The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Harnessing Chaperones to Generate Small-Molecule Inhibitors of Amyloid ß Aggregation
Abstract
Protein aggregation is involved in the pathogenesis of neurodegenerative diseases and hence is considered an attractive target for therapeutic intervention. However, protein-protein interactions are exceedingly difficult to inhibit. Small molecules lack sufficient steric bulk to prevent interactions between large peptide surfaces. To yield potent inhibitors of β-amyloid (Aβ) aggregation, we synthesized small molecules that increase their steric bulk by binding to chaperones but also have a moiety available for interaction with Aβ. This strategy yields potent inhibitors of Aβ aggregation and could lead to therapeutics for Alzheimer's disease and other forms of neurodegeneration.
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Cites
The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864
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
[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
Peptidylprolyl Cis / Trans Isomerases (Immunophilins): Biological Diversity - Targets - Functions
Galat, A. (2003) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026033451862 · Cited by 360
Transgenic mouse models of Alzheimer’s disease
Janus, C., Chishti, M. A., & Westaway, D. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(00)00033-8 · Cited by 101
Drugs targeting alzheimer’s disease: Some things old and some things new
Michaelis, M. L. (2003) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.102.035840 · Cited by 78
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Friml, J., Yang, X., Michniewicz, M., Weijers, D., Quint, A., Tietz, O., Benjamins, R., Ouwerkerk, P. B. F., Ljung, K., Sandberg, G., et al. (2004) · Science · doi:10.1126/science.1100618 · Cited by 789
Chemically induced proximity in biology and medicine
Stanton, B. Z., Chory, E. J., & Crabtree, G. R. (2018) · Science · doi:10.1126/science.aao5902 · Cited by 475
Self-citationUnifying principles of bifunctional, proximity-inducing small molecules
Gerry, C. J., & Schreiber, S. L. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0469-1 · Cited by 199
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Metadata
- Authors
- Gestwicki, J. E., Crabtree, G. R., & Graef, I. A.
- Venue
- Science
- Published
- 2004-10-29
- Volume
- 306
- Issue
- 5697
- Pages
- 865-869
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2095927366
- Cited by
- 200
- References
- 6
- FWCI
- 9.50
- Type
- journal article
- Language
- en
- Open access
- closed
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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.
