The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
Principles of protein folding, misfolding and aggregation
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Cites
Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291
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
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-citationFrom Levinthal to pathways to funnels
Dill, K. A., & Chan, H. S. (1997) · Nature Structural & Molecular Biology · doi:10.1038/nsb0197-10 · Cited by 2,293
Crystal structure of the ribosome at 5.5 Å resolution
Yusupov, M. M., Yusupova, G. Z., Baucom, A., Lieberman, K., Earnest, T. N., Cate, J. H. D., & Noller, H. F. (2001) · Science · doi:10.1126/science.1060089 · Cited by 1,944
Caughey, B., & Lansbury, P. T. (2003) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.010302.081142 · Cited by 1,650
Unfolding the role of protein misfolding in neurodegenerative diseases
Soto, C. (2003) · Nature Reviews Neuroscience · doi:10.1038/nrn1007 · Cited by 1,506
Rationalization of the effects of mutations on peptide andprotein aggregation rates
Chiti, F., Stefani, M., Taddei, N., Ramponi, G., & Dobson, C. M. (2003) · Nature · doi:10.1038/nature01891 · Cited by 1,072
Self-citationEllis, R. J., & Minton, A. P. (2003) · Nature · doi:10.1038/425027a · Cited by 894
Targeted pharmacological depletion of serum amyloid P component for treatment of human amyloidosis
Pepys, M. B., Herbert, J., Hutchinson, W. L., Tennent, G. A., Lachmann, H. J., Gallimore, J. R., Lovat, L. B., Bartfai, T., Alanine, A., Hertel, C., et al. (2002) · Nature · doi:10.1038/417254a · Cited by 540
Cited by
Protein aggregation and neurodegenerative disease
Ross, C. A., & Poirier, M. A. (2004) · Nature Medicine · doi:10.1038/nm1066 · Cited by 3,454
Islet Amyloid Polypeptide, Islet Amyloid, and Diabetes Mellitus
Westermark, P., Andersson, A., & Westermark, G. T. (2011) · Physiological Reviews · doi:10.1152/physrev.00042.2009 · Cited by 1,044
Protein quality control in the early secretory pathway
Anelli, T., & Sitia, R. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601974 · Cited by 623
Xie, H., Vucetic, S., Iakoucheva, L. M., Oldfield, C. J., Dunker, A. K., Obradovic, Z., & Uversky, V. N. (2007) · Journal of Proteome Research · doi:10.1021/pr060394e · Cited by 382
Andrews, J. M., & Roberts, C. J. (2007) · The Journal of Physical Chemistry B · doi:10.1021/jp070212j · Cited by 250
Metadata
- Authors
- Dobson, C. M.
- Venue
- Seminars in Cell & Developmental Biology
- Publisher
- Elsevier BV
- Published
- 2004-02
- Volume
- 15
- Issue
- 1
- Pages
- 3-16
- ISSN
- 1084-9521 (ISSN-L)
- OpenAlex
- W2058469726
- Cited by
- 904
- References
- 12
- FWCI
- 17.93
- Type
- journal article
- Language
- en
- Open access
- closed
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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- CoChat. (2026). Citation check: Principles of protein folding, misfolding and aggregation. https://app.cochat.ai/papers/10.1016/j.semcdb.2003.12.008
- The paper
- Dobson, C. M. (2004). Principles of protein folding, misfolding and aggregation. Seminars in Cell & Developmental Biology. https://doi.org/10.1016/j.semcdb.2003.12.008
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.
