The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Structural insight into substrate and inhibitor discrimination by human P-glycoprotein
Open accessAbstract
To transport or not to transport: Therapeutic drug delivery into cells is complicated by membrane proteins like ABCB1 (also termed P-glycoprotein) that shuttle diverse compounds out of cells. Alam et al. determined high-resolution cryo–electron microscopy structures of ABCB1 bound either to a substrate, the cancer drug Taxol, or to the ABCB1 inhibitor zosuquidar. The conformational changes that facilitate drug transport are caused by hydrolysis of adenosine triphosphate (ATP). The structures show that, although Taxol and zosquidar bind to the same site, subtle structural differences lead to altered conformations of the nucleotide binding domains that are responsible for ATP hydrolysis. Science , this issue p. 753
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PHENIX : a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716
RELION: Implementation of a Bayesian approach to cryo-EM structure determination
Scheres, S. H. W. (2012) · Journal of Structural Biology · doi:10.1016/j.jsb.2012.09.006 · Cited by 5,446
Structure of P-Glycoprotein Reveals a Molecular Basis for Poly-Specific Drug Binding
Aller, S. G., Yu, J., Ward, A., Weng, Y., Chittaboina, S., Zhuo, R., Harrell, P. M., Trinh, Y. T., Zhang, Q., Urbatsch, I. L., et al. (2009) · Science · doi:10.1126/science.1168750 · Cited by 1,929
Importance of P-glycoprotein at blood–tissue barriers
Fromm, M. F. (2004) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2004.06.002 · Cited by 592
Cited by
ABCG2 transports anticancer drugs via a closed-to-open switch
Orlando, B. J., & Liao, M. (2020) · Nature Communications · doi:10.1038/s41467-020-16155-2 · Cited by 198
An embedded lipid in the multidrug transporter LmrP suggests a mechanism for polyspecificity
Debruycker, V., Hutchin, A., Masureel, M., Ficici, E., Martens, C., Legrand, P., Stein, R. A., Mchaourab, H. S., Faraldo-Gómez, J. D., Remaut, H., et al. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0464-y · Cited by 69
Dong, X.-D., Zhang, M., Cai, C.-Y., Teng, Q.-X., Wang, J.-Q., Fu, Y.-G., Cui, Q., Patel, K., Wang, D.-T., & Chen, Z.-S. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.843829 · Cited by 29
Structural insights into binding-site access and ligand recognition by human ABCB1
Kurre, D., Dang, P. X., Le, L. T. M., Gadkari, V. V., & Alam, A. (2025) · The EMBO Journal · doi:10.1038/s44318-025-00361-z · Cited by 25
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Metadata
- Authors
- Alam, A., Kowal, J., Broude, E., Roninson, I., & Locher, K. P.
- Venue
- Science
- Published
- 2019-02-15
- Volume
- 363
- Issue
- 6428
- Pages
- 753-756
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2913173637
- Cited by
- 469
- References
- 4
- FWCI
- 23.31
- Type
- journal article
- Language
- en
- Open access
- green
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