The significance of the location of mutations for the native-state dynamics of human lysozyme
The conversion of human lysozyme into amyloid fibrils is associated with a rare but fatal hereditary form of nonneuropathic systemic amyloidosis. The accumulation of large amounts of aggregated protein is thought to be initiated by the formation of transient intermediate species of disease-related l...
Main Authors: | Ahn, M, Hagan, C, Bernardo-Gancedo, A, De Genst, E, Newby, F, Christodoulou, J, Dhulesia, A, Dumoulin, M, Robinson, C, Dobson, C, Kumita, J |
---|---|
Format: | Journal article |
Language: | English |
Published: |
Elsevier
2016
|
Similar Items
-
A non-natural variant of human lysozyme (I59T) mimics the in vitro behaviour of the I56T variant that is responsible for a form of familial amyloidosis.
by: Hagan, C, et al.
Published: (2010) -
Analysis of the native structure, stability and aggregation of biotinylated human lysozyme.
by: Minkoo Ahn, et al.
Published: (2012-01-01) -
Impact of the native-state stability of human lysozyme variants on protein secretion by Pichia pastoris.
by: Kumita, JR, et al.
Published: (2006) -
Rationalising lysozyme amyloidosis: insights from the structure and solution dynamics of T70N lysozyme.
by: Johnson, R, et al.
Published: (2005) -
A nanobody binding to non-amyloidogenic regions of the protein human lysozyme enhances partial unfolding but inhibits amyloid fibril formation.
by: De Genst, E, et al.
Published: (2013)