflicting over 20 million people worldwide. Two decades of findings from cell biology, genetic, neuropathological, biochemical and animal studies overwhelmingly point to the β-amyloid peptide (Aβ) as the key protein in the disease’s pathology (see review by Hardy and Selkoe, 20001). Aβ appears to be a soluble component of normal brain. However, in AD brain the peptide accumulates as β-amyloid, an insoluble semi-crystalline deposit that is the hallmark of the disease pathology.
Rudy Tanzi, Ph.D.Robert Moir, Ph.D.Charles Glabe, Ph.D.2009
$250,000
Selected Publications
These published papers resulted from Cure Alzheimer’s Fund support.
, "Crystal structure of a conformation-dependent rabbit IgG Fab specific for amyloid prefibrillar oligomers" , Biochim Biophys Acta , 1820(12) , Dec 2012 , 1908-14, "Crystal structure of a conformation-dependent rabbit IgG Fab specific for amyloid prefibrillar oligomers" , Biochimica et Biophysica Acta , Aug 24, 2012, "Prion-like behaviour and tau-dependent cytotoxicity of pyroglutamylated amyloid-β" , Nature , 485 , May 2, 2012 , 651-655, "Days to criterion as an indicator of toxicity associated with human Alzheimer amyloid-β oligomers" , Annals of Neurology , Volume 68, Issue 2 , August 2010, "Annular protofibrils are a structurally and functionally distinct type of amyloid oligomer" , J Biol Chem , 284 , February 13, 2009 , 4230-4237, "Structural classification of toxic amyloid oligomers" , J Biol Chem , 283 , October 31, 2008 , 29639-29643
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