The DOI matches its Crossref record; 57 of the 57 references it cites were found in a registry or an index.
Targeting proteins with metal complexes
Abstract
Unique properties of metal complexes, such as structural diversity, adjustable ligand exchange kinetics, fine-tuned redox activities, and distinct spectroscopic signatures, make them exciting scaffolds not only for binding to nucleic acids but increasingly also to proteins as non-traditional targets. This feature article discusses recent trends in this field. These include the use of chemically inert metal complexes as structural scaffolds for the design of enzyme inhibitors, new strategies for inducing selective coordination chemistry at the protein binding site, recent advances in the development of catalytic enzyme inhibitors, and the design of metal complexes that can inject electrons or holes into redox enzymes. A common theme in many of the discussed examples is that binding selectivity is at least in part achieved through weak interactions between the ligand sphere and the protein binding site. These examples hint to an exciting future in which "organic-like" molecular recognition principles are combined with properties that are unique to metals and thus promise to yield compounds with novel and unprecedented properties.
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Rhule, J. T., Hill, C. L., Judd, D. A., & Schinazi, R. F. (1998) · Chemical Reviews · doi:10.1021/cr960396q · Cited by 1,892
Crystal Structure of the PTEN Tumor Suppressor
Lee, J.-O., Yang, H., Georgescu, M.-M., Di Cristofano, A., Maehama, T., Shi, Y., Dixon, J. E., Pandolfi, P., & Pavletich, N. P. (1999) · Cell · doi:10.1016/s0092-8674(00)81663-3 · Cited by 1,014
Shaw, C. F. (1999) · Chemical Reviews · doi:10.1021/cr980431o · Cited by 990
Guo, Z., & Sadler, P. J. (1999) · Angewandte Chemie International Edition · doi:10.1002/(sici)1521-3773(19990601)38:11<1512::aid-anie1512>3.0.co;2-y · Cited by 834
Mechanism of Inhibition of Protein-tyrosine Phosphatases by Vanadate and Pervanadate
Huyer, G., Liu, S., Kelly, J., Moffat, J., Payette, P., Kennedy, B., Tsaprailis, G., Gresser, M. J., & Ramachandran, C. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.2.843 · Cited by 815
Metal-based antitumour drugs in the post genomic era
Dyson, P. J., & Sava, G. (2006) · Dalton Transactions · doi:10.1039/b601840h · Cited by 771
Using coordination chemistry to design new medicines
Ronconi, L., & Sadler, P. J. (2007) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2006.11.017 · Cited by 608
Fancy, D. A., & Kodadek, T. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.11.6020 · Cited by 576
Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site
Bourne, Y. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg005 · Cited by 488
Functional Mimics of Superoxide Dismutase Enzymes as Therapeutic Agents
Riley, D. P. (1999) · Chemical Reviews · doi:10.1021/cr980432g · Cited by 434
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Gasser, G., Ott, I., & Metzler-Nolte, N. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm100020w · Cited by 1,624
Metallodrugs in Medicinal Inorganic Chemistry
Mjos, K. D., & Orvig, C. (2014) · Chemical Reviews · doi:10.1021/cr400460s · Cited by 1,289
Zeng, L., Gupta, P., Chen, Y., Wang, E., Ji, L., Chao, H., & Chen, Z.-S. (2017) · Chemical Society Reviews · doi:10.1039/c7cs00195a · Cited by 1,017
Application of Metal Coordination Chemistry To Explore and Manipulate Cell Biology
Haas, K. L., & Franz, K. J. (2009) · Chemical Reviews · doi:10.1021/cr900134a · Cited by 984
Exploration of the medical periodic table: towards new targets
Barry, N. P. E., & Sadler, P. J. (2013) · Chemical Communications · doi:10.1039/c3cc41143e · Cited by 717
Metadata
- Authors
- Meggers, E.
- Venue
- Chemical Communications
- Publisher
- Royal Society of Chemistry (RSC)
- Published
- 2009
- Issue
- 9
- Pages
- 1001
- ISSN
- 1359-7345 (ISSN-L)
- 1364-548X
- OpenAlex
- W2072961231
- Cited by
- 450
- References
- 57
- FWCI
- 15.66
- Type
- journal article
- Language
- en
- Open access
- closed
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