The DOI matches its Crossref record; 16 of the 16 references it cites were found in a registry or an index.
Recent Advances in Zinc Enzymology
Abstract
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTRecent Advances in Zinc EnzymologyWilliam N. Lipscomb and Norbert SträterView Author Information Department of Chemistry and Chemical Biology, Harvard University, 12 Oxford Street, Cambridge, Massachusetts 02138 Cite this: Chem. Rev. 1996, 96, 7, 2375–2434Publication Date (Web):November 7, 1996Publication History Received2 May 1996Revised25 July 1996Published online7 November 1996Published inissue 1 January 1996https://pubs.acs.org/doi/10.1021/cr950042jhttps://doi.org/10.1021/cr950042jresearch-articleACS PublicationsCopyright © 1996 American Chemical SocietyRequest reuse permissionsArticle Views5120Altmetric-Citations1184LEARN 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,Metals,Monomers,Peptides and proteins,Zinc Get e-Alerts
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Cites
Electrochemical Photolysis of Water at a Semiconductor Electrode
FUJISHIMA, A., & HONDA, K. (1972) · Nature · doi:10.1038/238037a0 · Cited by 34,169
Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes
Liu, J., Farmer, J. D., Lane, W. S., Friedman, J., Weissman, I., & Schreiber, S. L. (1991) · Cell · doi:10.1016/0092-8674(91)90124-h · Cited by 4,116
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 general two-metal-ion mechanism for catalytic RNA
Steitz, T. A., & Steitz, J. A. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.14.6498 · Cited by 1,171
Dyda, F., Hickman, A. B., Jenkins, T. M., Engelman, A., Craigie, R., & Davies, D. R. (1994) · Science · doi:10.1126/science.7801124 · Cited by 810
Christianson, D. W., & Lipscomb, W. N. (1989) · Accounts of Chemical Research · doi:10.1021/ar00158a003 · Cited by 606
Self-citationCrystal structure of the ribonuclease H domain of HIV-1 reverse transcriptase
Davies, J. F., Hostomska, Z., Hostomsky, Z., Jordan, S. R., & Matthews, D. A. (1991) · Science · doi:10.1126/science.1707186 · Cited by 570
Johnson, M. S., McClure, M. A., Feng, D. F., Gray, J., & Doolittle, R. F. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.20.7648 · Cited by 480
Zinc binding in proteins and solution: A simple but accurate nonbonded representation
Stote, R. H., & Karplus, M. (1995) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340230104 · Cited by 354
[21] Snake venom metalloendopeptidases: Reprolysins
Bjarnason, J. B., & Fox, J. W. (1995) · Methods in Enzymology · doi:10.1016/0076-6879(95)48023-4 · Cited by 286
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Nguyen, B. T., & Anslyn, E. V. (2006) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2006.04.009 · Cited by 668
Analysis of zinc binding sites in protein crystal structures
Alberts, I. L., Nadassy, K., & Wodak, S. J. (1998) · Protein Science · doi:10.1002/pro.5560070805 · Cited by 423
Bacterial proteases, untapped antimicrobial drug targets
Culp, E., & Wright, G. D. (2017) · The Journal of Antibiotics · doi:10.1038/ja.2016.138 · Cited by 244
Trace elements at the intersection of marine biological and geochemical evolution
Robbins, L. J., Lalonde, S. V., Planavsky, N. J., Partin, C. A., Reinhard, C. T., Kendall, B., Scott, C., Hardisty, D. S., Gill, B. C., Alessi, D. S., et al. (2016) · Earth-Science Reviews · doi:10.1016/j.earscirev.2016.10.013 · Cited by 227
Biogeochemical signatures through time as inferred from whole microbial genomes
Zerkle, A. L. (2005) · American Journal of Science · doi:10.2475/ajs.305.6-8.467 · Cited by 223
Carboxylate Binding Modes in Zinc Proteins: A Theoretical Study
Ryde, U. (1999) · Biophysical Journal · doi:10.1016/s0006-3495(99)77110-9 · Cited by 127
Kinetics and Comparative Reactivity of Human Class I and Class IIb Histone Deacetylases
Schultz, B. E., Misialek, S., Wu, J., Tang, J., Conn, M. T., Tahilramani, R., & Wong, L. (2004) · Biochemistry · doi:10.1021/bi0494471 · Cited by 88
Andreesen, J. R. (2004) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2004.08.002 · Cited by 86
Recruiting Zn2+to Mediate Potent, Specific Inhibition of Serine Proteases
Katz, B. A., & Luong, C. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3071 · Cited by 34
Konuma, T., Takai, T., Tsuchiya, C., Nishida, M., Hashiba, M., Yamada, Y., Shirai, H., Motoda, Y., Nagadoi, A., Chikaishi, E., et al. (2024) · Protein Science · doi:10.1002/pro.5002 · Cited by 1
Metadata
- Authors
- Lipscomb, W. N., & Sträter, N.
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 1996-01-01
- Volume
- 96
- Issue
- 7
- Pages
- 2375-2434
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W1986894327
- Cited by
- 1,366
- References
- 16
- FWCI
- 1.56
- Type
- journal article
- Language
- en
- Open access
- closed
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