Reduced global cooperativity is a common feature underlying the amyloidogenicity of pathogenic lysozyme mutations.
One of the 20 or so human amyloid diseases is associated with the deposition in vital organs of full-length mutational variants of the antibacterial protein lysozyme. Here, we report experimental data that permit a detailed comparison to be made of the behaviour of two of these amyloidogenic variant...
Autors principals: | Dumoulin, M, Canet, D, Last, A, Pardon, E, Archer, D, Muyldermans, S, Wyns, L, Matagne, A, Robinson, C, Redfield, C, Dobson, C |
---|---|
Format: | Journal article |
Idioma: | English |
Publicat: |
2005
|
Ítems similars
-
Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme.
per: Canet, D, et al.
Publicat: (2002) -
A nanobody binding to non-amyloidogenic regions of the protein human lysozyme enhances partial unfolding but inhibits amyloid fibril formation.
per: De Genst, E, et al.
Publicat: (2013) -
A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme.
per: Dumoulin, M, et al.
Publicat: (2003) -
The solution dynamics of amyloidogenic Asp67His variant of human lysozyme: Insights from hydrogen exchange
per: Canet, D, et al.
Publicat: (2000) -
Mechanistic studies of the folding of human lysozyme and the origin of amyloidogenic behavior in its disease-related variants.
per: Canet, D, et al.
Publicat: (1999)