The DOI matches its Crossref record; 21 of the 21 references it cites were found in a registry or an index.
Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding
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Citations
Cites
Prusiner, S. B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13363 · Cited by 5,373
Transmissions to mice indicate that ‘new variant’ CJD is caused by the BSE agent
Bruce, M. E., Will, R. G., Ironside, J. W., McConnell, I., Drummond, D., Suttie, A., McCardle, L., Chree, A., Hope, J., Birkett, C., et al. (1997) · Nature · doi:10.1038/39057 · Cited by 1,967
Harper, J. D., & Lansbury, P. T. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.385 · Cited by 1,652
Cell-free formation of protease-resistant prion protein
Kocisko, D. A., Come, J. H., Priola, S. A., Chesebro, B., Raymond, G. J., Lansbury, P. T., & Caughey, B. (1994) · Nature · doi:10.1038/370471a0 · Cited by 883
Telling, G. C., Scott, M., Mastrianni, J., Gabizon, R., Torchia, M., Cohen, F. E., DeArmond, S. J., & Prusiner, S. B. (1995) · Cell · doi:10.1016/0092-8674(95)90236-8 · Cited by 857
Mouse polyclonal and monoclonal antibody to scrapie-associated fibril proteins
Kascsak, R. J., Rubenstein, R., Merz, P. A., Tonna-DeMasi, M., Fersko, R., Carp, R. I., Wisniewski, H. M., & Diringer, H. (1987) · Journal of Virology · doi:10.1128/jvi.61.12.3688-3693.1987 · Cited by 766
PATHOLOGIC CONFORMATIONS OF PRION PROTEINS
Cohen, F. E., & Prusiner, S. B. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.793 · Cited by 533
Variant Creutzfeldt-Jakob disease
Collinge, J. (1999) · The Lancet · doi:10.1016/s0140-6736(99)05128-4 · Cited by 512
Creutzfeldt–Jakob Disease and Related Transmissible Spongiform Encephalopathies
Johnson, R. T., & Gibbs, C. J. (1998) · New England Journal of Medicine · doi:10.1056/nejm199812313392707 · Cited by 373
Kocisko, D. A., Priola, S. A., Raymond, G. J., Chesebro, B., Lansbury, P. T., & Caughey, B. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.9.3923 · Cited by 341
Cited by
Caughey, B., & Lansbury, P. T. (2003) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.010302.081142 · Cited by 1,650
Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases
Soto, C., & Pritzkow, S. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0235-9 · Cited by 1,180
Self-citationDegradation of misfolded proteins in neurodegenerative diseases: Therapeutic targets and strategies
Ciechanover, A., & Kwon, Y. T. (2015) · Experimental & Molecular Medicine · doi:10.1038/emm.2014.117 · Cited by 898
Formation of native prions from minimal components in vitro
Deleault, N. R., Harris, B. T., Rees, J. R., & Supattapone, S. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702662104 · Cited by 631
The expanding amyloid family: Structure, stability, function, and pathogenesis
Sawaya, M. R., Hughes, M. P., Rodriguez, J. A., Riek, R., & Eisenberg, D. S. (2021) · Cell · doi:10.1016/j.cell.2021.08.013 · Cited by 475
Metadata
- Authors
- Saborio, G. P., Permanne, B., & Soto, C.
- Venue
- Nature
- Published
- 2001-06-14
- Volume
- 411
- Issue
- 6839
- Pages
- 810-813
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2138468217
- Cited by
- 1,310
- References
- 21
- FWCI
- 14.44
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. https://app.cochat.ai/papers/10.1038/35081095
- The paper
- Saborio, G. P., Permanne, B., & Soto, C. (2001). Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature. https://doi.org/10.1038/35081095
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.
