New for 2007: Our laboratory is now extending its field of interest to cover areas within the Parkinson's Diseases and Alzheimer's Disease field. As well as metal binding studies we are also developing projects related to regulation of gene transcription.

David Brown helped to found the Cambridge Prion Consortium established in December 1999.  Dr. Brown left Cambridge in 2001 to re-establish his research group at the University of Bath within the Department of Biology and Biochemistry. The work of his group focuses on research encompassing the prion diseases, transmissible spongiform encephalopathies, prions or the normal cellular protein, the prion protein.
 
 

The following link will take you to a list of the research conducted by the group of Professor. David Brown
his team and collaborators.
 

Some Background Information on Prions

Prion diseases or spongiform encephalopathies are diseases of the central nervous system. These diseases are characterized by neurodegeneration which leads to death of brain cells. This loss of cells has fatal consequences. These diseases include Creutzfeldt-Jakob disease, Bovine Spongiform Encephalopathy, scrapie and others.

Prions are proteins that transmit conformational modification between cells in a non-Mendellian manner (i.e.. DNA is not involved) such that the same protein expressed by the "infected" cell shows the conformational state of the infecting prion which is characterized as abnormal. Two proteins have been shown to have these effects and are both expressed by yeast. However, most people these days accept that the mammalian protein - the prion protein also has such a rogue isoform.

The prion protein is a normal protein expressed by brain cells and cells of the immune system. It is highly expressed in neurones. It is cell surface glycoprotein that binds copper and possible acts as an anti-oxidant protein in synapses and elsewhere on the cell surface.