1
However, the presence of amyloid fibrils in semen remained to be demonstrated.
2
Our findings illustrate that glycation causes BSA to self-assemble into amyloid fibrils.
3
However, in most instances, only single enzyme-functionalized amyloid fibrils have so far been studied.
4
This assay is also widely used for the characterization of in vitro amyloid fibrils.
5
Misfolded proteins have propensities to form fibrils termed amyloid fibrils.
6
The formation of amyloid fibrils in vivo is poorly understood.
7
A minimum 14 residue peptide was identified that formed typical amyloid fibrils under physiological conditions.
8
Molecules designed to inhibit amyloid fibrils function by eliminating toxic oligomers or reducing fibril formation.
9
Background: Transthyretin amyloid cardiomyopathy is caused by the deposition of transthyretin amyloid fibrils in the myocardium.
10
Extracellular amyloid fibrils were identified by electron microscopy and were immunogold decorated with A beta antibody.
11
A recombinant variable domain of the light chain SMA was used to form amyloid fibrils in vitro.
12
However, no extracellular amyloid fibrils were seen.
13
We propose that the hierarchical assembly model describes a general mechanism of assembly for all amyloid fibrils.
14
These results reveal the importance of the β-sheet region of lysozyme for initiating self-assembly into amyloid fibrils.
15
Human transthyretin has an intrinsic tendency to form amyloid fibrils and is heavily implicated in senile systemic amyloidosis.
16
At low pH, a relatively unfolded intermediate conformation is populated for SMA and rapidly leads to amyloid fibrils.