The DOI matches its Crossref record; 151 of the 151 references it cites were found in a registry or an index.
Oligomeric Intermediates in Amyloid Formation: Structure Determination and Mechanisms of Toxicity
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Citations
Cites
2 retracted
RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
Lesné, S., Koh, M. T., Kotilinek, L., Kayed, R., Glabe, C. G., Yang, A., Gallagher, M., & Ashe, K. H. (2006) · Nature · doi:10.1038/nature04533 · Cited by 2,769
RetractedTsigelny, I. F., Crews, L., Desplats, P., Shaked, G. M., Sharikov, Y., Mizuno, H., Spencer, B., Rockenstein, E., Trejo, M., Platoshyn, O., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003135 · Cited by 281
RetractedPrusiner, S. B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13363 · Cited by 5,373
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744
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
Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β
Nakagawa, T., Zhu, H., Morishima, N., Li, E., Xu, J., Yankner, B. A., & Yuan, J. (2000) · Nature · doi:10.1038/47513 · Cited by 3,256
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
1H, 13C and 15N chemical shift referencing in biomolecular NMR
Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., & Sykes, B. D. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00211777 · Cited by 2,359
Atomic structures of amyloid cross-β spines reveal varied steric zippers
Sawaya, M. R., Sambashivan, S., Nelson, R., Ivanova, M. I., Sievers, S. A., Apostol, M. I., Thompson, M. J., Balbirnie, M., Wiltzius, J. J. W., McFarlane, H. T., et al. (2007) · Nature · doi:10.1038/nature05695 · Cited by 2,271
Cited by
ThT 101: a primer on the use of thioflavin T to investigate amyloid formation
Gade Malmos, K., Blancas-Mejia, L. M., Weber, B., Buchner, J., Ramirez-Alvarado, M., Naiki, H., & Otzen, D. (2017) · Amyloid · doi:10.1080/13506129.2017.1304905 · Cited by 445
Neuropathology and biochemistry of Aβ and its aggregates in Alzheimer’s disease
Thal, D. R., Walter, J., Saido, T. C., & Fändrich, M. (2015) · Acta Neuropathologica · doi:10.1007/s00401-014-1375-y · Cited by 319
Self-citationAA Amyloidosis: Pathogenesis and Targeted Therapy
Westermark, G. T., Fändrich, M., & Westermark, P. (2015) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathol-020712-163913 · Cited by 264
Self-citationGoure, W. F., Krafft, G. A., Jerecic, J., & Hefti, F. (2014) · Alzheimer's Research & Therapy · doi:10.1186/alzrt272 · Cited by 190
Galectin-3 promotes Aβ oligomerization and Aβ toxicity in a mouse model of Alzheimer’s disease
Tao, C.-C., Cheng, K.-M., Ma, Y.-L., Hsu, W.-L., Chen, Y.-C., Fuh, J.-L., Lee, W.-J., Chao, C.-C., & Lee, E. H. Y. (2020) · Cell Death & Differentiation · doi:10.1038/s41418-019-0348-z · Cited by 138
Metadata
- Authors
- Fändrich, M.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2012-08
- Volume
- 421
- Issue
- 4-5
- Pages
- 427-440
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W2039706105
- Cited by
- 340
- References
- 151
- FWCI
- 23.59
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Oligomeric Intermediates in Amyloid Formation: Structure Determination and Mechanisms of Toxicity. https://app.cochat.ai/papers/10.1016/j.jmb.2012.01.006
- The paper
- Fändrich, M. (2012). Oligomeric Intermediates in Amyloid Formation: Structure Determination and Mechanisms of Toxicity. Journal of Molecular Biology. https://doi.org/10.1016/j.jmb.2012.01.006
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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.
