Zinc biochemistry: From a single zinc enzyme to a key element of life
Open accessAbstract
The nutritional essentiality of zinc for the growth of living organisms had been recognized long before zinc biochemistry began with the discovery of zinc in carbonic anhydrase in 1939. Painstaking analytical work then demonstrated the presence of zinc as a catalytic and structural cofactor in a few hundred enzymes. In the 1980s, the field again gained momentum with the new principle of "zinc finger" proteins, in which zinc has structural functions in domains that interact with other biomolecules. Advances in structural biology and a rapid increase in the availability of gene/protein databases now made it possible to predict zinc-binding sites from metal-binding motifs detected in sequences. This procedure resulted in the definition of zinc proteomes and the remarkable estimate that the human genome encodes ∼3000 zinc proteins. More recent developments focus on the regulatory functions of zinc(II) ions in intra- and intercellular information transfer and have tantalizing implications for yet additional functions of zinc in signal transduction and cellular control. At least three dozen proteins homeostatically control the vesicular storage and subcellular distribution of zinc and the concentrations of zinc(II) ions. Novel principles emerge from quantitative investigations on how strongly zinc interacts with proteins and how it is buffered to control the remarkably low cellular and subcellular concentrations of free zinc(II) ions. It is fair to conclude that the impact of zinc for health and disease will be at least as far-reaching as that of iron.
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Zinc influences the structure and proper functioning of the skin and mucous membranes.
“The element influences the structure and proper functioning of the skin and mucous membranes [98,100].”
From Bioactive Compounds for Skin Health: A Review (2021) · cites this paper as [100]
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Cites
The Pfam Protein Families Database
Bateman, A. G. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.1.276 · Cited by 14,062 · see citing works
The biochemical basis of zinc physiology
Vallée, B. L., & Falchuk, K. H. (1993) · Physiological Reviews · doi:10.1152/physrev.1993.73.1.79 · Cited by 3,005 · see citing works
The Pfam protein families database
Finn, R. D., Mistry, J., Tate, J., Coggill, P., Heger, A., Pollington, J. E., Gavin, O. L., Gunasekaran, P., Ceric, G., Forslund, K., et al. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkp985 · Cited by 2,694 · see citing works
Repetitive zinc‐binding domains in the protein transcription factor IIIA from Xenopus oocytes.
Miller, J., McLachlan, A., & Klug, A. (1985) · The EMBO Journal · doi:10.1002/j.1460-2075.1985.tb03825.x · Cited by 2,476 · see citing works
The neurobiology of zinc in health and disease
Frederickson, C. J., Koh, J., & Bush, A. I. (2005) · Nature reviews. Neuroscience · doi:10.1038/nrn1671 · Cited by 1,841 · see citing works
Zinc coordination, function, and structure of zinc enzymes and other proteins
Vallée, B. L., & Auld, D. S. (1990) · Biochemistry · doi:10.1021/bi00476a001 · Cited by 1,784 · see citing works
Zinc finger proteins: new insights into structural and functional diversity.
Laity, J., Lee, B., & Wright, P. (2001) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(00)00167-6 · Cited by 1,473 · see citing works
Zinc requirements and the risks and benefits of zinc supplementation
Maret, W., & Sandstead, H. H. (2006) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2006.01.006 · Cited by 1,122 · see citing works
Self-citationCounting the Zinc-Proteins Encoded in the Human Genome
Andreini, C., Banci, L., Bertini, I., & Rosato, A. (2006) · Journal of Proteome Research · doi:10.1021/pr050361j · Cited by 1,109 · see citing works
Syndrome of iron deficiency anemia, hepatosplenomegaly, hypogonadism, dwarfism, and geophagia
Prasad, A. S., Halsted, J. A., & Nadimi, M. (1961) · The American Journal of Medicine · doi:10.1016/0002-9343(61)90137-1 · Cited by 791 · see citing works
Mammalian Zinc Transporters: Nutritional and Physiologic Regulation
Lichten, L. A., & Cousins, R. J. (2009) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-033009-083312 · Cited by 732 · see citing works
Uchida, Y., Takio, K., Titani, K., Ihara, Y., & Tomonaga, M. (1991) · Neuron · doi:10.1016/0896-6273(91)90272-2 · Cited by 700 · see citing works
High-Affinity Zinc Inhibition of NMDA NR1–NR2A Receptors
Paoletti, P., Ascher, P., & Neyton, J. (1997) · Journal of Neuroscience · doi:10.1523/jneurosci.17-15-05711.1997 · Cited by 650 · see citing works
Zinc through the Three Domains of Life
Andreini, C., Banci, L., Bertini, I., & Rosato, A. (2006) · Journal of Proteome Research · doi:10.1021/pr0603699 · Cited by 648 · see citing works
Coordination Dynamics of Zinc in Proteins
Maret, W., & Li, Y. (2009) · Chemical Reviews · doi:10.1021/cr800556u · Cited by 644 · see citing works
Self-citationZinc is a novel intracellular second messenger
Yamasaki, S., Sakata-Sogawa, K., Hasegawa, A., Suzuki, T., Kabu, K., Sato, E., Kurosaki, T., Yamashita, S., Tokunaga, M., Nishida, K., et al. (2007) · Journal of Cell Biology · doi:10.1083/jcb.200702081 · Cited by 592 · see citing works
Thiolate ligands in metallothionein confer redox activity on zinc clusters
Maret, W., & Vallée, B. L. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.7.3478 · Cited by 576 · see citing works
Self-citationEukaryotic zinc transporters and their regulation
Gaither, L. A., & Eide, D. J. (2001) · BioMetals · doi:10.1023/a:1012988914300 · Cited by 526 · see citing works
Sticky fingers: zinc-fingers as protein-recognition motifs
Gamsjaeger, R., LIEW, C., Loughlin, F. E., Crossley, M., & Mackay, J. P. (2007) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.12.007 · Cited by 451 · see citing works
Cytosolic zinc buffering and muffling: Their role in intracellular zinc homeostasis
Colvin, R. A., Holmes, W. R., Fontaine, C. P., & Maret, W. (2010) · Metallomics · doi:10.1039/b926662c · Cited by 428 · see citing works
Self-citationGenetically encoded FRET sensors to monitor intracellular Zn2+ homeostasis
Vinkenborg, J. L., Nicolson, T. J., Bellomo, E. A., Koay, M. S. T., Rutter, G. A., & Merkx, M. (2009) · Nature Methods · doi:10.1038/nmeth.1368 · Cited by 426 · see citing works
Zinc-buffering capacity of a eukaryotic cell at physiological pZn
Krężel, A., & Maret, W. (2006) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-006-0150-5 · Cited by 406 · see citing works
Self-citationZINC IN THE NUTRITION OF THE RAT
Todd, W. R., Elvehjem, C. A., & Hart, E. B. (1933) · American Journal of Physiology-Legacy Content · doi:10.1152/ajplegacy.1933.107.1.146 · Cited by 394 · see citing works
Inhibitory sites in enzymes: Zinc removal and reactivation by thionein
Maret, W., Jacob, C., Vallée, B. L., & Fischer, E. H. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.5.1936 · Cited by 385 · see citing works
Self-citationMicrobial metalloproteomes are largely uncharacterized
Cvetkovic, A., Menon, A. L., Thorgersen, M. P., Scott, J. W., Poole, F. L., Jenney, F. E., Lancaster, W. A., Praissman, J. L., Shanmukh, S., Vaccaro, B. J., et al. (2010) · Nature · doi:10.1038/nature09265 · Cited by 363 · see citing works
The taste of heavy metals: Gene regulation by MTF-1
Günther, V., Lindert, U., & Schaffner, W. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.01.005 · Cited by 342 · see citing works
Refined crystal structure of Cd, Zn metallothionein at 2·0 Å resolution
Robbins, A. H. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)80126-f · Cited by 341 · see citing works
Discovery of human zinc deficiency: 50 years later
Prasad, A. S. (2012) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2012.04.004 · Cited by 336 · see citing works
The Metallobiochemistry of Zinc Enzymes
Vallée, B. L., & Galdes, A. (1984) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470123027.ch5 · Cited by 310 · see citing works
Arseniev, A., Schultze, P., Wörgötter, E., Braun, W. A., Wagner, G., Vašák, M., Kägi, J. H. R., & Kurt Wüthrich, A. (1988) · Journal of Molecular Biology · doi:10.1016/0022-2836(88)90644-4 · Cited by 309 · see citing works
Qin, Y., Dittmer, P. J., Park, J. G., Jansen, K. B., & Palmer, A. E. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1015686108 · Cited by 307 · see citing works
Crystal structure of human leukotriene A(4) hydrolase, a bifunctional enzyme in inflammation.
Thunnissen, M. M. G. M., Nordlund, P., & Haeggström, J. Z. (2001) · Nature Structural Biology · doi:10.1038/84117 · Cited by 300 · see citing works
Molecular and genetic features of zinc transporters in physiology and pathogenesis
Fukada, T., & Kambe, T. (2011) · Metallomics · doi:10.1039/c1mt00011j · Cited by 295 · see citing works
Dual Nanomolar and Picomolar Zn(II) Binding Properties of Metallothionein
Krężel, A., & Maret, W. (2007) · Journal of the American Chemical Society · doi:10.1021/ja071979s · Cited by 283 · see citing works
Self-citationZinc and Sulfur: A Critical Biological Partnership
Maret, W. (2004) · Biochemistry · doi:10.1021/bi036340p · Cited by 270 · see citing works
Self-citationLaity, J. H., & Andrews, G. K. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.03.019 · Cited by 267 · see citing works
Taylor, K. M., Hiscox, S., Nicholson, R. I., Högstrand, C., & Kille, P. (2012) · Science Signaling · doi:10.1126/scisignal.2002585 · Cited by 266 · see citing works
Bordo, D., Pesce, A., Bolognesi, M., Stroppolo, M., FALCONI, M., & DESIDERI, A. (2006) · Wiley eBooks · doi:10.1002/0470028637 · Cited by 264 · see citing works
Maret, W. (2009) · BioMetals · doi:10.1007/s10534-008-9186-z · Cited by 261 · see citing works
Self-citationGüneş, Ç., Heuchel, R. L., Georgiev, O., Müller, K., Lichtlen, P., Blüthmann, H., Marino, S., Aguzzi, A., & Schaffner, W. (1998) · The EMBO Journal · doi:10.1093/emboj/17.10.2846 · Cited by 258 · see citing works
Zinc in Specialized Secretory Tissues: Roles in the Pancreas, Prostate, and Mammary Gland
Kelleher, S. L., McCormick, N. H., Velasquez, V., & López, V. (2011) · Advances in Nutrition · doi:10.3945/an.110.000232 · Cited by 258 · see citing works
Structural basis for autoregulation of the zinc transporter YiiP
Lu, M., Chai, J. L., & Fu, D. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1662 · Cited by 251 · see citing works
Zinc Sparks Are Triggered by Fertilization and Facilitate Cell Cycle Resumption in Mammalian Eggs
Kim, A. M., Bernhardt, M. L., Kong, B. Y., Ahn, R. W., Vogt, S., Woodruff, T. K., & O’Halloran, T. V. (2011) · ACS Chemical Biology · doi:10.1021/cb200084y · Cited by 247 · see citing works
Bozym, R. A., Thompson, R. B., Stoddard, A. K., & Fierke, C. A. (2006) · ACS Chemical Biology · doi:10.1021/cb500043a · Cited by 240 · see citing works
Krężel, A., Hao, Q., & Maret, W. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.02.017 · Cited by 236 · see citing works
Self-citationde Ruiter, G., Tartakovsky, E., Oded, N., & van der Boom, M. E. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200906382 · Cited by 229 · see citing works
Excitation-Transcription Coupling Mediated by Zinc Influx through Voltage-dependent Calcium Channels
Atar, D., Backx, P. H., Appel, M., Gao, W. D., & Marbán, E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.6.2473 · Cited by 228 · see citing works
Zinc transporters and cancer: a potential role for ZIP7 as a hub for tyrosine kinase activation
Högstrand, C., Kille, P., Nicholson, R. I., & Taylor, K. M. (2009) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2009.01.004 · Cited by 222 · see citing works
Maret, W. (2011) · BioMetals · doi:10.1007/s10534-010-9406-1 · Cited by 219 · see citing works
Self-citationZinc Fingers in Caenorhabditis elegans : Finding Families and Probing Pathways
Clarke, N. D., & Berg, J. M. (1998) · Science · doi:10.1126/science.282.5396.2018 · Cited by 198 · see citing works
Insights into Zn2+ homeostasis in neurons from experimental and modeling studies
Colvin, R. A., Bush, A. I., Volitakis, I., Fontaine, C. P., Thomas, D. G., Kikuchi, K., & Holmes, W. R. (2008) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00541.2007 · Cited by 188 · see citing works
Zinc transporter ZnT-3 regulates presynaptic Erk1/2 signaling and hippocampus-dependent memory
Sindreu, C. B., Palmiter, R. D., & Storm, D. R. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1019166108 · Cited by 176 · see citing works
Metallothionein redox biology in the cytoprotective and cytotoxic functions of zinc
Maret, W. (2007) · Experimental Gerontology · doi:10.1016/j.exger.2007.11.005 · Cited by 174 · see citing works
Self-citationThe concentrations of free Mg2+ and free Zn2+ in equine blood plasma.
Magneson, G. R., Puvathingal, J. M., & Ray, W. J. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)60936-6 · Cited by 172 · see citing works
Metalloproteomics, metalloproteomes, and the annotation of metalloproteins
Maret, W. (2010) · Metallomics · doi:10.1039/b915804a · Cited by 172 · see citing works
Self-citationZinc signals promote IL‐2‐dependent proliferation of T cells
Kaltenberg, J., Plum, L. M., Ober-Blöbaum, J. L., Hönscheid, A., Rink, L., & Haase, H. (2010) · European Journal of Immunology · doi:10.1002/eji.200939574 · Cited by 161 · see citing works
Flow cytometric measurement of labile zinc in peripheral blood mononuclear cells
Haase, H., Hebel, S., Engelhardt, G., & Rink, L. (2006) · Analytical Biochemistry · doi:10.1016/j.ab.2006.02.009 · Cited by 158 · see citing works
Wilson, M., Högstrand, C., & Maret, W. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.c111.320796 · Cited by 158 · see citing works
Self-citationKeilin, D., & Mann, T. (1939) · Nature · doi:10.1038/144442b0 · Cited by 154 · see citing works
Intracellular free zinc and zinc buffering in human red blood cells
Simons, T. J. B. (1991) · The Journal of Membrane Biology · doi:10.1007/bf01993964 · Cited by 151 · see citing works
Redox biochemistry of mammalian metallothioneins
Maret, W. (2011) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-011-0800-0 · Cited by 147 · see citing works
Self-citationThionein/metallothionein control Zn(II) availability and the activity of enzymes
Krężel, A., & Maret, W. (2007) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-007-0330-y · Cited by 144 · see citing works
Self-citationMinimal Functional Sites Allow a Classification of Zinc Sites in Proteins
Andreini, C., Bertini, I., & Cavallaro, G. (2011) · PLoS ONE · doi:10.1371/journal.pone.0026325 · Cited by 136 · see citing works
Different redox states of metallothionein/thionein in biological tissue
Krężel, A., & Maret, W. (2007) · Biochemical Journal · doi:10.1042/bj20061044 · Cited by 134 · see citing works
Self-citationLeukotriene A4 hydrolase: An epoxide hydrolase with peptidase activity
Haeggström, J. Z., Wetterholm, A., Vallée, B. L., & Samuelsson, B. O. (1990) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(05)81076-9 · Cited by 131 · see citing works
Zinc: what is its role in biology?
Williams, R. J. P. (1984) · Endeavour · doi:10.1016/0160-9327(84)90040-1 · Cited by 124 · see citing works
Copper-thionein from fetal bovine liver
Hartmann, H., & Weser, U. (1977) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(77)90057-5 · Cited by 120 · see citing works
Leukotriene A4 hydrolase: A zinc metalloenzyme
Haeggström, J. Z., Wetterholm, A., Shapiro, R., Vallée, B. L., & Samuelsson, B. O. (1990) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(90)91540-9 · Cited by 119 · see citing works
Danscher, G., & Stoltenberg, M. (2005) · Journal of Histochemistry & Cytochemistry · doi:10.1369/jhc.4r6460.2005 · Cited by 118 · see citing works
Bellomo, E. A., Meur, G., & Rutter, G. A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.246082 · Cited by 117 · see citing works
Transient fluctuations of intracellular zinc ions in cell proliferation
Li, Y., & Maret, W. (2009) · Experimental Cell Research · doi:10.1016/j.yexcr.2009.05.016 · Cited by 116 · see citing works
Self-citationMaret, W., Larsen, K. S., & Vallée, B. L. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.6.2233 · Cited by 113 · see citing works
Self-citationCARBOXYPEPTIDASE, A ZINC METALLOPROTEIN
Vallée, B. L., & Neurath, H. (1954) · Journal of the American Chemical Society · doi:10.1021/ja01648a088 · Cited by 106 · see citing works
New Sensors for Quantitative Measurement of Mitochondrial Zn2+
Park, J. G., Qin, Y., Galati, D. F., & Palmer, A. E. (2012) · ACS Chemical Biology · doi:10.1021/cb300171p · Cited by 104 · see citing works
Tóth, K. (2011) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-072610-145218 · Cited by 101 · see citing works
Tanzi, R. E., & Hyman, B. T. (1991) · Nature · doi:10.1038/350564a0 · Cited by 97 · see citing works
Metal Complexes of Phosphoglucomutase in Vivo
Peck, E. J., & Ray, W. J. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62444-5 · Cited by 96 · see citing works
Feng, W., Benz, F. W., Cai, J., Pierce, W. M. J., & Kang, Y. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506956200 · Cited by 92 · see citing works
Ayaz, M., & Turan, B. (2005) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00754.2005 · Cited by 83 · see citing works
Structural Characterization of the Human ProteomePreprint
Müller, A. M., MacCallum, R. M., & Sternberg, M. J. E. (2002) · Genome Research · doi:10.1101/gr.221202 · Cited by 80 · see citing works
Mechanism of Nitrogen Excitation in the Night Sky
Cabannes, J., & Aynard, R. (1939) · Nature · doi:10.1038/144442a0 · Cited by 79 · see citing works
Human metallothionein metallomics
Li, Y., & Maret, W. (2008) · Journal of Analytical Atomic Spectrometry · doi:10.1039/b802220h · Cited by 73 · see citing works
Self-citationMcCranor, B. J., Bozym, R. A., Vitolo, M. I., Fierke, C. A., Bambrick, L. L., Polster, B. M., Fiskum, G. M., & Thompson, R. B. (2012) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-012-9427-2 · Cited by 64 · see citing works
Syndrome of Iron Deficiency Anemia, Hepatosplenomegaly, Hypogonadism, Dwarfism and Geophagia
Prasad, A. S., Halsted, J. A., Nadimi, M., & Iran, S. (2009) · Nutrition Reviews · doi:10.1111/j.1753-4887.1983.tb07160.x · Cited by 63 · see citing works
Rink, L. (2011) · Cited by 58 · see citing works
Maret, W. (2012) · Metal ions in life sciences · doi:10.1007/978-94-007-5561-1_14 · Cited by 57 · see citing works
Self-citationMaret, W. (2004) · Journal of Analytical Atomic Spectrometry · doi:10.1039/b307540k · Cited by 55 · see citing works
Self-citationTHOMAS, R. C., Coles, J. A., & DEITMER, J. W. (1991) · Nature · doi:10.1038/350564b0 · Cited by 51 · see citing works
Inhibition of human erythrocyte Ca2+-ATPase by Zn2+
Högstrand, C. (1999) · Toxicology · doi:10.1016/s0300-483x(99)00020-7 · Cited by 44 · see citing works
Cellular and Molecular Biology of Metals
Zalups, R. K., & Koropatnick, J. D. (2010) · CRC Press eBooks · doi:10.1201/9781420059984 · Cited by 39 · see citing works
Metal Binding Ability of Cysteine-Rich Peptide Domain of ZIP13 Zn2+ Ions Transporter
Potocki, S., Rowińska‐Żyrek, M., Valensin, D., Krzywoszyńska, K., Witkowska, D., Łuczkowski, M., & Kozłowski, H. (2011) · Inorganic Chemistry · doi:10.1021/ic200270p · Cited by 38 · see citing works
Álvarez, L., González-Iglesias, H., García, M., Ghosh, S., Sanz-Medel, A., & Coca‐Prados, M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.365015 · Cited by 30 · see citing works
Cima, R. R., Dubach, J. M., Wieland, A. M., Walsh, B. M., & Soybel, D. I. (2005) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00501.2004 · Cited by 27 · see citing works
Bioinformatics in bioinorganic chemistry
Bertini, I., & Cavallaro, G. (2009) · Metallomics · doi:10.1039/b912156k · Cited by 19 · see citing works
Zinc proteomics and the annotation of the human zinc proteome
Maret, W. (2008) · Pure and Applied Chemistry · doi:10.1351/pac200880122679 · Cited by 17 · see citing works
Self-citationThe Regulatory and Signaling Functions of Zinc Ions in Human Cellular Physiology
Haase, H., & Maret, W. (2010) · CRC Press eBooks · doi:10.1201/9781420059984-11 · Cited by 14 · see citing works
Self-citationThe Significance of Zinc in the Living Organism.
Drinker, K. R., & Collier, E. (1926) · Journal of Industrial Hygiene · Cited by 14 · see citing works
Auld, D. S. (2004) · Handbook of Metalloproteins · doi:10.1002/0470028637.met014 · Cited by 13 · see citing works
History and status of zinc in nutrition. Introduction.
Bl, O. (1984) · PubMed · Cited by 3 · see citing works
Maret, W. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.201006236 · Cited by 3 · see citing works
Self-citation
Flagged first, then by citations
1 of the 101 references couldn’t be matched to a known paper.
Research works printed but not linked: 4
- Raulin J. Etudes chimiques sur la vegetation. Ann Sci Nat Bot Biol Veg. 1869;11:92-299.
- Lutz RE. The normal occurrence of zinc in biologic material. J Ind Hyg. 1926;8:127.
- Magneson GR, Puvathingal JM, Ray WJ. The concentration of free Mg 2+ and free Zn 2+ in equine blood plasma. J Biol Chem. 1987;262: 11140-8.
- Hogstrand C, Verbost PM, Wendelaar Bonga SE. Inhibition of human Ca 2+ -ATPase by Zn 2+ . Toxicology. 1999;133:139-45.
Cited by
Sorted by citations
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Biomarkers of Nutrition for Development—Folate Review
Bailey, L. B., Stover, P. J., McNulty, H., Fenech, M. F., Gregory, J. F., Mills, J. L., Pfeiffer, C. M., Fazili, Z., Zhang, M., Ueland, P. M., et al. (2015) · Journal of Nutrition · doi:10.3945/jn.114.206599 · Cited by 1,147 · see citing works
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Marreiro, D., Cruz, K., Morais, J., Beserra, J., Severo, J., & De Oliveira, A. (2017) · Antioxidants · doi:10.3390/antiox6020024 · Cited by 679 · see citing works
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King, J. C., Brown, K. H., Gibson, R. S., Krebs, N. F., Lowe, N. M., Siekmann, J. H., & Raiten, D. J. (2016) · Journal of Nutrition · doi:10.3945/jn.115.220079 · Cited by 581 · see citing works
Nutrition and Metabolism of Minerals in Fish
Lall, S. P., & Kaushik, S. (2021) · Animals · doi:10.3390/ani11092711 · Cited by 488 · see citing works
Critical Role of Zinc as Either an Antioxidant or a Prooxidant in Cellular Systems
Lee, S. R. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/9156285 · Cited by 458 · see citing works
Zinc in Cellular Regulation: The Nature and Significance of “Zinc Signals”
Maret, W. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18112285 · Cited by 451 · see citing works
Self-citationThe Role of Copper and Zinc Toxicity in Innate Immune Defense against Bacterial Pathogens
Djoko, K. Y., Ong, C.-L. Y., Walker, M. J., & McEwan, A. G. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.r115.647099 · Cited by 417 · see citing works
Role of Zinc in Immune System and Anti-Cancer Defense Mechanisms
Skrajnowska, D., & Bobrowska‐Korczak, B. (2019) · Nutrients · doi:10.3390/nu11102273 · Cited by 426 · see citing works
Bioactive Compounds for Skin Health: A Review
Michalak, M., Pierzak, M., Kręcisz, B., & Suliga, E. (2021) · Nutrients · doi:10.3390/nu13010203 · Cited by 345 · see citing works
“Zn is essential for the division and differentiation of new cells, and it plays a role in apoptosis and the ageing of the body [99,100].”
BackgroundThe emerging role of zinc transporters in cellular homeostasis and cancer
Bafaro, E. M., Liu, Y., Xu, Y., & Dempski, R. E. (2017) · Signal Transduction and Targeted Therapy · doi:10.1038/sigtrans.2017.29 · Cited by 309 · see citing works
Zinc: From Biological Functions to Therapeutic Potential
Costa, M. I., Sarmento‐Ribeiro, A. B., & Gonçalves, A. C. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24054822 · Cited by 257 · see citing works
Elsheery, N. I., Helaly, M. N., El-Hoseiny, H. M., & Alam‐Eldein, S. M. (2020) · Agronomy · doi:10.3390/agronomy10040558 · Cited by 257 · see citing works
Toxicity of heavy metals and metal-containing nanoparticles on plants
Mustafa, G., & Komatsu, S. (2016) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2016.02.020 · Cited by 247 · see citing works
Deshpande, P., Dapkekar, A., Oak, M. D., Paknikar, K. M., & Rajwade, J. M. (2017) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2017.02.061 · Cited by 242 · see citing works
Que, E. L., Bleher, R., Duncan, F. E., Kong, B. Y., Gleber, S. C., Vogt, S., Chen, S., Garwin, S. A., Bayer, A. R., Dravid, V. P., et al. (2014) · Nature Chemistry · doi:10.1038/nchem.2133 · Cited by 237 · see citing works
The redox biology of redox-inert zinc ions
Maret, W. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.01.006 · Cited by 237 · see citing works
Self-citationRaiten, D. J., Ashour, F. A. S., Ross, A. C., Meydani, S. N., Dawson, H. D., Stephensen, C. B., Brabin, B. J., Suchdev, P. S., & van Ommen, B. (2015) · The Journal of Nutrition · doi:10.3945/jn.114.194571 · Cited by 234 · see citing works
Zinc Toxicity: Understanding the Limits
Schoofs, H., Schmit, J., & Rink, L. (2024) · Molecules · doi:10.3390/molecules29133130 · Cited by 231 · see citing works
Metal binding properties, stability and reactivity of zinc fingers
Kluska, K., Adamczyk, J., & Krężel, A. (2018) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2018.04.009 · Cited by 222 · see citing works
Wrobel, A. T., Johnstone, T. C., Liang, A. D., Lippard, S. J., & Rivera‐Fuentes, P. (2014) · Journal of the American Chemical Society · doi:10.1021/ja500315x · Cited by 211 · see citing works
The Role of Zinc in Bone Tissue Health and Regeneration—a Review
Molenda, M., & Kolmas, J. (2023) · Biological Trace Element Research · doi:10.1007/s12011-023-03631-1 · Cited by 211 · see citing works
The Bioinorganic Chemistry of Mammalian Metallothioneins
Krężel, A., & Maret, W. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00371 · Cited by 210 · see citing works
Self-citationCopper as a key regulator of cell signalling pathways
Grubman, A., & White, A. R. (2014) · Expert Reviews in Molecular Medicine · doi:10.1017/erm.2014.11 · Cited by 199 · see citing works
The Role of Fe, Zn, and Cu in Pregnancy
Grzeszczak, K., Kwiatkowski, S., & Kosik-Bogacka, D. (2020) · Biomolecules · doi:10.3390/biom10081176 · Cited by 169 · see citing works
Zinc oxide nanoparticles for therapeutic purposes in cancer medicine
Wiesmann, N., Tremel, W., & Brieger, J. (2020) · Journal of Materials Chemistry B · doi:10.1039/d0tb00739k · Cited by 187 · see citing works
Kochańczyk, T., Drozd, A., & Krężel, A. (2014) · Metallomics · doi:10.1039/c4mt00094c · Cited by 185 · see citing works
Interactions of zinc- and redox-signaling pathways
Hübner, C., & Haase, H. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101916 · Cited by 186 · see citing works
Zinc Biofortification in Food Crops Could Alleviate the Zinc Malnutrition in Human Health
Praharaj, S., Skalický, M., Maitra, S., Bhadra, P., Shankar, T., Brestič, M., Hejnák, V., Vachová, P., & Hossain, A. (2021) · Molecules · doi:10.3390/molecules26123509 · Cited by 162 · see citing works
TRPM7, Magnesium, and Signaling
Zou, Z., Rios, F. J. O., Montezano, A. C. I., & Touyz, R. M. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20081877 · Cited by 164 · see citing works
Can Zn Be a Critical Element in COVID-19 Treatment?
Rahman, M. T., & Idid, S. Z. I. S. O. (2020) · Biological Trace Element Research · doi:10.1007/s12011-020-02194-9 · Cited by 157 · see citing works
Arabidopsis bZIP19 and bZIP23 act as zinc sensors to control plant zinc status
Lilay, G. H., Persson, D. P., Castro, P. H., Liao, F., Alexander, R. D., Aarts, M. G. M., & Assunção, A. G. L. (2021) · Nature Plants · doi:10.1038/s41477-021-00856-7 · Cited by 156 · see citing works
Zinc Homeostasis and isotopic fractionation in plants: a review
Caldelas, C., & Weiss, D. J. (2016) · Plant and Soil · doi:10.1007/s11104-016-3146-0 · Cited by 152 · see citing works
Stępień, M., Jenab, M., Freisling, H., Becker, N., Czuban, M., Tjønneland, A. M., Olsen, A., Overvad, K., Boutron‐Ruault, M., Mancini, F. R., et al. (2017) · Carcinogenesis · doi:10.1093/carcin/bgx051 · Cited by 152 · see citing works
Zinc transporter 8 (ZnT8) and β cell function
Davidson, H. W., Wenzlau, J. M., & O’Brien, R. M. (2014) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2014.03.008 · Cited by 151 · see citing works
Introductory Chapter: Introducing Heavy Metals
Koller, M., & Saleh, H. M. (2018) · InTech eBooks · doi:10.5772/intechopen.74783 · Cited by 150 · see citing works
Molecular Mechanisms of Arsenic-Induced Disruption of DNA Repair
Tam, L. M., Price, N. E., & Wang, Y. (2020) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.9b00464 · Cited by 153 · see citing works
Zinc in Pancreatic Islet Biology, Insulin Sensitivity, and Diabetes
Maret, W. (2017) · Preventive Nutrition and Food Science · doi:10.3746/pnf.2017.22.1.1 · Cited by 147 · see citing works
Self-citationThe Role of Antioxidants in the Interplay between Oxidative Stress and Senescence
Varesi, A., Chirumbolo, S., Campagnoli, L. I. M., Pierella, E., Piccini, G. B., Carrara, A., Ricevuti, G., Scassellati, C., Bonvicini, C., & Pascale, A. (2022) · Antioxidants · doi:10.3390/antiox11071224 · Cited by 145 · see citing works
Metal ligands in micronutrient acquisition and homeostasis
Clemens, S. (2019) · Plant Cell & Environment · doi:10.1111/pce.13627 · Cited by 142 · see citing works
Zaman, Q. U., Aslam, Z., Yaseen, M., Ihsan, M. Z., Khaliq, A., Fahad, S., Bashir, S., Ramzani, P. M. A., & Naeem, M. S. (2017) · Archives of Agronomy and Soil Science · doi:10.1080/03650340.2017.1338343 · Cited by 129 · see citing works
Coger, V., Million, N., Rehbock, C., Sures, B., Nachev, M., Barcikowski, S., Wistuba, N., Strauß, S., & Vogt, P. M. (2018) · Biological Trace Element Research · doi:10.1007/s12011-018-1600-y · Cited by 125 · see citing works
Ingelsson, B., Appelgren, D., Strid, T., Söderberg, A., Bergh, A.-C., Loitto, V. M., Lotfi, K., Segelmark, M., Spyrou, G., & Rosén, A. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1711950115 · Cited by 127 · see citing works
Trace Elements, PPARs, and Metabolic Syndrome
Shi, Y., Zou, Y., Shen, Z., Xiong, Y., Zhang, W., Liu, C., & Chen, S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21072612 · Cited by 121 · see citing works
Regulation of zinc-dependent enzymes by metal carrier proteins
Thompson, M. W. (2022) · BioMetals · doi:10.1007/s10534-022-00373-w · Cited by 121 · see citing works
Role of zinc in female reproduction
Garner, T. B., Hester, J., Carothers, A., & Díaz, F. J. (2021) · Biology of Reproduction · doi:10.1093/biolre/ioab023 · Cited by 119 · see citing works
ZIP9, a novel membrane androgen receptor and zinc transporter protein
Thomas, P., Converse, A., & Berg, H. (2017) · General and Comparative Endocrinology · doi:10.1016/j.ygcen.2017.04.016 · Cited by 116 · see citing works
The Zinc Sensing Receptor, ZnR/GPR39, in Health and Disease
Hershfinkel, M. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19020439 · Cited by 94 · see citing works
On the Metal Cofactor in the Tyrosinase Family
Solano, F. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19020633 · Cited by 118 · see citing works
Maret, W. (2013) · Metal ions in life sciences · doi:10.1007/978-94-007-7500-8_12 · Cited by 121 · see citing works
Self-citationMitochondrial and ER-Targeted eCALWY Probes Reveal High Levels of Free Zn2+
CHABOSSEAU, P. L., Tuncay, E., Meur, G., Bellomo, E. A., Hessels, A. M., Hughes, S. J., Johnson, P., Bugliani, M., Marchetti, P., Turan, B., et al. (2014) · ACS Chemical Biology · doi:10.1021/cb5004064 · Cited by 117 · see citing works
Çakmak, İ., Brown, P. H., Colmenero-Flores, J. M., Husted, S., Kutman, B. Y., Nikolić, M., Rengel, Z., Schmidt, S. B., & Zhao, F. J. (2023) · Elsevier eBooks · doi:10.1016/b978-0-12-819773-8.00017-4 · Cited by 115 · see citing works
SLC30A8 mutations in type 2 diabetes
Rutter, G. A., & Chimienti, F. (2014) · Diabetologia · doi:10.1007/s00125-014-3405-7 · Cited by 112 · see citing works
Zn and Fe biofortification: The right chemical environment for human bioavailability
Clemens, S. (2014) · Plant Science · doi:10.1016/j.plantsci.2014.05.014 · Cited by 111 · see citing works
Dabbagh-Bazarbachi, H., Clergeaud, G., Quesada, I., Ortiz, M., O’Sullivan, C. K., & Fernández-Larrea, J. (2014) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf5014633 · Cited by 109 · see citing works
Molecular Mechanisms of Metal Toxicity in the Pathogenesis of Alzheimer’s Disease
Kabir, M. T., Uddin, M. S., Zaman, S., Begum, Y., Ashraf, G. M., Bin-Jumah, M. N., BUNGAU, S. G., Mousa, S. A., & Abdel‐Daim, M. M. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-02096-w · Cited by 109 · see citing works
The Complex Relationship between Metals and Carbonic Anhydrase: New Insights and Perspectives
Lionetto, M. G., Caricato, R., Giordano, M., & Schettino, T. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17010127 · Cited by 106 · see citing works
Wang, X., Liu, S., Li, M., Yu, P., Chu, X., Li, L., Tan, G., Wang, Y., Chen, X., Zhang, Y., et al. (2016) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2016.07.019 · Cited by 105 · see citing works
Liang, Z., Chen, F., Park, S., Balasubramanian, B., & Liu, W. (2022) · Frontiers in Veterinary Science · doi:10.3389/fvets.2022.906084 · Cited by 104 · see citing works
New advances in molecular mechanisms and emerging therapeutic targets in alcoholic liver diseases
Williams, J., Manley, S., & Ding, W. (2014) · World Journal of Gastroenterology · doi:10.3748/wjg.v20.i36.12908 · Cited by 102 · see citing works
Advances in the molecular understanding of biological zinc transport
Blindauer, C. A. (2015) · Chemical Communications · doi:10.1039/c4cc10174j · Cited by 101 · see citing works
Association of Zinc with Anemia
Jeng, S.-S., & Chen, Y. (2022) · Nutrients · doi:10.3390/nu14224918 · Cited by 101 · see citing works
Alterations in Intestinal Permeability: The Role of the “Leaky Gut” in Health and Disease
Stewart, A. S., Pratt-Phillips, S. E., & Gonzalez, L. M. (2017) · Journal of Equine Veterinary Science · doi:10.1016/j.jevs.2017.02.009 · Cited by 100 · see citing works
Unexplored nutritive potential of tomato to combat global malnutrition
Vats, S., Bansal, R., Rana, N., Kumawat, S., Bhatt, V. D., Jadhav, P. V., Kale, V., Sathe, A. P., Sonah, H., Jugdaohsingh, R., et al. (2020) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2020.1832954 · Cited by 101 · see citing works
(FEEDAP), E. P. O. A. A. P. O. S. U. I. A. F. (2014) · EFSA Journal · doi:10.2903/j.efsa.2014.3668 · Cited by 98 · see citing works
Zinc at the crossroads of exercise and proteostasis
Hernández‐Camacho, J. D., Vicente‐García, C., Parsons, D. S., & Navas‐Enamorado, I. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101529 · Cited by 97 · see citing works
Wang, X., Kim, G., Chu, J. L., Song, T., Yang, Z., Guo, W., Shao, X., Oelze, M. L., Li, K. C., & Lu, Y. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.1c11543 · Cited by 96 · see citing works
Mg2+ions: do they bind to nucleobase nitrogens?
Leonarski, F., D’Ascenzo, L., & Auffinger, P. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw1175 · Cited by 95 · see citing works
eZinCh-2: A Versatile, Genetically Encoded FRET Sensor for Cytosolic and Intraorganelle Zn2+ Imaging
Hessels, A. M., CHABOSSEAU, P. L., Bakker, M. H., Engelen, W., Rutter, G. A., Taylor, K. M., & Merkx, M. (2015) · ACS Chemical Biology · doi:10.1021/acschembio.5b00211 · Cited by 93 · see citing works
Yu, Y., Liu, K., Wen, Z., Liu, W., Zhang, L., & Su, J. (2020) · RSC Advances · doi:10.1039/d0ra01465f · Cited by 93 · see citing works
Synthetic fluorescent probes to map metallostasis and intracellular fate of zinc and copper
Sfrazzetto, G. T., Satriano, C., Tomaselli, G. A., & Rizzarelli, E. (2015) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2015.11.012 · Cited by 90 · see citing works
Zinc and Cadmium in the Aetiology and Pathogenesis of Osteoarthritis and Rheumatoid Arthritis
Frangos, T., & Maret, W. (2020) · Nutrients · doi:10.3390/nu13010053 · Cited by 90 · see citing works
Self-citationSkalny, A. V., Aschner, M., Lei, X. G., Гриценко, В. А., Santamarı́a, A., Alekseenko, S. I., Prakash, N. T., Chang, J., Sizova, E. A., Chao, J. C.-J., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222313074 · Cited by 90 · see citing works
Mayer, L., Uciechowski, P., Meyer, S., Schwerdtle, T., Rink, L., & Haase, H. (2014) · Metallomics · doi:10.1039/c4mt00051j · Cited by 90 · see citing works
The Importance of Natural Antioxidants in Female Reproduction
Vašková, J., Klepcová, Z., Špaková, I., Urdzík, P., Štofilová, J., Bertková, I., Kľoc, M., & Rabajdová, M. (2023) · Antioxidants · doi:10.3390/antiox12040907 · Cited by 95 · see citing works
Photoactivatable Sensors for Detecting Mobile Zinc
Goldberg, J. M., Wang, F., Sessler, C. D., Vogler, N. W., Zhang, D. Y., Loucks, W. H., Tzounopoulos, T., & Lippard, S. J. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.7b12766 · Cited by 87 · see citing works
Beyond zinc coordination: Bioimaging applications of Zn(II)-complexes
Kumar, N., Roopa, Bhalla, V., & Kumar, M. (2020) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2020.213550 · Cited by 87 · see citing works
Yu, J. X., Martins, A. F., Preihs, C., Jordan, V. C., Chirayil, S., Zhao, P., Wu, Y., Nasr, K., Kiefer, G. E., & Sherry, A. D. (2015) · Journal of the American Chemical Society · doi:10.1021/jacs.5b09158 · Cited by 86 · see citing works
Clemens, S. (2021) · Journal of Experimental Botany · doi:10.1093/jxb/erab481 · Cited by 85 · see citing works
Gharpure, S., Yadwade, R., & Ankamwar, B. G. (2022) · ACS Omega · doi:10.1021/acsomega.1c05324 · Cited by 88 · see citing works
Zinc Homeostasis at the Bacteria/Host Interface—From Coordination Chemistry to Nutritional Immunity
Wątły, J., Potocki, S., & Rowińska‐Żyrek, M. (2016) · Chemistry - A European Journal · doi:10.1002/chem.201602376 · Cited by 82 · see citing works
Atrián‐Blasco, E., Santoro, A., Pountney, D. L., Meloni, G., Hureau, C., & Faller, P. (2017) · Chemical Society Reviews · doi:10.1039/c7cs00448f · Cited by 80 · see citing works
Zhang, J., Li, X., Shen, L., Khan, N. U., Zhang, X., Chen, L., Zhao, H., & Luo, P. (2021) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2021.126782 · Cited by 79 · see citing works
Cryo-EM structures of human ZnT8 in both outward- and inward-facing conformations
Xue, J., Xie, T., Zeng, W., Jiang, Y., & Bai, X.-C. (2020) · eLife · doi:10.7554/elife.58823 · Cited by 78 · see citing works
Intracellular zinc in insulin secretion and action: a determinant of diabetes risk?
Rutter, G. A., CHABOSSEAU, P. L., Bellomo, E. A., Maret, W., Mitchell, R. K., Hodson, D. J., Solomou, A., & Hu, M. (2015) · Proceedings of The Nutrition Society · doi:10.1017/s0029665115003237 · Cited by 77 · see citing works
Self-citationSayed, E. T., Abdelkareem, M. A., Obaideen, K., Elsaid, K., Wilberforce, T., Maghrabie, H. M., & Olabi, A. G. (2021) · Carbon Resources Conversion · doi:10.1016/j.crcon.2021.04.004 · Cited by 76 · see citing works
Zn 2+ influx activates ERK and Akt signaling pathways
Anson, K. J., Corbet, G. A., & Palmer, A. E. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2015786118 · Cited by 71 · see citing works
Circulating copper and zinc levels and risk of hepatobiliary cancers in Europeans
Stępień, M., Hughes, D., Hybsier, S., Bamia, C., Tjønneland, A., Overvad, K., Affret, A., His, M., Boutron-Ruault, M., Katzke, V., et al. (2017) · British Journal of Cancer · doi:10.1038/bjc.2017.1 · Cited by 130 · see citing works
Aberrance of Zinc Metalloenzymes-Induced Human Diseases and Its Potential Mechanisms
Cheng, Y., & Chen, H.-P. (2021) · Nutrients · doi:10.3390/nu13124456 · Cited by 63 · see citing works
Convergent Ca 2+ and Zn 2+ signaling regulates apoptotic Kv2.1 K + currents
McCord, M. C., & Aizenman, E. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1306238110 · Cited by 69 · see citing works
Kasana, S., Din, J., & Maret, W. (2014) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2014.10.003 · Cited by 67 · see citing works
Self-citationTang, K. S. (2019) · Life Sciences · doi:10.1016/j.lfs.2019.117011 · Cited by 71 · see citing works
Han, J., Zou, Q., Su, W., & Yan, X. (2020) · Chemical Engineering Journal · doi:10.1016/j.cej.2020.124987 · Cited by 66 · see citing works
Zhou, J., Lin, H., Wang, Z., Zhang, S.-W., Huang, D., Gao, C., Yan, H., & Wang, X. (2020) · Environmental Pollution · doi:10.1016/j.envpol.2020.114290 · Cited by 65 · see citing works
The coronavirus disease (COVID-19) – A supportive approach with selected micronutrients
Gröber, U., & Holick, M. F. (2021) · International Journal for Vitamin and Nutrition Research · doi:10.1024/0300-9831/a000693 · Cited by 66 · see citing works
Dastidar, D. G., Mukherjee, P., Ghosh, D., & Banerjee, D. (2020) · Colloids and Surfaces A Physicochemical and Engineering Aspects · doi:10.1016/j.colsurfa.2020.125781 · Cited by 64 · see citing works
Barresi, V., Valenti, G., Spampinato, G., Musso, N., Castorina, S., Rizzarelli, E., & Condorelli, D. F. (2018) · Journal of Cellular Biochemistry · doi:10.1002/jcb.27285 · Cited by 64 · see citing works
Si, H., Sheng, R., Li, Q., Feng, J., Li, L., & Tang, B. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.7b05268 · Cited by 63 · see citing works
Asbaghi, O., Sadeghian, M., Fouladvand, F., Panahande, S. B., Nasiri, M., Khodadost, M., Shokri, A., Pirouzi, A., & Sadeghi, O. (2020) · Nutrition Metabolism and Cardiovascular Diseases · doi:10.1016/j.numecd.2020.03.021 · Cited by 63 · see citing works
- Authors
- Maret, W.
- Affiliations
- King's College London (GB)
- Corresponding author
- Maret, Wolfgang
- ORCID
- Maret, Wolfgang
- Venue
- Advances in Nutrition
- Publisher
- Elsevier BV
- Published
- 2013-01
- Volume
- 4
- Issue
- 1
- Pages
- 82-91
- ISSN
- 2156-5376 (ISSN-L)
- 2161-8313
- PMC
- PMC3648744
- OpenAlex
- W2097951289
- Cited by
- 818
- References
- 101
- Citations by year
- 2026: 74 · 2025: 84 · 2024: 77 · 2023: 86 · 2022: 63 · 2021: 79 · 2020: 74 · 2019: 63 · 2018: 53 · 2017: 47 · 2016: 40 · 2015: 32 · 2014: 35 · 2013: 11
- FWCI
- 4.44
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Advances in Nutrition (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
- Physical Sciences › Environmental Science › Health, Toxicology and Mutagenesis › Heavy Metal Exposure and Toxicity
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Keywords
- zinc metalloenzyme, carbonic anhydrase, zinc finger proteins, zinc binding site, zinc homeostasis, zinc regulation, signal transduction, metal-binding motifs
- MeSH terms
- Binding Sites, Carbonic Anhydrases, Catalysis, Homeostasis, Humans, Kinetics, Proteins, Zinc, Signal Transduction, Zinc Fingers, Protein Structure, Tertiary
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