Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Echinobase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.

Profile Publications(25)

Dr.  Charles G Glabe



Research Description

Research in the Glabe lab focuses on the structure, aggregation and mechanisms of pathogenesis of amyloids in degenerative diseases. The main research programs center on the production of conformation dependent antibodies that specifically recognize distinct assembly states of amyloids, the use of these antibodies in dissecting the pathogenic mechanisms of amyloids and their applications in vaccine development. Other areas of interest include the mechanism of membrane permeabilization by amyloid oligomers. Dr. Glabe and his colleagues have discovered that fibrils and prefibrillar oligomers represent alternative aggregation pathways for many different types of amyloids and that they have distinct underlying structural motifs that are generic to the particular aggregation state and are recognized by specific conformation dependent antibodies. The prefibrillar oligomer antibody recognizes the oligomeric conformation of all amyloids tested and not the native conformation, random coil monomer or fibrillar amyloids regardless of protein sequence. We found that this antibody neutralizes the toxicity of amyloid oligomers in vitro and that vaccination of transgenic mouse models against the prefibrillar oligomers prevents amyloid deposition and cognitive dysfunction. The fibril specific antibody recognizes fibrils and soluble fibrillar oligomers of many different types of amyloids, but not prefibrillar oligomers, monomer or natively folded proteins. This indicates that fibrils have a generic structure that is distinct from that of prefibrillar oligomers, implying that they may have distinct toxic mechanisms. These discoveries indicate that amyloids share common structures and imply that they also share a common primary mechanism of amyloid oligomer pathogenesis. This suggests that therapies that specifically target these common structures may be effective for many different types of amyloid related degenerative diseases. Current work is focused on characterizing the detailed structures of these aggregation states and the common mechanisms of toxicity, which may involve the permeabilization of cellular membranes by prefibrillar oligomers.


University of California Irvine
3228 McGaugh Hall
Mail Code: 3900
Irvine, CA
92697, USA


Web Page:

General/Lab Fax:  (949) 824-8551
Phone:  (949)824-6081 ext. 4229