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- 2022
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Mark
Role of Hydrophobicity at the N-Terminal Region of Aβ42 in Secondary Nucleation
(
- Contribution to journal › Article
- 2021
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Mark
pH-Responsive Capsules with a Fibril Scaffold Shell Assembled from an Amyloidogenic Peptide
(
- Contribution to journal › Article
- 2020
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Mark
The properties of α-synuclein secondary nuclei are dominated by the solution conditions rather than the seed fibril strain
(
- Contribution to journal › Article
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Mark
Kinetic diversity of amyloid oligomers
(
- Contribution to journal › Article
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Mark
Thermodynamic and kinetic design principles for amyloid-aggregation inhibitors
2020) In Proceedings of the National Academy of Sciences of the United States of America 117(39). p.24251-24257(
- Contribution to journal › Article
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Mark
The role of fibril structure and surface hydrophobicity in secondary nucleation of amyloid fibrils
2020) In Proceedings of the National Academy of Sciences of the United States of America 117(41). p.25272-25283(
- Contribution to journal › Article
- 2018
-
Mark
On the role of sidechain size and charge in the aggregation of Aβ42 with familial mutations
2018) In Proceedings of the National Academy of Sciences of the United States of America 115(26). p.5849-5858(
- Contribution to journal › Article
- 2016
-
Mark
Analysis of the length distribution of amyloid fibrils by centrifugal sedimentation
(
- Contribution to journal › Article
- 2014
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Mark
The chaperone domain BRICHOS prevents CNS toxicity of amyloid-beta peptide in Drosophila melanogaster
(
- Contribution to journal › Article
- 2010
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Mark
Amyloid beta-Protein Aggregation Produces Highly Reproducible Kinetic Data and Occurs by a Two-Phase Process
(
- Contribution to journal › Article