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Protein misfolding and disease; protein refolding and therapy
Author(s) -
Soto Claudio
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02486-3
Subject(s) - protein folding , protein aggregation , mechanism (biology) , amyloid (mycology) , amyloid fibril , amyloidosis , chemistry , disease , computational biology , medicine , biochemistry , biology , amyloid β , pathology , philosophy , epistemology
Diverse human disorders, including several neurodegenerative diseases and systemic amyloidosis, are thought to arise from the misfolding and aggregation of an underlying protein. Recent findings strongly support this hypothesis and have increased our understanding of the molecular mechanism of protein conformational disorders. Many questions are still pending, but the data overall suggest that correction of protein misfolding constitutes a viable therapeutic strategy for conformational diseases.