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@article{Kubánková:2019:10.1021/acs.analchem.9b01221,
author = {Kubánková, M and Lin, X and Albrecht, T and Edel, JB and Kuimova, MK},
doi = {10.1021/acs.analchem.9b01221},
journal = {Analytical Chemistry},
pages = {6880--6886},
title = {Rapid fragmentation during seeded lysozyme aggregation revealed at the single molecule level},
url = {http://dx.doi.org/10.1021/acs.analchem.9b01221},
volume = {91},
year = {2019}
}

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TY  - JOUR
AB  - Protein aggregation is associated with neurodegenerative disorders such as Alzheimer's and Parkinson's diseases. The poorly understood pathogenic mechanism of amyloid diseases makes early stage diagnostics or therapeutic intervention a challenge. Seeded polymerization that reduces the duration of the lag phase and accelerates fibril growth is a widespread model to study amyloid formation. Seeding effects are hypothesized to be important in the "infectivity" of amyloids and are linked to the development of systemic amyloidosis in vivo. The exact mechanism of seeding is unclear yet critical to illuminating the propagation of amyloids. Here we report on the lateral and axial fragmentation of seed fibrils in the presence of lysozyme monomers at short time scales, followed by the generation of oligomers and growth of fibrils.
AU  - Kubánková,M
AU  - Lin,X
AU  - Albrecht,T
AU  - Edel,JB
AU  - Kuimova,MK
DO  - 10.1021/acs.analchem.9b01221
EP  - 6886
PY  - 2019///
SN  - 0003-2700
SP  - 6880
TI  - Rapid fragmentation during seeded lysozyme aggregation revealed at the single molecule level
T2  - Analytical Chemistry
UR  - http://dx.doi.org/10.1021/acs.analchem.9b01221
UR  - https://www.ncbi.nlm.nih.gov/pubmed/30999745
UR  - http://hdl.handle.net/10044/1/69428
VL  - 91
ER  -

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Professor Joshua B. Edel

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