The DOI matches its Crossref record; 142 of the 142 references it cites were found in a registry or an index.
Mode of Action of Bi- and Trinuclear Zinc Hydrolases and Their Synthetic Analogues
Abstract
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTMode of Action of Bi- and Trinuclear Zinc Hydrolases and Their Synthetic AnaloguesJennie WestonView Author Information Institut für Organische und Makromolekulare Chemie, Friedrich-Schiller-Universität, D-07743 Jena, Germany Cite this: Chem. Rev. 2005, 105, 6, 2151–2174Publication Date (Web):March 24, 2005Publication History Received19 June 2002Published online24 March 2005Published inissue 1 June 2005https://pubs.acs.org/doi/10.1021/cr020057zhttps://doi.org/10.1021/cr020057zresearch-articleACS PublicationsCopyright © 2005 American Chemical SocietyRequest reuse permissionsArticle Views2220Altmetric-Citations283LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose SUBJECTS:Ions,Ligands,Metals,Peptides and proteins,Zinc Get e-Alerts
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On the size of the active site in proteases. I. Papain
Schechter, I., & Berger, A. (1967) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(67)80055-x · Cited by 5,204
A Chemist's Guide to Density Functional Theory
Koch, W., & Holthausen, M. C. (2001) · Wiley eBooks · doi:10.1002/3527600043 · Cited by 4,880
The crisis in antibiotic resistance
Neu, H. C. (1992) · Science · doi:10.1126/science.257.5073.1064 · Cited by 2,834
Structural and Functional Aspects of Metal Sites in Biology
Holm, R. H., Kennepohl, P., & Solomon, E. I. (1996) · Chemical Reviews · doi:10.1021/cr9500390 · Cited by 2,541
Ambler, R. P. (1980) · Philosophical Transactions of the Royal Society of London. B, Biological Sciences · doi:10.1098/rstb.1980.0049 · Cited by 1,823
Sigel, H., & Martin, R. B. (1982) · Chemical Reviews · doi:10.1021/cr00050a003 · Cited by 1,611
Recent Advances in Zinc Enzymology
Lipscomb, W. N., & Sträter, N. (1996) · Chemical Reviews · doi:10.1021/cr950042j · Cited by 1,366
Reaction mechanism of alkaline phosphatase based on crystal structures
Kim, E. E., & Wyckoff, H. W. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)90724-k · Cited by 944
Synthetic Analogues Relevant to the Structure and Function of Zinc Enzymes
Parkin, G. (2004) · Chemical Reviews · doi:10.1021/cr0206263 · Cited by 931
Wilcox, D. E. (1996) · Chemical Reviews · doi:10.1021/cr950043b · Cited by 893
Cited by
Protein Design: Toward Functional Metalloenzymes
Yu, F., Cangelosi, V. M., Zastrow, M. L., Tegoni, M., Plegaria, J. S., Tebo, A. G., Mocny, C. S., Ruckthong, L., Qayyum, H., & Pecoraro, V. L. (2014) · Chemical Reviews · doi:10.1021/cr400458x · Cited by 441
Metadata
- Authors
- Weston, J.
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2005-03-24
- Volume
- 105
- Issue
- 6
- Pages
- 2151-2174
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W1981748997
- Cited by
- 311
- References
- 142
- FWCI
- 0.95
- Type
- journal article
- Language
- en
- Open access
- closed
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