TY - JOUR
T1 - Protein misfolding disorders and rational design of antimisfolding agents.
AU - Estrada, Lisbell D.
AU - Yowtak, June
AU - Soto, Claudio
PY - 2006
Y1 - 2006
N2 - 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.
AB - 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.
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U2 - 10.1385/1-59745-116-9:277
DO - 10.1385/1-59745-116-9:277
M3 - Review article
C2 - 16957342
AN - SCOPUS:33749070570
SN - 1064-3745
VL - 340
SP - 277
EP - 293
JO - Methods in molecular biology (Clifton, N.J.)
JF - Methods in molecular biology (Clifton, N.J.)
ER -