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Synthetic Analogues Relevant to the Structure and Function of Zinc Enzymes
Abstract
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTSynthetic Analogues Relevant to the Structure and Function of Zinc EnzymesGerard ParkinView Author Information Department of Chemistry, Columbia University, New York, New York 10027 Cite this: Chem. Rev. 2004, 104, 2, 699–768Publication Date (Web):January 24, 2004Publication History Received14 July 2003Published online24 January 2004Published inissue 1 February 2004https://pubs.acs.org/doi/10.1021/cr0206263https://doi.org/10.1021/cr0206263research-articleACS PublicationsCopyright © 2004 American Chemical SocietyRequest reuse permissionsArticle Views7617Altmetric-Citations829LEARN 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:Anions,Ligands,Monomers,Peptides and proteins,Zinc Get e-Alerts
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Citations
Cites
Nagase, H., & Woessner, J. F. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.31.21491 · Cited by 3,912
J Antimicrob Chemother 1994; 33: 350–351
O'SHAUGHNESSY, E. M., & DAS, S. S. (1994) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/33.2.350 · Cited by 3,746
Matrix metalloproteinases and their inhibitors in connective tissue remodeling
Woessner, J. F. (1991) · The FASEB Journal · doi:10.1096/fasebj.5.8.1850705 · Cited by 3,282
Relativistic effects in structural chemistry
Pyykko, P. (1988) · Chemical Reviews · doi:10.1021/cr00085a006 · Cited by 3,046
The biochemical basis of zinc physiology
Vallee, B. L., & Falchuk, K. H. (1993) · Physiological Reviews · doi:10.1152/physrev.1993.73.1.79 · Cited by 2,990
Matrix Metalloproteinase Inhibitors and Cancer—Trials and Tribulations
Coussens, L. M., Fingleton, B., & Matrisian, L. M. (2002) · Science · doi:10.1126/science.1067100 · Cited by 2,761
Zinc coordination, function, and structure of zinc enzymes and other proteins
Vallee, B. L., & Auld, D. S. (1990) · Biochemistry · doi:10.1021/bi00476a001 · Cited by 1,777
Zinc finger proteins: new insights into structural and functional diversity
Laity, J. H., Lee, B. M., & Wright, P. E. (2001) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(00)00167-6 · Cited by 1,534
Recent Advances in Zinc Enzymology
Lipscomb, W. N., & Sträter, N. (1996) · Chemical Reviews · doi:10.1021/cr950042j · Cited by 1,366
Sundberg, R. J., & Martin, R. B. (1974) · Chemical Reviews · doi:10.1021/cr60290a003 · Cited by 1,147
Structure and mechanism of carbonic anhydrase
Lindskog, S. (1997) · Pharmacology & Therapeutics · doi:10.1016/s0163-7258(96)00198-2 · Cited by 1,022
Biomimetic Chemistry and Artificial Enzymes: Catalysis by Design
Breslow, R. (1995) · Accounts of Chemical Research · doi:10.1021/ar00051a008 · Cited by 989
Design and Therapeutic Application of Matrix Metalloproteinase Inhibitors
Whittaker, M., Floyd, C. D., Brown, P., & Gearing, A. J. H. (1999) · Chemical Reviews · doi:10.1021/cr9804543 · Cited by 982
ZINC PROTEINS: Enzymes, Storage Proteins, Transcription Factors, and Replication Proteins
Coleman, J. E. (1992) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.61.070192.004341 · Cited by 978
Structural classification of zinc fingers: SURVEY AND SUMMARY
Krishna, S. S. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg161 · Cited by 917
Wilcox, D. E. (1996) · Chemical Reviews · doi:10.1021/cr950043b · Cited by 893
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
Families of zinc metalloproteases
Hooper, N. M. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)01079-x · Cited by 790
Stöcker, W., Grams, F., Reinemer, P., Bode, W., Baumann, U., Gomis‐Rüth, F., & Mckay, D. B. (1995) · Protein Science · doi:10.1002/pro.5560040502 · Cited by 726
Springman, E. B., Angleton, E. L., Birkedal-Hansen, H., & Van Wart, H. E. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.1.364 · Cited by 713
Snake venoms and the hemostatic system
Markland, F. S. (1998) · Toxicon · doi:10.1016/s0041-0101(98)00126-3 · Cited by 703
Structural basis of the action of thermolysin and related zinc peptidases
Matthews, B. W. (1988) · Accounts of Chemical Research · doi:10.1021/ar00153a003 · Cited by 687
Two‐Metal Ion Catalysis in Enzymatic Acyl‐ and Phosphoryl‐Transfer Reactions
Sträter, N., Lipscomb, W. N., Klabunde, T., & Krebs, B. (1996) · Angewandte Chemie International Edition in English · doi:10.1002/anie.199620241 · Cited by 611
Christianson, D. W., & Lipscomb, W. N. (1989) · Accounts of Chemical Research · doi:10.1021/ar00158a003 · Cited by 606
Carbonic Anhydrase: New Insights for an Ancient Enzyme
Tripp, B. C., Smith, K., & Ferry, J. G. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.r100045200 · Cited by 565
Metalloenzymes, Structural Motifs, and Inorganic Models
Karlin, K. D. (1993) · Science · doi:10.1126/science.7688141 · Cited by 554
Håkansson, K., Carlsson, M., Svensson, L. A., & Liljas, A. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90531-n · Cited by 511
Carbonic anhydrase. Purification and nature of the enzyme
Keilin, D., & Mann, T. (1940) · Biochemical Journal · doi:10.1042/bj0341163 · Cited by 493
Carbonic Anhydrase: Evolution of the Zinc Binding Site by Nature and by Design
Christianson, D. W., & Fierke, C. A. (1996) · Accounts of Chemical Research · doi:10.1021/ar9501232 · Cited by 475
Developing artificial hydrolytic metalloenzymes by a unified mechanistic approach
Chin, J. (1991) · Accounts of Chemical Research · doi:10.1021/ar00005a004 · Cited by 471
Principles Governing Mg, Ca, and Zn Binding and Selectivity in Proteins
Dudev, T., & Lim, C. (2003) · Chemical Reviews · doi:10.1021/cr020467n · Cited by 464
Structure of thermolysin refined at 1.6 Å resolution
Holmes, M. A., & Matthews, B. W. (1982) · Journal of Molecular Biology · doi:10.1016/0022-2836(82)90319-9 · Cited by 439
Active-site zinc ligands and activated H2O of zinc enzymes.
Vallee, B. L., & Auld, D. S. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.1.220 · Cited by 437
Crystal Structure of a Purple Acid Phosphatase Containing a Dinuclear Fe(III)-Zn(II) Active Site
Sträter, N., Klabunde, T., Tucker, P., Witzel, H., & Krebs, B. (1995) · Science · doi:10.1126/science.7770774 · Cited by 434
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
Three classes of C2H2 zinc finger proteins
Iuchi, S. (2001) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000885 · Cited by 415
Zinc: biological functions and coordination motifs
Vallee, B. L., & Auld, D. S. (1993) · Accounts of Chemical Research · doi:10.1021/ar00034a005 · Cited by 412
Dinuclear metallo-phosphodiesterase models: application of calix[4]arenes as molecular scaffolds
Molenveld, P., Engbersen, J. F. J., & Reinhoudt, D. N. (2000) · Chemical Society Reviews · doi:10.1039/a804295k · Cited by 392
(1989) · ILSI Human Nutrition Reviews · doi:10.1007/978-1-4471-3879-2 · Cited by 382
Catalysis By Metal-Activated Hydroxide in Zinc and Manganese Metalloenzymes
Christianson, D. W., & Cox, J. D. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.33 · Cited by 377
Mechanism of Fe(III) – Zn(II) Purple Acid Phosphatase Based on Crystal Structures
Klabunde, T., Sträter, N., Fröhlich, R., Witzel, H., & Krebs, B. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0354 · Cited by 365
Coleman, J. E. (1998) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(98)80064-1 · Cited by 362
A zinc(II) complex of 1,5,9-triazacyclododecane ([12]aneN3) as a model for carbonic anhydrase
Kimura, E., Shiota, T., Koike, T., Shiro, M., & Kodama, M. (1990) · Journal of the American Chemical Society · doi:10.1021/ja00171a020 · Cited by 359
Multiple Origins of Lichen Symbioses in Fungi Suggested by SSU rDNA Phylogeny
Gargas, A., DePriest, P. T., Grube, M., & Tehler, A. (1995) · Science · doi:10.1126/science.7770775 · Cited by 357
The biological chemistry of lead
Godwin, H. A. (2001) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(00)00194-0 · Cited by 356
Metalloaminopeptidases: Common Functional Themes in Disparate Structural Surroundings
Lowther, W. T., & Matthews, B. W. (2002) · Chemical Reviews · doi:10.1021/cr0101757 · Cited by 350
Geometry of metal–ligand interactions in proteins
Harding, M. M. (2001) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444900019168 · Cited by 348
Structural properties of matrix metalloproteinases
Bode, W., Fernandez-Catalan, C., Grams, H. T., & Maskos, H. N. (1999) · Cellular and Molecular Life Sciences (CMLS) · doi:10.1007/s000180050320 · Cited by 329
Guan, Y., Manuel, R. C., Arvai, A. S., Parikh, S. S., Mol, C. D., Miller, J. H., Lloyd, R. S., & Tainer, J. A. (1998) · Nature Structural Biology · doi:10.1038/4168 · Cited by 325
Modeling Coordination Sites in Metallobiomolecules
Ibers, J. A., & Holm, R. H. (1980) · Science · doi:10.1126/science.7384796 · Cited by 324
A revised mechanism for the alkaline phosphatase reaction involving three metal ions
Stec, B., Holtz, K. M., & Kantrowitz, E. R. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3799 · Cited by 305
Molecular Mechanisms of Lead Neurotoxicity
Bressler, J., Kim, K.-A., Chakraborti, T., & Goldstein, G. (1999) · Neurochemical Research · doi:10.1023/a:1022596115897 · Cited by 297
Deletion of the Paired α5(IV) and α6(IV) Collagen Genes in Inherited Smooth Muscle Tumors
Zhou, J., Mochizuki, T., Smeets, H., Antignac, C., Laurila, P., de Paepe, A., Tryggvason, K., & Reeders, S. T. (1993) · Science · doi:10.1126/science.8356449 · Cited by 296
Cobalamin-Dependent Methyltransferases
Matthews, R. G. (2001) · Accounts of Chemical Research · doi:10.1021/ar0000051 · Cited by 285
Metal Ions in Biological Systems
(2001) · CRC Press eBooks · doi:10.1201/9781482270150 · Cited by 275
A Novel pH‐Sensitive MRI Contrast Agent
Zhang, S., Wu, K., & Sherry, A. D. (1999) · Angewandte Chemie International Edition · Cited by 259
Structural features of a superfamily of zinc-endopeptidases: the metzincins
Stöcker, W., & Bode, W. (1995) · Current Opinion in Structural Biology · doi:10.1016/0959-440x(95)80101-4 · Cited by 241
New perspective on zinc biochemistry: Cocatalytic sites in multi-zinc enzymes
Vallee, B. L., & Auld, D. S. (1993) · Biochemistry · doi:10.1021/bi00077a001 · Cited by 235
Where freedom is given, liberties are taken
Kleywegt, G. J., & Jones, T. A. (1995) · Structure · doi:10.1016/s0969-2126(01)00187-3 · Cited by 229
The geometry of metal–ligand interactions relevant to proteins
Harding, M. M. (1999) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444999007374 · Cited by 229
Molecular Reactions of Protein PhosphatasesInsights from Structure and Chemistry
Jackson, M. D., & Denu, J. M. (2001) · Chemical Reviews · doi:10.1021/cr000247e · Cited by 216
Looney, A., Han, R., Gorrell, I. B., Cornebise, M., Yoon, K., Parkin, G., & Rheingold, A. L. (1995) · Organometallics · doi:10.1021/om00001a041 · Cited by 208
Self-citationDudev, T., Lin, Dudev, M., & Lim, C. (2003) · Journal of the American Chemical Society · doi:10.1021/ja0209722 · Cited by 205
Looney, A., Han, R., McNeill, K., & Parkin, G. (1993) · Journal of the American Chemical Society · doi:10.1021/ja00064a033 · Cited by 197
Self-citationModel Studies for Molecular Recognition of Carbonic Anhydrase and Carboxypeptidase
Kimura, E. (2001) · Accounts of Chemical Research · doi:10.1021/ar000001w · Cited by 190
Metal Substitutions and Inhibition of Thermolysin: Spectra of the Cobalt Enzyme
Holmquist, B., & Vallee, B. L. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42460-5 · Cited by 189
Structural analysis of zinc substitutions in the active site of thermolysin
Holland, D. R., Hausrath, A. C., Juers, D., & Matthews, B. W. (1995) · Protein Science · doi:10.1002/pro.5560041001 · Cited by 187
Krämer, R. (1999) · Coordination Chemistry Reviews · doi:10.1016/s0010-8545(98)00235-5 · Cited by 179
Agarwal, P. K., Webb, S. P., & Hammes-Schiffer, S. (2000) · Journal of the American Chemical Society · doi:10.1021/ja994456w · Cited by 178
Lead poisoning, haem synthesis and 5-aminolaevulinic acid dehydratase
Warren, M. J., Cooper, J. B., Wood, S. P., & Shoolingin-Jordan, P. M. (1998) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(98)01219-5 · Cited by 169
Hartwig, A., Asmuß, M., Blessing, H., Hoffmann, S. A., Jahnke, G., Khandelwal, S. K., Pelzer, A., & Bürkle, A. (2002) · Food and Chemical Toxicology · doi:10.1016/s0278-6915(02)00043-1 · Cited by 151
Zinc Gluconate Lozenges for Treating the Common Cold in Children: A Randomized Controlled Trial
Macknin, M. L., PIEDMONTE, M. R., Calendine, C. L., Janosky, J. J., & Wald, E. R. (1998) · JAMA · doi:10.1001/jama.279.24.1962 · Cited by 150
Porphobilinogen synthase, the first source of Heme's asymmetry
Jaffe, E. K. (1995) · Journal of Bioenergetics and Biomembranes · doi:10.1007/bf02110032 · Cited by 150
Metal-binding sites in proteins
Tainer, J. A., Roberts, V. A., & Getzoff, E. D. (1991) · Current Opinion in Biotechnology · doi:10.1016/0958-1669(91)90084-i · Cited by 150
Progress towards synthetic enzymes for phosphoester hydrolysis
Komiyama, M., & Sumaoka, J. (1998) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(98)80113-0 · Cited by 146
X-ray structure of 5-aminolaevulinate dehydratase, a hybrid aldolase
Erskine, P. T., Senior, N., Awan, S. J., et al. (1997) · Nature Structural Biology · doi:10.1038/nsb1297-1025 · Cited by 145
Inhibition and catalysis of carbonic anhydrase
Liljas, A., HÅKANSSON, K., JONSSON, B. H., & Xue, Y. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.tb19909.x · Cited by 140
Wetmur, J. G., Lehnert, G., & Desnick, R. J. (1991) · Environmental Research · doi:10.1016/s0013-9351(05)80001-5 · Cited by 139
Characterization of cobalt(II) bovine carbonic anhydrase and of its derivatives
Bertini, I., Canti, G., Luchinat, C., & Scozzafava, A. (1978) · Journal of the American Chemical Society · doi:10.1021/ja00483a038 · Cited by 138
Lipscomb, W. N. (1970) · Accounts of Chemical Research · doi:10.1021/ar50027a001 · Cited by 137
Enzyme-catalyzed methyl transfers to thiols: the role of zinc
Matthews, R. G., & Goulding, C. W. (1997) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(97)80070-1 · Cited by 137
Cobalt(II) as a probe of the structure and function of carbonic anhydrase
Bertini, I., & Luchinat, C. (1983) · Accounts of Chemical Research · doi:10.1021/ar00092a002 · Cited by 132
Holland, D. R., Tronrud, D. E., Pley, H. W., Flaherty, K. M., Stark, W., Jansonius, J. N., McKay, D., & Matthews, B. W. (1992) · Biochemistry · doi:10.1021/bi00161a008 · Cited by 131
Bergquist, C., Fillebeen-Khan, T., Morlok, M. M., & Parkin, G. (2003) · Journal of the American Chemical Society · doi:10.1021/ja034711j · Cited by 131
Self-citation[14] Removal and replacement of metal ions in metallopeptidases
Auld, D. S. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(95)48016-1 · Cited by 128
Comparison of the structures of carboxypeptidase A and thermolysin.
Kester, W. R., & Matthews, B. W. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)41025-8 · Cited by 128
Jedrzejas, M. J., & Setlow, P. (2001) · Chemical Reviews · doi:10.1021/cr000253a · Cited by 128
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
Solvent Dynamics and Mechanism of Proton Transfer in Human Carbonic Anhydrase II
Toba, S., Colombo, G., & Merz, K. M. (1999) · Journal of the American Chemical Society · doi:10.1021/ja983579y · Cited by 126
Koike, T., Kimura, E., Nakamura, I., Hashimoto, Y., & Shiro, M. (1992) · Journal of the American Chemical Society · doi:10.1021/ja00045a002 · Cited by 126
Structure of carboxypeptidase B at 2.8 Å resolution
Schmid, M. F., & Herriott, J. R. (1976) · Journal of Molecular Biology · doi:10.1016/0022-2836(76)90058-9 · Cited by 124
Peariso, K., Goulding, C. W., Huang, S., Matthews, R. G., & Penner‐Hahn, J. E. (1998) · Journal of the American Chemical Society · doi:10.1021/ja980581g · Cited by 123
STRUCTURE AND CATALYSIS OF ENZYMES
Lipscomb, W. N. (1983) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.52.070183.000313 · Cited by 121
Adamalysins: A Family of Metzincins Including TNF‐α Converting Enzyme (TACE)
Killar, L. M., White, J. M., Black, R. A., & Peschon, J. J. (1999) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1999.tb07701.x · Cited by 114
Exploring the structure and function of zinc metallopeptidases: old enzymes and new discoveries
Turner, A. J. (2003) · Biochemical Society Transactions · doi:10.1042/bst0310723 · Cited by 110
Examination of Novel Zinc-Binding Groups for Use in Matrix Metalloproteinase Inhibitors
Puerta, D. T., & Cohen, S. M. (2003) · Inorganic Chemistry · doi:10.1021/ic026029g · Cited by 109
Harding, M. M. (2000) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444900005849 · Cited by 109
Smedarchina, Z. K., Siebrand, W., Fernández‐Ramos, A., & Cui, Q. (2002) · Journal of the American Chemical Society · doi:10.1021/ja0210594 · Cited by 109
Garmer, D. R., & Gresh, N. (1994) · Journal of the American Chemical Society · doi:10.1021/ja00087a049 · Cited by 106
Terminal steps of haem biosynthesis
Dailey, H. A. (2002) · Biochemical Society Transactions · doi:10.1042/bst0300590 · Cited by 105
Catalytic Mechanism of Matrix Metalloproteinases: Two-Layered ONIOM Study
Pelmenschikov, V., & Siegbahn, P. E. M. (2002) · Inorganic Chemistry · doi:10.1021/ic0255656 · Cited by 105
Factors Governing the Protonation State of Cysteines in Proteins: An Ab Initio/CDM Study
Dudev, T., & Lim, C. (2002) · Journal of the American Chemical Society · doi:10.1021/ja012620l · Cited by 104
The porphobilinogen synthase family of metalloenzymes
Jaffe, E. K. (2000) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444999014894 · Cited by 104
Zinc Pyrazolylborate Complexes Relevant to the Biological Function of Carbonic Anhydrase
Looney, A. G., Parkin, G., Alsfasser, R., Ruf, M., & Vahrenkamp, H. (1992) · Angewandte Chemie International Edition in English · doi:10.1002/anie.199200921 · Cited by 102
Self-citationWhy zinc in zinc enzymes? From biological roles to DNA base-selective recognition
Kimura, E., & Kikuta, E. (2000) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s007750050359 · Cited by 101
LIANG, Z., Xue, Y., Behravan, G., Jonsson, B., & LINDSKOG, S. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb17614.x · Cited by 98
Erskine, P. T., Norton, E., Cooper, J. B., Lambert, R., Coker, A. R., Lewis, G., Spencer, P., Sarwar, M., Wood, S., Warren, M. J., et al. (1999) · Biochemistry · doi:10.1021/bi982137w · Cited by 97
CLEAVER, E. J., & States, J. C. (1997) · Biochemical Journal · doi:10.1042/bj3280001 · Cited by 95
Sigel, H., & Martin, R. B. (1994) · Chemical Society Reviews · doi:10.1039/cs9942300083 · Cited by 95
Cross, J. B., Duca, J. S., Kaminski, J. J., & Madison, V. (2002) · Journal of the American Chemical Society · doi:10.1021/ja0201810 · Cited by 93
Bracey, M. H., Christiansen, J., Tovar, P., Cramer, S. P., & Bartlett, S. G. (1994) · Biochemistry · doi:10.1021/bi00248a023 · Cited by 92
Brand, U., Rombach, M., Seebacher, J., et al. (2001) · Inorganic Chemistry · doi:10.1021/ic0105112 · Cited by 92
Structure of cobalt carbonic anhydrase complexed with bicarbonate
Håkansson, K., & Wehnert, A. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90327-g · Cited by 90
Allen, C. S., Chuang, C.-L., Cornebise, M., & Canary, J. W. (1995) · Inorganica Chimica Acta · doi:10.1016/0020-1693(95)04710-7 · Cited by 89
Dihydroorotase from Escherichia coli. Purification and characterization.
Washabaugh, M. W., & Collins, K. D. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)43293-5 · Cited by 87
Solution structure of the DNA methyl phosphotriester repair domain of Escherichia coli Ada
Myers, L. C., Verdine, G. L., & Wagner, G. (1993) · Biochemistry · doi:10.1021/bi00214a003 · Cited by 86
Zinc-catalyzed sulfur alkylation: insights from protein farnesyltransferase
Hightower, K. E., & Fierke, C. A. (1999) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(99)80030-1 · Cited by 85
Quantitative Reactivity Model for the Hydration of Carbon Dioxide by Biomimetic Zinc Complexes
Bräuer, M., Lustres, J. L. P., Weston, J., & Anders, E. (2002) · Inorganic Chemistry · doi:10.1021/ic0010510 · Cited by 85
Kremer‐Aach, A., Kläui, W., Bell, R., Strerath, A., Wunderlich, H., & Mootz, D. (1997) · Inorganic Chemistry · doi:10.1021/ic961434r · Cited by 83
Tainer, J. A., Roberts, V. A., & Getzoff, E. D. (1992) · Current Opinion in Biotechnology · doi:10.1016/0958-1669(92)90166-g · Cited by 82
Elucidating Drug-Metalloprotein Interactions with Tris(pyrazolyl)borate Model Complexes
Puerta, D. T., & Cohen, S. M. (2002) · Inorganic Chemistry · doi:10.1021/ic0204272 · Cited by 81
Nakata, K., Shimomura, N., Shiina, N., Izumi, M., Ichikawa, K., & Shiro, M. (2002) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(01)00419-6 · Cited by 80
Hammes, B. S., & Carrano, C. J. (2001) · Inorganic Chemistry · doi:10.1021/ic001178p · Cited by 78
Matsuda, S., Ishikubo, A., Kuzuya, A., Yashiro, M., & Komiyama, M. (1998) · Angewandte Chemie International Edition · Cited by 78
Short and long spacer sequences and other structural features of zinc binding sites in zinc enzymes
Vallée, B. L., & Auld, D. S. (1989) · FEBS Letters · doi:10.1016/0014-5793(89)81805-8 · Cited by 78
The structure of neutral protease from Bacillus cereus at 0.2‐nm resolution
Stark, W., Pauptit, R. A., Wilson, K. S., & Jansonius, J. N. (1992) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1992.tb17109.x · Cited by 78
Suárez, D., Brothers, E. N., & Merz, K. M. (2002) · Biochemistry · doi:10.1021/bi0121860 · Cited by 77
Porphobilinogen Synthase from Escherichia coli is a Zn(II) Metalloenzyme Stimulated by Mg(II)
Mitchell, L. W., & Jaffe, E. K. (1993) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1993.1024 · Cited by 74
Lead, glass and the environment
Hynes, M. J., & Jonson, B. (1997) · Chemical Society Reviews · doi:10.1039/cs9972600133 · Cited by 73
Thermolysin and neutral protease. Mechanistic considerations
Pangburn, M. K., & Walsh, K. A. (1975) · Biochemistry · doi:10.1021/bi00689a019 · Cited by 73
An Unusual Phylogenetic Variation in the Metal Ion Binding Sites of Porphobilinogen Synthase
Jaffe, E. K. (2003) · Chemistry & Biology · doi:10.1016/s1074-5521(02)00296-x · Cited by 73
Motekaitis, R. J., Martell, A. E., & Welch, M. J. (1990) · Inorganic Chemistry · doi:10.1021/ic00333a005 · Cited by 70
CysxHisyZn2+ interactions: Thiol vs. thiolate coordination
Simonson, T., & Calimet, N. (2002) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.10200 · Cited by 70
Hydrolysis of phosphates, esters and related substrates by models of biological catalysts
Bashkin, J. K. (1999) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(99)00036-8 · Cited by 69
Practical hardness scales for metal ion complexes
Martin, R. B. (2002) · Inorganica Chimica Acta · doi:10.1016/s0020-1693(02)00922-2 · Cited by 68
Trachtman, M., Markham, G. D., GLUSKER, J. P., George, P., & Bock, C. W. (1998) · Inorganic Chemistry · doi:10.1021/ic971613o · Cited by 68
[22] Atrolysins: Metalloproteinases from Crotalus atrox venom
Fox, J. W., & Bjarnason, J. B. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(95)48024-2 · Cited by 66
Silver, A., Koch, S. A., & Millar, M. M. (1993) · Inorganica Chimica Acta · doi:10.1016/s0020-1693(00)87348-x · Cited by 65
Petrus, E. J., Lawson, K. A., Bucci, L. R., & Blum, K. (1998) · Current Therapeutic Research · doi:10.1016/s0011-393x(98)85058-3 · Cited by 61
Kumar, V., & Kannan, K. K. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1491 · Cited by 60
Ichikawa, K., Tarnai, M., Uddin, M. K., Nakata, K., & Sato, S. (2002) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(02)00452-x · Cited by 59
Merkx, M., & Averill, B. A. (1999) · Journal of the American Chemical Society · doi:10.1021/ja9837147 · Cited by 57
Pyrazolylborate−Zinc−Hydrosulfide Complexes and Their Reactions
Rombach, M., & Vahrenkamp, H. (2001) · Inorganic Chemistry · doi:10.1021/ic010510+ · Cited by 55
Dowling, C., & Parkin, G. (1996) · Polyhedron · doi:10.1016/0277-5387(96)00014-9 · Cited by 55
Self-citationLipton, A. S., Buchko, G. W., Sears, J. A., Kennedy, M. A., & Ellis, P. D. (2001) · Journal of the American Chemical Society · doi:10.1021/ja003720e · Cited by 54
Kaptein, B., Barf, G. A., Kellogg, R. M., et al. (1990) · The Journal of Organic Chemistry · doi:10.1021/jo00293a039 · Cited by 54
Frère, F., Schubert, W., Stauffer, F., Frankenberg‐Dinkel, N., Neier, R., Jahn, D., & Heinz, D. W. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00472-2 · Cited by 53
The catalytic mechanism of carbonic anhydrase
Silverman, D. N. (1991) · Canadian Journal of Botany · doi:10.1139/b91-137 · Cited by 51
LEAD-THE TOXIC METAL TO STAY WITH HUMAN
Srianujata, S. (1998) · The Journal of Toxicological Sciences · doi:10.2131/jts.23.supplementii_237 · Cited by 48
Kervinen, J., Jaffe, E. K., Stauffer, F., Neier, R., Wlodawer, A., & Zdanov, A. S. (2001) · Biochemistry · doi:10.1021/bi010656k · Cited by 48
Buchko, G. W., Hess, N. J., & Kennedy, M. A. (2000) · Carcinogenesis · doi:10.1093/carcin/21.5.1051 · Cited by 48
The schiff base complex of yeast 5‐aminolaevulinic acid dehydratase with laevulinic acid
Erskine, P. T., Newbold, R., Roper, J., Coker, A. R., Warren, M. J., Shoolingin‐Jordan, P. M., Wood, S., & Cooper, J. B. (1999) · Protein Science · doi:10.1110/ps.8.6.1250 · Cited by 46
Bridgewater, B. M., & Parkin, G. (2001) · Inorganic Chemistry Communications · doi:10.1016/s1387-7003(00)00218-5 · Cited by 42
Self-citationTanase, T., 犬飼裕美, Onaka, T., Kato, M., Yano, S., & Lippard, S. J. (2001) · Inorganic Chemistry · doi:10.1021/ic001419t · Cited by 41
Drug-Resistant HIV-1: The Virus Strikes Back
Mayers, D. L. (1998) · JAMA · doi:10.1001/jama.279.24.2000 · Cited by 41
Lipton, A. S., Bergquist, C., Parkin, G., & Ellis, P. D. (2003) · Journal of the American Chemical Society · doi:10.1021/ja021328q · Cited by 41
Self-citationSpencer, P., & Jordan, P. M. (1994) · Biochemical Journal · doi:10.1042/bj3000373 · Cited by 41
Conservation of cytoplasmic poly(A)-containing RNA in mouse and rat
Rosbash, M., Campo, M. S., & Gummerson, K. S. (1975) · Nature · doi:10.1038/258682a0 · Cited by 40
Campagna, D., Huel, G., Girard, F., Sahuquillo, J., & Blot, P. (1999) · Toxicology · doi:10.1016/s0300-483x(99)00031-1 · Cited by 38
Kimura, E., Gotoh, T., Aoki, S., & Shiro, M. (2002) · Inorganic Chemistry · doi:10.1021/ic020087k · Cited by 37
Erskine, P. T., Duke, E., Tickle, I. J., Senior, N., Warren, M. J., & Cooper, J. B. (2000) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444900000597 · Cited by 36
Hambidge, M., & Krebs, N. F. (1999) · The Journal of Pediatrics · doi:10.1016/s0022-3476(99)70080-6 · Cited by 34
Gockel, P., Gelinsky, M., Vogler, R., & Vahrenkamp, H. (1998) · Inorganica Chimica Acta · doi:10.1016/s0020-1693(97)05875-1 · Cited by 33
Predicting the Zn(II) Ligands in Metalloproteins: Case Study, Porphobilinogen Synthase
Jaffe, E. K. (1993) · Comments on Inorganic Chemistry · doi:10.1080/02603599308035837 · Cited by 33
Otto, J., Jolk, I., Viland, T., Wonnemann, R., & Krebs, B. (1999) · Inorganica Chimica Acta · doi:10.1016/s0020-1693(98)00351-x · Cited by 31
5-Aminolaevulinic acid dehydratase: metals, mutants and mechanism
Shoolingin‐Jordan, P. M., Spencer, P., Sarwar, M., Erskine, P. T., Cheung, K.-M., Cooper, J. B., & Norton, E. (2002) · Biochemical Society Transactions · doi:10.1042/bst0300584 · Cited by 31
Arias, C. F., Bell, J. R., Lenches, E. M., et al. (1983) · Journal of Molecular Biology · doi:10.1016/s0022-2836(83)80324-6 · Cited by 30
On the Role of Structural Zinc in Bis(Cysteinyl) Protein Sequences
Meißner, A., Haehnel, W., & Vahrenkamp, H. (1997) · Chemistry - A European Journal · doi:10.1002/chem.19970030215 · Cited by 30
Denisov, V. P., Jonsson, B., & Halle, B. (1999) · Journal of the American Chemical Society · doi:10.1021/ja983930f · Cited by 29
Kurisu, G., Kai, Y., & Harada, S. (2000) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(00)00136-7 · Cited by 27
Species-specific Inhibition of Porphobilinogen Synthase by 4-Oxosebacic Acid
Jaffe, E. K., Kervinen, J., Martins, J., Stauffer, F., Neier, R., Wlodawer, A., & Zdanov, A. S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201486200 · Cited by 24
Zinc lozenges for the common cold
Macknin, M. L. (1999) · Cleveland Clinic Journal of Medicine · doi:10.3949/ccjm.66.1.27 · Cited by 21
Toward Ligand Identification within a CCHHC Zinc-Binding Domain from the NZF/MyT1 Family
Blasie, C. A., & Berg, J. M. (1999) · Inorganic Chemistry · doi:10.1021/ic990913y · Cited by 20
Acceleration of p-Nitrophenyl Ester Cleavage by Zn(II)-Organized Molecular Receptors
Tecilla, P., Tonellato, U., VERONESE, A. C., Felluga, F., & Scrimin, P. (1997) · The Journal of Organic Chemistry · doi:10.1021/jo970783f · Cited by 19
Witter, R., Seyfart, L., Greiner, G., Reißmann, S., Weston, J., Anders, E., & Sternberg, U. (2002) · Journal of Biomolecular NMR · doi:10.1023/a:1021625231147 · Cited by 18
Crustacean Eye Fine Structure Seen with Scanning Electron Microscopy
Waterman, T. H., & Pooley, A. S. (1980) · Science · doi:10.1126/science.209.4453.235 · Cited by 17
A Topical Carbonic Anhydrase Inhibitor Finally Arrives
Palmberg, P. F. (1995) · Archives of Ophthalmology · doi:10.1001/archopht.1995.01100080035025 · Cited by 14
Bertini, I., & Luchinat, C. (1984) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1984.tb12318.x · Cited by 13
X-ray diffraction studies on carboxypeptidase A complexes: the zinc stereochemistry
Mangani, S., Carloni, P., & Orioli, P. (1992) · Coordination Chemistry Reviews · doi:10.1016/0010-8545(92)80057-x · Cited by 12
Buchko, G. W., Iakoucheva, L. M., Kennedy, M. A., Ackerman, E. J., & Hess, N. J. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.9890 · Cited by 12
Hydrolysis of 4-Nitrophenyl Phosphate by (Amino Acidato)zinc Complexes
Viladkar, S., Kamaluddin, K., & Nath, M. (1993) · Bulletin of the Chemical Society of Japan · doi:10.1246/bcsj.66.2922 · Cited by 8
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Metadata
- Authors
- Parkin, G.
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2004-01-24
- Volume
- 104
- Issue
- 2
- Pages
- 699-768
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W2041114202
- Cited by
- 931
- References
- 181
- FWCI
- 2.35
- Type
- journal article
- Language
- en
- Open access
- closed
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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.
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Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.