The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
A small-molecule, nonpeptide CCR5 antagonist with highly potent and selective anti-HIV-1 activity
Open accessAbstract
The β-chemokine receptor CCR5 is considered to be an attractive target for inhibition of macrophage-tropic (CCR5-using or R5) HIV-1 replication because individuals having a nonfunctional receptor (a homozygous 32-bp deletion in the CCR5 coding region) are apparently normal but resistant to infection with R5 HIV-1. In this study, we found that TAK-779, a nonpeptide compound with a small molecular weight (Mr 531.13), antagonized the binding of RANTES (regulated on activation, normal T cell expressed and secreted) to CCR5-expressing Chinese hamster ovary cells and blocked CCR5-mediated Ca 2+signaling at nanomolar concentrations. The inhibition of β-chemokine receptors by TAK-779 appeared to be specific to CCR5 because the compound antagonized CCR2b to a lesser extent but did not affect CCR1, CCR3, or CCR4. Consequently, TAK-779 displayed highly potent and selective inhibition of R5 HIV-1 replication without showing any cytotoxicity to the host cells. The compound inhibited the replication of R5 HIV-1 clinical isolates as well as a laboratory strain at a concentration of 1.6–3.7 nM in peripheral blood mononuclear cells, though it was totally inactive against T-cell line-tropic (CXCR4-using or X4) HIV-1.
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Yung-Chi, C., & Prusoff, W. H. (1973) · Biochemical Pharmacology · doi:10.1016/0006-2952(73)90196-2 · Cited by 12,922
Cited by
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Murphy, P. M., Baggiolini, M., Charo, I. F., Hébert, C. A., Horuk, R., Matsushima, K., Miller, L. H., Oppenheim, J. J., & Power, C. A. (2000) · Pharmacological Reviews · doi:10.1016/s0031-6997(24)01439-x · Cited by 1,817
The SCF ubiquitin ligase: insights into a molecular machine
Cardozo, T., & Pagano, M. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1471 · Cited by 1,114
Structure, Function, and Inhibition of Chemokines
Fernandez, E. J., & Lolis, E. (2002) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.42.091901.115838 · Cited by 609
A sensitive and specific enzyme-based assay detecting HIV-1 virion fusion in primary T lymphocytes
Cavrois, M., de Noronha, C., & Greene, W. C. (2002) · Nature Biotechnology · doi:10.1038/nbt745 · Cited by 475
Tan, M. C. B., Goedegebuure, P. S., Belt, B. A., Flaherty, B., Sankpal, N., Gillanders, W. E., Eberlein, T. J., Hsieh, C.-S., & Linehan, D. C. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.182.3.1746 · Cited by 450
Metadata
- Authors
- Baba, M., Nishimura, O., Kanzaki, N., Okamoto, M., Sawada, H., Iizawa, Y., Shiraishi, M., Aramaki, Y., Okonogi, K., Ogawa, Y., Meguro, K., & Fujino, M.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1999-05-11
- Volume
- 96
- Issue
- 10
- Pages
- 5698-5703
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2140478082
- Cited by
- 751
- References
- 1
- FWCI
- 19.69
- Type
- journal article
- Language
- en
- Open access
- green
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- Baba, M., Nishimura, O., Kanzaki, N., Okamoto, M., Sawada, H., Iizawa, Y., Shiraishi, M., Aramaki, Y., Okonogi, K., Ogawa, Y., Meguro, K., & Fujino, M. (1999). A small-molecule, nonpeptide CCR5 antagonist with highly potent and selective anti-HIV-1 activity. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.96.10.5698
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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