Reference : Normal and aberrant biological self-assembly: Insights from studies of human lysozyme...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Normal and aberrant biological self-assembly: Insights from studies of human lysozyme and its amyloidogenic variants
Dumoulin, Mireille mailto [Université de Liège - ULiège > Département des sciences de la vie > Enzymologie et repliement des protéines >]
Kumita, Janet [ > > ]
Dobson, Christopher M [ > > ]
Accounts of Chemical Research
American Chemical Society
Yes (verified by ORBi)
[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.

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