The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index.
Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation
Open accessAbstract
It is increasingly recognized that molecular chaperones play a key role in modulating the formation of amyloid fibrils, a process associated with a wide range of human disorders. Understanding the detailed mechanisms by which they perform this function, however, has been challenging because of the great complexity of the protein aggregation process itself. In this work, we build on a previous kinetic approach and develop a model that considers pairwise interactions between molecular chaperones and different protein species to identify the protein components targeted by the chaperones and the corresponding microscopic reaction steps that are inhibited. We show that these interactions conserve the topology of the unperturbed reaction network but modify the connectivity weights between the different microscopic steps. Moreover, by analysing several protein-molecular chaperone systems, we reveal the striking diversity in the microscopic mechanisms by which molecular chaperones act to suppress amyloid formation.
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Cites
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Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
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Self-citationMolecular chaperones in protein folding and proteostasis
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Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein
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Adapting Proteostasis for Disease Intervention
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Self-citationThe Amyloid State of Proteins in Human Diseases
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Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism
Cohen, S. I. A., Linse, S., Luheshi, L. M., Hellstrand, E., White, D. A., Rajah, L., Otzen, D. E., Vendruscolo, M., Dobson, C. M., & Knowles, T. P. J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1218402110 · Cited by 1,440
Self-citationEGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers
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Cited by
Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade
Chiti, F., & Dobson, C. M. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-045115 · Cited by 2,629
Self-citationUpdate on Alzheimer’s Disease Therapy and Prevention Strategies
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AlphaFold and the amyloid landscape
Pinheiro, F., Santos, J., & Ventura, S. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167059 · Cited by 88
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Abelein, A., Ciofi-Baffoni, S., Mörman, C., Kumar, R., Giachetti, A., Piccioli, M., & Biverstål, H. (2022) · JACS Au · doi:10.1021/jacsau.2c00438 · Cited by 52
Metadata
- Authors
- Arosio, P., Michaels, T. C. T., Linse, S., Månsson, C., Emanuelsson, C., Presto, J., Johansson, J., Vendruscolo, M., Dobson, C. M., & Knowles, T. P. J.
- Venue
- Nature Communications
- Published
- 2016-03-24
- Volume
- 7
- Issue
- 1
- Pages
- 10948-10948
- ISSN
- 2041-1723 (ISSN-L)
- OpenAlex
- W2309071467
- Cited by
- 265
- References
- 48
- FWCI
- 13.39
- Type
- journal article
- Language
- en
- Open access
- gold
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- Arosio, P., Michaels, T. C. T., Linse, S., Månsson, C., Emanuelsson, C., Presto, J., Johansson, J., Vendruscolo, M., Dobson, C. M., & Knowles, T. P. J. (2016). Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation. Nature Communications. https://doi.org/10.1038/ncomms10948
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