A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme.
Amyloid diseases are characterized by an aberrant assembly of a specific protein or protein fragment into fibrils and plaques that are deposited in various organs and tissues, often with serious pathological consequences. Non-neuropathic systemic amyloidosis is associated with single point mutations...
Auteurs principaux: | Dumoulin, M, Last, A, Desmyter, A, Decanniere, K, Canet, D, Larsson, G, Spencer, A, Archer, D, Sasse, J, Muyldermans, S, Wyns, L, Redfield, C, Matagne, A, Robinson, C, Dobson, C |
---|---|
Format: | Journal article |
Langue: | English |
Publié: |
2003
|
Documents similaires
-
Engineering a camelid antibody fragment that binds to the active site of human lysozyme and inhibits its conversion into amyloid fibrils.
par: Chan, P, et autres
Publié: (2008) -
Reduced global cooperativity is a common feature underlying the amyloidogenicity of pathogenic lysozyme mutations.
par: Dumoulin, M, et autres
Publié: (2005) -
Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme.
par: Canet, D, et autres
Publié: (2002) -
A nanobody binding to non-amyloidogenic regions of the protein human lysozyme enhances partial unfolding but inhibits amyloid fibril formation.
par: De Genst, E, et autres
Publié: (2013) -
Investigation of non-covalent interactions of amyloidogenic human lysozyme variants and camelid antibodies
par: Caddy, G, et autres
Publié: (2002)