The DOI matches its Crossref record; 149 of the 149 references it cites were found in a registry or an index.
Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world
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Cites
Prusiner, S. B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13363 · Cited by 5,373
Lusis, A. J. (2000) · Nature · doi:10.1038/35025203 · Cited by 4,839
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064
A map of human genome sequence variation containing 1.42 million single nucleotide polymorphisms
The International SNP Map Working Group, Laboratories:, C. S. H., Sachidanandam, R., Weissman, D., Schmidt, S. C., Kakol, J. M., Stein, L. D., National Center for Biotechnology Information:, Marth, G., Sherry, S., et al. (2001) · Nature · doi:10.1038/35057149 · Cited by 2,977
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-citationProtein degradation and protection against misfolded or damaged proteins.
Goldberg, A. L. (2003) · Nature · doi:10.1038/nature02263 · Cited by 2,088
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
Aggresomes, inclusion bodies and protein aggregation
Kopito, R. R. (2000) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)01852-3 · Cited by 1,921
Common core structure of amyloid fibrils by synchrotron X-ray diffraction 1 1Edited by F. E. Cohen
Sunde, M., Serpell, L. C., Bartlam, M., Fraser, P. E., Pepys, M. B., & Blake, C. C. F. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1348 · Cited by 1,707
Stefani, M., & Dobson, C. M. (2003) · Journal of Molecular Medicine · doi:10.1007/s00109-003-0464-5 · Cited by 1,651
Self-citation
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The DIX domain of Dishevelled confers Wnt signaling by dynamic polymerization
Schwarz-Romond, T., Fiedler, M., Shibata, N., Butler, P. J. G., Kikuchi, A., Higuchi, Y., & Bienz, M. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1247 · Cited by 435
Folding versus aggregation: Polypeptide conformations on competing pathways
Jahn, T. R., & Radford, S. E. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.05.015 · Cited by 428
Chaperones in control of protein disaggregation
Liberek, K., Lewandowska, A., & Ziętkiewicz, S. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601970 · Cited by 425
Oxidative Stress in Neurodegenerative Diseases
(2013) · Metal‐based Neurodegeneration · doi:10.1002/9781118553480.ch04 · Cited by 371
Metadata
- Authors
- Stefani, M.
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
- Publisher
- Elsevier BV
- Published
- 2004-12
- Volume
- 1739
- Issue
- 1
- Pages
- 5-25
- ISSN
- 0925-4439 (ISSN-L)
- OpenAlex
- W2097647470
- Cited by
- 428
- References
- 149
- FWCI
- 5.47
- Type
- journal article
- Language
- en
- Open access
- bronze
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- CoChat. (2026). Citation check: Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world. https://app.cochat.ai/papers/10.1016/j.bbadis.2004.08.004
- The paper
- Stefani, M. (2004). Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world. Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. https://doi.org/10.1016/j.bbadis.2004.08.004
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.
