The DOI matches its Crossref record; 57 of the 57 references it cites were found in a registry or an index.
Targeting Metalloenzymes for Therapeutic Intervention
Open accessAbstract
Metalloenzymes are central to a wide range of essential biological activities, including nucleic acid modification, protein degradation, and many others. The role of metalloenzymes in these processes also makes them central for the progression of many diseases and, as such, makes metalloenzymes attractive targets for therapeutic intervention. Increasing awareness of the role metalloenzymes play in disease and their importance as a class of targets has amplified interest in the development of new strategies to develop inhibitors and ultimately useful drugs. In this Review, we provide a broad overview of several drug discovery efforts focused on metalloenzymes and attempt to map out the current landscape of high-value metalloenzyme targets.
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Cites
Histone demethylation mediated by the nuclear amine oxidase homolog LSD1
Shi, Y., Lan, F., Matson, C., Mulligan, P., Whetstine, J. R., Cole, P. A., Casero, R. A., & Shi, Y. (2004) · Cell · doi:10.1016/j.cell.2004.12.012 · Cited by 4,051
Prostaglandins and Leukotrienes: Advances in Eicosanoid Biology
Funk, C. D. (2001) · Science · doi:10.1126/science.294.5548.1871 · Cited by 3,817
Multicopper oxidases and oxygenases
Solomon, E. I., Sundaram, U. M., & Machonkin, T. E. (1996) · Chemical Reviews · doi:10.1021/cr950046o · Cited by 3,664
Histone methylation: a dynamic mark in health, disease and inheritance
Greer, E. L., & Shi, Y. (2012) · Nature Reviews Genetics · doi:10.1038/nrg3173 · Cited by 2,241
The progression from hypertension to congestive heart failure
Levy, D. (1996) · JAMA: The Journal of the American Medical Association · doi:10.1001/jama.1996.03530440037034 · Cited by 2,155
The Global Burden of Latent Tuberculosis Infection: A Re-estimation Using Mathematical Modelling
Houben, R. M. G. J., & Dodd, P. J. (2016) · PLOS Medicine · doi:10.1371/journal.pmed.1002152 · Cited by 2,054
Crystal structure at 3.5 A resolution of HIV-1 reverse transcriptase complexed with an inhibitor
Kohlstaedt, L. A., Wang, J., Friedman, J. M., Rice, P. A., & Steitz, T. A. (1992) · Science · doi:10.1126/science.1377403 · Cited by 1,914
A genomic and functional inventory of deubiquitinating enzymes.
Nijman, S. M. B., Luna-Vargas, M. P. A., Velds, A., Brummelkamp, T. R., Dirac, A. M. G., Sixma, T. K., & Bernards, R. (2005) · Cell · doi:10.1016/j.cell.2005.11.007 · Cited by 1,854
Three Decades of β-Lactamase Inhibitors
Drawz, S. M., & Bonomo, R. A. (2010) · Clinical Microbiology Reviews · doi:10.1128/cmr.00037-09 · Cited by 1,709
Pathogenetic Mechanisms of Septic Shock
Epstein, F. H., & Parrillo, J. E. (1993) · New England Journal of Medicine · doi:10.1056/nejm199305203282008 · Cited by 1,548
Cited by
Yang, B., Chen, Y., & Shi, J. (2019) · Advanced Materials · doi:10.1002/adma.201901778 · Cited by 601
Cong, Y., Yang, S., & Rao, X. (2020) · Journal of Advanced Research · doi:10.1016/j.jare.2019.10.005 · Cited by 527
Chaudhary, D., Chong, F., Neupane, T., Choi, J., & Jee, J.-G. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222413661 · Cited by 14
Metadata
- Authors
- Chen, A. Y., Adamek, R. N., Dick, B. L., Credille, C. V., Morrison, C. N., & Cohen, S. M.
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2018-09-07
- Volume
- 119
- Issue
- 2
- Pages
- 1323-1455
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W2889619860
- Cited by
- 270
- References
- 57
- FWCI
- 3.00
- Type
- journal article
- Language
- en
- Open access
- green
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- Chen, A. Y., Adamek, R. N., Dick, B. L., Credille, C. V., Morrison, C. N., & Cohen, S. M. (2019). Targeting Metalloenzymes for Therapeutic Intervention. Chemical Reviews. https://doi.org/10.1021/acs.chemrev.8b00201
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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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