The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.
The structural basis of yeast prion strain variants
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Cites
NMRPipe: A multidimensional spectral processing system based on UNIX pipes
Delaglio, F., Grzesiek, S., Vuister, G., Zhu, G., Pfeifer, J., & Bax, A. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00197809 · Cited by 15,965
Protein Misfolding, Functional Amyloid, and Human Disease
Chiti, F., & Dobson, C. M. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.101304.123901 · Cited by 6,423
Atomic structures of amyloid cross-β spines reveal varied steric zippers
Sawaya, M. R., Sambashivan, S., Nelson, R., Ivanova, M. I., Sievers, S. A., Apostol, M. I., Thompson, M. J., Balbirnie, M., Wiltzius, J. J. W., McFarlane, H. T., et al. (2007) · Nature · doi:10.1038/nature05695 · Cited by 2,271
University of California, San Francisco
(1974) · Medical History · doi:10.1017/s0025727300019682 · Cited by 2,222
Structure of the cross-β spine of amyloid-like fibrils
Nelson, R., Sawaya, M. R., Balbirnie, M., Madsen, A. Ø., Riekel, C., Grothe, R., & Eisenberg, D. (2005) · Nature · doi:10.1038/nature03680 · Cited by 2,202
3D structure of Alzheimer's amyloid-β(1–42) fibrils
Lührs, T., Ritter, C., Adrian, M., Riek-Loher, D., Bohrmann, B., Döbeli, H., Schubert, D., & Riek, R. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506723102 · Cited by 1,996
Sattler, M. (1999) · Progress in Nuclear Magnetic Resonance Spectroscopy · doi:10.1016/s0079-6565(98)00025-9 · Cited by 1,722
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-citationGlover, J. R., Kowal, A. S., Schirmer, E. C., Patino, M. M., Liu, J.-J., & Lindquist, S. (1997) · Cell · doi:10.1016/s0092-8674(00)80264-0 · Cited by 597
The physical basis of how prion conformations determine strain phenotypes
Tanaka, M., Collins, S. R., Toyama, B. H., & Weissman, J. S. (2006) · Nature · doi:10.1038/nature04922 · Cited by 593
Self-citation
Cited by
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
Distinct Tau Prion Strains Propagate in Cells and Mice and Define Different Tauopathies
Sanders, D. W., Kaufman, S. K., DeVos, S. L., Sharma, A. M., Mirbaha, H., Li, A., Barker, S. J., Foley, A. C., Thorpe, J. R., Serpell, L. C., et al. (2014) · Neuron · doi:10.1016/j.neuron.2014.04.047 · Cited by 986
Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging
Morimoto, R. I. (2008) · Genes & Development · doi:10.1101/gad.1657108 · Cited by 872
Structural Classification of Toxic Amyloid Oligomers
Glabe, C. G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800016200 · Cited by 783
Prion-like mechanisms in neurodegenerative diseases
Frost, B., & Diamond, M. I. (2010) · Nature Reviews Neuroscience · doi:10.1038/nrn2786 · Cited by 776
Metadata
- Authors
- Toyama, B. H., Kelly, M. J. S., Gross, J. D., & Weissman, J. S.
- Venue
- Nature
- Published
- 2007-09-02
- Volume
- 449
- Issue
- 7159
- Pages
- 233-237
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1979575360
- Cited by
- 338
- References
- 32
- FWCI
- 11.97
- Type
- journal article
- Language
- en
- Open access
- closed
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- Toyama, B. H., Kelly, M. J. S., Gross, J. D., & Weissman, J. S. (2007). The structural basis of yeast prion strain variants. Nature. https://doi.org/10.1038/nature06108
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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.