Metals in Neurobiology: Probing Their Chemistry and Biology with Molecular Imaging

Principles of neural science

(1982) · Trends in Neurosciences · doi:10.1016/0166-2236(82)90076-5 · Cited by 9,089

The Metabolic Basis of Inherited Disease.

(1988) · Annals of Internal Medicine · doi:10.7326/0003-4819-108-3-503_7 · Cited by 7,786

Molecular Biology of the Cell

Alberts, B., Johnson, A., Lewis, J., Morgan, D., Raff, M., Roberts, K., & Walter, P. (2017) · W.W. Norton eBooks · doi:10.1201/9781315735368 · Cited by 6,365

Hepcidin Regulates Cellular Iron Efflux by Binding to Ferroportin and Inducing Its Internalization

Nemeth, E., Tuttle, M. S., Powelson, J., Vaughn, M. B., Donovan, A., Ward, D. M., Ganz, T., & Kaplan, J. (2004) · Science · doi:10.1126/science.1104742 · Cited by 4,803

Calcium Signaling

Clapham, D. E. (2007) · Cell · doi:10.1016/j.cell.2007.11.028 · Cited by 4,175

Chronic systemic pesticide exposure reproduces features of Parkinson's disease

Betarbet, R., Sherer, T. B., MacKenzie, G., Garcia-Osuna, M., Panov, A. V., & Greenamyre, J. T. (2000) · Nature Neuroscience · doi:10.1038/81834 · Cited by 3,683

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

The ferritins: molecular properties, iron storage function and cellular regulation

Harrison, P. M., & Arosio, P. (1996) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(96)00022-9 · Cited by 2,667

In vivo near-infrared fluorescence imaging

Frangioni, J. V. (2003) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2003.08.007 · Cited by 2,653

The growing applications of click chemistry

Moses, J. E., & Moorhouse, A. D. (2007) · Chem. Soc. Rev. · doi:10.1039/b613014n · Cited by 2,367

New calcium indicators and buffers with high selectivity against magnesium and protons: design, synthesis, and properties of prototype structures

Tsien, R. Y. (1980) · Biochemistry · doi:10.1021/bi00552a018 · Cited by 2,236

Neuronal Calcium Signaling

Berridge, M. J. (1998) · Neuron · doi:10.1016/s0896-6273(00)80510-3 · Cited by 2,188

Copper, iron and zinc in Alzheimer's disease senile plaques

Lovell, M. A., Robertson, J. D., Teesdale, W. J., Campbell, J. L., & Markesbery, W. R. (1998) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(98)00092-6 · Cited by 2,120

Calcium - a life and death signal

Berridge, M. J., Bootman, M. D., & Lipp, P. (1998) · Nature · doi:10.1038/27094 · Cited by 2,063

The Galvanization of Biology: A Growing Appreciation for the Roles of Zinc

Berg, J. M., & Shi, Y. (1996) · Science · doi:10.1126/science.271.5252.1081 · Cited by 1,929

The neurobiology of zinc in health and disease

Frederickson, C. J., Koh, J.-Y., & Bush, A. I. (2005) · Nature Reviews Neuroscience · doi:10.1038/nrn1671 · Cited by 1,850

Iron, brain ageing and neurodegenerative disorders

Zecca, L., Youdim, M. B. H., Riederer, P., Connor, J. R., & Crichton, R. R. (2004) · Nature Reviews Neuroscience · doi:10.1038/nrn1537 · Cited by 1,801

Copper Homeostasis and Neurodegenerative Disorders (Alzheimer's, Prion, and Parkinson's Diseases and Amyotrophic Lateral Sclerosis)

Gaggelli, E., Kozlowski, H., Valensin, D., & Valensin, G. (2006) · Chemical Reviews · doi:10.1021/cr040410w · Cited by 1,729

Positional cloning of zebrafish ferroportin1 identifies a conserved vertebrate iron exporter

Donovan, A., Brownlie, A., Zhou, Y., Shepard, J., Pratt, S. J., Moynihan, J., Paw, B. H., Drejer, A., Barut, B., Zapata, A., et al. (2000) · Nature · doi:10.1038/35001596 · Cited by 1,667

Molecular Pathways of Neurodegeneration in Parkinson's Disease

Dawson, T. M., & Dawson, V. L. (2003) · Science · doi:10.1126/science.1087753 · Cited by 1,663

Undetectable Intracellular Free Copper: The Requirement of a Copper Chaperone for Superoxide Dismutase

Rae, T. D., Schmidt, P. J., Pufahl, R. A., Culotta, V. C., & V. O'Halloran, T. (1999) · Science · doi:10.1126/science.284.5415.805 · Cited by 1,629

Fluorescent indicators for cytosolic calcium based on rhodamine and fluorescein chromophores

Minta, A., Kao, J. P. Y., & Tsien, R. Y. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83165-9 · Cited by 1,613

Mechanisms for copper acquisition, distribution and regulation

Kim, B.-E., Nevitt, T., & Thiele, D. J. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.72 · Cited by 1,588

Oxidative Damage Linked to Neurodegeneration by Selective α-Synuclein Nitration in Synucleinopathy Lesions

Giasson, B. I., Duda, J. E., Murray, I. V. J., Chen, Q., Souza, J. M., Hurtig, H. I., Ischiropoulos, H., Trojanowski, J. Q., & -Y. Lee, V. M. (2000) · Science · doi:10.1126/science.290.5493.985 · Cited by 1,546

Principles of bioinorganic chemistry

(1995) · Choice Reviews Online · doi:10.5860/choice.32-4515 · Cited by 1,534

Rapid induction of Alzheimer A beta amyloid formation by zinc

Bush, A., Pettingell, W., Multhaup, G., d Paradis, M., Vonsattel, J., Gusella, J., Beyreuther, K., Masters, C., & Tanzi, R. (1994) · Science · doi:10.1126/science.8073293 · Cited by 1,522

Chemistry in living systems

Prescher, J. A., & Bertozzi, C. R. (2005) · Nature Chemical Biology · doi:10.1038/nchembio0605-13 · Cited by 1,456

The effect of age on the non-haemin iron in the human brain

Hallgren, B., & Sourander, P. (1958) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1958.tb12607.x · Cited by 1,427

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

The metallobiology of Alzheimer's disease

Bush, A. I. (2003) · Trends in Neurosciences · doi:10.1016/s0166-2236(03)00067-5 · Cited by 1,315

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 cellular prion protein binds copper in vivo

Brown, D. R., Qin, K., Herms, J. W., Madlung, A., Manson, J., Strome, R., Fraser, P. E., Kruck, T., von Bohlen, A., Schulz-Schaeffer, W., et al. (1997) · Nature · doi:10.1038/37783 · Cited by 1,273

A Novel Mammalian Iron-regulated Protein Involved in Intracellular Iron Metabolism

Abboud, S., & Haile, D. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000713200 · Cited by 1,267

Regulating the fate of mRNA: the control of cellular iron metabolism

Klausner, R. D., Rouault, T. A., & Harford, J. B. (1993) · Cell · doi:10.1016/0092-8674(93)90046-s · Cited by 1,210

Iron Transport and Storage Proteins

Aisen, P., & Listowsky, I. (1980) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.49.070180.002041 · Cited by 1,171

In vivo visualization of gene expression using magnetic resonance imaging

Louie, A. Y., Hüber, M. M., Ahrens, E. T., Rothbächer, U., Moats, R., Jacobs, R. E., Fraser, S. E., & Meade, T. J. (2000) · Nature Biotechnology · doi:10.1038/73780 · Cited by 1,141

Iron Biology in Immune Function, Muscle Metabolism and Neuronal Functioning

Beard, J. L. (2001) · The Journal of Nutrition · doi:10.1093/jn/131.2.568s · Cited by 1,134

Release of endogenous Zn2+ from brain tissue during activity

Assaf, S. Y., & Chung, S.-H. (1984) · Nature · doi:10.1038/308734a0 · Cited by 1,118

Metal-triggered Structural Transformations, Aggregation, and Fibrillation of Human α-Synuclein

Uversky, V. N., Li, J., & Fink, A. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105343200 · Cited by 1,103

Hephaestin, a ceruloplasmin homologue implicated in intestinal iron transport, is defective in the sla mouse

Vulpe, C. D., Kuo, Y.-M., Murphy, T. L., Cowley, L., Askwith, C., Libina, N., Gitschier, J., & Anderson, G. J. (1999) · Nature Genetics · doi:10.1038/5979 · Cited by 1,084

Neurobiology of Zinc and Zinc-Containing Neurons

Frederickson, C. J. (1989) · International Review of Neurobiology · doi:10.1016/s0074-7742(08)60279-2 · Cited by 1,075

The Role of Zinc in Selective Neuronal Death After Transient Global Cerebral Ischemia

Koh, J.-Y., Suh, S. W., Gwag, B. J., He, Y. Y., Hsu, C. Y., & Choi, D. W. (1996) · Science · doi:10.1126/science.272.5264.1013 · Cited by 1,071

Transferrin receptor on endothelium of brain capillaries

Jefferies, W. A., Brandon, M. R., Hunt, S. V., Williams, A. F., Gatter, K. C., & Mason, D. Y. (1984) · Nature · doi:10.1038/312162a0 · Cited by 1,061

Alterations in the levels of iron, ferritin and other trace metals in Parkinson's disease and other neurodegenerative diseases affecting the basal ganglia

DEXTER, D. T., CARAYON, A., JAVOY-AGID, F., AGID, Y., WELLS, F. R., DANIEL, S. E., LEES, A. J., JENNER, P., & MARSDEN, C. D. (1991) · Brain · doi:10.1093/brain/114.4.1953 · Cited by 1,043

Handbook of fluorescent probes and research products

Haugland, R. P. (2002) · Cited by 1,036

Fluorescent detection of zinc in biological systems: recent development on the design of chemosensors and biosensors

Jiang, P., & Guo, Z. (2004) · Coordination Chemistry Reviews · doi:10.1016/j.cct.2003.10.013 · Cited by 989

Metal-Protein Attenuation With Iodochlorhydroxyquin (Clioquinol) Targeting Aβ Amyloid Deposition and Toxicity in Alzheimer Disease: A Pilot Phase 2 Clinical Trial

Ritchie, C. W., Bush, A. I., Mackinnon, A., Macfarlane, S., Mastwyk, M., MacGregor, L., Kiers, L., Cherny, R., Li, Q.-X., Tammer, A., et al. (2003) · Archives of Neurology · doi:10.1001/archneur.60.12.1685 · Cited by 988

A Long-Wavelength Fluorescent Chemodosimeter Selective for Cu(II) Ion in Water

Dujols, V., Ford, F., & Czarnik, A. W. (1997) · Journal of the American Chemical Society · doi:10.1021/ja971221g · Cited by 987

Increased nigral iron content in postmortem parkinsonian brain

Dexter, D. T., Wells, F. R., Agid, F., Agid, Y., Lees, A. J., Jenner, P., & Marsden, C. D. (1987) · The Lancet · doi:10.1016/s0140-6736(87)91361-4 · Cited by 963

C ERULOPLASMIN M ETABOLISM AND F UNCTION

Hellman, N. E., & Gitlin, J. D. (2002) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.22.012502.114457 · Cited by 933

The Role of Copper in Neurodegenerative Disease

Waggoner, D. J., Bartnikas, T. B., & Gitlin, J. D. (1999) · Neurobiology of Disease · doi:10.1006/nbdi.1999.0250 · Cited by 863

The Copper Chaperone for Superoxide Dismutase

Culotta, V. C., Klomp, L. W. J., Strain, J., Casareno, R. L. B., Krems, B., & Gitlin, J. D. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.38.23469 · Cited by 850

Micromolar concentrations of Zn2+ antagonize NMDA and GABA responses of hippocampal neurons

Westbrook, G. L., & Mayer, M. L. (1987) · Nature · doi:10.1038/328640a0 · Cited by 848

The labile iron pool: characterization, measurement, and participation in cellular processes1 1This article is part of a series of reviews on “Iron and Cellular Redox Status.” The full list of papers may be found on the homepage of the journal.

Kakhlon, O., & Cabantchik, Z. I. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01006-7 · Cited by 839

Prevalence of parkinsonism and Parkinson's disease in Europe: the EUROPARKINSON Collaborative Study. European Community Concerted Action on the Epidemiology of Parkinson's disease.

de Rijk, M. C., Tzourio, C., Breteler, M. M., Dartigues, J. F., Amaducci, L., Lopez-Pousa, S., Manubens-Bertran, J. M., Alperovitch, A., & Rocca, W. A. (1997) · Journal of Neurology, Neurosurgery & Psychiatry · doi:10.1136/jnnp.62.1.10 · Cited by 833

A Selective Turn-On Fluorescent Sensor for Imaging Copper in Living Cells

Zeng, L., Miller, E. W., Pralle, A., Isacoff, E. Y., & Chang, C. J. (2006) · Journal of the American Chemical Society · doi:10.1021/ja055064u · Cited by 806

Stimulation-induced uptake and release of zinc in hippocampal slices

Howell, G. A., Welch, M. G., & Frederickson, C. J. (1984) · Nature · doi:10.1038/308736a0 · Cited by 803

COPPER-ZINC SUPEROXIDE DISMUTASE AND AMYOTROPHIC LATERAL SCLEROSIS

Valentine, J. S., Doucette, P. A., & Zittin Potter, S. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.72.121801.161647 · Cited by 785

ZINC AND BRAIN INJURY

Choi, D. W., & Koh, J. Y. (1998) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.21.1.347 · Cited by 752

Histochemical demonstration of heavy metals: A revised version of the sulphide silver method suitable for both light and electronmicroscopy

Danscher, G. (1981) · Histochemistry · doi:10.1007/bf00592566 · Cited by 746

Fluorescent Sensors for Zn2+Based on a Fluorescein Platform: Synthesis, Properties and Intracellular Distribution

Burdette, S. C., Walkup, G. K., Spingler, B., Tsien, R. Y., & Lippard, S. J. (2001) · Journal of the American Chemical Society · doi:10.1021/ja010059l · Cited by 744

Principles of Neural Science

Rothwell, J. (1982) · Journal of Neurology, Neurosurgery & Psychiatry · doi:10.1136/jnnp.45.5.476 · Cited by 744

Blood–brain barrier dysfunction in parkinsonian midbrain in vivo

Kortekaas, R., Leenders, K. L., van Oostrom, J. C. H., Vaalburg, W., Bart, J., Willemsen, A. T. M., & Hendrikse, N. H. (2005) · Annals of Neurology · doi:10.1002/ana.20369 · Cited by 733

Metals and neuroscience

Bush, A. (2000) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(99)00073-3 · Cited by 731

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

Altered Reactivity of Superoxide Dismutase in Familial Amyotrophic Lateral Sclerosis

Wiedau-Pazos, M., Goto, J. J., Rabizadeh, S., Gralla, E. B., Roe, J. A., Lee, M. K., Valentine, J. S., & Bredesen, D. E. (1996) · Science · doi:10.1126/science.271.5248.515 · Cited by 719

ZnT-3, a putative transporter of zinc into synaptic vesicles

Palmiter, R. D., Cole, T. B., Quaife, C. J., & Findley, S. D. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.25.14934 · Cited by 709

Altered Brain Metabolism of Iron as a Cause of Neurodegenerative Diseases?

Gerlach, M., Ben‐Shachar, D., Riederer, P., & Youdim, M. B. H. (1994) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1994.63030793.x · Cited by 703

A Selective and Sensitive Fluoroionophore for HgII, AgI, and CuIIwith Virtually Decoupled Fluorophore and Receptor Units

Rurack, K., Kollmannsberger, M., Resch-Genger, U., & Daub, J. (2000) · Journal of the American Chemical Society · doi:10.1021/ja992630a · Cited by 685

The Herbicide Paraquat Causes Up-regulation and Aggregation of α-Synuclein in Mice

Manning-Bog, A. B., McCormack, A. L., Li, J., Uversky, V. N., Fink, A. L., & Di Monte, D. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c100560200 · Cited by 684

The elusive function of metallothioneins

Palmiter, R. D. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.15.8428 · Cited by 679

The Amyloid Precursor Protein of Alzheimer's Disease in the Reduction of Copper(II) to Copper(I)

Multhaup, G., Schlicksupp, A., Hesse, L., Beher, D., Ruppert, T., Masters, C. L., & Beyreuther, K. (1996) · Science · doi:10.1126/science.271.5254.1406 · Cited by 678

Zinc Selectively Blocks the Action of N -Methyl-D-Aspartate on Cortical Neurons

Peters, S., Koh, J., & Choi, D. W. (1987) · Science · doi:10.1126/science.2883728 · Cited by 672

I RON R EGULATORY P ROTEINS AND THE M OLECULAR C ONTROL OF M AMMALIAN I RON M ETABOLISM

Eisenstein, R. S. (2000) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.20.1.627 · Cited by 653

High-Affinity Zinc Inhibition of NMDA NR1–NR2A Receptors

Paoletti, P., Ascher, P., & Neyton, J. (1997) · The Journal of Neuroscience · doi:10.1523/jneurosci.17-15-05711.1997 · Cited by 649

Chemical and physiological characterization of fluo-4 Ca2+-indicator dyes

Gee, K. R., Brown, K. A., Chen, W.-N. U., Bishop-Stewart, J., Gray, D., & Johnson, I. (2000) · Cell Calcium · doi:10.1054/ceca.1999.0095 · Cited by 643

Iron Homeostasis

Andrews, N. C., & Schmidt, P. J. (2007) · Annual Review of Physiology · doi:10.1146/annurev.physiol.69.031905.164337 · Cited by 642

Mitoferrin is essential for erythroid iron assimilation

Shaw, G. C., Cope, J. J., Li, L., Corson, K., Hersey, C., Ackermann, G. E., Gwynn, B., Lambert, A. J., Wingert, R. A., Traver, D., et al. (2006) · Nature · doi:10.1038/nature04512 · Cited by 624

Late endosomal membranes rich in lysobisphosphatidic acid regulate cholesterol transport

Kobayashi, T., Beuchat, M.-H., Lindsay, M., Frias, S., Palmiter, R. D., Sakuraba, H., Parton, R. G., & Gruenberg, J. (1999) · Nature Cell Biology · doi:10.1038/10084 · Cited by 620

A Selective Fluorescent Sensor for Imaging Cd2+ in Living Cells

Peng, X., Du, J., Fan, J., Wang, J., Wu, Y., Zhao, J., Sun, S., & Xu, T. (2007) · Journal of the American Chemical Society · doi:10.1021/ja0643319 · Cited by 617

Induction of nitric oxide-dependent apoptosis in motor neurons by zinc-deficient superoxide dismutase

Estévez, A. G., Crow, J. P., Sampson, J. B., Reiter, C., Zhuang, Y., Richardson, G. J., Tarpey, M. M., Barbeito, L., & Beckman, J. S. (1999) · Science · doi:10.1126/science.286.5449.2498 · Cited by 596

Copper Stimulates Endocytosis of the Prion Protein

Pauly, P. C., & Harris, D. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.50.33107 · Cited by 589

Metalloenzyme-like Activity of Alzheimer's Disease β-Amyloid

Opazo, C., Huang, X., Cherny, R. A., Moir, R. D., Roher, A. E., White, A. R., Cappai, R., Masters, C. L., Tanzi, R. E., Inestrosa, N. C., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206428200 · Cited by 579

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

A New Cell-Permeable Fluorescent Probe for Zn2+

Walkup, G. K., Burdette, S. C., Lippard, S. J., & Tsien, R. Y. (2000) · Journal of the American Chemical Society · doi:10.1021/ja000868p · Cited by 571

h CTR1: A human gene for copper uptake identified by complementation in yeast

Zhou, B., & Gitschier, J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.14.7481 · Cited by 567

Metal Binding and Oxidation of Amyloid-β within Isolated Senile Plaque Cores: Raman Microscopic Evidence

Dong, J., Atwood, C. S., Anderson, V. E., Siedlak, S. L., Smith, M. A., Perry, G., & Carey, P. R. (2003) · Biochemistry · doi:10.1021/bi0272151 · Cited by 562

Aceruloplasminemia: molecular characterization of this disorder of iron metabolism.

Harris, Z. L., Takahashi, Y., Miyajima, H., Serizawa, M., MacGillivray, R. T., & Gitlin, J. D. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.7.2539 · Cited by 558

Copper and iron disorders of the brain

Madsen, E., & Gitlin, J. D. (2007) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.30.051606.094232 · Cited by 557

Copper binding to the prion protein: Structural implications of four identical cooperative binding sites

Viles, J. H., Cohen, F. E., Prusiner, S. B., Goodin, D. B., Wright, P. E., & Dyson, H. J. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.5.2042 · Cited by 552

An iron-responsive element type II in the 5'-untranslated region of the Alzheimer's amyloid precursor protein transcript

Rogers, J. T., Randall, J. D., Cahill, C. M., Eder, P. S., Huang, X., Gunshin, H., Leiter, L., McPhee, J., Sarang, S. S., Utsuki, T., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207435200 · Cited by 551

Elimination of zinc from synaptic vesicles in the intact mouse brain by disruption of the ZnT 3 gene

Cole, T. B., Wenzel, H. J., Kafer, K. E., Schwartzkroin, P. A., & Palmiter, R. D. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.4.1716 · Cited by 545

Labile iron pool: the main determinant of cellular response to oxidative stress

Kruszewski, M. (2003) · Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis · doi:10.1016/j.mrfmmm.2003.08.004 · Cited by 533

A quinoline fluorescence method for visualizing and assaying the histochemically reactive zinc (bouton zinc) in the brain

Frederickson, C. J., Kasarskis, E. J., Ringo, D., & Frederickson, R. E. (1987) · Journal of Neuroscience Methods · doi:10.1016/0165-0270(87)90042-2 · Cited by 527

Normal prion protein has an activity like that of superoxide dismutase

BROWN, D. R., WONG, B.-S., HAFIZ, F., CLIVE, C., HASWELL, S. J., & JONES, I. M. (1999) · Biochemical Journal · doi:10.1042/bj3440001 · Cited by 524

Prion Protein Selectively Binds Copper(II) Ions

Stöckel, J., Safar, J., Wallace, A. C., Cohen, F. E., & Prusiner, S. B. (1998) · Biochemistry · doi:10.1021/bi972827k · Cited by 518

Ratiometric and Selective Fluorescent Sensor for CuIIBased on Internal Charge Transfer (ICT)

Xu, Z., Xiao, Y., Qian, X., Cui, J., & Cui, D. (2005) · Organic Letters · doi:10.1021/ol0473445 · Cited by 518

Emission Ratiometric Imaging of Intracellular Zinc: Design of a Benzoxazole Fluorescent Sensor and Its Application in Two-Photon Microscopy

Taki, M., Wolford, J. L., & O'Halloran, T. V. (2004) · Journal of the American Chemical Society · doi:10.1021/ja039073j · Cited by 513

On the Development of Sensor Molecules that Display FeIII-amplified Fluorescence

Bricks, J. L., Kovalchuk, A., Trieflinger, C., Nofz, M., Büschel, M., Tolmachev, A. I., Daub, J., & Rurack, K. (2005) · Journal of the American Chemical Society · doi:10.1021/ja050652t · Cited by 510

In Vivo Monitoring of Mercury Ions Using a Rhodamine-Based Molecular Probe

Ko, S.-K., Yang, Y.-K., Tae, J., & Shin, I. (2006) · Journal of the American Chemical Society · doi:10.1021/ja065114a · Cited by 509

Copper in disorders with neurological symptoms: Alzheimer’s, Menkes, and Wilson diseases

Strausak, D., Mercer, J. F. B., Dieter, H. H., Stremmel, W., & Multhaup, G. (2001) · Brain Research Bulletin · doi:10.1016/s0361-9230(01)00454-3 · Cited by 505

Location and properties of metal-binding sites on the human prion protein

Jackson, G. S., Murray, I., Hosszu, L. L. P., Gibbs, N., Waltho, J. P., Clarke, A. R., & Collinge, J. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.151038498 · Cited by 497

Characterization of , a Yeast Gene Involved in Copper Metabolism and Assembly of Cytochrome Oxidase

Glerum, D. M., Shtanko, A., & Tzagoloff, A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.24.14504 · Cited by 497

The role of iron and copper molecules in the neuronal vulnerability of locus coeruleus and substantia nigra during aging

Zecca, L., Stroppolo, A., Gatti, A., Tampellini, D., Toscani, M., Gallorini, M., Giaveri, G., Arosio, P., Santambrogio, P., Fariello, R. G., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403495101 · Cited by 495

The Actions of Synaptically Released Zinc at Hippocampal Mossy Fiber Synapses

Vogt, K., Mellor, J., Tong, G., & Nicoll, R. (2000) · Neuron · doi:10.1016/s0896-6273(00)81149-6 · Cited by 490

The regional distribution and cellular localization of iron in the rat brain

Hill, J. M., & Switzer, R. C. (1984) · Neuroscience · doi:10.1016/0306-4522(84)90046-0 · Cited by 486

Aqueous Dissolution of Alzheimer's Disease Aβ Amyloid Deposits by Biometal Depletion

Cherny, R. A., Legg, J. T., McLean, C. A., Fairlie, D. P., Huang, X., Atwood, C. S., Beyreuther, K., Tanzi, R. E., Masters, C. L., & Bush, A. I. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.33.23223 · Cited by 482

Oxidative stress: Free radical production in neural degeneration

Götz, M. E., Künig, G., Riederer, P., & Youdim, M. B. H. (1994) · Pharmacology & Therapeutics · doi:10.1016/0163-7258(94)90055-8 · Cited by 482

Selective accumulation of aluminum and iron in the neurofibrillary tangles of Alzheimer's disease: A laser microprobe (LAMMA) study

Good, P. F., Perl, D. P., Bierer, L. M., & Schmeidler, J. (1992) · Annals of Neurology · doi:10.1002/ana.410310310 · Cited by 476

Identification and Cloning of a β-Cell–Specific Zinc Transporter, ZnT-8, Localized Into Insulin Secretory Granules

Chimienti, F., Devergnas, S., Favier, A., & Seve, M. (2004) · Diabetes · doi:10.2337/diabetes.53.9.2330 · Cited by 470

Control of zinc transfer between thionein, metallothionein, and zinc proteins

Jacob, C., Maret, W., & Vallee, B. L. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.7.3489 · Cited by 466

Measurement of Intracellular Free Zinc in Living Cortical Neurons: Routes of Entry

Sensi, S. L., Canzoniero, L. M. T., Yu, S. P., Ying, H. S., Koh, J.-Y., Kerchner, G. A., & Choi, D. W. (1997) · The Journal of Neuroscience · doi:10.1523/jneurosci.17-24-09554.1997 · Cited by 465

ZnT-2, a mammalian protein that confers resistance to zinc by facilitating vesicular sequestration.

Palmiter, R. D., Cole, T. B., & Findley, S. D. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00527.x · Cited by 446

Brain iron and ferritin in Parkinson’s and Alzheimer’s diseases

Jellinger, K., Paulus, W., Grundke-Iqbal, I., Riederer, P., & Youdim, M. B. H. (1990) · Journal of Neural Transmission - Parkinson's Disease and Dementia Section · doi:10.1007/bf02252926 · Cited by 445

PARACEST Agents: Modulating MRI Contrast via Water Proton Exchange

Zhang, S., Merritt, M., Woessner, D. E., Lenkinski, R. E., & Sherry, A. D. (2003) · Accounts of Chemical Research · doi:10.1021/ar020228m · Cited by 436

Oxidative stress induces amyloid-like aggregate formation of NACP/α-synuclein in vitro

Hashimoto, M., Hsu, L. J., Xia, Y., Takeda, A., Sisk, A., Sundsmo, M., & Masliah, E. (1999) · NeuroReport · doi:10.1097/00001756-199903170-00011 · Cited by 429

Neuromelanin-containing neurons of the substantia nigra accumulate iron and aluminum in Parkinson's disease: a LAMMA study

Good, P. F., Olanow, C. W., & Perl, D. P. (1992) · Brain Research · doi:10.1016/0006-8993(92)91334-b · Cited by 427

Iron metabolism

Aisen, P., Wessling-Resnick, M., & Leibold, E. A. (1999) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(99)80033-7 · Cited by 427

Improvement and Biological Applications of Fluorescent Probes for Zinc, ZnAFs

Hirano, T., Kikuchi, K., Urano, Y., & Nagano, T. (2002) · Journal of the American Chemical Society · doi:10.1021/ja025567p · Cited by 422

Iron uptake and metabolism in the new millennium

Dunn, L. L., Rahmanto, Y. S., & Richardson, D. R. (2007) · Trends in Cell Biology · doi:10.1016/j.tcb.2006.12.003 · Cited by 420

Molecular Features of the Copper Binding Sites in the Octarepeat Domain of the Prion Protein

Burns, C. S., Aronoff-Spencer, E., Dunham, C. M., Lario, P., Avdievich, N. I., Antholine, W. E., Olmstead, M. M., Vrielink, A., Gerfen, G. J., Peisach, J., et al. (2002) · Biochemistry · doi:10.1021/bi011922x · Cited by 417

The Function of Zinc Metallothionein: A Link between Cellular Zinc and Redox State

Maret, W. (2000) · The Journal of Nutrition · doi:10.1093/jn/130.5.1455s · Cited by 416

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

A Role for the Saccharomyces cerevisiae ATX1 Gene in Copper Trafficking and Iron Transport

Lin, S.-J., Pufahl, R. A., Dancis, A., O'Halloran, T. V., & Culotta, V. C. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.14.9215 · Cited by 411

Preferential Zn 2+ influx through Ca 2+ -permeable AMPA/kainate channels triggers prolonged mitochondrial superoxide production

Sensi, S. L., Yin, H. Z., Carriedo, S. G., Rao, S. S., & Weiss, J. H. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.5.2414 · Cited by 408

Structural characterization of copper(II) binding to α-synuclein: Insights into the bioinorganic chemistry of Parkinson's disease

Rasia, R. M., Bertoncini, C. W., Marsh, D., Hoyer, W., Cherny, D., Zweckstetter, M., Griesinger, C., Jovin, T. M., & Fernández, C. O. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407881102 · Cited by 408

Overview of mammalian zinc transporters

Kambe, T., Yamaguchi-Iwai, Y., Sasaki, R., & Nagao, M. (2004) · Cellular and Molecular Life Sciences (CMLS) · doi:10.1007/s00018-003-3148-y · Cited by 407

Detection and Imaging of Zinc Secretion from Pancreatic β-Cells Using a New Fluorescent Zinc Indicator

Gee, K. R., Zhou, Z.-L., Qian, W.-J., & Kennedy, R. (2002) · Journal of the American Chemical Society · doi:10.1021/ja011774y · Cited by 406

Modulation of mitochondrial function by endogenous Zn 2+ pools

Sensi, S. L., Ton-That, D., Sullivan, P. G., Jonas, E. A., Gee, K. R., Kaczmarek, L. K., & Weiss, J. H. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1031598100 · Cited by 406

Structural basis for copper transfer by the metallochaperone for the Menkes/Wilson disease proteins.

Rosenzweig, A. C., Wernimont, A. K., Huffman, D. L., Lamb, A. L., & O’Halloran, T. V. (2000) · Nature Structural Biology · doi:10.1038/78999 · Cited by 405

The Transcription Factor MTF-1 Mediates Metal Regulation of the Mouse ZnT1 Gene

Langmade, S. J., Ravindra, R., Daniels, P. J., & Andrews, G. K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m007339200 · Cited by 405

Information processing in the axon

Debanne, D. (2004) · Nature Reviews Neuroscience · doi:10.1038/nrn1397 · Cited by 400

Copper Binding in the Prion Protein

Millhauser, G. L. (2004) · Accounts of Chemical Research · doi:10.1021/ar0301678 · Cited by 392

A Bright and Specific Fluorescent Sensor for Mercury in Water, Cells, and Tissue

Yoon, S., Miller, E. W., He, Q., Do, P. H., & Chang, C. J. (2007) · Angewandte Chemie International Edition · doi:10.1002/anie.200701785 · Cited by 390

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

Inhibitory sites in enzymes: Zinc removal and reactivation by thionein

Maret, W., Jacob, C., Vallee, B. L., & Fischer, E. H. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.5.1936 · Cited by 386

Crosstalk between Nitric Oxide and Zinc Pathways to Neuronal Cell Death Involving Mitochondrial Dysfunction and p38-Activated K+ Channels

Bossy-Wetzel, E., Talantova, M. V., Lee, W. D., Schölzke, M. N., Harrop, A., Mathews, E., Götz, T., Han, J., Ellisman, M. H., Perkins, G. A., et al. (2004) · Neuron · doi:10.1016/s0896-6273(04)00015-7 · Cited by 384

Imaging of the intracellular topography of copper with a fluorescent sensor and by synchrotron x-ray fluorescence microscopy

Yang, L., McRae, R., Henary, M. M., Patel, R., Lai, B., Vogt, S., & Fahrni, C. J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0406547102 · Cited by 383

Recent development of zinc-fluorophores

Kimura, E., & Koike, T. (1998) · Chemical Society Reviews · doi:10.1039/a827179z · Cited by 378

Glycosylphosphatidylinositol-anchored ceruloplasmin is required for iron efflux from cells in the central nervous system

Jeong, S. Y., & David, S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301988200 · Cited by 377

Iron regulates ferritin mRNA translation through a segment of its 5′-untranslated region.

Aziz, N., & Munro, H. N. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.23.8478 · Cited by 368

Evidence of Presynaptic Location and Function of the Prion Protein

Herms, J., Tings, T., Gall, S., Madlung, A., Giese, A., Siebert, H., Schürmann, P., Windl, O., Brose, N., & Kretzschmar, H. (1999) · The Journal of Neuroscience · doi:10.1523/jneurosci.19-20-08866.1999 · Cited by 365

MRI of brain iron

Drayer, B., Burger, P., Darwin, R., Riederer, S., Herfkens, R., & Johnson, G. (1986) · American Journal of Roentgenology · doi:10.2214/ajr.147.1.103 · Cited by 365

Synaptically released zinc: Physiological functions and pathological effects

Frederickson, C. J., & Bush, A. I. (2001) · Biometals · doi:10.1023/a:1012934207456 · Cited by 363

ZP4, an Improved Neuronal Zn2+ Sensor of the Zinpyr Family

Burdette, S. C., Frederickson, C. J., Bu, W., & Lippard, S. J. (2003) · Journal of the American Chemical Society · doi:10.1021/ja0287377 · Cited by 363

Evidence for Cu(II) Reduction as a Component of Copper Uptake by Saccharomyces cerevisiae

Hassett, R., & Kosman, D. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.1.128 · Cited by 363

Zinc enzymes

Coleman, J. E. (1998) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(98)80064-1 · Cited by 362

Overexpression of Alzheimer's Disease Amyloid-β Opposes the Age-dependent Elevations of Brain Copper and Iron

Maynard, C. J., Cappai, R., Volitakis, I., Cherny, R. A., White, A. R., Beyreuther, K., Masters, C. L., Bush, A. I., & Li, Q.-X. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204379200 · Cited by 353

Selective Zinc Sensor Molecules with Various Affinities for Zn2+, Revealing Dynamics and Regional Distribution of Synaptically Released Zn2+ in Hippocampal Slices

Komatsu, K., Kikuchi, K., Kojima, H., Urano, Y., & Nagano, T. (2005) · Journal of the American Chemical Society · doi:10.1021/ja050301e · Cited by 352

Ultrastructural localization of zinc transporter-3 (ZnT-3) to synaptic vesicle membranes within mossy fiber boutons in the hippocampus of mouse and monkey

Wenzel, H. J., Cole, T. B., Born, D. E., Schwartzkroin, P. A., & Palmiter, R. D. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.23.12676 · Cited by 352

Binding of a Cytosolic Protein to the Iron-Responsive Element of Human Ferritin Messenger RNA

Rouault, T. A., Hentze, M. W., Caughman, S. W., Harford, J. B., & Klausner, R. D. (1988) · Science · doi:10.1126/science.3413484 · Cited by 351

Histochemically-reactive zinc in amyloid plaques, angiopathy, and degenerating neurons of Alzheimer's diseased brains

Suh, S. W., Jensen, K. B., Jensen, M. S., Silva, D. S., Kesslak, P. J., Danscher, G., & Frederickson, C. J. (2000) · Brain Research · doi:10.1016/s0006-8993(99)02096-x · Cited by 350

An iron-binding component in human blood plasma

Schade, A. L., & Caroline, L. (1946) · Science · doi:10.1126/science.104.2702.340 · Cited by 348

Copper-stimulated Endocytosis and Degradation of the Human Copper Transporter, hCtr1

Petris, M. J., Smith, K., Lee, J., & Thiele, D. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209455200 · Cited by 345

Biological inorganic and bioinorganic chemistry of neurodegeneration based on prion and Alzheimer diseases

Brown, D. R., & Kozlowski, H. (2004) · Dalton Transactions · doi:10.1039/b401985g · Cited by 343

The Relevance of Iron in the Pathogenesis of Parkinson's Disease

GÖTZ, M. E., DOUBLE, K., GERLACH, M., YOUDIM, M. B. H., & RIEDERERE, P. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1306.017 · Cited by 342

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

Clinical, biochemical and molecular genetic correlations in Friedreich's ataxia

Bradley, J. L. (2000) · Human Molecular Genetics · doi:10.1093/hmg/9.2.275 · Cited by 339

High‐field magnetic resonance imaging of brain iron: birth of a biomarker?

Schenck, J. F., & Zimmerman, E. A. (2004) · NMR in Biomedicine · doi:10.1002/nbm.922 · Cited by 337

Copper(II)-induced self-oligomerization of α-synuclein

Paik, S. R., Shin, H.-J., Lee, J., Chang, C., & Kim, J. (1999) · Biochemical Journal · doi:10.1042/0264-6021:3400821 · Cited by 337

Activation of microglia by human neuromelanin is NF‐κB‐dependent and involves p38 mitogen‐activated protein kinase: implications for Parkinson's disease

Wilms, H., Rosenstiel, P., Sievers, J., Deuschl, G., Zecca, L., & Lucius, R. (2003) · The FASEB Journal · doi:10.1096/fj.02-0314fje · Cited by 337

Development of a Ratiometric Fluorescent Zinc Ion Probe in Near-Infrared Region, Based on Tricarbocyanine Chromophore

Kiyose, K., Kojima, H., Urano, Y., & Nagano, T. (2006) · Journal of the American Chemical Society · doi:10.1021/ja060399c · Cited by 337

Specific Copper Transfer from the Cox17 Metallochaperone to Both Sco1 and Cox11 in the Assembly of Yeast Cytochrome c Oxidase

Horng, Y.-C., Cobine, P. A., Maxfield, A. B., Carr, H. S., & Winge, D. R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404747200 · Cited by 333

Induction and Activation by Zinc of NADPH Oxidase in Cultured Cortical Neurons and Astrocytes

Noh, K.-M., & Koh, J.-Y. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-23-j0001.2000 · Cited by 332

Aqueous Coordination Chemistry of Quinoline-Based Fluorescence Probes for the Biological Chemistry of Zinc

Fahrni, C. J., & O'Halloran, T. V. (1999) · Journal of the American Chemical Society · doi:10.1021/ja992709f · Cited by 332

Modulation of A beta adhesiveness and secretase site cleavage by zinc.

Bush, A. I., Pettingell, W. H., Paradis, M. D., & Tanzi, R. E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32694-7 · Cited by 331

Metallothionein III is expressed in neurons that sequester zinc in synaptic vesicles

Masters, B., Quaife, C., Erickson, J., Kelly, E., Froelick, G., Zambrowicz, B., Brinster, R., & Palmiter, R. (1994) · The Journal of Neuroscience · doi:10.1523/jneurosci.14-10-05844.1994 · Cited by 330

A “Smart” Magnetic Resonance Imaging Agent That Reports on Specific Enzymatic Activity

Moats, R. A., Fraser, S. E., & Meade, T. J. (1997) · Angewandte Chemie International Edition in English · doi:10.1002/anie.199707261 · Cited by 330

A Fluorogenic Probe for the Copper(I)-Catalyzed Azide−Alkyne Ligation Reaction: Modulation of the Fluorescence Emission via 3(n,π*)−(π,π*) Inversion

Zhou, Z., & Fahrni, C. J. (2004) · Journal of the American Chemical Society · doi:10.1021/ja049684r · Cited by 329

Cellular zinc sensors: MTF-1 regulation of gene expression

Andrews, G. K. (2001) · Biometals · doi:10.1023/a:1012932712483 · Cited by 325

Increased iron‐related MRI contrast in the substantia nigra in Parkinson's disease

Gorell, J. M., Ordidge, R. J., Brown, G. G., Deniau, J.-C., Buderer, N. M., & Helpern, J. A. (1995) · Neurology · doi:10.1212/wnl.45.6.1138 · Cited by 324

Assessment of relative brain iron concentrations using T2‐weighted and T2*‐weighted MRI at 3 Tesla

Ordidge, R. J., Gorell, J. M., Deniau, J. C., Knight, R. A., & Helpern, J. A. (1994) · Magnetic Resonance in Medicine · doi:10.1002/mrm.1910320309 · Cited by 323

SCO1 and SCO2 Act as High Copy Suppressors of a Mitochondrial Copper Recruitment Defect in Saccharomyces cerevisiae

Glerum, D. M., Shtanko, A., & Tzagoloff, A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.34.20531 · Cited by 323

Zinc sensing for cellular application

Kikuchi, K., Komatsu, K., & Nagano, T. (2004) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2004.02.007 · Cited by 320

Copper trafficking to the mitochondrion and assembly of copper metalloenzymes

Cobine, P. A., Pierrel, F., & Winge, D. R. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.03.002 · Cited by 317

Copper Binding to the N-Terminal Tandem Repeat Region of Mammalian and Avian Prion Protein: Structural Studies Using Synthetic Peptides

Hornshaw, M. P., Mcdermott, J. R., Candy, J. M., & Lakey, J. H. (1995) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1995.2384 · Cited by 317

Regulation of the zinc transporter ZnT-1 by dietary zinc

McMahon, R. J., & Cousins, R. J. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.9.4841 · Cited by 316

Human whole-body copper metabolism

Turnlund, Jr. (1998) · The American Journal of Clinical Nutrition · doi:10.1093/ajcn/67.5.960s · Cited by 315

Iron-melanin complex in substantia nigra of parkinsonian brains: an x-ray microanalysis

Jellinger, K., Kienzl, E., Rumpelmair, G., Riederer, P., Stachelberger, H., Ben‐Shachar, D., & Youdim, M. B. H. (1992) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1992.tb08362.x · Cited by 313

Illuminating Zinc in Biological Systems

Lim, N. C., Freake, H. C., & Brückner, C. (2005) · Chemistry – A European Journal · doi:10.1002/chem.200400599 · Cited by 311

A Novel, Cell-Permeable, Fluorescent Probe for Ratiometric Imaging of Zinc Ion

Maruyama, S., Kikuchi, K., Hirano, T., Urano, Y., & Nagano, T. (2002) · Journal of the American Chemical Society · doi:10.1021/ja026442n · Cited by 307

Intracellular Copper Transport in Mammals

Prohaska, J. R., & Gybina, A. A. (2004) · The Journal of Nutrition · doi:10.1093/jn/134.5.1003 · Cited by 307

Copper-binding-site-null SOD1 causes ALS in transgenic mice: aggregates of non-native SOD1 delineate a common feature

Wang, J., Slunt, H., Gonzales, V., Fromholt, D., Coonfield, M., Copeland, N. G., Jenkins, N. A., & Borchelt, D. R. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg312 · Cited by 306

Nerve endings from rat brain tissue release copper upon depolarization. A possible role in regulating neuronal excitability

Kardos, J., Kovács, I., Hajós, F., Kálmán, M., & Simonyi, M. (1989) · Neuroscience Letters · doi:10.1016/0304-3940(89)90565-x · Cited by 302

Ca2+-dependent regulation in neuronal gene expression

Bito, H., Deisseroth, K., & Tsien, R. W. (1997) · Current Opinion in Neurobiology · doi:10.1016/s0959-4388(97)80072-4 · Cited by 299

Distribution of divalent metal transporter 1 and metal transport protein 1 in the normal and Belgrade rat

Burdo, J. R., Menzies, S. L., Simpson, I. A., Garrick, L. M., Garrick, M. D., Dolan, K. G., Haile, D. J., Beard, J. L., & Connor, J. R. (2001) · Journal of Neuroscience Research · doi:10.1002/jnr.1256 · Cited by 297

The Yeast Fre1p/Fre2p Cupric Reductases Facilitate Copper Uptake and Are Regulated by the Copper-modulated Mac1p Activator

Georgatsou, E., Mavrogiannis, L. A., Fragiadakis, G. S., & Alexandraki, D. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.21.13786 · Cited by 296

Water-soluble porphyrins as a dual-function molecular imaging platform for MRI and fluorescence zinc sensing

Zhang, X.-A., Lovejoy, K. S., Jasanoff, A., & Lippard, S. J. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702393104 · Cited by 294

Alterations in levels of iron, ferritin, and other trace metals in neurodegenerative diseases affecting the basal ganglia

Dexter, D. T., Jenner, P., Schapira, A. H. V., Marsden, C. D., & The Royal Kings and Queens Parkinson's Disease Research Group (1992) · Annals of Neurology · doi:10.1002/ana.410320716 · Cited by 292

IRON, FERRITIN, AND NUTRITION

Theil, E. C. (2004) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.24.012003.132212 · Cited by 292

Brain iron uptake and homeostatic mechanisms: An overview

Burdo, J. R., & Connor, J. R. (2003) · Biometals · doi:10.1023/a:1020718718550 · Cited by 290

NMDA Receptor Activation Mediates Copper Homeostasis in Hippocampal Neurons

Schlief, M. L., Craig, A. M., & Gitlin, J. D. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.3699-04.2005 · Cited by 290

The ATX1 gene of Saccharomyces cerevisiae encodes a small metal homeostasis factor that protects cells against reactive oxygen toxicity.

Lin, S. J., & Culotta, V. C. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.9.3784 · Cited by 289

A novel zinc(II) binding site modulates the function of the beta A4 amyloid protein precursor of Alzheimer's disease

Bush, A. I., Multhaup, G., Moir, R. D., Williamson, T. G., Small, D. H., Rumble, B., Pollwein, P., Beyreuther, K., & Masters, C. L. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85394-2 · Cited by 286

Copper levels are increased in the cerebral cortex and liver of APP and APLP2 knockout mice

White, A. R., Reyes, R., Mercer, J. F. B., Camakaris, J., Zheng, H., Bush, A. I., Multhaup, G., Beyreuther, K., Masters, C. L., & Cappai, R. (1999) · Brain Research · doi:10.1016/s0006-8993(99)01861-2 · Cited by 282

Alpha-synuclein and Parkinson's disease

Lücking, C. B., & Brice*, A. (2000) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000671 · 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

Structure of the Alzheimer's Disease Amyloid Precursor Protein Copper Binding Domain

Barnham, K. J., McKinstry, W. J., Multhaup, G., Galatis, D., Morton, C. J., Curtain, C. C., Williamson, N. A., White, A. R., Hinds, M. G., Norton, R. S., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300629200 · Cited by 275

Video image analysis of labile zinc in viable pancreatic islet cells using a specific fluorescent probe for zinc.

Zalewski, P. D., Millard, S. H., Forbes, I. J., Kapaniris, O., Slavotinek, A., Betts, W. H., Ward, A. D., Lincoln, S. F., & Mahadevan, I. (1994) · Journal of Histochemistry & Cytochemistry · doi:10.1177/42.7.8014471 · Cited by 272

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