The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Modulation of Protein–Protein Interactions with Small Organic Molecules
Abstract
Many proteins exert their biological roles as components of complexes, and the functions of proteins are often determined by their specific interactions with other proteins. Because of the central importance of protein–protein interactions for cellular processes, the ability to interfere with specific protein–protein interactions provides a powerful means of influencing the function of selected proteins within the cell. Cell‐permeable small organic modulators of protein–protein interactions are thus highly desirable tools both for the study of physiological cellular processes and for the treatment of numerous diseased states. Herein a number of protein–protein interactions that are considered to be pharmaceutical targets are presented, which will familiarize the reader with the strategies that have been employed for the successful identification of small molecule modulators of these protein–protein interactions. These encouraging examples suggest that combined research efforts in the areas of functional proteomics, assay development, and organic synthesis will open up novel possibilities for the treatment of human diseases in the future.
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Cites
The L-Arginine-Nitric Oxide Pathway
Epstein, F. H., Moncada, S., & Higgs, A. (1993) · New England Journal of Medicine · doi:10.1056/nejm199312303292706 · Cited by 6,678
Nitric oxide synthases: structure, function and inhibition
ALDERTON, W. K., COOPER, C. E., & KNOWLES, R. G. (2001) · Biochemical Journal · doi:10.1042/bj3570593 · Cited by 4,110
Principles of protein-protein interactions
Jones, S., & Thornton, J. M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.1.13 · Cited by 2,684
Structure of the MDM2 Oncoprotein Bound to the p53 Tumor Suppressor Transactivation Domain
Kussie, P. H., Gorina, S., Marechal, V., Elenbaas, B., Moreau, J., Levine, A. J., & Pavletich, N. P. (1996) · Science · doi:10.1126/science.274.5289.948 · Cited by 2,206
Anatomy of hot spots in protein interfaces
Bogan, A. A., & Thorn, K. S. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1843 · Cited by 1,988
Amplification of a gene encoding a p53-associated protein in human sarcomas
Oliner, J. D., Kinzler, K. W., Meltzer, P. S., George, D. L., & Vogelstein, B. (1992) · Nature · doi:10.1038/358080a0 · Cited by 1,949
Regulation of p53 in response to DNA damage
Lakin, N. D., & Jackson, S. P. (1999) · Oncogene · doi:10.1038/sj.onc.1203015 · Cited by 987
Brefeldin A Acts to Stabilize an Abortive ARF–GDP–Sec7 Domain Protein Complex
Peyroche, A., Antonny, B., Robineau, S., Acker, J., Cherfils, J., & Jackson, C. L. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80455-4 · Cited by 453
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Small-molecule inhibitors of protein–protein interactions: progressing towards the dream
Arkin, M. R., & Wells, J. A. (2004) · Nature Reviews Drug Discovery · doi:10.1038/nrd1343 · Cited by 1,705
Potential therapeutic applications of autophagy
Rubinsztein, D. C., Gestwicki, J. E., Murphy, L. O., & Klionsky, D. J. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2272 · Cited by 862
Inhibition of α-helix-mediated protein–protein interactions using designed molecules
Azzarito, V., Long, K., Murphy, N. S., & Wilson, A. J. (2013) · Nature Chemistry · doi:10.1038/nchem.1568 · Cited by 727
A surface on the androgen receptor that allosterically regulates coactivator binding
Estébanez-Perpiñá, E., Arnold, L. A., Nguyen, P., Rodrigues, E. D., Mar, E., Bateman, R., Pallai, P., Shokat, K. M., Baxter, J. D., Guy, R. K., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0708036104 · Cited by 307
Buchwald, P. (2010) · IUBMB Life · doi:10.1002/iub.383 · Cited by 133
Metadata
- Authors
- Berg, T.
- Venue
- Angewandte Chemie International Edition
- Publisher
- Wiley
- Published
- 2003-06-05
- Volume
- 42
- Issue
- 22
- Pages
- 2462-2481
- ISSN
- 1433-7851 (ISSN-L)
- 1521-3773
- OpenAlex
- W1998492578
- Cited by
- 292
- References
- 8
- FWCI
- 8.47
- Type
- journal article
- Language
- en
- Open access
- closed
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