I hope it will prompt a lot of people interested in protein folding in vitro to try to relate their work to efforts to understand disease.

We have previously shown that the ability to form protein aggregates, known as amyloid fibrils, that are normally associated with just a few proteins involved in conditions such as Alzheimer's Disease or the transmissible spongiform encephalopathies (including vCJD) may be a common or "generic" feature of all our proteins. This paper suggests that the species which form initially during the conversion of a normally soluble protein to the amyloid form may be generally toxic to cells. Taken together these results support the idea that these diseases—many of which are primarily associated with aging—fundamentally result from the loss of the regulating or "housekeeping" functions of living organisms rather than from some specific aberrant conformational properties of the proteins associated with these diseases.

We have long been interested in understanding the mechanism of protein folding, and more recently in how and why proteins can fail to fold or to remain properly folded. The recognition that these events were linked to some of the most debilitating and common human diseases prompted us to focus much of our efforts in this area of research.