The DOI matches its Crossref record; 67 of the 67 references it cites were found in a registry or an index.
Metal Complexes as Enzyme Inhibitors
Abstract
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTMetal Complexes as Enzyme InhibitorsAngelique Y. Louie and Thomas J. MeadeView Author Information Department of Biology, Biological Imaging Center, Beckman Institute, California Institute of Technology, Pasadena, California 91125 Cite this: Chem. Rev. 1999, 99, 9, 2711–2734Publication Date (Web):July 29, 1999Publication History Received15 February 1999Revised14 June 1999Published online29 July 1999Published inissue 8 September 1999https://pubs.acs.org/doi/10.1021/cr9804285https://doi.org/10.1021/cr9804285research-articleACS PublicationsCopyright © 1999 American Chemical SocietyRequest reuse permissionsArticle Views3968Altmetric-Citations249LEARN 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:Inhibition,Inhibitors,Ions,Metals,Peptides and proteins Get e-Alerts
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Szer, J. (1999) · Medical Journal of Australia · doi:10.5694/j.1326-5377.1999.tb127745.x · Cited by 3,353
Isolation of nitric oxide synthetase, a calmodulin-requiring enzyme.
Bredt, D. S., & Snyder, S. H. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.2.682 · Cited by 3,284
Nitric oxide, a novel neuronal messenger
Bredt, D. S., & Snyder, S. H. (1992) · Neuron · doi:10.1016/0896-6273(92)90104-l · Cited by 1,846
Huang, H., Chopra, R., Verdine, G. L., & Harrison, S. C. (1998) · Science · doi:10.1126/science.282.5394.1669 · Cited by 1,420
Atwood, C. S., Moir, R. D., Huang, X., Scarpa, R. C., Bacarra, N. M. E., Romano, D. M., Hartshorn, M. A., Tanzi, R. E., & Bush, A. I. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.21.12817 · Cited by 1,009
Molecular Recognition of Protein−Ligand Complexes: Applications to Drug Design
Babine, R. E., & Bender, S. L. (1997) · Chemical Reviews · doi:10.1021/cr960370z · Cited by 892
Nitric oxide synthase: Aspects concerning structure and catalysis
Marletta, M. A. (1994) · Cell · doi:10.1016/0092-8674(94)90268-2 · Cited by 854
Transition Metals in Control of Gene Expression
O'Halloran, T. V. (1993) · Science · doi:10.1126/science.8342038 · Cited by 626
Zinc Metabolism in the Brain: Relevance to Human Neurodegenerative Disorders
Cuajungco, M. P., & Lees, G. J. (1997) · Neurobiology of Disease · doi:10.1006/nbdi.1997.0163 · Cited by 541
Golub, L. M., Ramamurthy, N. S., McNamara, T. F., Greenwald, R. A., & Rifkin, B. R. (1991) · Critical Reviews in Oral Biology & Medicine · doi:10.1177/10454411910020030201 · Cited by 522
Mechanism of Inhibition of HIV-1 Reverse Transcriptase by Nonnucleoside Inhibitors
Spence, R. A., Kati, W. M., Anderson, K. S., & Johnson, K. A. (1995) · Science · doi:10.1126/science.7532321 · Cited by 522
Hamelin, B. (1998) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(97)01147-4 · Cited by 468
Mantyh, P. W., Ghilardi, J. R., Rogers, S., DeMaster, E., Allen, C. J., Stimson, E. R., & Maggio, J. E. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb03639.x · Cited by 465
PIN: An Associated Protein Inhibitor of Neuronal Nitric Oxide Synthase
Jaffrey, S. R., & Snyder, S. H. (1996) · Science · doi:10.1126/science.274.5288.774 · Cited by 453
Metal ions in biological systems
Vesely, J. (1982) · Journal of Electroanalytical Chemistry · doi:10.1016/0022-0728(82)87095-2 · Cited by 419
Inhibitory sites in enzymes: Zinc removal and reactivation by thionein
Maret, W., Jacob, C., Vallee, B. L., & Fischer, E. H. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.5.1936 · Cited by 386
Dyrks, T., Dyrks, E., Hartmann, T., Masters, C., & Beyreuther, K. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)37174-1 · Cited by 343
Gene targeting — homing in on α2-adrenoceptor-subtype function
MacDonald, E., Kobilka, B. K., & Scheinin, M. (1997) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(97)01063-8 · Cited by 310
Metal Ions in Biological Systems: Volume 29: Biological Properties of Metal Alkyl Derivatives
Sigel, H., & Sigel, A. (2024) · CRC Press eBooks · doi:10.1201/9781003573890 · Cited by 288
Regulation by Heme of Mitochondrial Protein Transport Through a Conserved Amino Acid Motif
Lathrop, J. T., & Timko, M. P. (1993) · Science · doi:10.1126/science.8424176 · Cited by 287
Metal Compounds in Therapy and Diagnosis
Abrams, M. J., & Murrer, B. A. (1993) · Science · doi:10.1126/science.8102010 · Cited by 281
Principles and Practice of Ophthalmology
Straatsma, B. R. (1994) · Archives of Ophthalmology · doi:10.1001/archopht.1994.01090210037012 · Cited by 260
LaFemina, R. L., Schneider, C. L., Robbins, H. L., Callahan, P. L., LeGrow, K., Roth, E., Schleif, W. A., & Emini, E. A. (1992) · Journal of Virology · doi:10.1128/jvi.66.12.7414-7419.1992 · Cited by 259
Brauman, J. I. (1993) · Science · doi:10.1126/science.8342030 · Cited by 248
Toney, J. H., Fitzgerald, P. M. D., Grover-Sharma, N., Olson, S. H., May, W. J., Sundelof, J. G., Vanderwall, D. E., Cleary, K. A., Grant, S. K., Wu, J. K., et al. (1998) · Chemistry & Biology · doi:10.1016/s1074-5521(98)90632-9 · Cited by 241
Gene targeting — homing in on α2-adrenoceptor-subtype function
MacDonald, E., Kobilka, B. K., & Scheinin, M. (1997) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(97)90625-8 · Cited by 230
Meffert, M. K., Haley, J. E., Schuman, E. M., Schulman, H., & Madison, D. V. (1994) · Neuron · doi:10.1016/0896-6273(94)90060-4 · Cited by 221
Novel Fold and Putative Receptor Binding Site of Granulocyte-Macrophage Colony-Stimulating Factor
Diederichs, K., Boone, T., & Karplus, P. A. (1991) · Science · doi:10.1126/science.1837174 · Cited by 202
Identification and Characterization of Zinc Binding Sites in Protein Kinase C
Hubbard, S. R., Bishop, W. R., Kirschmeier, P., George, S. J., Cramer, S. P., & Hendrickson, W. A. (1991) · Science · doi:10.1126/science.1763327 · Cited by 193
Hu, Y., Su, L., & Snow, E. T. (1998) · Mutation Research/DNA Repair · doi:10.1016/s0921-8777(98)00035-4 · Cited by 184
Design of potent selective zinc-mediated serine protease inhibitors
Katz, B. A., Clark, J. M., Finer-Moore, J. S., Jenkins, T. E., Johnson, C. R., Ross, M. J., Luong, C., Moore, W. R., & Stroud, R. M. (1998) · Nature · doi:10.1038/35422 · Cited by 150
Promotion of transition metal-induced reactive oxygen species formation by β-amyloid
Bondy, S. C., Guo‐Ross, S. X., & Truong, A. T. (1998) · Brain Research · doi:10.1016/s0006-8993(98)00461-2 · Cited by 141
Identification of the SH3 Domain of GAP as an Essential Sequence for Ras-GAP-Mediated Signaling
Duchesne, M., Schweighoffer, F., Parker, F., Clerc, F., Frobert, Y., THANG, M. N., & Tocqué, B. (1993) · Science · doi:10.1126/science.7678707 · Cited by 138
From Vanadis to Atropos: vanadium compounds as pharmacological tools in cell death signalling
Morinville, A., Maysinger, D., & Shaver, A. G. (1998) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(98)01257-7 · Cited by 121
Increased faecal mucin sulphatase activity in ulcerative colitis: a potential target for treatment.
Tsai, H. H., Dwarakanath, A. D., Hart, C. A., Milton, J. D., & Rhodes, J. M. (1995) · Gut · doi:10.1136/gut.36.4.570 · Cited by 111
Inhibition of poly(ADP-ribose) polymerase by arsenite
Yager, J. W., & Wiencke, J. K. (1997) · Mutation Research/Reviews in Mutation Research · doi:10.1016/s1383-5742(97)00011-2 · Cited by 110
Karlström, A. R., & Levine, R. L. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.13.5552 · Cited by 109
Bone, R. F., Frank, D., Kettner, C. A., & Agard, D. A. (1989) · Biochemistry · doi:10.1021/bi00445a015 · Cited by 88
Galbraith, R. A., Drummond, G. S., & Kappas, A. (1992) · PEDIATRICS · doi:10.1542/peds.89.2.175 · Cited by 76
Farnet, C. M., Wang, B., Hansen, M. S. T., Lipford, J. R., Zalkow, L. H., Robinson, W. E., Siegel, J. S., & Bushman, F. D. (1998) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.42.9.2245 · Cited by 73
Regulation of serine protease activity by aluminum: implications for Alzheimer disease.
Clauberg, M., & Joshi, J. G. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.3.1009 · Cited by 66
Aluminum inhibition of hexokinase activity in vitro: A study in biological availability
Exley, C., Birchall, J. D., & Price, N. C. (1994) · Journal of Inorganic Biochemistry · doi:10.1016/0162-0134(94)80035-9 · Cited by 64
In vitro inhibition of glutathione reductase by arsenotriglutathione
Stýblo, M., & Thomas, D. J. (1995) · Biochemical Pharmacology · doi:10.1016/0006-2952(95)00008-n · Cited by 64
Effects of transition metals on nitric oxide synthase catalysis
Perry, J. M., & Marletta, M. A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.19.11101 · Cited by 61
Silva, J.-L. D., Tiefenthaler, M., Park, E., Escalante, B., Schwartzman, M. L., Levere, R. D., & Abraham, N. G. (1994) · The American Journal of the Medical Sciences · doi:10.1097/00000441-199403000-00003 · Cited by 55
Pharmaceutics and Drug Delivery Aspects of Heme and Porphyrin Therapy
Cannon, J. B. (1993) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.2600820502 · Cited by 54
Effect of Heme Oxygenase Inhibitors on Soluble Guanylyl Cyclase Activity
Serfass, L., & Burstyn, J. N. (1998) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1998.0887 · Cited by 53
Effect of nitroso compounds on Na/K-ATPase
Болдырев, А. А., Bulygina, E. R., Kramarenko, G. G., & Vanin, A. F. (1997) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(97)00053-4 · Cited by 52
Miche, H., Brumas, V., & Berthon, G. (1997) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(97)00005-6 · Cited by 51
Fitzgerald, D. J. (1995) · Science · doi:10.1126/science.7604269 · Cited by 43
Mariotto, S., Cuzzolin, L., Adami, A., et al. (1995) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.1995.tb13320.x · Cited by 41
Inhibition of Ecto-5′-nucleotidase by Nitric Oxide Donors
Siegfried, G., Amiel, C., & Friedlander, G. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.9.4659 · Cited by 39
The Inactivation of Methionine Synthase in Isolated Rat Hepatocytes by Sodium Nitroprusside
Nicolaou, A., Waterfield, C. J., Kenyon, S. H., et al. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.00876.x · Cited by 38
Effects of nickel ions on polymerase activity and fidelity during DNA replication in vitro
Snow, E. T., Xu, L., & Kinney, P. L. (1993) · Chemico-Biological Interactions · doi:10.1016/0009-2797(93)90089-h · Cited by 33
Antifungal nickel(II) complexes derived from amino sugars against pathogenic yeast, Candida albicans
Yano, S., Inoue, S., Nouchi, R., Mogami, K., Shinohara, Y., Yasuda, Y., Kato, M., Tanase, T., Kakuchi, T., Mikata, Y., et al. (1998) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(97)10004-6 · Cited by 26
Myette, M. S., Elford, H. L., & Chitambar, C. R. (1998) · Cancer Letters · doi:10.1016/s0304-3835(98)00104-9 · Cited by 26
Koch, T., & Gloddek, B. (1991) · European Archives of Oto-Rhino-Laryngology · doi:10.1007/bf00627634 · Cited by 25
Modulation of carbon monoxide production and enhanced spatial learning by tin protoporphyrin
Bing, O., Grundemar, L., Ny, L., et al. (1995) · Neuroreport · doi:10.1097/00001756-199507100-00002 · Cited by 23
Biomarkers: The Clues to Genetic Susceptibility.
Zeiger, M. (1994) · Environmental Health Perspectives · doi:10.1289/ehp.9410250 · Cited by 21
Vickroy, T. W., & Malphurs, W. L. (1995) · Neurochemical Research · doi:10.1007/bf00969546 · Cited by 19
Kinetics of aluminum-induced inhibition of δ-aminolevulinic acid dehydratase In vitro
Schroeder, T. M., & Caspers, M. L. (1996) · Biochemical Pharmacology · doi:10.1016/0006-2952(96)00449-2 · Cited by 18
Weiss, G., Lutton, J., Fuchs, D., Werner-Felmayer, G., Bock, G., Abraham, N., Kappas, A., Levere, R., & Wachter, H. (1993) · Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine · doi:10.3181/00379727-202-43561 · Cited by 17
Current Concepts in the Treatment of Rheumatoid Arthritis
Baker, D. G., & Rabinowitz, J. L. (1986) · The Journal of Clinical Pharmacology · doi:10.1002/j.1552-4604.1986.tb02896.x · Cited by 14
De novo drug design of a new copper chelate molecule acting as HIV-1 protease inhibitor
Lebon, F., de Rosny, E., Reboud‐Ravaux, M., & Durant, F. (1998) · European Journal of Medicinal Chemistry · doi:10.1016/s0223-5234(98)80032-9 · Cited by 13
Nocentini, G., & Barzi, A. (1996) · Biochemical Pharmacology · doi:10.1016/0006-2952(96)00139-6 · Cited by 12
Functional and Structural Effects of ACE Inhibitors on the Cardiovascular System
Heagerty, A. M. (2008) · Cardiology · doi:10.1159/000174899 · Cited by 10
Copper complex of a new ribonucleotide reductase inhibitor characterized by antitumoral properties
Nocentini, G., Federici, F., Grifantini, M., & Barzi, A. (1992) · Pharmacological Research · doi:10.1016/1043-6618(92)90421-7 · Cited by 5
Cited by
Potential applications of peroxidases
Hamid, M., & Khalil-ur-Rehman (2009) · Food Chemistry · doi:10.1016/j.foodchem.2009.02.035 · Cited by 312
Smith, A. J. T., Zhang, X., Leach, A. G., & Houk, K. N. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm800498e · Cited by 193
Metadata
- Authors
- Louie, A. Y., & Meade, T. J.
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 1999-07-29
- Volume
- 99
- Issue
- 9
- Pages
- 2711-2734
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W2014044312
- Cited by
- 301
- References
- 67
- FWCI
- 0.41
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.