The DOI matches its Crossref record; 95 of the 95 references it cites were found in a registry or an index.
Therapeutic strategies for human amyloid diseases
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Citations
Cites
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Vassar, R., Bennett, B. D., Babu-Khan, S., Kahn, S., Mendiaz, E. A., Denis, P., Teplow, D. B., Ross, S., Amarante, P., Loeloff, R., et al. (1999) · Science · doi:10.1126/science.286.5440.735 · Cited by 3,876
Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse
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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
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
Aβ peptide vaccination prevents memory loss in an animal model of Alzheimer's disease
Morgan, D., Diamond, D. M., Gottschall, P. E., Ugen, K. E., Dickey, C., Hardy, J., Duff, K., Jantzen, P., DiCarlo, G., Wilcock, D., et al. (2000) · Nature · doi:10.1038/35050116 · Cited by 1,498
Production of the Alzheimer Amyloid β Protein by Normal Proteolytic Processing
Shoji, M., Golde, T. E., Ghiso, J., Cheung, T. T., Estus, S., Shaffer, L. M., Cai, X.-D., McKay, D. M., Tintner, R., Frangione, B., et al. (1992) · Science · doi:10.1126/science.1439760 · Cited by 1,447
A subset of NSAIDs lower amyloidogenic Aβ42 independently of cyclooxygenase activity
Weggen, S., Eriksen, J. L., Das, P., Sagi, S. A., Wang, R., Pietrzik, C. U., Findlay, K. A., Smith, T. E., Murphy, M. P., Bulter, T., et al. (2001) · Nature · doi:10.1038/35102591 · Cited by 1,388 · cited 1×
“cgi?l=23621">β-secretase inhibitors are now available as potential therapeutics to prevent the processing of APP into the amyloid-β peptide — the 39–43-residue peptide that assembles into Alzheimer's fibril”
BackgroundAggregation and Motor Neuron Toxicity of an ALS-Linked SOD1 Mutant Independent from Wild-Type SOD1
Bruijn, L. I., Houseweart, M. K., Kato, S., Anderson, K. L., Anderson, S. D., Ohama, E., Reaume, A. G., Scott, R. W., & Cleveland, D. W. (1998) · Science · doi:10.1126/science.281.5384.1851 · Cited by 1,228
Cited by
Gut microbiota regulate motor deficits and neuroinflammation in a model of Parkinson's disease
Sampson, T. R., Debelius, J. W., Thron, T., Janssen, S., Shastri, G. G., Ilhan, Z. E., Challis, C., Schretter, C. E., Rocha, S., Gradinaru, V., et al. (2016) · Cell · doi:10.1016/j.cell.2016.11.018 · Cited by 3,622
Protein aggregation and neurodegenerative disease
Ross, C. A., & Poirier, M. A. (2004) · Nature Medicine · doi:10.1038/nm1066 · Cited by 3,454
Unfolding the role of protein misfolding in neurodegenerative diseases
Soto, C. (2003) · Nature Reviews Neuroscience · doi:10.1038/nrn1007 · Cited by 1,506
EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers
Ehrnhoefer, D. E., Bieschke, J., Boeddrich, A., Herbst, M., Masino, L., Lurz, R., Engemann, S., Pastore, A., & Wanker, E. E. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1437 · Cited by 1,434
Therapeutic approaches to protein-misfolding diseases
Cohen, F. E., & Kelly, J. W. (2003) · Nature · doi:10.1038/nature02265 · Cited by 800
Self-citation
Metadata
- Authors
- Sacchettini, J. C., & Kelly, J. W.
- Venue
- Nature Reviews Drug Discovery
- Published
- 2002-04
- Volume
- 1
- Issue
- 4
- Pages
- 267-275
- ISSN
- 1474-1776 (ISSN-L)
- 1474-1784
- OpenAlex
- W2044788929
- Cited by
- 261
- References
- 95
- FWCI
- 1.23
- Type
- journal article
- Language
- en
- Open access
- closed
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- Sacchettini, J. C., & Kelly, J. W. (2002). Therapeutic strategies for human amyloid diseases. Nature Reviews Drug Discovery. https://doi.org/10.1038/nrd769
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.
