- Abstract:
-
The measurement of molecular interactions with pathological protein aggregates, including amyloid fibrils, is of central importance in the context of the development of diagnostic and therapeutic strategies against protein misfolding disorders. Probing such interactions by conventional methods can, however, be challenging because of the supramolecular nature of protein aggregates, their heterogeneity, and their often dynamic nature. Here we demonstrate that direct measurement of diffusion on ...
Expand abstract - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Version:
- Accepted Manuscript
- Files:
-
-
(pdf, 36.7mb)
-
- Publisher copy:
- 10.1002/cbic.201600384
-
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- Publisher:
- Wiley-VCH Verlag Publisher's website
- Journal:
- ChemBioChem Journal website
- Volume:
- 17
- Issue:
- 20
- Pages:
- 1920-1924
- Publication date:
- 2016-07-29
- DOI:
- EISSN:
-
1439-7633
- ISSN:
-
1439-4227
- Pubs id:
-
pubs:640790
- URN:
-
uri:3db31f19-be45-40f6-ae3b-006b3251c881
- UUID:
-
uuid:3db31f19-be45-40f6-ae3b-006b3251c881
- Local pid:
- pubs:640790
- Language:
- English
- Keywords:
- Copyright holder:
- Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim
- Copyright date:
- 2016
- Notes:
-
Copyright © 2016 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim. This is the accepted manuscript version of the article. The final version is available online from Wiley-VCH Verlag at: https://doi.org/10.1002/cbic.201600384
Journal article
Protein aggregate-ligand binding assays based on microfluidic diffusional separation
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