The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers
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Citations
Cites
Protein folding and misfolding
Dobson, C. M. (2003) · Nature · doi:10.1038/nature02261 · Cited by 4,791
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
[18] Quantification of β-sheet amyloid fibril structures with thioflavin T
LeVine, H. (1999) · Methods in Enzymology · doi:10.1016/s0076-6879(99)09020-5 · Cited by 1,365
Iwai, A., Masliah, E., Yoshimoto, M., Ge, N., Flanagan, L., Rohan de Silva, H. A., Kittel, A., & Saitoh, T. (1995) · Neuron · doi:10.1016/0896-6273(95)90302-x · Cited by 1,316
Toxic Proteins in Neurodegenerative Disease
Taylor, J. P., Hardy, J., & Fischbeck, K. H. (2002) · Science · doi:10.1126/science.1067122 · Cited by 1,251
Amyloid β-Protein Fibrillogenesis
Walsh, D. M., Hartley, D. M., Kusumoto, Y., Fezoui, Y., Condron, M. M., Lomakin, A., Benedek, G. B., Selkoe, D. J., & Teplow, D. B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25945 · Cited by 1,046
Cited by
Plant Polyphenols: Chemical Properties, Biological Activities, and Synthesis
Quideau, S., Deffieux, D., Douat‐Casassus, C., & Pouységu, L. (2011) · Angewandte Chemie International Edition · doi:10.1002/anie.201000044 · Cited by 2,730
Nguyen, P. H., Ramamoorthy, A., Sahoo, B. R., Zheng, J., Faller, P., Straub, J. E., Dominguez, L., Shea, J.-E., Dokholyan, N. V., De Simone, A., et al. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c01122 · Cited by 678
α-Synuclein misfolding and Parkinson's disease
Breydo, L., Wu, J. W., & Uversky, V. N. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.10.002 · Cited by 657
Lee, S. J. C., Nam, E., Lee, H. J., Savelieff, M. G., & Lim, M. H. (2017) · Chemical Society Reviews · doi:10.1039/c6cs00731g · Cited by 576
Using Graphene Oxide High Near‐Infrared Absorbance for Photothermal Treatment of Alzheimer's Disease
Li, M., Yang, X., Ren, J., Qu, K., & Qu, X. (2012) · Advanced Materials · doi:10.1002/adma.201104864 · Cited by 535
Metadata
- Authors
- Ehrnhoefer, D. E., Bieschke, J., Boeddrich, A., Herbst, M., Masino, L., Lurz, R., Engemann, S., Pastore, A., & Wanker, E. E.
- Venue
- Nature Structural & Molecular Biology
- Published
- 2008-05-30
- Volume
- 15
- Issue
- 6
- Pages
- 558-566
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- OpenAlex
- W2048940684
- Cited by
- 1,434
- References
- 7
- FWCI
- 36.59
- Type
- journal article
- Language
- en
- Open access
- closed
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How to cite
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- This page
- CoChat. (2026). Citation check: EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers. https://app.cochat.ai/papers/10.1038/nsmb.1437
- The paper
- Ehrnhoefer, D. E., Bieschke, J., Boeddrich, A., Herbst, M., Masino, L., Lurz, R., Engemann, S., Pastore, A., & Wanker, E. E. (2008). EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers. Nature Structural & Molecular Biology. https://doi.org/10.1038/nsmb.1437
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.
