Samo Curk
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Samo Curk has a total of 8 co-authors. Here are the top co-authors by number of shared publications:
- Anđela Šarić
Institute of Science and Technology Austria, Klosterneuburg, Austria
2 shared publications - Daan Frenkel
Yusuf Hamied Department of Chemistry, University of Cambridge , Lensfield Road, Cambridge CB2 1EW
2 shared publications - Georg Meisl
Yusuf Hamied Department of Chemistry University of Cambridge Cambridge UK
2 shared publications - Johannes Krausser
Department of Physics and Astronomy, Laboratory for Molecular Cell Biology, University College London, London WC1E 6BT, United Kingdom
2 shared publications - Sara Linse
Biochemistry and Structural Biology, Lund University, Lund, Sweden
2 shared publications - Thomas C. T. Michaels
Department of Biology, Institute of Biochemistry, ETH Zurich, Zurich, Switzerland
2 shared publications
Latest Publications
- Open Access
- 9 February 2024
- Published by National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 121 (7)
Self-replication of A β 42 aggregates occurs on small and isolated fibril sites
Self-replication of amyloid fibrils via secondary nucleation is an intriguing physicochemical phenomenon in which existing fibrils catalyze the formation of their own copies. The molecular events behind this fibril surface-mediated process remain largely inaccessible to current structural and imaging techniques. Using statistical mechanics, computer modeling, and chemical kinetics, we show that the catalytic structure of the fibril surface can be inferred from the aggregation behavior in the presence and absence of a fibril-binding inhibitor. We apply our approach to the case of Alzheimer’s A β 42 amyloid fibrils formed in the presence of proSP-C Brichos inhibitors. We find that self-replication of A β 42 fibrils occurs on small catalytic sites on the fibril surface, which are far apart from each other, and each of which can be covered by a single Brichos inhibitor.
- 9 February 2024
- Published by National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 121 (7)
Open AccessSelf-replication of A β 42 aggregates occurs on small and isolated fibril sites
Self-replication of amyloid fibrils via secondary nucleation is an intriguing physicochemical phenomenon in which existing fibrils catalyze the formation of their own copies. The molecular events behind this fibril surface-mediated process remain largely inaccessible to current structural and imaging techniques. Using statistical mechanics, computer modeling, and chemical kinetics, we show that the catalytic structure of the fibril surface can be inferred from the aggregation behavior in the presence and absence of a fibril-binding inhibitor. We apply our approach to the case of Alzheimer’s A β 42 amyloid fibrils formed in the presence of proSP-C Brichos inhibitors. We find that self-replication of A β 42 fibrils occurs on small catalytic sites on the fibril surface, which are far apart from each other, and each of which can be covered by a single Brichos inhibitor.
- Open Access
Self-replication of A β 42 aggregates occurs on small and isolated fibril sites
Self-replication of amyloid fibrils via secondary nucleation is an intriguing physicochemical phenomenon in which existing fibrils catalyse the formation of their own copies. The molecular events behind this fibril surface-mediated process remain largely inaccessible to current structural and imaging techniques. Using statistical mechanics, computer modelling, and chemical kinetics, we show that the catalytic structure of the fibril surface can be inferred from the aggregation behaviour in the presence and absence of a fibril-binding inhibitor. We apply our approach to the case of Alzheimer’s A β 42 amyloid fibrils formed in the presence of proSP-C Brichos inhibitors. We find that self-replication of A β 42 fibrils occurs on small catalytic sites on the fibril surface, which are far apart from each other, and each of which can be covered by a single Brichos inhibitor.
Open AccessSelf-replication of A β 42 aggregates occurs on small and isolated fibril sites
Self-replication of amyloid fibrils via secondary nucleation is an intriguing physicochemical phenomenon in which existing fibrils catalyse the formation of their own copies. The molecular events behind this fibril surface-mediated process remain largely inaccessible to current structural and imaging techniques. Using statistical mechanics, computer modelling, and chemical kinetics, we show that the catalytic structure of the fibril surface can be inferred from the aggregation behaviour in the presence and absence of a fibril-binding inhibitor. We apply our approach to the case of Alzheimer’s A β 42 amyloid fibrils formed in the presence of proSP-C Brichos inhibitors. We find that self-replication of A β 42 fibrils occurs on small catalytic sites on the fibril surface, which are far apart from each other, and each of which can be covered by a single Brichos inhibitor.