Systemic amyloidosis is caused by misfolding and aggregation of globular proteins in vivo for which effective treatments are urgently needed. Inhibition of protein self-aggregation represents an attractive therapeutic strategy. Studies on the amyloidogenic variant of \u3b22-microglobulin, D76N, causing hereditary systemic amyloidosis, have become particularly relevant since fibrils are formed in vitro in physiologically relevant conditions. Here we compare the potency of two previously described inhibitors of wild type \u3b22-microglobulin fibrillogenesis, doxycycline and single domain antibodies (nanobodies). The \u3b22-microglobulin -binding nanobody, Nb24, more potently inhibits D76N \u3b22-microglobulin fibrillogenesis than doxycycline ...
The amyloidogenic variant of β2-microglobulin, D76N, can readily convert into genuine fibrils under ...
Inhibition of amyloid fibril formation could benefit patients with systemic amyloidosis. In this gro...
The D76N variant of human β2-microglobulin (β2m) is the causative agent of a hereditary amyloid dise...
Systemic amyloidosis is caused by misfolding and aggregation of globular proteins in vivo for which ...
Atomic-level structural investigation of the key conformational intermediates of amyloidogenesis rem...
We report the effects of the interaction of two camelid antibody fragments, generally called nanobod...
Six variants of human lysozyme (single-point mutations I56T, F57I, W64R, D67H and double mutations ...
This research was originally published in the Journal of Biological Chemistry. Daisaku Ozawa, Kazuhi...
Protein aggregation including the formation of dimers and multimers in solution, underlies an array ...
We report the effects of the interaction of two camelid antibody fragments, generally called nanobod...
Six variants of human lysozyme (single-point mutatants I56T, F57I, W64R, D67H and double mutants F57...
Inhibiting amyloid aggregation through high-turnover dynamic interactions could be an efficient stra...
This research focused on development of nanoparticle- based therapeutics against amyloid fibrils. Am...
D76N is the first natural variant of human \u3b2-2 microglobulin (\u3b22m) so far identified. Contra...
Availability of living organisms to mimic key step of amyloidogenesis of human protein has become an...
The amyloidogenic variant of β2-microglobulin, D76N, can readily convert into genuine fibrils under ...
Inhibition of amyloid fibril formation could benefit patients with systemic amyloidosis. In this gro...
The D76N variant of human β2-microglobulin (β2m) is the causative agent of a hereditary amyloid dise...
Systemic amyloidosis is caused by misfolding and aggregation of globular proteins in vivo for which ...
Atomic-level structural investigation of the key conformational intermediates of amyloidogenesis rem...
We report the effects of the interaction of two camelid antibody fragments, generally called nanobod...
Six variants of human lysozyme (single-point mutations I56T, F57I, W64R, D67H and double mutations ...
This research was originally published in the Journal of Biological Chemistry. Daisaku Ozawa, Kazuhi...
Protein aggregation including the formation of dimers and multimers in solution, underlies an array ...
We report the effects of the interaction of two camelid antibody fragments, generally called nanobod...
Six variants of human lysozyme (single-point mutatants I56T, F57I, W64R, D67H and double mutants F57...
Inhibiting amyloid aggregation through high-turnover dynamic interactions could be an efficient stra...
This research focused on development of nanoparticle- based therapeutics against amyloid fibrils. Am...
D76N is the first natural variant of human \u3b2-2 microglobulin (\u3b22m) so far identified. Contra...
Availability of living organisms to mimic key step of amyloidogenesis of human protein has become an...
The amyloidogenic variant of β2-microglobulin, D76N, can readily convert into genuine fibrils under ...
Inhibition of amyloid fibril formation could benefit patients with systemic amyloidosis. In this gro...
The D76N variant of human β2-microglobulin (β2m) is the causative agent of a hereditary amyloid dise...