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Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
A range of human degenerative conditions, including Alzheimer's disease, light-chain amyloidosis and the spongiform encephalopathies, is associated with the deposition in tissue of proteinaceousExpand
Rationalization of the effects of mutations on peptide andprotein aggregation rates
In order for any biological system to function effectively, it is essential to avoid the inherent tendency of proteins to aggregate and form potentially harmful deposits. In each of the variousExpand
Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution
The deposition of proteins in the form of amyloid fibrils and plaques is the characteristic feature of more than 20 degenerative conditions affecting either the central nervous system or a variety ofExpand
Designing conditions for in vitro formation of amyloid protofilaments and fibrils.
We have been able to convert a small alpha/beta protein, acylphosphatase, from its soluble and native form into insoluble amyloid fibrils of the type observed in a range of pathological conditions.Expand
A causative link between the structure of aberrant protein oligomers and their toxicity.
The aberrant assembly of peptides and proteins into fibrillar aggregates proceeds through oligomeric intermediates that are thought to be the primary pathogenic species in many protein depositionExpand
Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world.
  • M. Stefani
  • Biology, Medicine
  • Biochimica et biophysica acta
  • 24 December 2004
The data reported in the past 5 years have highlighted new aspects of protein misfolding and aggregation. Firstly, it appears that protein aggregation may be a generic property of polypeptide chainsExpand
Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding
Muscle acylphosphatase (AcP) is a small protein that folds very slowly with two-state behavior. The conformational stability and the rates of folding and unfolding have been determined for a numberExpand
The Polyphenol Oleuropein Aglycone Protects TgCRND8 Mice against Aß Plaque Pathology
The claimed beneficial effects of the Mediterranean diet include prevention of several age-related dysfunctions including neurodegenerative diseases and Alzheimer-like pathology. These effects haveExpand
Relative influence of hydrophobicity and net charge in the aggregation of two homologous proteins.
A potentially amyloidogenic protein has to be at least partially unfolded to form amyloid aggregates. However, aggregation of the partially or totally unfolded state of a protein is modulated by atExpand
Cholesterol in Alzheimer's disease: unresolved questions.
The role of cholesterol as a susceptibility factor or a protective agent in neurodegeneration and, more generally, in amyloid-induced cytotoxicity is still controversial. Epidemiological studies onExpand
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