The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
Amyloid fibrils from muscle myoglobin
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Citations
Cites
Principles that Govern the Folding of Protein Chains
Anfinsen, C. B. (1973) · Science · doi:10.1126/science.181.4096.223 · Cited by 7,096
Prusiner, S. B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13363 · Cited by 5,373
Protein misfolding, evolution and disease
Dobson, C. M. (1999) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01445-0 · Cited by 1,952
Self-citationStructure of Myoglobin: A Three-Dimensional Fourier Synthesis at 2 Å. Resolution
KENDREW, J. C., DICKERSON, R. E., STRANDBERG, B. E., HART, R. G., DAVIES, D. R., PHILLIPS, D. C., & SHORE, V. C. (1960) · Nature · doi:10.1038/185422a0 · Cited by 1,352
Cleavage of the haem-protein link by acid methylethylketone
Teale, F. W. J. (1959) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(59)90407-x · Cited by 1,236
Amyloid fibrillogenesis: themes and variations
Rochet, J.-C., & Lansbury, P. T. (2000) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(99)00049-4 · Cited by 1,095
Designing conditions for in vitro formation of amyloid protofilaments and fibrils
Chiti, F., Webster, P., Taddei, N., Clark, A., Stefani, M., Ramponi, G., & Dobson, C. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.7.3590 · Cited by 1,039
Self-citationSUNDE, M., & BLAKE, C. C. F. (1998) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583598003400 · Cited by 457
Eliezer, D., Yao, J., Dyson, H. J., & Wright, P. E. (1998) · Nature Structural Biology · doi:10.1038/nsb0298-148 · Cited by 371
TAN, S. Y., & PEPYS, M. B. (1994) · Histopathology · doi:10.1111/j.1365-2559.1994.tb00001.x · Cited by 230
Cited by
Fabrication of novel biomaterials through molecular self-assembly
Zhang, S. (2003) · Nature Biotechnology · doi:10.1038/nbt874 · Cited by 3,347
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Zurdo, J., Taddei, N., Ramponi, G., Dobson, C. M., & Stefani, M. (2002) · Nature · doi:10.1038/416507a · Cited by 2,434
Self-citationUnfolding the role of protein misfolding in neurodegenerative diseases
Soto, C. (2003) · Nature Reviews Neuroscience · doi:10.1038/nrn1007 · Cited by 1,506
Aggeli, A., Nyrkova, I. A., Bell, M., Harding, R., Carrick, L., McLeish, T. C. B., Semenov, A. N., & Boden, N. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.191250198 · 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
Metadata
- Authors
- Fändrich, M., Fletcher, M. A., & Dobson, C. M.
- Venue
- Nature
- Published
- 2001-03
- Volume
- 410
- Issue
- 6825
- Pages
- 165-166
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2089491263
- Cited by
- 799
- References
- 10
- FWCI
- 16.72
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Amyloid fibrils from muscle myoglobin. https://app.cochat.ai/papers/10.1038/35065514
- The paper
- Fändrich, M., Fletcher, M. A., & Dobson, C. M. (2001). Amyloid fibrils from muscle myoglobin. Nature. https://doi.org/10.1038/35065514
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.