The DOI matches its Crossref record; 16 of the 16 references it cites were found in a registry or an index.
Structure-Based Design of Potent Small-Molecule Inhibitors of Anti-Apoptotic Bcl-2 Proteins
Open accessAbstract
A structure-based approach was employed to design a new class of small-molecule inhibitors of Bcl-2. The most potent compound 5 (TW-37) binds to Bcl-2 with a K(i) value of 290 nM and also to Bcl-xL and Mcl-1 with high affinities. Compound 5 potently inhibits cell growth in PC-3 prostate cancer cells with an IC(50) value of 200 nM and effectively induces apoptosis in a dose-dependent manner.
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Citations
Cites
The Bcl-2 Protein Family: Arbiters of Cell Survival
Adams, J. M., & Cory, S. (1998) · Science · doi:10.1126/science.281.5381.1322 · Cited by 5,332
An inhibitor of Bcl-2 family proteins induces regression of solid tumours
Oltersdorf, T., Elmore, S. W., Shoemaker, A. R., Armstrong, R. C., Augeri, D. J., Belli, B. A., Bruncko, M., Deckwerth, T. L., Dinges, J., Hajduk, P. J., et al. (2005) · Nature · doi:10.1038/nature03579 · Cited by 3,416
BCL-2 FAMILY: Regulators of Cell Death
Chao, D. T., & Korsmeyer, S. J. (1998) · Annual Review of Immunology · doi:10.1146/annurev.immunol.16.1.395 · Cited by 1,685
Structure of Bcl-x L -Bak Peptide Complex: Recognition Between Regulators of Apoptosis
Sattler, M., Liang, H., Nettesheim, D., Meadows, R. P., Harlan, J. E., Eberstadt, M., Yoon, H. S., Shuker, S. B., Chang, B. S., Minn, A. J., et al. (1997) · Science · doi:10.1126/science.275.5302.983 · Cited by 1,476
Wang, J.-L., Liu, D., Zhang, Z.-J., Shan, S., Han, X., Srinivasula, S. M., Croce, C. M., Alnemri, E. S., & Huang, Z. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.13.7124 · Cited by 1,201
Identification of small-molecule inhibitors of interaction between the BH3 domain and Bcl-xL
Degterev, A., Lugovskoy, A., Cardone, M., Mulley, B., Wagner, G., Mitchison, T., & Yuan, J. (2001) · Nature Cell Biology · doi:10.1038/35055085 · Cited by 550
A Protein-Counting Mechanism for Telomere Length Regulation in Yeast
Marcand, S., Gilson, E., & Shore, D. (1997) · Science · doi:10.1126/science.275.5302.986 · Cited by 524
Solution structure of the antiapoptotic protein bcl-2
Petros, A. M., Medek, A., Nettesheim, D. G., Kim, D. H., Yoon, H. S., Swift, K., Matayoshi, E. D., Oltersdorf, T., & Fesik, S. W. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.041619798 · Cited by 458
Antimycin A mimics a cell-death-inducing Bcl-2 homology domain 3
Tzung, S.-P., Kim, K. M., Basañez, G., Giedt, C. D., Simon, J., Zimmerberg, J., Zhang, K. Y. J., & Hockenbery, D. M. (2001) · Nature Cell Biology · doi:10.1038/35055095 · Cited by 452
PETROS, A. M., NETTESHEIM, D. G., WANG, Y., OLEJNICZAK, E. T., MEADOWS, R. P., MACK, J., SWIFT, K., MATAYOSHI, E. D., ZHANG, H., THOMPSON, C. B., et al. (2000) · Protein Science · doi:10.1017/s096183680000331x · Cited by 412
Kitada, S., Leone, M., Sareth, S., Zhai, D., Reed, J. C., & Pellecchia, M. (2003) · Journal of Medicinal Chemistry · doi:10.1021/jm030190z · Cited by 379
Discovery of Small-Molecule Inhibitors of Bcl-2 through Structure-Based Computer Screening
Enyedy, I. J., Ling, Y., Nacro, K., Tomita, Y., Wu, X., Cao, Y., Guo, R., Li, B., Zhu, X., Huang, Y., et al. (2001) · Journal of Medicinal Chemistry · doi:10.1021/jm010016f · Cited by 315
Self-citationDiscovery of a Potent Inhibitor of the Antiapoptotic Protein Bcl-x L from NMR and Parallel Synthesis
Petros, A. M., Dinges, J., Augeri, D. J., Baumeister, S. A., Betebenner, D. A., Bures, M. G., Elmore, S. W., Hajduk, P. J., Joseph, M. K., Landis, S. K., et al. (2006) · Journal of Medicinal Chemistry · doi:10.1021/jm0507532 · Cited by 292
Bcl-2 Family Proteins: Strategies for Overcoming Chemoresistance in Cancer
Reed, J. C. (1997) · Advances in pharmacology · doi:10.1016/s1054-3589(08)61070-4 · Cited by 124
Recent Progress on the Regulation of Apoptosis by Bcl-2 Family Members
Minn, A. J., Swain, R. E., Ma, A. I., & Thompson, C. B. (1998) · Advances in immunology · doi:10.1016/s0065-2776(08)60388-0 · Cited by 69
Apoptosis in Hormone-Responsive Malignancies
Denmeade, S. R., McCloskey, D. E., Joseph, I. B. J., Hahm, H. A., Isaacs, J. T., & Davidson, N. E. (1997) · Advances in pharmacology · doi:10.1016/s1054-3589(08)61072-8 · Cited by 13
Cited by
Zhu, Y., Tchkonia, T., Fuhrmann‐Stroissnigg, H., Dai, H. M., Ling, Y. Y., Stout, M. B., Pirtskhalava, T., Giorgadze, N., Johnson, K. O., Giles, C. B., et al. (2016) · Aging Cell · doi:10.1111/acel.12445 · Cited by 1,148
Small molecules, big targets: drug discovery faces the protein–protein interaction challenge
Scott, D. E., Bayly, A. R., Abell, C., & Skidmore, J. (2016) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.29 · Cited by 1,137
Broad targeting of resistance to apoptosis in cancer
Mohammad, R. M., Muqbil, I., Lowe, L., Yedjou, C., Hsu, H.-Y., Lin, L.-T., Siegelin, M. D., Fimognari, C., Kumar, N. B., Dou, Q. P., et al. (2015) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2015.03.001 · Cited by 864
BCL-2 family antagonists for cancer therapy
Lessene, G., Czabotar, P. E., & Colman, P. M. (2008) · Nature Reviews Drug Discovery · doi:10.1038/nrd2658 · Cited by 621
The MCL-1 BH3 helix is an exclusive MCL-1 inhibitor and apoptosis sensitizer
Stewart, M. L., Fire, E., Keating, A. E., & Walensky, L. D. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.391 · Cited by 418
Metadata
- Authors
- Wang, G., Nikolovska-Coleska, Z., Yang, C.-Y., Wang, R., Tang, G., Guo, J., Shangary, S., Qiu, S., Gao, W., Yang, D., Meagher, J., Stuckey, J., Krajewski, K., Jiang, S., Roller, P. P., Abaan, H. O., Tomita, Y., & Wang, S.
- Venue
- Journal of Medicinal Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2006-09-12
- Volume
- 49
- Issue
- 21
- Pages
- 6139-6142
- ISSN
- 0022-2623 (ISSN-L)
- 1520-4804
- OpenAlex
- W1980727670
- Cited by
- 292
- References
- 16
- FWCI
- 8.35
- Type
- journal article
- Language
- en
- Open access
- green
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