The DOI matches its Crossref record; 40 of the 40 references it cites were found in a registry or an index.
Alternative conformations of amyloidogenic proteins govern their behavior
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Cites
Pan, K. M., Baldwin, M., Nguyen, J., Gasset, M., Serban, A., Groth, D., Mehlhorn, I., Huang, Z., Fletterick, R. J., & Cohen, F. E. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.23.10962 · Cited by 2,277
Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids
Seubert, P., Vigo-Pelfrey, C., Esch, F., Lee, M., Dovey, H., Davis, D., Sinha, S., Schiossmacher, M., Whaley, J., Swindlehurst, C., et al. (1992) · Nature · doi:10.1038/359325a0 · Cited by 1,731
Production of the Alzheimer Amyloid β Protein by Normal Proteolytic Processing
Shoji, M., Golde, T. E., Ghiso, J., Cheung, T. T., Estus, S., Shaffer, L. M., Cai, X.-D., McKay, D. M., Tintner, R., Frangione, B., et al. (1992) · Science · doi:10.1126/science.1439760 · Cited by 1,447
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
Caughey, B. W., Dong, A., Bhat, K. S., Ernst, D., Hayes, S. F., & Caughey, W. S. (1991) · Biochemistry · doi:10.1021/bi00245a003 · Cited by 822
Blake, C. C. F., Geisow, M. J., Oatley, S. J., Rérat, B., & Rérat, C. (1978) · Journal of Molecular Biology · doi:10.1016/0022-2836(78)90368-6 · Cited by 791
Human lysozyme gene mutations cause hereditary systemic amyloidosis
Pepys, M. B., Hawkins, P. N., Booth, D. R., Vigushin, D. M., Tennent, G. A., Soutar, A. K., Totty, N., Nguyen, O., Blake, C. C. F., Terry, C. J., et al. (1993) · Nature · doi:10.1038/362553a0 · Cited by 657
Lai, Z., Colón, W., & Kelly, J. W. (1996) · Biochemistry · doi:10.1021/bi952501g · Cited by 574
Self-citationPartial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro
Colon, W., & Kelly, J. W. (1992) · Biochemistry · doi:10.1021/bi00151a036 · Cited by 573
Self-citationNon-genetic propagation of strain-specific properties of scrapie prion protein
Bessen, R. A., Kocisko, D. A., Raymond, G. J., Nandan, S., Lansbury, P. T., & Caughey, B. (1995) · Nature · doi:10.1038/375698a0 · Cited by 525
Cited by
Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
Booth, D. R., Sunde, M., Bellotti, V., Robinson, C. V., Hutchinson, W. L., Fraser, P. E., Hawkins, P. N., Dobson, C. M., Radford, S. E., Blake, C. C. F., et al. (1997) · Nature · doi:10.1038/385787a0 · Cited by 1,048
Conformational constraints for amyloid fibrillation: the importance of being unfolded
Uversky, V. N., & Fink, A. L. (2004) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2003.12.008 · Cited by 1,015
Protein transmission in neurodegenerative disease
Peng, C., Trojanowski, J. Q., & Lee, V. M.-Y. (2020) · Nature Reviews Neurology · doi:10.1038/s41582-020-0333-7 · Cited by 625
Nanohedra: Using symmetry to design self assembling protein cages, layers, crystals, and filaments
Padilla, J. E., Colovos, C., & Yeates, T. O. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.041614998 · Cited by 441
Lindgren, M., Sörgjerd, K., & Hammarström, P. (2005) · Biophysical Journal · doi:10.1529/biophysj.104.049700 · Cited by 349
Metadata
- Authors
- Kelly, J. W.
- Venue
- Current Opinion in Structural Biology
- Publisher
- Elsevier BV
- Published
- 1996-02
- Volume
- 6
- Issue
- 1
- Pages
- 11-17
- ISSN
- 0959-440X (ISSN-L)
- OpenAlex
- W2090797167
- Cited by
- 593
- References
- 40
- FWCI
- 5.01
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Alternative conformations of amyloidogenic proteins govern their behavior. https://app.cochat.ai/papers/10.1016/s0959-440x(96)80089-3
- The paper
- Kelly, J. W. (1996). Alternative conformations of amyloidogenic proteins govern their behavior. Current Opinion in Structural Biology. https://doi.org/10.1016/s0959-440x(96)80089-3
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.
