Article (Scientific journals)
Normal and aberrant biological self-assembly: Insights from studies of human lysozyme and its amyloidogenic variants
Dumoulin, Mireille; Kumita, Janet; Dobson, Christopher M
2006In Accounts of Chemical Research, 39, p. 603-610
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Abstract :
[en] Studies of lysozyme have played a major role over several decades in defining the general principles underlying protein structure, folding, and stability. Following the discovery some 10 years ago that two mutational variants of lysozyme are associated with systemic amyloidosis, these studies have been extended to investigate the mechanism of amyloid fibril formation. This Account describes our present knowledge of lysozyme folding and misfolding, and how the latter can give rise to amyloid disease. It also discusses the significance of these studies for our general understanding of normal and aberrant protein folding in the context of human health and disease.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Dumoulin, Mireille  ;  Université de Liège - ULiège > Département des sciences de la vie > Enzymologie et repliement des protéines
Kumita, Janet
Dobson, Christopher M
Language :
English
Title :
Normal and aberrant biological self-assembly: Insights from studies of human lysozyme and its amyloidogenic variants
Publication date :
2006
Journal title :
Accounts of Chemical Research
ISSN :
0001-4842
eISSN :
1520-4898
Publisher :
American Chemical Society
Volume :
39
Pages :
603-610
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 15 September 2009

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