The DOI matches its Crossref record; 38 of the 38 references it cites were found in a registry or an index.
Acridine and phenothiazine derivatives as pharmacotherapeutics for prion disease
Open accessAbstract
Prion diseases in humans and animals are invariably fatal. Prions are composed of a disease-causing isoform (PrP Sc ) of the normal host prion protein (PrP C ) and replicate by stimulating the conversion of PrP C into nascent PrP Sc . We report here that tricyclic derivatives of acridine and phenothiazine exhibit half-maximal inhibition of PrP Sc formation at effective concentrations (EC 50 ) between 0.3 μM and 3 μM in cultured cells chronically infected with prions. The EC 50 for chlorpromazine was 3 μM, whereas quinacrine was 10 times more potent. A variety of 9-substituted, acridine-based analogues of quinacrine were synthesized, which demonstrated variable antiprion potencies similar to those of chlorpromazine and emphasized the importance of the side chain in mediating the inhibition of PrP Sc formation. Thus, our studies show that tricyclic compounds with an aliphatic side chain at the middle ring moiety constitute a new class of antiprion reagents. Because quinacrine and chlorpromazine have been used in humans for many years as antimalarial and antipsychotic drugs, respectively, and are known to pass the blood–brain barrier, we suggest that they are immediate candidates for the treatment of Creutzfeldt–Jakob disease and other prion diseases.
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The Pharmacological Basis of Therapeutics
(1976) · American Journal of Health-System Pharmacy · doi:10.1093/ajhp/33.4.373a · Cited by 8,209
Goodman & Gilman's The Pharmacological Basis of Therapeutics
Brunton, L. L. (1985) · Cited by 7,321
Novel Proteinaceous Infectious Particles Cause Scrapie
Prusiner, S. B. (1982) · Science · doi:10.1126/science.6801762 · Cited by 5,118
Self-citationPan, K. M., Baldwin, M., Nguyen, J., Gasset, M., Serban, A., Groth, D., Mehlhorn, I., Huang, Z., Fletterick, R. J., & Cohen, F. E. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.23.10962 · Cited by 2,277
Self-citationScrapie prions aggregate to form amyloid-like birefringent rods
Prusiner, S. B., McKinley, M. P., Bowman, K. A., Bolton, D. C., Bendheim, P. E., Groth, D. F., & Glenner, G. G. (1983) · Cell · doi:10.1016/0092-8674(83)90168-x · Cited by 1,043
Self-citationKnapp, M. J. (1994) · JAMA · doi:10.1001/jama.271.13.985 · Cited by 1,004
Telling, G. C., Parchi, P., DeArmond, S. J., Cortelli, P., Montagna, P., Gabizon, R., Mastrianni, J., Lugaresi, E., Gambetti, P., & Prusiner, S. B. (1996) · Science · doi:10.1126/science.274.5295.2079 · Cited by 865
Self-citationNeurodegenerative Diseases and Prions
Prusiner, S. B. (2001) · New England Journal of Medicine · doi:10.1056/nejm200105173442006 · Cited by 772
Self-citationDoes the Agent of Scrapie Replicate without Nucleic Acid ?
ALPER, T., CRAMP, W. A., HAIG, D. A., & CLARKE, M. C. (1967) · Nature · doi:10.1038/214764a0 · Cited by 691
Unconventional Viruses and the Origin and Disappearance of Kuru
Gajdusek, D. C. (1977) · Science · doi:10.1126/science.142303 · Cited by 671
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Metadata
- Authors
- Korth, C., May, B. C. H., Cohen, F. E., & Prusiner, S. B.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2001-08-14
- Volume
- 98
- Issue
- 17
- Pages
- 9836-9841
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2135301408
- Cited by
- 673
- References
- 38
- FWCI
- 16.50
- Type
- journal article
- Language
- en
- Open access
- green
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