Protein misfolding disorders and rational design of antimisfolding agents.

Lisbell D. Estrada, June Guillet, Claudio Soto

Research output: Contribution to journalReview article

9 Citations (Scopus)

Abstract

Compelling evidence strongly suggests that the conversion of a normal soluble protein into a beta-sheet-rich oligomeric structure and further fibril formation is the critical step in the pathogenesis of several human diseases, termed protein misfolding disorders. Therefore, a promising therapeutic strategy consists of the design of molecules that prevent the misfolding and aggregation of these proteins. In this chapter, we survey the mechanism of protein misfolding and some strategies to rationally produce inhibitors of this process.

Original languageEnglish (US)
Pages (from-to)277-293
Number of pages17
JournalMethods in molecular biology (Clifton, N.J.)
Volume340
StatePublished - Jan 1 2006

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Proteostasis Deficiencies
Proteins
Therapeutics

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

Cite this

Protein misfolding disorders and rational design of antimisfolding agents. / Estrada, Lisbell D.; Guillet, June; Soto, Claudio.

In: Methods in molecular biology (Clifton, N.J.), Vol. 340, 01.01.2006, p. 277-293.

Research output: Contribution to journalReview article

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