Corruption and spread of pathogenic proteins in neurodegenerative diseases

Lary C. Walker, Harry LeVine

Research output: Contribution to journalReview articlepeer-review

58 Scopus citations

Abstract

With advancing age, the brain becomes increasingly susceptible to neurodegenerative diseases, most of which are characterized by the misfolding and errant aggregation of certain proteins. The induction of aggregation involves a crystallization-like seeding mechanism by which a specific protein is structurally corrupted by its misfolded conformer. The latest research indicates that, once formed, proteopathic seeds can spread from one locale to another via cellular uptake, transport, and release. Impeding this process could represent a unified therapeutic strategy for slowing the progression of a wide range of currently intractable disorders.

Original languageEnglish
Pages (from-to)33109-33115
Number of pages7
JournalJournal of Biological Chemistry
Volume287
Issue number40
DOIs
StatePublished - Sep 28 2012

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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