The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Protein aggregation kinetics, mechanism, and curve-fitting: A review of the literature
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Citations
Cites
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
Shankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., Brett, F. M., Farrell, M. A., Rowan, M. J., Lemere, C. A., et al. (2008) · Nature Medicine · doi:10.1038/nm1782 · Cited by 3,685
Aβ Oligomers – a decade of discovery
Walsh, D. M., & Selkoe, D. J. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04426.x · Cited by 1,938
Caughey, B., & Lansbury, P. T. (2003) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.010302.081142 · Cited by 1,650
Evidence for a Partially Folded Intermediate in α-Synuclein Fibril Formation
Uversky, V. N., Li, J., & Fink, A. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010907200 · Cited by 1,096
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
Three-dimensional reconstruction of the 14-filament fibers of hemoglobin S
Dykes, G. W., Crepeau, R. H., & Edelstein, S. J. (1979) · Journal of Molecular Biology · doi:10.1016/0022-2836(79)90434-0 · Cited by 186
Cited by
Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade
Chiti, F., & Dobson, C. M. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-045115 · Cited by 2,629
Therapeutic protein aggregation: mechanisms, design, and control
Roberts, C. J. (2014) · Trends in Biotechnology · doi:10.1016/j.tibtech.2014.05.005 · Cited by 455
Recent advances in our understanding of neurodegeneration
Jellinger, K. A. (2009) · Journal of Neural Transmission · doi:10.1007/s00702-009-0240-y · Cited by 274
Production of prone-to-aggregate proteins
Lebendiker, M., & Danieli, T. (2014) · FEBS Letters · doi:10.1016/j.febslet.2013.10.044 · Cited by 163
Bentea, L., Watzky, M. A., & Finke, R. G. (2017) · The Journal of Physical Chemistry C · doi:10.1021/acs.jpcc.6b12021 · Cited by 154
Self-citation
Metadata
- Authors
- Morris, A. M., Watzky, M. A., & Finke, R. G.
- Venue
- Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
- Publisher
- Elsevier BV
- Published
- 2009-03
- Volume
- 1794
- Issue
- 3
- Pages
- 375-397
- ISSN
- 1570-9639 (ISSN-L)
- OpenAlex
- W1965420960
- Cited by
- 680
- References
- 7
- FWCI
- 14.88
- 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: Protein aggregation kinetics, mechanism, and curve-fitting: A review of the literature. https://app.cochat.ai/papers/10.1016/j.bbapap.2008.10.016
- The paper
- Morris, A. M., Watzky, M. A., & Finke, R. G. (2009). Protein aggregation kinetics, mechanism, and curve-fitting: A review of the literature. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. https://doi.org/10.1016/j.bbapap.2008.10.016
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.