The DOI matches its Crossref record; 217 of the 217 references it cites were found in a registry or an index.
Multiple Binding Modes of Inhibitors to Carbonic Anhydrases: How to Design Specific Drugs Targeting 15 Different Isoforms?
Open accessAbstract
Carbonic anhydrases (CAs, EC 4.2.1.1) are ubiquitous metalloenzymes, present throughout most living organisms and encoded by five evolutionarily unrelated gene families: the α-, β-, γ-, δ-, and ζ-CAs The α- β- and δ-CAs contain a Zn(II) ion at the active site, the γ-CAs are probably Fe(II) enzymes (but they are active also with Zn(II) or Co(II) ions), while the metal ion is usually replaced by cadmium in the ζ-CAs. Herein we report a state of the art structural crystallographyc investigation.
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Antioxidant and radical scavenging properties of curcumin
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Esterase Activities of Human Carbonic Anhydrases B and C
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Le Roy, N., Jackson, D. J., Marie, B., Ramos-Silva, P., & Marin, F. (2014) · Frontiers in Zoology · doi:10.1186/s12983-014-0075-8 · Cited by 131
Nguyen, G. T. H., Bennett, J. L., Liu, S., Hancock, S. E., Winter, D. L., Glover, D. J., & Donald, W. A. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.1c10408 · Cited by 66
Metadata
- Authors
- Alterio, V., Di Fiore, A., D’Ambrosio, K., Supuran, C. T., & De Simone, G.
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2012-05-18
- Volume
- 112
- Issue
- 8
- Pages
- 4421-4468
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W1972547175
- Cited by
- 1,238
- References
- 217
- FWCI
- 6.03
- Type
- journal article
- Language
- en
- Open access
- green
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