Amyloid pores from pathogenic mutations

Hilal A. Lashuel, Dean Hartley, Benjamin M. Petre, Thomas Walz and Peter T. Lansbury ()
Additional contact information
Hilal A. Lashuel: Center for Neurologic Diseases, Harvard Medical School
Dean Hartley: Center for Neurologic Diseases, Harvard Medical School
Benjamin M. Petre: Harvard Medical School
Thomas Walz: Harvard Medical School
Peter T. Lansbury: Center for Neurologic Diseases, Harvard Medical School

Nature, 2002, vol. 418, issue 6895, 291-291

Abstract: Abstract Alzheimer's and Parkinson's diseases are associated with the formation in the brain of amyloid fibrils from β-amyloid and α-synuclein proteins, respectively. It is likely that oligomeric fibrillization intermediates (protofibrils), rather than the fibrils themselves, are pathogenic, but the mechanism by which they cause neuronal death remains a mystery. We show here that mutant amyloid proteins associated with familial Alzheimer's and Parkinson's diseases form morphologically indistinguishable annular protofibrils that resemble a class of pore-forming bacterial toxins, suggesting that inappropriate membrane permeabilization might be the cause of cell dysfunction and even cell death in amyloid diseases.

Date: 2002
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/418291a Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:418:y:2002:i:6895:d:10.1038_418291a

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/418291a

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().