Zinc, antioxidant systems and metallothionein in metal mediated-apoptosis: Biochemical and cytochemical aspects

Apoptosis: A Basic Biological Phenomenon with Wideranging Implications in Tissue Kinetics

Kerr, J. F. R., Wyllie, A. H., & Currie, A. R. (1972) · British Journal of Cancer · doi:10.1038/bjc.1972.33 · Cited by 15,725

Free radicals, metals and antioxidants in oxidative stress-induced cancer

Valko, M., Rhodes, C. J., Moncol, J., Izakovic, M., & Mazur, M. (2006) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2005.12.009 · Cited by 6,680

Mitochondrial formation of reactive oxygen species

Turrens, J. F. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2003.049478 · Cited by 5,084

Annexin V for flow cytometric detection of phosphatidylserine expression on B cells undergoing apoptosis

Koopman, G., Reutelingsperger, C., Kuijten, G., Keehnen, R., Pals, S., & van Oers, M. (1994) · Blood · doi:10.1182/blood.v84.5.1415.1415 · Cited by 2,681

Mammalian thioredoxin is a direct inhibitor of apoptosis signal‐regulating kinase (ASK) 1

Saitoh, M., Nishitoh, H., Fujii, M., Takeda, K., Tobiume, K., Sawada, Y., Kawabata, M., Miyazono, K., & Ichijo, H. (1998) · The EMBO Journal · doi:10.1093/emboj/17.9.2596 · Cited by 2,377

Oxidative stress as a mediator of apoptosis

Buttke, T. M., & Sandstrom, P. A. (1994) · Immunology Today · doi:10.1016/0167-5699(94)90018-3 · Cited by 2,165

Antioxidant enzymes and human diseases

MatÉs, J. M., Pérez-Gómez, C., & De Castro, I. N. (1999) · Clinical Biochemistry · doi:10.1016/s0009-9120(99)00075-2 · Cited by 2,099

Strategies of antioxidant defense

SIES, H. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb18025.x · Cited by 1,976

A Novel Duodenal Iron-Regulated Transporter, IREG1, Implicated in the Basolateral Transfer of Iron to the Circulation

McKie, A. T., Marciani, P., Rolfs, A., Brennan, K., Wehr, K., Barrow, D., Miret, S., Bomford, A., Peters, T. J., Farzaneh, F., et al. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80425-6 · Cited by 1,422

Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress.

Hentze, M. W., & Kühn, L. C. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.16.8175 · Cited by 1,292

The Antioxidant Properties of Zinc

Powell, S. R. (2000) · The Journal of Nutrition · doi:10.1093/jn/130.5.1447s · Cited by 1,292

Novel mechanisms of natural antioxidant compounds in biological systems: involvement of glutathione and glutathione-related enzymes

Masella, R., Di Benedetto, R., Varì, R., Filesi, C., & Giovannini, C. (2005) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2005.05.013 · Cited by 1,107

The physiological role of zinc as an antioxidant

Bray, T. M., & Bettger, W. J. (1990) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(90)90076-u · Cited by 892

Oxygen free radicals and metallothionein

Sato, M., & Bremner, I. (1993) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(93)90029-t · Cited by 847

Molecular mechanisms of copper uptake and distribution

Puig, S., & Thiele, D. J. (2002) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(02)00298-3 · Cited by 719

Cell suicide for beginners

Raff, M. (1998) · Nature · doi:10.1038/24055 · Cited by 688

Interaction of reactive oxygen species with ion transport mechanisms

Kourie, J. I. (1998) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1998.275.1.c1 · Cited by 643

Functions of zinc in signaling, proliferation and differentiation of mammalian cells

Beyersmann, D., & Haase, H. (2001) · Biometals · doi:10.1023/a:1012905406548 · Cited by 635

Targeted disruption of metallothionein I and II genes increases sensitivity to cadmium.

Masters, B. A., Kelly, E. J., Quaife, C. J., Brinster, R. L., & Palmiter, R. D. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.2.584 · Cited by 621

Reactive oxygen species are downstream mediators of p53-dependent apoptosis.

Johnson, T. M., Yu, Z. X., Ferrans, V. J., Lowenstein, R. A., & Finkel, T. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.21.11848 · Cited by 596

Thiolate ligands in metallothionein confer redox activity on zinc clusters

Maret, W., & Vallee, B. L. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.7.3478 · Cited by 577

Zinc Is a Potent Inhibitor of the Apoptotic Protease, Caspase-3

Perry, D. K., Smyth, M. J., Stennicke, H. R., Salvesen, G. S., Duriez, P., Poirier, G. G., & Hannun, Y. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.30.18530 · Cited by 494

Morphological and biochemical characterization and analysis of apoptosis

Allen, R. T., Hunter, W. J., & Agrawal, D. K. (1997) · Journal of Pharmacological and Toxicological Methods · doi:10.1016/s1056-8719(97)00033-6 · Cited by 477

Essential role for mammalian copper transporter Ctr1 in copper homeostasis and embryonic development

Lee, J., Prohaska, J. R., & Thiele, D. J. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.111058698 · Cited by 472

Major DNA Fragmentation Is a Late Event in Apoptosis

Collins, J. A., Schandl, C. A., Young, K. K., Vesely, J., & Willingham, M. C. (1997) · Journal of Histochemistry & Cytochemistry · doi:10.1177/002215549704500702 · Cited by 471

The role of iron in cell cycle progression and the proliferation of neoplastic cells

Le, N. (2002) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/s0304-419x(02)00068-9 · Cited by 453

The role of zinc in caspase activation and apoptotic cell death

Truong-Tran, A. Q., Carter, J., Ruffin, R. E., & Zalewski, P. D. (2001) · Biometals · doi:10.1023/a:1012993017026 · Cited by 450

Metallothioneins in human tumors and potential roles in carcinogenesis

Cherian, M. G., Jayasurya, A., & Bay, B.-H. (2003) · Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis · doi:10.1016/j.mrfmmm.2003.07.013 · Cited by 437

Induction, Regulation, Degradation, and Biological Significance of Mammalian Metallothioneins

Miles, A. T., Hawksworth, G. M., Beattie, J. H., & Rodilla, V. (2000) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230091169168 · Cited by 429

Metallothionein Expression in Animals: A Physiological Perspective on Function

Davis, S. R., & Cousins, R. J. (2000) · The Journal of Nutrition · doi:10.1093/jn/130.5.1085 · Cited by 413

Metallothioneins: new functional and structural insights

Vasák, M. (2000) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(00)00082-x · Cited by 412

DNA-dependent protein kinase is one of a subset of autoantigens specifically cleaved early during apoptosis.

Casciola-Rosen, L. A., Anhalt, G. J., & Rosen, A. (1995) · The Journal of experimental medicine · doi:10.1084/jem.182.6.1625 · Cited by 412

Glutathione, a first line of defense against cadmium toxicity

Singhal, R. K., Anderson, M. E., & Meister, A. (1987) · The FASEB Journal · doi:10.1096/fasebj.1.3.2887478 · Cited by 396

The copper transporter CTR1 provides an essential function in mammalian embryonic development

Kuo, Y.-M., Zhou, B., Cosco, D., & Gitschier, J. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.111057298 · Cited by 396

Roles of the metallothionein family of proteins in the central nervous system

Hidalgo, J., Aschner, M., Zatta, P., & Vašák, M. (2001) · Brain Research Bulletin · doi:10.1016/s0361-9230(01)00452-x · Cited by 387

Signaling events for metallothionein induction

Haq, F., Mahoney, M., & Koropatnick, J. (2003) · Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis · doi:10.1016/j.mrfmmm.2003.07.014 · Cited by 383

Identification and Functional Expression of HAH1, a Novel Human Gene Involved in Copper Homeostasis

Klomp, L. W. J., Lin, S.-J., S.Yuan, D., Klausner, R. D., Culotta, V. C., & Gitlin, J. D. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.14.9221 · Cited by 379

Inflammation in central nervous system injury

Allan, S. M., & Rothwell, N. J. (2003) · Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences · doi:10.1098/rstb.2003.1358 · Cited by 345

Antioxidant role of metallothioneins: a comparative overview.

Viarengo, A., Burlando, B., Ceratto, N., & Panfoli, I. (2000) · PubMed · Cited by 341

Oxidative metal release from metallothionein via zinc-thiol/disulfide interchange.

Maret, W. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.1.237 · Cited by 340

Role of Cysteine Residues in Regulation of p53 Function

Rainwater, R., Parks, D., Anderson, M. E., Tegtmeyer, P., & Mann, K. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.7.3892 · Cited by 306

Enhanced Sensitivity to Oxidative Stress in Cultured Embryonic Cells from Transgenic Mice Deficient in Metallothionein I and II Genes

Lazo, J. S., Kondo, Y., Dellapiazza, D., Michalska, A. E., Choo, K. H. A., & Pitt, B. R. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.10.5506 · Cited by 301

The glutathione redox couple modulates zinc transfer from metallothionein to zinc-depleted sorbitol dehydrogenase

Jiang, L.-J., Maret, W., & Vallee, B. L. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.7.3483 · Cited by 294

The Human ZIP1 Transporter Mediates Zinc Uptake in Human K562 Erythroleukemia Cells

Gaither, L. A., & Eide, D. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101772200 · Cited by 288

Advances in the structure and chemistry of metallothioneins

Romero-Isart, N., & Vašák, M. (2002) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(01)00347-6 · Cited by 279

Nitric Oxide Destroys Zinc-Sulfur Clusters Inducing Zinc Release from Metallothionein and Inhibition of the Zinc Finger-Type Yeast Transcription Activator LAC9

Kroncke, K. D., Fehsel, K., Schmidt, T., Zenke, F. T., Dasting, I., Wesener, J. R., Bettermann, H., Breunig, K. D., & Kolbbachofen, V. (1994) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1994.1564 · Cited by 278

Interaction of the copper chaperone HAH1 with the Wilson disease protein is essential for copper homeostasis

Hamza, I., Schaefer, M., Klomp, L. W. J., & Gitlin, J. D. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.23.13363 · Cited by 276

Differential oxidation of thioredoxin-1, thioredoxin-2, and glutathione by metal ions*

Hansen, J. M., Zhang, H., & Jones, D. P. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.09.023 · Cited by 249

Metallothionein protects against the cytotoxic and DNA-damaging effects of nitric oxide.

Schwarz, M. A., Lazo, J. S., Yalowich, J. C., Allen, W. P., Whitmore, M., Bergonia, H. A., Tzeng, E., Billiar, T. R., Robbins, P. D., & Lancaster, J. R. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.10.4452 · Cited by 246

Regulation of Iron Metabolism in Eukaryotes

(1997) · Current Topics in Cellular Regulation · doi:10.1016/s0070-2137(97)80001-5 · Cited by 240

Metalloregulation of the tumor suppressor protein p53: zinc mediates the renaturation of p53 after exposure to metal chelators in vitro and in intact cells

Méplan, C., Richard, M.-J., & Hainaut, P. (2000) · Oncogene · doi:10.1038/sj.onc.1203907 · Cited by 234

Protective effect of metallothionein against the toxicity of cadmium and other metals11Supported by NIH grant ES-01142.

Park, J. D., Liu, Y., & Klaassen, C. D. (2001) · Toxicology · doi:10.1016/s0300-483x(01)00375-4 · Cited by 219

Metallothionein Redox Cycle and Function

Kang, Y. J. (2006) · Experimental Biology and Medicine · doi:10.1177/153537020623100903 · Cited by 214

The orchestration of body iron intake: how and where do enterocytes receive their cues?

Frazer, D. M., & Anderson, G. J. (2003) · Blood Cells, Molecules, and Diseases · doi:10.1016/s1079-9796(03)00039-1 · Cited by 214

Zinc transfer from transcription factor IIIA fingers to thionein clusters.

Zeng, J., Vallee, B. L., & Kägi, J. H. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.22.9984 · Cited by 204

Isolation of a murine copper transporter gene, tissue specific expression and functional complementation of a yeast copper transport mutant

Lee, J., Prohaska, J. R., Dagenais, S. L., Glover, T. W., & Thiele, D. J. (2000) · Gene · doi:10.1016/s0378-1119(00)00287-0 · Cited by 203

The Redox Regulation of Thiol Dependent Signaling Pathways in Cancer

Giles, G. (2006) · Current Pharmaceutical Design · doi:10.2174/138161206779010549 · Cited by 182

Enhanced Apoptosis in Metallothionein Null Cells

Kondo, Y., Rusnak, J. M., Hoyt, D. G., Settineri, C. E., Pitt, B. R., & Lazo, J. S. (1997) · Molecular Pharmacology · doi:10.1124/mol.52.2.195 · Cited by 181

Regulation of caspase activation and apoptosis by cellular zinc fluxes and zinc deprivation: A review

Chai, F., Truong‐Tran, A. Q., Ho, L. H., & Zalewski, P. D. (1999) · Immunology & Cell Biology · doi:10.1046/j.1440-1711.1999.00825.x · Cited by 172

Role of oxidative stress in single‐dose, cadmium‐induced testicular cancer

Koizumi, T., & Li, Z. G. (1992) · Journal of Toxicology and Environmental Health · doi:10.1080/15287399209531654 · Cited by 169

Identification of Apoptotic Cells by Formamide-induced DNA Denaturation in Condensed Chromatin

Frankfurt, O. S., & Krishan, A. (2001) · Journal of Histochemistry & Cytochemistry · doi:10.1177/002215540104900311 · Cited by 169

The menkes protein (ATP7A; MNK) cycles via the plasma membrane both in basal and elevated extracellular copper using a C-terminal di-leucine endocytic signal

Petris, M. (1999) · Human Molecular Genetics · doi:10.1093/hmg/8.11.2107 · Cited by 168

Cytoplasmic metallothionein overexpression protects NIH 3T3 cells from tert-butyl hydroperoxide toxicity.

Schwarz, M. A., Lazo, J. S., Yalowich, J. C., Reynolds, I., Kagan, V. E., Tyurin, V., Kim, Y. M., Watkins, S. C., & Pitt, B. R. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36597-3 · Cited by 164

Metallothionein Is a Potential Negative Regulator of Apoptosis

Shimoda, R. (2003) · Toxicological Sciences · doi:10.1093/toxsci/kfg095 · Cited by 164

Fatty acid-mediated intracellular iron translocation: A synergistic mechanism of oxidative injury

Yao, D., Shi, W., Gou, Y., Zhou, X., Yee Aw, T., Zhou, Y., & Liu, Z. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.07.015 · Cited by 163

Nuclear localization of metallothionein during cell proliferation and differentiation.

Cherian, M. G., & Apostolova, M. D. (2000) · PubMed · Cited by 162

Metallothionein/disulfide interactions, oxidative stress, and the mobilization of cellular zinc

Maret, W. (1995) · Neurochemistry International · doi:10.1016/0197-0186(94)00173-r · Cited by 161

The Essential Role of Mitochondria in the Biogenesis of Cellular Iron-Sulfur Proteins

Lill, R., Diekert, K., Kaut, A., Lange, H., Pelzer, W., Prohl, C., & Kispál, G. (1999) · Biological Chemistry · doi:10.1515/bc.1999.147 · Cited by 156

Copper Transport: An Overview

Harris, E. D. (1991) · Experimental Biology and Medicine · doi:10.3181/00379727-196-43171b · Cited by 151

[3] Toxicological significance of metallothionein

Templeton, D. M., & Cherian, M. G. (1991) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(91)05079-b · Cited by 148

Oxidants, Antioxidants, and Free Radicals

(2017) · CRC Press eBooks · doi:10.1201/9780203744673 · Cited by 146

Activation of nuclear factor kappaB: potential role in metallothionein-mediated mitogenic response.

Abdel‐Mageed, A. B., & AGRAWAL, K. C. (1998) · PubMed · Cited by 145

Direct Reaction of H2O2with Sulfhydryl Groups in HL-60 Cells: Zinc-Metallothionein and Other Sites

Quesada, A. R., Byrnes, R. W., Krezoski, S. O., & Petering, D. H. (1996) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.0452 · Cited by 141

Megalin mediates renal uptake of heavy metal metallothionein complexes

Klassen, R. B., Crenshaw, K., Kozyraki, R., Verroust, P. J., Tío, L., Atrian, S., Allen, P., & Hammond, T. G. (2004) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00233.2003 · Cited by 140

Mammalian Copper Chaperone Cox17p Has an Essential Role in Activation of Cytochrome c Oxidase and Embryonic Development

Takahashi, Y., Kako, K., Kashiwabara, S., Takehara, A., Inada, Y., Arai, H., Nakada, K., Kodama, H., Hayashi, J., Baba, T., et al. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.21.7614-7621.2002 · Cited by 139

Regulation of metallothionein gene expression

Ghoshal, K., & Jacob, S. T. (2000) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(00)66034-8 · Cited by 137

Cell death in development: shaping the embryo

Penaloza, C. G., Lin, L., Lockshin, R. A., & Zakeri, Z. F. (2006) · Histochemistry and Cell Biology · doi:10.1007/s00418-006-0214-1 · Cited by 136

Metallothionein reduces central nervous system inflammation, neurodegeneration, and cell death following kainic acid‐induced epileptic seizures

Penkowa, M., Florit, S., Giralt, M., Quintana, A., Molinero, A., Carrasco, J., & Hidalgo, J. (2004) · Journal of Neuroscience Research · doi:10.1002/jnr.20387 · Cited by 132

Metallothioneins and Cell Death by Anticancer Drugs

Lazo, J. S., & Pitt, B. R. (1995) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pa.35.040195.003223 · Cited by 123

Normal iron metabolism and the pathophysiology of iron overload disorders.

Siah, C. W., Ombiga, J., Adams, L. A., Trinder, D., & Olynyk, J. K. (2006) · PubMed · Cited by 121

Reversible zinc exchange between metallothionein and the estrogen receptor zinc finger

Cano-Gauci, D. F., & Sarkar, B. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00356-0 · Cited by 116

New Evidence of Iron and Zinc Interplay at the Enterocyte and Neural Tissues

Kordas, K., & Stoltzfus, R. J. (2004) · Journal of Nutrition · doi:10.1093/jn/134.6.1295 · Cited by 110

Metallothionein transfers zinc to mitochondrial aconitase through a direct interaction in mouse hearts

Feng, W., Cai, J., Pierce, W. M. J., FRANKLIN, R. B., Maret, W., Benz, F. W., & Kang, Y. J. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.04.170 · Cited by 105

Catalytic selenols couple the redox cycles of metallothionein and glutathione

Chen, Y., & Maret, W. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02250.x · Cited by 99

Physiological role for zinc in prevention of apoptosis (gene-directed death).

Zalewski, P. D., Forbes, I. J., & Giannakis, C. (1991) · PubMed · Cited by 94

The LEC rat: a model for human hepatitis, liver cancer, and much more.

Mori, M., Hattori, A., Sawaki, M., Tsuzuki, N., Sawada, N., Oyamada, M., Sugawara, N., & Enomoto, K. (1994) · PubMed Central · Cited by 94

Iron Chelators Inhibit the Growth and Induce the Apoptosis of Kaposi's Sarcoma Cells and of their Putative Endothelial Precursors

Simonart, T., Heenen, M., Degraef, C., Andreï, G., Mosselmans, R., Hermans, P., Vooren, J. V., Noël, J., Boelaert, J. R., & Snoeck, R. (2000) · Journal of Investigative Dermatology · doi:10.1046/j.1523-1747.2000.00119.x · Cited by 92

A role for extracellular metallothioneins in CNS injury and repair

Chung, R. S., & West, A. K. (2003) · Neuroscience · doi:10.1016/j.neuroscience.2003.10.019 · Cited by 92

Alterations in zinc homeostasis underlie endothelial cell death induced by oxidative stress from acute exposure to hydrogen peroxide

Wiseman, D. A., Wells, S. M., Hubbard, M., Welker, J. E., & Black, S. M. (2006) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00459.2005 · Cited by 86

Role of Structural and Functional Elements of Mouse Methionine-S-Sulfoxide Reductase in Its Subcellular Distribution

Kim, H., & Gladyshev, V. N. (2005) · Biochemistry · doi:10.1021/bi0501131 · Cited by 85

Zinc Therapy Increases Duodenal Concentrations of Metallothionein and Iron in Wilson's Disease Patients

Sturniolo, G. C., Mestriner, C., Irato, P., Albergoni, V., Longo, G., & Renata D'Incà (1999) · The American Journal of Gastroenterology · doi:10.1016/s0002-9270(98)00732-1 · Cited by 80

Reoxygenation injury and antioxidant protection: A tale of two paradoxes

Gutteridge, J. M. C., & Halliwell, B. B. (1990) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(90)90635-c · Cited by 80

Metallothionein-Independent Zinc Protection from Alcoholic Liver Injury

Zhou, Z., Sun, X., Lambert, J. C., Saari, J. T., & Kang, Y. J. (2002) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)61174-1 · Cited by 80

The Many Faces of the Copper Metabolism Protein MURR1/COMMD1

de Bie, P., van de Sluis, B., Klomp, L., & Wijmenga, C. (2005) · Journal of Heredity · doi:10.1093/jhered/esi110 · Cited by 80

Intracellular Pathways of Copper Trafficking in Yeast and Humans

Culotta, V., Lin, S.-J., Schmidt, P. J., Klomp, L. W. J., Casareno, R. L. B., & Gitlin, J. D. (1999) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-4859-1_22 · Cited by 76

Role of iron and ferritin in TNFα‐induced apoptosis in HeLa cells

Cozzi, A., Levi, S., Corsi, B., Santambrogio, P., Campanella, A., Gerardi, G., & Arosio, P. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00114-5 · Cited by 76

Zinc and vitamin A supplementation in Indigenous Australian children hospitalised with lower respiratory tract infection: a randomised controlled trial

Chang, A. B., Torzillo, P. J., STEWART, P. M., Boyce, N. C., White, A. V., Wheaton, G. R., Purdie, D. M., Wakerman, J., & Valery, P. C. (2006) · The Medical Journal of Australia · doi:10.5694/j.1326-5377.2006.tb00147.x · Cited by 76

Increased apoptosis in a variety of tissues of zinc-deficient rats

Nodera, M., Yanagisawa, H., & Wada, O. (2001) · Life Sciences · doi:10.1016/s0024-3205(01)01252-8 · Cited by 70

Induction of metallothionein by stress and its molecular mechanisms.

Jacob, S. T., Ghoshal, K., & Sheridan, J. F. (1999) · Europe PMC (PubMed Central) · Cited by 70

Newly delivered transferrin iron and oxidative cell injury

Breuer, W. V., Greenberg, E., & Cabantchik, Z. I. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00056-2 · Cited by 69

Expression of the Mouse Metallothionein-I and -II Genes Provides a Reproductive Advantage during Maternal Dietary Zinc Deficiency

Andrews, G. K., & Geiser, J. (1999) · Journal of Nutrition · doi:10.1093/jn/129.9.1643 · Cited by 69

Endothelial cell apoptosis is accelerated by inorganic iron and heat via an oxygen radical dependent mechanism

Jacob, A. K., Hotchkiss, R. S., DeMeester, S. L., Hiramatsu, M., Karl, I. E., Swanson, P. E., Cobb, J. P., & Buchman, T. G. (1997) · Surgery · doi:10.1016/s0039-6060(97)90015-5 · Cited by 67

Redox Regulation of Copper–Metallothionein

Fabisiak, J. P., Tyurin, V. A., Tyurina, Y. Y., Borisenko, G. G., Korotaeva, A., Pitt, B. R., Lazo, J. S., & Kagan, V. E. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1998.1077 · Cited by 66

Metal- and Tissue-Dependent Relationship between Metallothionein mRNA and Protein

Vasconcelos, M. H. (2002) · Toxicology and Applied Pharmacology · doi:10.1006/taap.2002.9428 · Cited by 62

Oxidants, Antioxidants, and Free Radicals

Furst, A. (1999) · International Journal of Toxicology · doi:10.1080/109158199225738 · Cited by 58

Transcriptional Induction of Metallothionein-I and -II Genes in the Livers of Cu,Zn-Superoxide Dismutase Knockout Mice

Ghoshal, K., Majumder, S., Li, Z., Bray, T. M., & Jacob, S. T. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.1563 · Cited by 58

Role of Deferoxamine in Tumor Therapy

Donfrancesco, A., Deb, G., Sio, L. D., Cozza, R., & Castellano, A. (2009) · Acta Haematologica · doi:10.1159/000203951 · Cited by 58

Nuclear trafficking of metallothionein requires oxidation of a cytosolic partner

Takahashi, Y., Ogra, Y., & Suzuki, K. T. (2004) · Journal of Cellular Physiology · doi:10.1002/jcp.20158 · Cited by 55

Ferroportin mutation in autosomal dominant hemochromatosis: loss of function, gain in understanding

Fleming, R. E., & Sly, W. S. (2001) · Journal of Clinical Investigation · doi:10.1172/jci13739 · Cited by 54

Lipopolysaccharide induces double-stranded DNA fragmentation in mouse thymus: protective effect of zinc pretreatment

Thomas, D. J., & Caffrey, T. C. (1991) · Toxicology · doi:10.1016/0300-483x(91)90078-f · Cited by 48

Selenocompounds Can Serve as Oxidoreductants with the Methionine Sulfoxide Reductase Enzymes

Sagher, D., Brunell, D. J., Brot, N., Vallée, B. L., & Weissbach, H. (2006) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84031-0 · Cited by 47

Measurement of radical-scavenging ability in hepatic metallothionein of rat using in vivo electron spin resonance spectroscopy

Yoshida, M., Saegusa, Y., Fukuda, A., Akama, Y., & Owada, S. (2005) · Toxicology · doi:10.1016/j.tox.2005.05.008 · Cited by 38

Biology of Large Bowel Cancer

Willson, J. K. V. (1989) · Hematology/Oncology Clinics of North America · doi:10.1016/s0889-8588(18)30565-3 · Cited by 30

Metal donation and apo-metalloenzyme activation by stable isotopically labeled metallothionein

Mason, A. Z., Perico, N., Moeller, R., Thrippleton, K., Potter, T., & Lloyd, D. (2004) · Marine Environmental Research · doi:10.1016/j.marenvres.2004.03.082 · Cited by 29

Response of primary rabbit kidney proximal tubule cells to estrogens

Han, H. J., Jung, J. C., & Taub, M. L. (1999) · Journal of Cellular Physiology · doi:10.1002/(sici)1097-4652(199901)178:1<1::aid-jcp1>3.0.co;2-q · Cited by 25

Efficacy of zinc treatment against iron‐induced toxicity in rat hepatoma cell line H4‐II‐E‐C3

Formigari, A., Santon, A., & Irato, P. (2006) · Liver International · doi:10.1111/j.1478-3231.2006.01389.x · Cited by 24

Effect of Zn treatment on wild type and MT-null cell lines in relation to apoptotic and/or necrotic processes and on MT isoform gene expression

Santon, A., Formigari, A., Albergoni, V., & Irato, P. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.01.008 · Cited by 17

Protection Against Chemically-Induced Oxidative Gastrointestinal Tissue Injury in Rats by Bismuth Salts

Bagchi, D., Carryl, O. R., Tran, M. X., Bagchi, M., Vuchetich, P. J., Krohn, R. L., Ray, S. D., Mitra, S., & STOHS, S. J. (1997) · Digestive Diseases and Sciences · doi:10.1023/a:1018811210175 · Cited by 14

Down‐modulation of CD4 antigen during programmed cell death in U937 cells

Malorni, W., Rivabene, R., Santini, M. T., Paradisi, S., Iosi, F., & Donelli, G. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80832-f · Cited by 14

Sensitivity of cells to apoptosis induced by iron deprivation can be reversibly changed by iron availability

Koc, M., Nadova, Z., & Kovár̆, J. (2006) · Cell Proliferation · doi:10.1111/j.1365-2184.2006.00411.x · Cited by 13

Phorbol ester‐induced cell death in PC‐12 cells overexpressing Bcl‐2 is dependent on the time at which cells are treated

Hahn, M. A., & Mayne, G. C. (2004) · Cell Biology International · doi:10.1016/j.cellbi.2004.02.003 · Cited by 4

The Essential Toxin: Impact of Zinc on Human Health

Plum, L. M., Rink, L., & Haase, H. (2010) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph7041342 · Cited by 1,577

Altered Expression of Genes Involved in Inflammation and Apoptosis in Frontal Cortex in Major Depression

Shelton, R. C., Claiborne, J., Sidoryk-Wegrzynowicz, M., Reddy, R., Aschner, M., Lewis, D. A., & Mirnics, K. (2011) · Molecular Psychiatry · doi:10.1038/mp.2010.52 · Cited by 511

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 253

Antioxidant Vitamins and Trace Elements in Critical Illness

Koekkoek, W. A. C. (., & van Zanten, A. R. H. (2016) · Nutrition in Clinical Practice · doi:10.1177/0884533616653832 · Cited by 203

Correlation of Phytochemical, Metal Contents and Antioxidant Activities of Black Glutinous Rice Bran and Potential Chemoprevention

Department of Agro-Industry, F. O. A. N. R. A. E., Ngamdee, P., Wichai, U., Department of Chemistry, F. O. S., Jiamyangyuen, S., & Department of Agro-Industry, F. O. A. N. R. A. E. (2016) · Food Technology and Biotechnology · doi:10.17113/ftb.54.03.16.4346 · Cited by 15