Common structure and toxic function of amyloid oligomers implies a common mechanism of pathogenesis

Charles G. Glabe, Rakez Kayed

Research output: Contribution to journalArticle

266 Citations (Scopus)

Abstract

Recent findings indicate that soluble amyloid oligomers may represent the primary pathologic species in degenerative diseases. These amyloid oligomers share common structural features and the ability to permeabilize membranes, suggesting that they also share a common primary mechanism of pathogenesis. Membrane permeabilization by amyloid oligomers may initiate a common group of downstream pathologic processes, including intracellular calcium dyshomeostasis, production of reactive oxygen species, altered signaling pathways, and mitochondrial dysfunction that represent key effectors of cellular dysfunction and cell death in amyloid-associated degenerative disease, such as sporadic inclusion-body myositis.

Original languageEnglish (US)
JournalNeurology
Volume66
Issue number2 SUPPL. 1
StatePublished - Jan 2006
Externally publishedYes

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Poisons
Amyloid
Inclusion Body Myositis
Membranes
Pathologic Processes
Reactive Oxygen Species
Cell Death
Calcium

ASJC Scopus subject areas

  • Neuroscience(all)

Cite this

Common structure and toxic function of amyloid oligomers implies a common mechanism of pathogenesis. / Glabe, Charles G.; Kayed, Rakez.

In: Neurology, Vol. 66, No. 2 SUPPL. 1, 01.2006.

Research output: Contribution to journalArticle

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