The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.
The physical basis of how prion conformations determine strain phenotypes
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Citations
Cites
Protein folding and misfolding
Dobson, C. M. (2003) · Nature · doi:10.1038/nature02261 · Cited by 4,791
Caughey, B., & Lansbury, P. T. (2003) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.010302.081142 · Cited by 1,650
Prion Diseases of Humans and Animals: Their Causes and Molecular Basis
Collinge, J. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.519 · Cited by 1,344
[URE3] as an Altered URE2 Protein: Evidence for a Prion Analog in Saccharomyces cerevisiae
Wickner, R. B. (1994) · Science · doi:10.1126/science.7909170 · Cited by 1,209
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The most infectious prion protein particles
Silveira, J. R., Raymond, G. J., Hughson, A. G., Race, R. E., Sim, V. L., Hayes, S. F., & Caughey, B. (2005) · Nature · doi:10.1038/nature03989 · Cited by 899
In Vitro Generation of Infectious Scrapie Prions
Castilla, J., Saá, P., Hetz, C., & Soto, C. (2005) · Cell · doi:10.1016/j.cell.2005.02.011 · Cited by 790
Conformational variations in an infectious protein determine prion strain differences
Tanaka, M., Chien, P., Naber, N., Cooke, R., & Weissman, J. S. (2004) · Nature · doi:10.1038/nature02392 · Cited by 770
Self-citationPrions as adaptive conduits of memory and inheritance
Shorter, J., & Lindquist, S. (2005) · Nature Reviews Genetics · doi:10.1038/nrg1616 · Cited by 555
Genesis and Variability of [PSI] Prion Factors in Saccharomyces cerevisiae
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Cited by
The amyloid state and its association with protein misfolding diseases.
Knowles, T. P. J., Vendruscolo, M., & Dobson, C. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3810 · Cited by 2,382
The Amyloid State of Proteins in Human Diseases
Eisenberg, D., & Jucker, M. (2012) · Cell · doi:10.1016/j.cell.2012.02.022 · Cited by 1,744
Self-propagation of pathogenic protein aggregates in neurodegenerative diseases
Jucker, M., & Walker, L. C. (2013) · Nature · doi:10.1038/nature12481 · Cited by 1,663
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
Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils
Paravastu, A. K., Leapman, R. D., Yau, W.-M., & Tycko, R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0806270105 · Cited by 1,160
Metadata
- Authors
- Tanaka, M., Collins, S. R., Toyama, B. H., & Weissman, J. S.
- Venue
- Nature
- Published
- 2006-06-28
- Volume
- 442
- Issue
- 7102
- Pages
- 585-589
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1978959047
- Cited by
- 593
- References
- 29
- FWCI
- 13.38
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: The physical basis of how prion conformations determine strain phenotypes. https://app.cochat.ai/papers/10.1038/nature04922
- The paper
- Tanaka, M., Collins, S. R., Toyama, B. H., & Weissman, J. S. (2006). The physical basis of how prion conformations determine strain phenotypes. Nature. https://doi.org/10.1038/nature04922
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
