메뉴 건너뛰기




Volumn 6, Issue 6, 2005, Pages 449-462

The neurobiology of zinc in health and disease

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINOBUTYRIC ACID A RECEPTOR; 4 AMINOBUTYRIC ACID B RECEPTOR; ADENOSINE RECEPTOR; AMINO ACID RECEPTOR; AMPA RECEPTOR; CALAMINE; CALCIUM; CATECHOLAMINE RECEPTOR; CHOLINERGIC RECEPTOR; DERMATOLOGICAL AGENT; DOPAMINE; DOPAMINE RECEPTOR; EXCITATORY AMINO ACID RECEPTOR; GLUTAMATE RECEPTOR; GLUTAMIC ACID; GLYCINE RECEPTOR; MELANOCORTIN RECEPTOR; METABOTROPIC RECEPTOR; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; OPIATE RECEPTOR; SEROTONIN RECEPTOR; ZINC; ZINC TRANSPORTER;

EID: 20144377557     PISSN: 1471003X     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrn1671     Document Type: Review
Times cited : (1611)

References (270)
  • 2
    • 0032747083 scopus 로고    scopus 로고
    • Small size, large scale Roman brass production in Germania Inferior
    • Rehren, T. Small size, large scale Roman brass production in Germania Inferior. J. Archaeol. Sci. 26, 1083-1087 (1999).
    • (1999) J. Archaeol. Sci. , vol.26 , pp. 1083-1087
    • Rehren, T.1
  • 3
    • 0033960382 scopus 로고    scopus 로고
    • Causes of iron and zinc deficiencies and their effects on brain
    • Sandstead, H. H. Causes of iron and zinc deficiencies and their effects on brain. J. Nutr. 130, 347S-349S (2000).
    • (2000) J. Nutr. , vol.130
    • Sandstead, H.H.1
  • 4
    • 0025255158 scopus 로고
    • Zinc fingers and other metal-binding domains. Elements for interactions between macromolecules
    • Berg, J. M. Zinc fingers and other metal-binding domains. Elements for interactions between macromolecules. J. Biol. Chem. 265, 6513-6516 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 6513-6516
    • Berg, J.M.1
  • 5
    • 0642340971 scopus 로고    scopus 로고
    • Comparative toxicity of a zinc salt, zinc powder and zinc oxide to Eisenia fetida. Enchytraeus albidus and Folsomia Candida
    • Lock, K. & Janssen, C. R. Comparative toxicity of a zinc salt, zinc powder and zinc oxide to Eisenia fetida. Enchytraeus albidus and Folsomia Candida. Chemosphere 53, 851-856 (2003).
    • (2003) Chemosphere , vol.53 , pp. 851-856
    • Lock, K.1    Janssen, C.R.2
  • 9
    • 0344010194 scopus 로고    scopus 로고
    • Intracellular zinc fluctuations modulate protein tyrosine phosphatase activity in insulin/insulin-like growth factor-1 signaling
    • Haase, H. & Maret, W. Intracellular zinc fluctuations modulate protein tyrosine phosphatase activity in insulin/insulin-like growth factor-1 signaling. Exp. Cell Res. 291, 289-298 (2003).
    • (2003) Exp. Cell Res. , vol.291 , pp. 289-298
    • Haase, H.1    Maret, W.2
  • 10
    • 0035969898 scopus 로고    scopus 로고
    • Enzyme regulation by reversible zinc inhibition: Glycerol phosphate dehydrogenase as an example
    • Maret, W., Yetman, C. A. & Jiang, L. Enzyme regulation by reversible zinc inhibition: glycerol phosphate dehydrogenase as an example. Chem. Biol. Interact. 130-132, 891-901 (2001). Reveals the role of thionein as a zinc-shuttle that carries zinc signals to specific proteins.
    • (2001) Chem. Biol. Interact. , vol.130-132 , pp. 891-901
    • Maret, W.1    Yetman, C.A.2    Jiang, L.3
  • 11
    • 0033514994 scopus 로고    scopus 로고
    • Inhibitory sites in enzymes: Zinc removal and reactivation by thionein
    • Maret, W., Jacob, C., Vallee, B. L. & Fischer, E. H. Inhibitory sites in enzymes: zinc removal and reactivation by thionein. Proc. Natl Acad. Sci. USA 96, 1936-1940 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1936-1940
    • Maret, W.1    Jacob, C.2    Vallee, B.L.3    Fischer, E.H.4
  • 13
    • 0024779411 scopus 로고
    • Neurobiology of zinc and zinc-containing neurons
    • Frederickson, C. J. Neurobiology of zinc and zinc-containing neurons. Int. Rev. Neurobiol. 31, 145-238 (1989).
    • (1989) Int. Rev. Neurobiol. , vol.31 , pp. 145-238
    • Frederickson, C.J.1
  • 14
    • 0035696287 scopus 로고    scopus 로고
    • Synaptically released zinc: Physiological functions and pathological effects
    • Frederickson, C. J. & Bush, A. I. Synaptically released zinc: physiological functions and pathological effects. Biometals 14, 353-366 (2001).
    • (2001) Biometals , vol.14 , pp. 353-366
    • Frederickson, C.J.1    Bush, A.I.2
  • 15
    • 0025188014 scopus 로고
    • Labeling of the neurons of origin of zinc-containing pathways by intraperitoneal injections of sodium selenite
    • Slomianka, L., Danscher, G. & Frederickson, C. J. Labeling of the neurons of origin of zinc-containing pathways by intraperitoneal injections of sodium selenite. Neuroscience 38, 843-854 (1990).
    • (1990) Neuroscience , vol.38 , pp. 843-854
    • Slomianka, L.1    Danscher, G.2    Frederickson, C.J.3
  • 16
    • 7244256599 scopus 로고
    • A new method for demonstrating A and B cells in the islands of Langerhans
    • Translation
    • Maske, H. A new method for demonstrating A and B cells in the islands of Langerhans. (Translation) Klin. Wochenschr. 33, 1058 (1955).
    • (1955) Klin. Wochenschr. , vol.33 , pp. 1058
    • Maske, H.1
  • 17
    • 0028354969 scopus 로고
    • Modulation of inhibitory and excitatory amino acid receptor ion channels by zinc
    • Smart, T. G., Xie, X. & Krishek, B. J. Modulation of inhibitory and excitatory amino acid receptor ion channels by zinc. Prog. Neurobiol. 42, 393-341 (1994).
    • (1994) Prog. Neurobiol. , vol.42 , pp. 393-341
    • Smart, T.G.1    Xie, X.2    Krishek, B.J.3
  • 19
    • 0036549214 scopus 로고    scopus 로고
    • Rapid, experience-dependent changes in levels of synaptic zinc in primary somatosensory cortex of the adult mouse
    • Brown, C. E. & Dyck, R. H. Rapid, experience-dependent changes in levels of synaptic zinc in primary somatosensory cortex of the adult mouse. J. Neurosci. 22, 2617-2625 (2002).
    • (2002) J. Neurosci. , vol.22 , pp. 2617-2625
    • Brown, C.E.1    Dyck, R.H.2
  • 20
    • 0026457056 scopus 로고
    • Postnatal development of zinc-containing cells and neuropil in the visual cortex of the mouse
    • Garrett, B. & Slomianka, L. Postnatal development of zinc-containing cells and neuropil in the visual cortex of the mouse. Anat. Embryol. (Berl.) 186, 487-496 (1992).
    • (1992) Anat. Embryol. (Berl.) , vol.186 , pp. 487-496
    • Garrett, B.1    Slomianka, L.2
  • 21
    • 0037139264 scopus 로고    scopus 로고
    • Zinc-rich neurones in the rat visual cortex give rise to two laminar segregated systems of connections
    • Casanovas-Aguilar, C., Miro-Bernie, N. & Perez-Clausell, J. Zinc-rich neurones in the rat visual cortex give rise to two laminar segregated systems of connections. Neuroscience 110, 445-458 (2002).
    • (2002) Neuroscience , vol.110 , pp. 445-458
    • Casanovas-Aguilar, C.1    Miro-Bernie, N.2    Perez-Clausell, J.3
  • 22
    • 0031814847 scopus 로고    scopus 로고
    • Zinc-rich afferents to the rat neocortex: Projections to the visual cortex traced with intracerebral selenite injections
    • Casanovas-Aguilar, C., Reblet, C., Perez-Clausell, J. & Bueno-Lopez, J. L. Zinc-rich afferents to the rat neocortex: projections to the visual cortex traced with intracerebral selenite injections. J. Chem. Neuroanat. 15, 97-109 (1998).
    • (1998) J. Chem. Neuroanat. , vol.15 , pp. 97-109
    • Casanovas-Aguilar, C.1    Reblet, C.2    Perez-Clausell, J.3    Bueno-Lopez, J.L.4
  • 23
    • 0028799714 scopus 로고
    • Callosal neurones give rise to zinc-rich boutons in the rat visual cortex
    • Casanovas-Aguilar, C. et al. Callosal neurones give rise to zinc-rich boutons in the rat visual cortex. Neuroreport 6, 497-500 (1995).
    • (1995) Neuroreport , vol.6 , pp. 497-500
    • Casanovas-Aguilar, C.1
  • 25
    • 0022388387 scopus 로고
    • The dithizone, Timm's sulphide silver and the selenium methods demonstrate a chelatable pool of zinc in CNS. A proton activation (PIXE) analysis of carbon tetrachloride extracts from rat brains and spinal cords intravitally treated with dithizone
    • Danscher, G., Howell, G., Perez-Clausell, J. & Hertel, N. The dithizone, Timm's sulphide silver and the selenium methods demonstrate a chelatable pool of zinc in CNS. A proton activation (PIXE) analysis of carbon tetrachloride extracts from rat brains and spinal cords intravitally treated with dithizone. Histochemistry 83, 419-422 (1985).
    • (1985) Histochemistry , vol.83 , pp. 419-422
    • Danscher, G.1    Howell, G.2    Perez-Clausell, J.3    Hertel, N.4
  • 27
    • 0041672236 scopus 로고    scopus 로고
    • Boutons containing vesicular zinc define a subpopulation of synapses with low AMPAR content in rat hippocampus
    • Sindreu, C. B., Varoqui, H., Erickson, J. D. & Perez-Clausell, J. Boutons containing vesicular zinc define a subpopulation of synapses with low AMPAR content in rat hippocampus. Cereb. Cortex 13, 823-829 (2003). Shows that almost half of synapses on some cortical dendrites are glutamate and zinc releasing, and that these are preferentially located at NMDA receptor-loaded spines.
    • (2003) Cereb. Cortex , vol.13 , pp. 823-829
    • Sindreu, C.B.1    Varoqui, H.2    Erickson, J.D.3    Perez-Clausell, J.4
  • 28
    • 0015056167 scopus 로고
    • Timm's sulfide silver reaction for zinc during experimental anterograde degeneration of hippocampal mossy fibers
    • Haug, F. M., Blackstad, T. W., Simonsen, A. H. & Zimmer, J. Timm's sulfide silver reaction for zinc during experimental anterograde degeneration of hippocampal mossy fibers. J. Comp. Neurol. 142, 23-31 (1971).
    • (1971) J. Comp. Neurol. , vol.142 , pp. 23-31
    • Haug, F.M.1    Blackstad, T.W.2    Simonsen, A.H.3    Zimmer, J.4
  • 29
    • 0021996332 scopus 로고
    • A selective loss of hippocampal mossy fiber Timm stain accompanies granule cell seizure activity induced by perforant path stimulation
    • Sloviter, R. S. A selective loss of hippocampal mossy fiber Timm stain accompanies granule cell seizure activity induced by perforant path stimulation. Brain Res. 330, 150-153 (1985).
    • (1985) Brain Res. , vol.330 , pp. 150-153
    • Sloviter, R.S.1
  • 30
    • 0023918015 scopus 로고
    • Loss of zinc staining from hippocampal mossy fibers during kainic acid induced seizures: A histofluorescence study
    • Frederickson, C. J., Hernandez, M. D., Goik, S. A., Morton, J. D. & McGinty, J. F. Loss of zinc staining from hippocampal mossy fibers during kainic acid induced seizures: a histofluorescence study. Brain Res. 446, 383-386 (1988).
    • (1988) Brain Res. , vol.446 , pp. 383-386
    • Frederickson, C.J.1    Hernandez, M.D.2    Goik, S.A.3    Morton, J.D.4    McGinty, J.F.5
  • 31
    • 1942520949 scopus 로고    scopus 로고
    • Response to kainic acid injections: Changes in staining for zinc, FOS, cell death and glial response in the rat forebrain
    • Riba-Bosch, A. & Perez-Clausell, J. Response to kainic acid injections: changes in staining for zinc, FOS, cell death and glial response in the rat forebrain. Neuroscience 125, 803-818 (2004).
    • (2004) Neuroscience , vol.125 , pp. 803-818
    • Riba-Bosch, A.1    Perez-Clausell, J.2
  • 32
    • 0032561715 scopus 로고    scopus 로고
    • Rapid disappearance of zinc positive terminals in focal brain ischemia
    • Sorensen, J. C., Mattsson, B., Andreasen, A. & Johansson, B. B. Rapid disappearance of zinc positive terminals in focal brain ischemia. Brain Res 812, 265-269 (1998).
    • (1998) Brain Res , vol.812 , pp. 265-269
    • Sorensen, J.C.1    Mattsson, B.2    Andreasen, A.3    Johansson, B.B.4
  • 33
    • 0033988750 scopus 로고    scopus 로고
    • Evidence that synaptically-released zinc contributes to neuronal injury after traumatic brain injury
    • Suh, S. W. et al. Evidence that synaptically-released zinc contributes to neuronal injury after traumatic brain injury. Brain Res. 852, 268-273 (2000).
    • (2000) Brain Res. , vol.852 , pp. 268-273
    • Suh, S.W.1
  • 34
    • 0031009848 scopus 로고    scopus 로고
    • Imaging free zinc in synaptic terminals in live hippocampal slices
    • Budde, T., Minta, A., White, J. A. & Kay, A. R. Imaging free zinc in synaptic terminals in live hippocampal slices. Neuroscience 79, 347-358 (1997).
    • (1997) Neuroscience , vol.79 , pp. 347-358
    • Budde, T.1    Minta, A.2    White, J.A.3    Kay, A.R.4
  • 36
    • 0022630133 scopus 로고
    • Release of zinc sulphide accumulations into synaptic clefts after in vivo injection of sodium sulphide
    • Perez-Clausell, J. & Danscher, G. Release of zinc sulphide accumulations into synaptic clefts after in vivo injection of sodium sulphide. Brain Res. 362, 358-361 (1986).
    • (1986) Brain Res. , vol.362 , pp. 358-361
    • Perez-Clausell, J.1    Danscher, G.2
  • 37
    • 1642415856 scopus 로고    scopus 로고
    • Hippocampal mossy fiber calcium transients are maintained during long-term potentiation and are inhibited by endogenous zinc
    • Quinta-Ferreira, M. E. & Matias, C. M. Hippocampal mossy fiber calcium transients are maintained during long-term potentiation and are inhibited by endogenous zinc. Brain Res. 1004, 52-60 (2004).
    • (2004) Brain Res. , vol.1004 , pp. 52-60
    • Quinta-Ferreira, M.E.1    Matias, C.M.2
  • 38
    • 0021287299 scopus 로고
    • 2+ from brain tissue during activity
    • 2+ from brain tissue during activity. Nature 308, 734-736 (1984).
    • (1984) Nature , vol.308 , pp. 734-736
    • Assaf, S.Y.1    Chung, S.H.2
  • 39
    • 0021220724 scopus 로고
    • Stimulation-induced uptake and release of zinc in hippocampal slices
    • Howell, G. A., Welch, M. G. & Frederickson, C. J. Stimulation-induced uptake and release of zinc in hippocampal slices. Nature 308, 736-738 (1984). The discovery that zinc is released in a calcium- and impulse-dependent manner from central neurons.
    • (1984) Nature , vol.308 , pp. 736-738
    • Howell, G.A.1    Welch, M.G.2    Frederickson, C.J.3
  • 40
    • 0023141269 scopus 로고
    • Selective release of endogenous zinc from the hippocampal mossy fibers in situ
    • Aniksztejn, L., Charton, G. & Ben Ari, Y. Selective release of endogenous zinc from the hippocampal mossy fibers in situ. Brain Res. 404, 58-64 (1987).
    • (1987) Brain Res. , vol.404 , pp. 58-64
    • Aniksztejn, L.1    Charton, G.2    Ben Ari, Y.3
  • 43
    • 20144368750 scopus 로고    scopus 로고
    • Zinc and glutamate signaling during ischemia and reperfusion
    • in the press
    • Zornow, M. et al. Zinc and glutamate signaling during ischemia and reperfusion. Neuroscience (in the press).
    • Neuroscience
    • Zornow, M.1
  • 44
    • 0034002451 scopus 로고    scopus 로고
    • Fluorescence microscopy of stimulated Zn(II) release from organotypic cultures of mammalian hippocampus using a carbonic anhydrase-based biosensor system
    • Thompson, R. B., Whetsell, W. O. Jr, Maliwal, B. P., Fierke, C. A. & Frederickson, C. J. Fluorescence microscopy of stimulated Zn(II) release from organotypic cultures of mammalian hippocampus using a carbonic anhydrase-based biosensor system. J. Neurosci. Methods 96, 35-45 (2000).
    • (2000) J. Neurosci. Methods , vol.96 , pp. 35-45
    • Thompson, R.B.1    Whetsell Jr., W.O.2    Maliwal, B.P.3    Fierke, C.A.4    Frederickson, C.J.5
  • 45
  • 46
    • 0037157834 scopus 로고    scopus 로고
    • 2+ spillover modulates heterosynaptic N-methyl-D-aspartate receptor activity in hippocampal CA3 circuits
    • 2+ spillover modulates heterosynaptic N-methyl-D-aspartate receptor activity in hippocampal CA3 circuits. J. Cell Biol. 158, 215-220 (2002).
    • (2002) J. Cell Biol. , vol.158 , pp. 215-220
    • Ueno, S.1
  • 47
    • 0015699567 scopus 로고
    • The hippocampus and behavioral maturation
    • Altman, J., Brunner, R. L. & Bayer, S. A. The hippocampus and behavioral maturation. Behav. Biol. 8, 557-596 (1973).
    • (1973) Behav. Biol. , vol.8 , pp. 557-596
    • Altman, J.1    Brunner, R.L.2    Bayer, S.A.3
  • 48
    • 0016266374 scopus 로고
    • Hippocampal development in the rat: Cytogenesis and morphogenesis examined with autoradiography and low-level X-irradiation
    • Bayer, S. A. & Altman, J. Hippocampal development in the rat: cytogenesis and morphogenesis examined with autoradiography and low-level X-irradiation. J. Comp. Neurol. 158, 55-79 (1974).
    • (1974) J. Comp. Neurol. , vol.158 , pp. 55-79
    • Bayer, S.A.1    Altman, J.2
  • 49
    • 0019441872 scopus 로고
    • Zinc dithizonate staining in the cat hippocampus: Relationship to the mossy-fiber neuropil and postnatal development
    • Frederickson, C. J., Howell, G. A. & Frederickson, M. H. Zinc dithizonate staining in the cat hippocampus: relationship to the mossy-fiber neuropil and postnatal development. Exp. Neurol. 73, 812-823 (1981).
    • (1981) Exp. Neurol. , vol.73 , pp. 812-823
    • Frederickson, C.J.1    Howell, G.A.2    Frederickson, M.H.3
  • 50
    • 0042133328 scopus 로고    scopus 로고
    • Evidence for chelatable zinc in the extracellular space of the hippocampus, but little evidence for synaptic release of Zn
    • Kay, A. R. Evidence for chelatable zinc in the extracellular space of the hippocampus, but little evidence for synaptic release of Zn. J. Neurosci. 23, 6847-6855 (2003).
    • (2003) J. Neurosci. , vol.23 , pp. 6847-6855
    • Kay, A.R.1
  • 52
    • 0030961933 scopus 로고    scopus 로고
    • Study of the interactions of cadmium and zinc ions with cellular calcium homoeostasis using 19F-NMR spectroscopy
    • Benters, J. et al. Study of the interactions of cadmium and zinc ions with cellular calcium homoeostasis using 19F-NMR spectroscopy. Biochem. J. 322, 793-799 (1997).
    • (1997) Biochem. J. , vol.322 , pp. 793-799
    • Benters, J.1
  • 53
    • 0002068190 scopus 로고    scopus 로고
    • Routes of zinc entry in mouse cortical neurons: Role in zinc-induced neurotoxictty
    • Marin, P., Israel, M., Glowinski, J. & Premont, J. Routes of zinc entry in mouse cortical neurons: role in zinc-induced neurotoxictty. Eur. J. Neurosci. 12, 8-18 (2000).
    • (2000) Eur. J. Neurosci. , vol.12 , pp. 8-18
    • Marin, P.1    Israel, M.2    Glowinski, J.3    Premont, J.4
  • 54
    • 0033624438 scopus 로고    scopus 로고
    • Zinc biosensing with multiphoton excitation using carbonic anhydrase and improved fluorophores
    • Thompson, R. B., Maliwal, B. P. & Zeng, H. H. Zinc biosensing with multiphoton excitation using carbonic anhydrase and improved fluorophores. J. Biomed. Opt. 5, 17-22 (2000).
    • (2000) J. Biomed. Opt. , vol.5 , pp. 17-22
    • Thompson, R.B.1    Maliwal, B.P.2    Zeng, H.H.3
  • 55
    • 0037101907 scopus 로고    scopus 로고
    • 2+ currents are mediated by calcium-permeable AMPA/kainate channels in cultured murine hippocampal neurones
    • 2+ currents are mediated by calcium-permeable AMPA/kainate channels in cultured murine hippocampal neurones. J. Physiol. (Lond.) 543, 35-48 (2002).
    • (2002) J. Physiol. (Lond.) , vol.543 , pp. 35-48
    • Jia, Y.1    Jeng, J.M.2    Sensi, S.L.3    Weiss, J.H.4
  • 56
    • 0031466709 scopus 로고    scopus 로고
    • Measurement of intracellular free zinc in living cortical neurons: Routes of entry
    • Sensi, S. L. et al. Measurement of intracellular free zinc in living cortical neurons: routes of entry. J. Neurosci. 17, 9554-9564 (1997).
    • (1997) J. Neurosci. , vol.17 , pp. 9554-9564
    • Sensi, S.L.1
  • 57
    • 0028860021 scopus 로고
    • Excitation-transcription coupling mediated by zinc influx through voltage-dependent calcium channels
    • Atar, D., Backx, P. H., Appel, M. M., Gao, W. D. & Marban, E. Excitation-transcription coupling mediated by zinc influx through voltage-dependent calcium channels. J. Biol. Chem. 270, 2473-2477 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 2473-2477
    • Atar, D.1    Backx, P.H.2    Appel, M.M.3    Gao, W.D.4    Marban, E.5
  • 60
    • 0034058549 scopus 로고    scopus 로고
    • The function of zinc metallothionein: A link between cellular zinc and redox state
    • Maret, W. The function of zinc metallothionein: a link between cellular zinc and redox state. J. Nutr. 130, 1455S-1458S (2000).
    • (2000) J. Nutr. , vol.130
    • Maret, W.1
  • 61
    • 0028082427 scopus 로고
    • Oxidative metal release from metallothionein via zinc-thiol/disulfide interchange
    • Maret, W. Oxidative metal release from metallothionein via zinc-thiol/disulfide interchange. Proc. Natl Acad. Sci. USA 91, 237-241 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 237-241
    • Maret, W.1
  • 62
    • 0029060897 scopus 로고
    • The function of metallothionein
    • Vallee, B. L. The function of metallothionein. Neurochem. Int. 27, 23-33 (1995).
    • (1995) Neurochem. Int. , vol.27 , pp. 23-33
    • Vallee, B.L.1
  • 63
    • 0032584166 scopus 로고    scopus 로고
    • Thiolate ligands in metallothioneins confer redox activity on zinc clusters
    • Maret, W. & Vallee, B. L. Thiolate ligands in metallothioneins confer redox activity on zinc clusters. Proc. Natl Acad. Sci. USA 95, 3478-3482 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3478-3482
    • Maret, W.1    Vallee, B.L.2
  • 64
    • 0034058549 scopus 로고    scopus 로고
    • The function of zinc metallothionein: A link between cellular zinc and redox state
    • Maret, W. The function of zinc metallothionein: a link between cellular zinc and redox state. J. Nutr. 130 (5S Suppl.), 145S-148S (2000).
    • (2000) J. Nutr. , vol.130 , Issue.5 S SUPPL.
    • Maret, W.1
  • 65
    • 0032584186 scopus 로고    scopus 로고
    • Control of zinc transfer between thionein, metallothionein, and zinc proteins
    • Jacob, C., Maret, W. & Vallee, B. L. Control of zinc transfer between thionein, metallothionein, and zinc proteins. Proc. Natl Acad. Sci. USA 95, 3489-3494 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3489-3494
    • Jacob, C.1    Maret, W.2    Vallee, B.L.3
  • 66
    • 0025768860 scopus 로고
    • The growth inhibitory factor that is deficient in the Alzheimers disease brain is a 68 aminoacid metallothionein-like protein
    • Uchida, Y., Taiko, K., Titani, K. I. Y. & Tomonaga, M. The growth inhibitory factor that is deficient in the Alzheimers disease brain is a 68 aminoacid metallothionein-like protein. Neuron 7, 337-347 (1991).
    • (1991) Neuron , vol.7 , pp. 337-347
    • Uchida, Y.1    Taiko, K.2    Titani, K.I.Y.3    Tomonaga, M.4
  • 68
    • 0344394903 scopus 로고    scopus 로고
    • Zinc released from metallothionein-III may contribute to hippocampal CA1 and thalamic neuronal death following acute brain injury
    • Lee, J. Y., Kim, J. H., Palmiter, R. D. & Koh, J. Y. Zinc released from metallothionein-III may contribute to hippocampal CA1 and thalamic neuronal death following acute brain injury. Exp. Neurol. 184, 337-347 (2003).
    • (2003) Exp. Neurol. , vol.184 , pp. 337-347
    • Lee, J.Y.1    Kim, J.H.2    Palmiter, R.D.3    Koh, J.Y.4
  • 71
    • 0034238089 scopus 로고    scopus 로고
    • 2+ permeable AMPA or kainate receptors: Possible key factors in selective neurodegeneration
    • 2+ permeable AMPA or kainate receptors: possible key factors in selective neurodegeneration. Trends Neurosci. 23, 365-371 (2000).
    • (2000) Trends Neurosci. , vol.23 , pp. 365-371
    • Weiss, J.H.1    Sensi, S.L.2
  • 72
    • 0034091981 scopus 로고    scopus 로고
    • Zinc transport in the bran: Routes of zinc influx and efflux in neurons
    • Colvin, R. A., Davis, N., Nipper, R. W. & Carter, P. A. Zinc transport in the bran: routes of zinc influx and efflux in neurons. J. Nutr. 130, 1484S-1487S (2000).
    • (2000) J. Nutr. , vol.130
    • Colvin, R.A.1    Davis, N.2    Nipper, R.W.3    Carter, P.A.4
  • 73
  • 74
    • 2142821384 scopus 로고    scopus 로고
    • 2+ during ischemia and reperfusion of hippocampus slices in rat
    • 2+ during ischemia and reperfusion of hippocampus slices in rat. Neuroscience 125, 867-877 (2004).
    • (2004) Neuroscience , vol.125 , pp. 867-877
    • Wei, G.1    Hough, C.J.2    Li, Y.3    Sarvey, J.M.4
  • 76
  • 77
    • 0033788519 scopus 로고    scopus 로고
    • Induction of neuronal apoptosis by thiol oxidation: Putative role of intracellular zinc release
    • Aizenman, E. et al. Induction of neuronal apoptosis by thiol oxidation: putative role of intracellular zinc release. J. Neurochem. 75, 1878-1888 (2000). Introduces the notion of thiol-liberated free zinc as a generic apoptosis death signal.
    • (2000) J. Neurochem. , vol.75 , pp. 1878-1888
    • Aizenman, E.1
  • 78
    • 0345276559 scopus 로고    scopus 로고
    • NMDA receptor regulation of nNOS phosphorylation and induction of neuron death
    • Rameau, G. A., Chiu, L. Y. & Ziff, E. B. NMDA receptor regulation of nNOS phosphorylation and induction of neuron death. Neurobiol. Aging 24, 1123-1133 (2003).
    • (2003) Neurobiol. Aging , vol.24 , pp. 1123-1133
    • Rameau, G.A.1    Chiu, L.Y.2    Ziff, E.B.3
  • 79
    • 1842790618 scopus 로고    scopus 로고
    • Bidirectional regulation of neuronal nitric-oxide synthase phosphorylation at serine 847 by the N-methyl-o-aspartate receptor
    • Rameau, G. A., Chiu, L. Y. & Ziff, E. B. Bidirectional regulation of neuronal nitric-oxide synthase phosphorylation at serine 847 by the N-methyl-o-aspartate receptor. J. Biol. Chem. 279, 14307-14314 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 14307-14314
    • Rameau, G.A.1    Chiu, L.Y.2    Ziff, E.B.3
  • 81
    • 0029906949 scopus 로고    scopus 로고
    • ZnT-3, a putative transporter of zinc into synaptic vesicles
    • Palmiter, R. D., Cole, T. B., Quaife, C. J. & Findley, S. D. ZnT-3, a putative transporter of zinc into synaptic vesicles. Proc. Natl Acad. Sci. USA 93, 14934-14939 (1996). The first evidence to indicate that the ZnT3 protein is necessary for zinc accumulation in neuronal vesicles.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14934-14939
    • Palmiter, R.D.1    Cole, T.B.2    Quaife, C.J.3    Findley, S.D.4
  • 82
    • 4644223422 scopus 로고    scopus 로고
    • A role for ZnT-1 in regulating cellular cation influx
    • Segal, D. et al. A role for ZnT-1 in regulating cellular cation influx. Biochem. Biophys. Res. Commun. 323, 1145-1150 (2004).
    • (2004) Biochem. Biophys. Res. Commun. , vol.323 , pp. 1145-1150
    • Segal, D.1
  • 84
    • 0030746608 scopus 로고    scopus 로고
    • High-affinity zinc inhibition of NMDA NR1-NR2A receptors
    • Paoletti, P., Ascher, P. & Neyton, J. High-affinity zinc inhibition of NMDA NR1-NR2A receptors. J. Neurosci. 17, 5711-5725 (1997).
    • (1997) J. Neurosci. , vol.17 , pp. 5711-5725
    • Paoletti, P.1    Ascher, P.2    Neyton, J.3
  • 85
    • 1642317185 scopus 로고    scopus 로고
    • Some precautions in using chelators to buffer metals in biological solutions
    • Patton, C., Thompson, S. & Epel, D. Some precautions in using chelators to buffer metals in biological solutions. Cell Calcium 35, 427-431 (2004).
    • (2004) Cell Calcium , vol.35 , pp. 427-431
    • Patton, C.1    Thompson, S.2    Epel, D.3
  • 86
    • 0036557830 scopus 로고    scopus 로고
    • Preparation of metal ion buffers for biological experimentation: A methods approach with emphasis on iron and zinc
    • Aslamkhan, A. G., Aslamkhan, A. & Ahearn, G. A. Preparation of metal ion buffers for biological experimentation: a methods approach with emphasis on iron and zinc. J. Exp. Zool. 292, 507-522 (2002).
    • (2002) J. Exp. Zool. , vol.292 , pp. 507-522
    • Aslamkhan, A.G.1    Aslamkhan, A.2    Ahearn, G.A.3
  • 87
    • 0037199267 scopus 로고    scopus 로고
    • Fluorescent zinc indicators for neurobiology
    • Thompson, R. B. et al. Fluorescent zinc indicators for neurobiology. J. Neurosci. Methods 118, 63-75 (2002).
    • (2002) J. Neurosci. Methods , vol.118 , pp. 63-75
    • Thompson, R.B.1
  • 88
    • 0023253615 scopus 로고
    • Zinc selectively blocks the action of N-methyl-D-aspartate on cortical neurons
    • Peters, S., Koh, J. & Choi, D. W. Zinc selectively blocks the action of N-methyl-D-aspartate on cortical neurons. Science 236, 589-593 (1987).
    • (1987) Science , vol.236 , pp. 589-593
    • Peters, S.1    Koh, J.2    Choi, D.W.3
  • 89
    • 0034718494 scopus 로고    scopus 로고
    • Molecular determinants of coordinated proton and zinc inhibition of N-methyl-o-aspartate NR1/NR2A receptors
    • Low, C. M., Zheng, F., Lyuboslavsky, P. & Traynelis, S. F. Molecular determinants of coordinated proton and zinc inhibition of N-methyl-o-aspartate NR1/NR2A receptors. Proc. Natl Acad. Sci. USA 97, 11062-11067 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 11062-11067
    • Low, C.M.1    Zheng, F.2    Lyuboslavsky, P.3    Traynelis, S.F.4
  • 90
    • 0035193095 scopus 로고    scopus 로고
    • 3H]ifenprodil binding site in rat brain membranes with the pharmacology of the voltage-independent ifenprodil site on N-methyl-D-aspartate receptors containing NR2B subunits
    • 3H]ifenprodil binding site in rat brain membranes with the pharmacology of the voltage-independent ifenprodil site on N-methyl-D-aspartate receptors containing NR2B subunits. J. Pharmacol. Exp. Ther. 296, 150-159 (2001).
    • (2001) J. Pharmacol. Exp. Ther. , vol.296 , pp. 150-159
    • Coughenour, L.L.1    Barr, B.M.2
  • 91
    • 0026638143 scopus 로고
    • NMDA receptor-mediated depolarizing action of proline on CA1 pyramidal cells
    • Martin, D., Ault, B. & Nadler, J. V. NMDA receptor-mediated depolarizing action of proline on CA1 pyramidal cells. Eur. J. Pharmacol. 219, 59-66 (1992).
    • (1992) Eur. J. Pharmacol. , vol.219 , pp. 59-66
    • Martin, D.1    Ault, B.2    Nadler, J.V.3
  • 92
    • 0033712121 scopus 로고    scopus 로고
    • The actions of synaptically released zinc at hippocampal mossy fiber synapses
    • Vogt, K., Mellor, J., Tong, G. & Nicoll, R. The actions of synaptically released zinc at hippocampal mossy fiber synapses. Neuron 26, 187-196 (2000).
    • (2000) Neuron , vol.26 , pp. 187-196
    • Vogt, K.1    Mellor, J.2    Tong, G.3    Nicoll, R.4
  • 93
    • 0027297786 scopus 로고
    • Proconvulsant action of diethyldithiocarbamate in stimulation of the perforant path
    • Mitchell, C. L. & Barnes, M. I. Proconvulsant action of diethyldithiocarbamate in stimulation of the perforant path. Neurotoxicol. Teratol. 15, 165-171 (1993).
    • (1993) Neurotoxicol. Teratol. , vol.15 , pp. 165-171
    • Mitchell, C.L.1    Barnes, M.I.2
  • 94
    • 0025059005 scopus 로고
    • Diethyldithiocarbamate and dithizone augment the toxicity of kainic acid
    • Mitchell, C. L., Barnes, M. I. & Grimes, L. M. Diethyldithiocarbamate and dithizone augment the toxicity of kainic acid. Brain Res. 506, 327-330 (1990).
    • (1990) Brain Res. , vol.506 , pp. 327-330
    • Mitchell, C.L.1    Barnes, M.I.2    Grimes, L.M.3
  • 95
    • 0037459799 scopus 로고    scopus 로고
    • Calretinin/PSA-NCAM immunoreactive granule cells after hippocampal damage produced by kainic acid and DEDTC treatment in mouse
    • Dominguez, M. I., Blasco-Ibanez, J. M., Crespo, C., Marques-Mari, A. I. & Martinez-Guijarro, F. J. Calretinin/PSA-NCAM immunoreactive granule cells after hippocampal damage produced by kainic acid and DEDTC treatment in mouse. Brain Res. 966, 206-217 (2003).
    • (2003) Brain Res. , vol.966 , pp. 206-217
    • Dominguez, M.I.1    Blasco-Ibanez, J.M.2    Crespo, C.3    Marques-Mari, A.I.4    Martinez-Guijarro, F.J.5
  • 97
    • 0035097912 scopus 로고    scopus 로고
    • Zinc-induced augmentation of excitatory synaptic currents and glutamate receptor responses in hippocampal CA3 neurons
    • Lin, D. D., Cohen, A. S. & Coulter, D. A. Zinc-induced augmentation of excitatory synaptic currents and glutamate receptor responses in hippocampal CA3 neurons. J. Neurophysiol. 85, 1185-1196 (2001).
    • (2001) J. Neurophysiol. , vol.85 , pp. 1185-1196
    • Lin, D.D.1    Cohen, A.S.2    Coulter, D.A.3
  • 98
    • 0035949572 scopus 로고    scopus 로고
    • Zinc induces a Src family kinase-mediated up-regulation of NMDA receptor activity and excitotoxicity
    • Manzerra, P. et al. Zinc induces a Src family kinase-mediated up-regulation of NMDA receptor activity and excitotoxicity. Proc. Natl Acad. Sci. USA 98, 11055-11061 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11055-11061
    • Manzerra, P.1
  • 99
    • 0036837439 scopus 로고    scopus 로고
    • Augmentation by zinc of NMDA receptor-mediated synaptic responses in CA1 of rat hippocampal slices: Mediation by Src family tyrosine kinases
    • Kim, T. Y., Hwang, J. J., Yun, S. H., Jung, M. W. & Koh, J. Y. Augmentation by zinc of NMDA receptor-mediated synaptic responses in CA1 of rat hippocampal slices: mediation by Src family tyrosine kinases. Synapse 46, 49-56 (2002).
    • (2002) Synapse , vol.46 , pp. 49-56
    • Kim, T.Y.1    Hwang, J.J.2    Yun, S.H.3    Jung, M.W.4    Koh, J.Y.5
  • 100
    • 0023160323 scopus 로고
    • 2+ antagonize NMDA and GABA responses of hippocampal neurons
    • 2+ antagonize NMDA and GABA responses of hippocampal neurons. Nature 328, 640-643 (1987).
    • (1987) Nature , vol.328 , pp. 640-643
    • Westbrook, G.L.1    Mayer, M.L.2
  • 101
    • 0020590772 scopus 로고
    • Pre- and postsynaptic effects of zinc on in vitro prepyriform neurones
    • Smart, T. G. & Constanti, A. Pre- and postsynaptic effects of zinc on in vitro prepyriform neurones. Neurosci. Lett. 40, 205-211 (1983).
    • (1983) Neurosci. Lett. , vol.40 , pp. 205-211
    • Smart, T.G.1    Constanti, A.2
  • 102
    • 0034786489 scopus 로고    scopus 로고
    • Zinc and copper influence excitability of rat orfactory bulb neurons by mutiiple mechanisms
    • Horning, M. S. & Trombley, P. Q. Zinc and copper influence excitability of rat orfactory bulb neurons by mutiiple mechanisms. J. Neurophysiol. 86, 1652-1650 (2001).
    • (2001) J. Neurophysiol. , vol.86 , pp. 1652-1650
    • Horning, M.S.1    Trombley, P.Q.2
  • 103
    • 0025729461 scopus 로고
    • Noncompetitive inhibition of γ-aminobutyric acidA channels by Zn
    • Legendre, P. & Westbrook, G. L. Noncompetitive inhibition of γ-aminobutyric acidA channels by Zn. Mol. Pharmacol. 39, 267-274 (1991).
    • (1991) Mol. Pharmacol. , vol.39 , pp. 267-274
    • Legendre, P.1    Westbrook, G.L.2
  • 104
    • 0025777271 scopus 로고
    • Zinc and GABA in developing brain
    • Ben Ari, Y., & Cherubini, E. Zinc and GABA in developing brain. Nature 353, 220 (1991).
    • (1991) Nature , vol.353 , pp. 220
    • Ben Ari, Y.1    Cherubini, E.2
  • 106
    • 0026089456 scopus 로고
    • A physiological role for endogenous zinc in rat hippocampal synaptic neurotransmission
    • Xie, X. M. & Smart, T. G. A physiological role for endogenous zinc in rat hippocampal synaptic neurotransmission. Nature 349, 521-524 (1991).
    • (1991) Nature , vol.349 , pp. 521-524
    • Xie, X.M.1    Smart, T.G.2
  • 108
    • 0028356960 scopus 로고
    • Modulation of GABA-mediated synaptic transmission by endogenous zinc in the immature rat hippocampus in vitro
    • Xie, X., Hider, R. C. & Smart, T. G. Modulation of GABA-mediated synaptic transmission by endogenous zinc in the immature rat hippocampus in vitro. J. Physiol. (Lond.) 478, 75-86 (1994).
    • (1994) J. Physiol. (Lond.) , vol.478 , pp. 75-86
    • Xie, X.1    Hider, R.C.2    Smart, T.G.3
  • 109
    • 0035824283 scopus 로고    scopus 로고
    • Zinc-enriched GABAergic terminals in mouse spinal cord
    • Wang, Z., Li, J. Y., Dahlstrom, A. & Danscher, G. Zinc-enriched GABAergic terminals in mouse spinal cord. Brain Res. 921, 165-172 (2001).
    • (2001) Brain Res. , vol.921 , pp. 165-172
    • Wang, Z.1    Li, J.Y.2    Dahlstrom, A.3    Danscher, G.4
  • 110
    • 0030593034 scopus 로고    scopus 로고
    • Zinc-induced collapse of augmented inhibition by GABA in a temporal lobe epilepsy model
    • Buhl, E. H., Otis, T. S. & Mody, I. Zinc-induced collapse of augmented inhibition by GABA in a temporal lobe epilepsy model. Science 271, 369-373 (1996).
    • (1996) Science , vol.271 , pp. 369-373
    • Buhl, E.H.1    Otis, T.S.2    Mody, I.3
  • 111
    • 0035202121 scopus 로고    scopus 로고
    • Epilepsy-associated plasticity in γ-aminobutyric acid receptor expression, function, and inhibitory synaptic properties
    • Coulter, D. A. Epilepsy-associated plasticity in γ-aminobutyric acid receptor expression, function, and inhibitory synaptic properties. Int. Rev. Neurobiol. 45, 237-252 (2001).
    • (2001) Int. Rev. Neurobiol. , vol.45 , pp. 237-252
    • Coulter, D.A.1
  • 113
    • 0035014174 scopus 로고    scopus 로고
    • A receptors in the pilocarpine model of epilepsy
    • A receptors in the pilocarpine model of epilepsy. J. Neurophysiol. 85, 1932-1940 (2001).
    • (2001) J. Neurophysiol. , vol.85 , pp. 1932-1940
    • Molnar, P.1    Nadler, J.V.2
  • 115
    • 0034996934 scopus 로고    scopus 로고
    • A receptor subunit expression predicts functional changes in hippocampal dentate granule cells during postnatal development
    • A receptor subunit expression predicts functional changes in hippocampal dentate granule cells during postnatal development. J. Neurochem. 77, 1266-1278 (2001).
    • (2001) J. Neurochem. , vol.77 , pp. 1266-1278
    • Brooks-Kayal, A.R.1
  • 117
    • 0032926451 scopus 로고    scopus 로고
    • Zinc modulates antagonist interactions with D2-like dopamine receptors through distinct molecular mechanisms
    • Schetz, J. A., Chu, A. & Sibley, D. R. Zinc modulates antagonist interactions with D2-like dopamine receptors through distinct molecular mechanisms. J. Pharmacol. Exp. Ther. 289, 956-964 (1999).
    • (1999) J. Pharmacol. Exp. Ther. , vol.289 , pp. 956-964
    • Schetz, J.A.1    Chu, A.2    Sibley, D.R.3
  • 118
    • 0030992175 scopus 로고    scopus 로고
    • Zinc allosterically modulates antagonist binding to cloned D1 and D2 dopamine receptors
    • Schetz, J. A. & Sibley, D. R. Zinc allosterically modulates antagonist binding to cloned D1 and D2 dopamine receptors. J. Neurochem. 68, 1990-1997 (1997).
    • (1997) J. Neurochem. , vol.68 , pp. 1990-1997
    • Schetz, J.A.1    Sibley, D.R.2
  • 119
    • 0029758490 scopus 로고    scopus 로고
    • Modulation of serotonin-induced currents by metals in mouse neuroblastoma cells
    • Uki, M. & Narahashi, T. Modulation of serotonin-induced currents by metals in mouse neuroblastoma cells. Arch. Toxicol. 70, 652-660 (1996).
    • (1996) Arch. Toxicol. , vol.70 , pp. 652-660
    • Uki, M.1    Narahashi, T.2
  • 121
    • 0033567440 scopus 로고    scopus 로고
    • Mechanisms of inhibitory effects of zinc and cadmium ions on agonist binding to adenosine A1 receptors in rat brain
    • Rosati, A. M. & Traversa, U. Mechanisms of inhibitory effects of zinc and cadmium ions on agonist binding to adenosine A1 receptors in rat brain. Biochem. Pharmacol. 58, 623-632 (1999).
    • (1999) Biochem. Pharmacol. , vol.58 , pp. 623-632
    • Rosati, A.M.1    Traversa, U.2
  • 122
    • 0030310274 scopus 로고    scopus 로고
    • Zinc and cadmium ions differently modulate A1 adenosine receptors
    • Traversa, U. & Rosati, A. Zinc and cadmium ions differently modulate A1 adenosine receptors. Acta Physiol. Hung. 84, 465-467 (1996).
    • (1996) Acta Physiol. Hung. , vol.84 , pp. 465-467
    • Traversa, U.1    Rosati, A.2
  • 124
    • 0035931126 scopus 로고    scopus 로고
    • Modulation of α2β4 neuronal nicotinic acetylcholine receptors by zinc
    • Garcia-Colunga, J., Gonzalez-Herrera, M. & Miledi, R. Modulation of α2β4 neuronal nicotinic acetylcholine receptors by zinc. Neuroreport 12, 147-150 (2001).
    • (2001) Neuroreport , vol.12 , pp. 147-150
    • Garcia-Colunga, J.1    Gonzalez-Herrera, M.2    Miledi, R.3
  • 125
    • 0036094667 scopus 로고    scopus 로고
    • Pharmacological characterization of glycine-gated chloride currents recorded in rat hippocampal slices
    • Chattipakorn, S. C. & McMahon, L. L. Pharmacological characterization of glycine-gated chloride currents recorded in rat hippocampal slices. J. Neurophysiol. 87, 1515-1525 (2002).
    • (2002) J. Neurophysiol. , vol.87 , pp. 1515-1525
    • Chattipakorn, S.C.1    McMahon, L.L.2
  • 127
    • 0036521882 scopus 로고    scopus 로고
    • ASIC-like, proton-activated currents in rat hippocampal neurons
    • Baron, A., Waldmann, R. & Lazdunski, M. ASIC-like, proton-activated currents in rat hippocampal neurons. J. Physiol. (Lond.) 539, 485-494 (2002).
    • (2002) J. Physiol. (Lond.) , vol.539 , pp. 485-494
    • Baron, A.1    Waldmann, R.2    Lazdunski, M.3
  • 128
    • 0035972116 scopus 로고    scopus 로고
    • Zinc colocalizes with GABA and glycine in synapses in the lamprey spinal cord
    • Birinyi, A., Parker, D., Antal, M. & Shupliakov, O. Zinc colocalizes with GABA and glycine in synapses in the lamprey spinal cord. J. Comp. Neurol. 433, 208-221 (2001).
    • (2001) J. Comp. Neurol. , vol.433 , pp. 208-221
    • Birinyi, A.1    Parker, D.2    Antal, M.3    Shupliakov, O.4
  • 129
    • 0028943569 scopus 로고
    • Modulation by zinc ions of native rat and recombinant human inhibitory glycine receptors
    • Laube, B. et al. Modulation by zinc ions of native rat and recombinant human inhibitory glycine receptors. J. Physiol. (Lond.) 483, 613-619 (1995).
    • (1995) J. Physiol. (Lond.) , vol.483 , pp. 613-619
    • Laube, B.1
  • 130
    • 0026783265 scopus 로고
    • The regulatory domain of protein kinase C coordinates four atoms of zinc
    • Quest, A. F., Bloomenthal, J., Bardes, E. S. & Bell, R. M. The regulatory domain of protein kinase C coordinates four atoms of zinc. J. Biol. Chem. 267, 10193-10197 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 10193-10197
    • Quest, A.F.1    Bloomenthal, J.2    Bardes, E.S.3    Bell, R.M.4
  • 132
    • 0030428903 scopus 로고    scopus 로고
    • Zinc neurotoxicity may contribute to selective neuronal death following transient global cerebral ischemia
    • Choi, D. W. Zinc neurotoxicity may contribute to selective neuronal death following transient global cerebral ischemia. Cold Spring Harb. Symp. Quant. Biol. 61, 385-387 (1996).
    • (1996) Cold Spring Harb. Symp. Quant. Biol. , vol.61 , pp. 385-387
    • Choi, D.W.1
  • 133
    • 0025092376 scopus 로고
    • Possible mechanisms limiting N-methyl-D-aspartate receptor overactivation and the therapeutic efficacy of N-methyl-D-aspartate antagonists
    • Choi, D. W. Possible mechanisms limiting N-methyl-D-aspartate receptor overactivation and the therapeutic efficacy of N-methyl-D-aspartate antagonists. Stroke 21, III20-III22 (1990).
    • (1990) Stroke , vol.21
    • Choi, D.W.1
  • 135
    • 0031849828 scopus 로고    scopus 로고
    • Molecular basis for differential inhibition of glutamate transporter subtypes by zinc ions
    • Vandenberg, R. J., Mitrovic, A. D. & Johnston, G. A. Molecular basis for differential inhibition of glutamate transporter subtypes by zinc ions. Mol. Pharmacol. 54, 189-196 (1998).
    • (1998) Mol. Pharmacol. , vol.54 , pp. 189-196
    • Vandenberg, R.J.1    Mitrovic, A.D.2    Johnston, G.A.3
  • 136
    • 0027455744 scopus 로고
    • Zinc modulation of drug binding, cocaine affinity states, and dopamine uptake on the dopamine uptake complex
    • Richfield, E. K. Zinc modulation of drug binding, cocaine affinity states, and dopamine uptake on the dopamine uptake complex. Mol. Pharmacol. 43, 100-108 (1993).
    • (1993) Mol. Pharmacol. , vol.43 , pp. 100-108
    • Richfield, E.K.1
  • 137
    • 0020406364 scopus 로고
    • The selective inhibition of hippocampal glutamic acid decarboxylase in zinc-induced epileptic seizures
    • Itoh, M. & Ebadi, M. The selective inhibition of hippocampal glutamic acid decarboxylase in zinc-induced epileptic seizures. Neurochem. Res. 7, 1287-1298 (1982).
    • (1982) Neurochem. Res. , vol.7 , pp. 1287-1298
    • Itoh, M.1    Ebadi, M.2
  • 138
    • 0025208325 scopus 로고
    • Effects of subcutaneous injections of zinc chloride on seizures induced by noise and by kainic acid
    • Morton, J. D., Howell, G. A. & Frederickson, C. J. Effects of subcutaneous injections of zinc chloride on seizures induced by noise and by kainic acid. Epilepsie 31, 139-144 (1990).
    • (1990) Epilepsie , vol.31 , pp. 139-144
    • Morton, J.D.1    Howell, G.A.2    Frederickson, C.J.3
  • 139
    • 0028244304 scopus 로고
    • Modulation of long-term potentiation in rat hippocampal pyramidal neurons by zinc
    • Xie, X. & Smart, T. G. Modulation of long-term potentiation in rat hippocampal pyramidal neurons by zinc. Pflugers Arch. 427, 481-486 (1994).
    • (1994) Pflugers Arch. , vol.427 , pp. 481-486
    • Xie, X.1    Smart, T.G.2
  • 141
    • 0024532022 scopus 로고
    • A heavy metal marker of the developing striatal mosaic
    • Vincent, S. R. & Semba, K. A heavy metal marker of the developing striatal mosaic. Brain Res. Dev. Brain Res. 45, 155-159 (1989).
    • (1989) Brain Res. Dev. Brain Res. , vol.45 , pp. 155-159
    • Vincent, S.R.1    Semba, K.2
  • 142
    • 0035858785 scopus 로고    scopus 로고
    • Transient expression of synaptic zinc during development of uncrossed retinogeniculate projections
    • Land, P. W. & Shamalla-Hannah, L. Transient expression of synaptic zinc during development of uncrossed retinogeniculate projections. J. Comp. Neurol. 433, 515-525 (2001).
    • (2001) J. Comp. Neurol. , vol.433 , pp. 515-525
    • Land, P.W.1    Shamalla-Hannah, L.2
  • 143
    • 0027461474 scopus 로고
    • Histochemical localization of synaptic zinc in the developing cat visual cortex
    • Dyck, R., Beaulieu, C. & Cynader, M. Histochemical localization of synaptic zinc in the developing cat visual cortex. J. Comp. Neurol. 329, 53-67 (1993).
    • (1993) J. Comp. Neurol. , vol.329 , pp. 53-67
    • Dyck, R.1    Beaulieu, C.2    Cynader, M.3
  • 144
    • 0033779649 scopus 로고    scopus 로고
    • 2+ is required for the induction of long-term potentiation at rat hippocampal mossy fiber-CA3 synapses
    • 2+ is required for the induction of long-term potentiation at rat hippocampal mossy fiber-CA3 synapses. Synapse 38, 187-197 (2000).
    • (2000) Synapse , vol.38 , pp. 187-197
    • Lu, Y.M.1
  • 145
    • 0014958594 scopus 로고
    • Intoxication following ingestion of elemental zinc
    • Murphy, J. V. Intoxication following ingestion of elemental zinc. JAMA 212, 2119-2120 (1970).
    • (1970) JAMA , vol.212 , pp. 2119-2120
    • Murphy, J.V.1
  • 146
    • 0023030987 scopus 로고
    • Brief exposure to zinc is toxic to cortical neurons
    • Yokoyama, M., Koh, J. & Choi, D. W. Brief exposure to zinc is toxic to cortical neurons. Neurosci. Lett. 71, 351-355 (1986).
    • (1986) Neurosci. Lett. , vol.71 , pp. 351-355
    • Yokoyama, M.1    Koh, J.2    Choi, D.W.3
  • 147
    • 0020502042 scopus 로고
    • Cytoarchitectonic distribution of zinc in the hippocampus of man and the rat
    • Frederickson, C. J., Klitenick, M. A., Manton, W. I. & Kirkpatrick, J. B. Cytoarchitectonic distribution of zinc in the hippocampus of man and the rat. Brain Res. 273, 335-339 (1983).
    • (1983) Brain Res. , vol.273 , pp. 335-339
    • Frederickson, C.J.1    Klitenick, M.A.2    Manton, W.I.3    Kirkpatrick, J.B.4
  • 148
    • 0027198869 scopus 로고
    • Basic mechanisms of traumatic brain damage
    • Siesjo, B. K. Basic mechanisms of traumatic brain damage. Ann. Emerg. Med. 22, 959-969 (1993).
    • (1993) Ann. Emerg. Med. , vol.22 , pp. 959-969
    • Siesjo, B.K.1
  • 150
    • 0027536881 scopus 로고
    • AMPA receptor activation potentiates zinc neurotoxicity
    • Weiss, J. H., Hartley, D. M., Koh, J. Y. & Choi, D. W. AMPA receptor activation potentiates zinc neurotoxicity. Neuron 10, 43-49 (1993).
    • (1993) Neuron , vol.10 , pp. 43-49
    • Weiss, J.H.1    Hartley, D.M.2    Koh, J.Y.3    Choi, D.W.4
  • 151
    • 0028343364 scopus 로고
    • Zinc toxicity on cultured cortical neurons: Involvement of N-methyl-D-aspartate receptors
    • Koh, J. Y. & Choi, D. W. Zinc toxicity on cultured cortical neurons: involvement of N-methyl-D-aspartate receptors. Neuroscience 60, 1049-1057 (1994).
    • (1994) Neuroscience , vol.60 , pp. 1049-1057
    • Koh, J.Y.1    Choi, D.W.2
  • 152
    • 0035175326 scopus 로고    scopus 로고
    • Mechanism of apoptosis induced by zinc deficiency in peripheral blood T lymphocytes
    • Kolenko, V. M. et al. Mechanism of apoptosis induced by zinc deficiency in peripheral blood T lymphocytes. Apoptosis 6, 419-429 (2001).
    • (2001) Apoptosis , vol.6 , pp. 419-429
    • Kolenko, V.M.1
  • 153
    • 0033205843 scopus 로고    scopus 로고
    • Measurement of intracellular free zinc concentrations accompanying zinc-induced neuronal death
    • Canzoniero, L. M., Turetsky, D. M. & Choi, D. W. Measurement of intracellular free zinc concentrations accompanying zinc-induced neuronal death. J. Neurosci. 19, RC31 (1999).
    • (1999) J. Neurosci. , vol.19
    • Canzoniero, L.M.1    Turetsky, D.M.2    Choi, D.W.3
  • 154
    • 0024477326 scopus 로고
    • Translocation of zinc may contribute to seizure-induced death of neurons
    • Frederickson, C. J., Hemandez, M. D. & McGinty J. F. Translocation of zinc may contribute to seizure-induced death of neurons. Brain Res. 480, 317-321 (1989). The discovery that zinc accumulates in neurons injured by excitotoxicity.
    • (1989) Brain Res. , vol.480 , pp. 317-321
    • Frederickson, C.J.1    Hemandez, M.D.2    McGinty, J.F.3
  • 155
    • 0025138527 scopus 로고
    • Possible role of zinc in the selective degeneration of dentate hilar neurons after cerebral ischemia in the adult rat
    • Tonder, N., Johansen, F. F., Frederickson, C. J., Zimmer, J. & Diemer, N. H. Possible role of zinc in the selective degeneration of dentate hilar neurons after cerebral ischemia in the adult rat. Neurosci. Lett. 109, 247-252 (1990).
    • (1990) Neurosci. Lett. , vol.109 , pp. 247-252
    • Tonder, N.1    Johansen, F.F.2    Frederickson, C.J.3    Zimmer, J.4    Diemer, N.H.5
  • 156
    • 0029777299 scopus 로고    scopus 로고
    • The role of zinc in selective neuronal death after transient global cerebral ischemia
    • Koh, J. Y. et al. The role of zinc in selective neuronal death after transient global cerebral ischemia. Science 272, 1013-1016 (1996). The first demonstation that chelation of metals can rescue neurons from ischaemic injury and death.
    • (1996) Science , vol.272 , pp. 1013-1016
    • Koh, J.Y.1
  • 157
    • 0037049243 scopus 로고    scopus 로고
    • Zinc translocation accelerates infarction after mild transient focal ischemia
    • Lee, J. M. et al. Zinc translocation accelerates infarction after mild transient focal ischemia. Neuroscience 115, 871-878 (2002).
    • (2002) Neuroscience , vol.115 , pp. 871-878
    • Lee, J.M.1
  • 158
  • 159
    • 3242699005 scopus 로고    scopus 로고
    • Zinc release contributes to hypoglycemia-induced neuronal death
    • Suh, S. W., Garnier, P., Aoyama, K., Chen, Y. & Swanson, R. A. Zinc release contributes to hypoglycemia-induced neuronal death. Neurobiol. Dis. 16, 538-545 (2004).
    • (2004) Neurobiol. Dis. , vol.16 , pp. 538-545
    • Suh, S.W.1    Garnier, P.2    Aoyama, K.3    Chen, Y.4    Swanson, R.A.5
  • 160
    • 0034202005 scopus 로고    scopus 로고
    • Accumulation of zinc in degenerating hippocampal neurons of ZnT3-null mice after seizures: Evidence against synaptic vesicle origin
    • Lee, J. Y., Cole, T. B., Palmiter, R. D. & Koh, J. Y. Accumulation of zinc in degenerating hippocampal neurons of ZnT3-null mice after seizures: evidence against synaptic vesicle origin. J. Neurosci. 20, RC79 (2000). The first study to show that zinc accumulation in injured neurons is independent of synpatic vesicle zinc.
    • (2000) J. Neurosci. , vol.20
    • Lee, J.Y.1    Cole, T.B.2    Palmiter, R.D.3    Koh, J.Y.4
  • 161
    • 0036943908 scopus 로고    scopus 로고
    • Depletion of intracellular zinc from neurons by use of an extracellular chelator in vivo and in vitro
    • Frederickson, C. J. et al. Depletion of intracellular zinc from neurons by use of an extracellular chelator in vivo and in vitro. J. Histochem. Cytochem. 50, 1659-1662 (2002).
    • (2002) J. Histochem. Cytochem. , vol.50 , pp. 1659-1662
    • Frederickson, C.J.1
  • 162
    • 0028922876 scopus 로고
    • The influence of zinc on apoptosis
    • Sunderman, F. W. Jr. The influence of zinc on apoptosis. Ann. Clin. Lab. Sci. 25, 134-142 (1995).
    • (1995) Ann. Clin. Lab. Sci. , vol.25 , pp. 134-142
    • Sunderman Jr., F.W.1
  • 163
    • 0032588001 scopus 로고    scopus 로고
    • 2+ entry produces oxidative neuronal necrosis in cortical cell cultures
    • 2+ entry produces oxidative neuronal necrosis in cortical cell cultures. Eur. J. Neurosci. 11, 327-334 (1999).
    • (1999) Eur. J. Neurosci. , vol.11 , pp. 327-334
    • Kim, E.Y.1
  • 164
    • 0033519569 scopus 로고    scopus 로고
    • 2+ permeable AMPA channels and consequent ROS production
    • 2+ permeable AMPA channels and consequent ROS production. Neuroreport 10, 1723-1727 (1999). Showed that calcium permeable AMPA/Kainate channels are the main route of zinc entry to postsynaptic neurons. Also links zinc and oxidative stress.
    • (1999) Neuroreport , vol.10 , pp. 1723-1727
    • Sensi, S.L.1    Yin, H.Z.2    Weiss, J.H.3
  • 165
    • 0344820731 scopus 로고    scopus 로고
    • Mediation by membrane protein kinase C of zinc-induced oxidative neuronal injury in mouse cortical cultures
    • Noh, K. M., Kim, Y. H. & Koh, J. Y. Mediation by membrane protein kinase C of zinc-induced oxidative neuronal injury in mouse cortical cultures. J. Neurochem. 72, 1609-1616 (1999).
    • (1999) J. Neurochem. , vol.72 , pp. 1609-1616
    • Noh, K.M.1    Kim, Y.H.2    Koh, J.Y.3
  • 166
    • 0006372708 scopus 로고    scopus 로고
    • Zinc-induced cortical neuronal death with features of apoptosis and necrosis: Mediation by free radicals
    • Kim, Y. H., Kim, E. Y., Gwag, B. J., Sohn, S. & Koh, J. Y. Zinc-induced cortical neuronal death with features of apoptosis and necrosis: mediation by free radicals. Neuroscience 89, 175-182 (1999).
    • (1999) Neuroscience , vol.89 , pp. 175-182
    • Kim, Y.H.1    Kim, E.Y.2    Gwag, B.J.3    Sohn, S.4    Koh, J.Y.5
  • 167
    • 0034903539 scopus 로고    scopus 로고
    • 2+-induced ERK activation mediated by reactive oxygen species cause cell death in differentiated PC12 cells
    • 2+-induced ERK activation mediated by reactive oxygen species cause cell death in differentiated PC12 cells. J. Neurochem. 78, 600-610 (2001).
    • (2001) J. Neurochem. , vol.78 , pp. 600-610
    • Seo, S.R.1
  • 168
    • 0034573392 scopus 로고    scopus 로고
    • Induction and activation by zinc of NADPH oxidase in cultured cortical neurons and astrocytes
    • Noh, K. M. & Koh, J. Y. Induction and activation by zinc of NADPH oxidase in cultured cortical neurons and astrocytes. J. Neurosci. 20, RC111 (2000). NADPH oxidase might be one of the effectors of zinc-induced oxidative stress.
    • (2000) J. Neurosci. , vol.20
    • Noh, K.M.1    Koh, J.Y.2
  • 169
    • 0034199204 scopus 로고    scopus 로고
    • Zinc-induced neuronal death in cortical neurons
    • Lobner, D. et al. Zinc-induced neuronal death in cortical neurons. Cell Mol. Biol. (Noisy-le-grand) 46, 797-806 (2000).
    • (2000) Cell Mol. Biol. (Noisy-le-grand) , vol.46 , pp. 797-806
    • Lobner, D.1
  • 170
    • 0034670369 scopus 로고    scopus 로고
    • NTR-associated death executor in neurons after zinc exposure in cortical culture or transient ischemia in the rat
    • NTR-associated death executor in neurons after zinc exposure in cortical culture or transient ischemia in the rat. J. Neurosci. 20, 9096-9103 (2000).
    • (2000) J. Neurosci. , vol.20 , pp. 9096-9103
    • Park, J.A.1    Lee, J.Y.2    Sato, T.A.3    Koh, J.Y.4
  • 171
  • 172
    • 0035861677 scopus 로고    scopus 로고
    • 2+ induces permeability transition pore opening and release of pro-apoptotic peptides from neuronal mitochondria
    • 2+ induces permeability transition pore opening and release of pro-apoptotic peptides from neuronal mitochondria. J. Biol. Chem. 276, 47524-47529 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 47524-47529
    • Jiang, D.1    Sullivan, P.G.2    Sensi, S.L.3    Steward, O.4    Weiss, J.H.5
  • 173
    • 0038641303 scopus 로고    scopus 로고
    • NTR and the associated death executor NADE in degenerating hippocampal neurons after kainate-induced seizures in the rat
    • NTR and the associated death executor NADE in degenerating hippocampal neurons after kainate-induced seizures in the rat. Neurosci. Lett. 347, 126-130 (2003).
    • (2003) Neurosci. Lett. , vol.347 , pp. 126-130
    • Yi, J.S.1    Lee, S.K.2    Sato, T.A.3    Koh, J.Y.4
  • 174
    • 0035826695 scopus 로고    scopus 로고
    • Differential fluorescence labeling of cysteinyl clusters uncovers high tissue levels of thionein
    • Yang, Y., Maret, W. & Vallee, B. L. Differential fluorescence labeling of cysteinyl clusters uncovers high tissue levels of thionein. Proc. Natl Acad. Sci. USA 98, 5556-5559 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 5556-5559
    • Yang, Y.1    Maret, W.2    Vallee, B.L.3
  • 175
    • 0037146612 scopus 로고    scopus 로고
    • Nitric oxide causes apparent release of zinc from presynaptic boutons
    • Frederickson, C. J., Cuajungco, M. P., LaBuda, C. J. & Suh, S. W. Nitric oxide causes apparent release of zinc from presynaptic boutons. Neuroscience 115, 471-474 (2002).
    • (2002) Neuroscience , vol.115 , pp. 471-474
    • Frederickson, C.J.1    Cuajungco, M.P.2    LaBuda, C.J.3    Suh, S.W.4
  • 176
    • 0036436238 scopus 로고    scopus 로고
    • The role of NADPH oxidase and neuronal nitric oxide synthase in zinc-induced poly (ADP-ribose) polymerase activation and cell death in cortical culture
    • Kim, Y. H. & Koh, J. Y. The role of NADPH oxidase and neuronal nitric oxide synthase in zinc-induced poly (ADP-ribose) polymerase activation and cell death in cortical culture. Exp. Neurol. 177, 407-418 (2002).
    • (2002) Exp. Neurol. , vol.177 , pp. 407-418
    • Kim, Y.H.1    Koh, J.Y.2
  • 177
    • 0033598713 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase is a mediator of necrotic cell death by ATP depletion
    • Ha, H. C. & Snyder, S. H. Poly(ADP-ribose) polymerase is a mediator of necrotic cell death by ATP depletion. Proc. Natl Acad. Sci. USA 96, 13978-13982 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13978-13982
    • Ha, H.C.1    Snyder, S.H.2
  • 178
    • 0032127666 scopus 로고    scopus 로고
    • Role of poly(ADP-ribose) synthetase in inflammation and ischaemia-reperfusion
    • Szabo, C. & Dawson, V. L. Role of poly(ADP-ribose) synthetase in inflammation and ischaemia-reperfusion. Trends Pharmacol. Sci. 19, 287-298 (1998).
    • (1998) Trends Pharmacol. Sci. , vol.19 , pp. 287-298
    • Szabo, C.1    Dawson, V.L.2
  • 179
    • 0141816712 scopus 로고    scopus 로고
    • Involvement of poly ADP ribosyl polymerase-1 in acute but not chronic zinc toxicity
    • Sheline, C. T., Wang, H., Cai, A.-L., Dawson, V. L. & Choi, D. W. Involvement of poly ADP ribosyl polymerase-1 in acute but not chronic zinc toxicity. Eur. J. Neurosci. 18, 1402-1409 (2003).
    • (2003) Eur. J. Neurosci. , vol.18 , pp. 1402-1409
    • Sheline, C.T.1    Wang, H.2    Cai, A.-L.3    Dawson, V.L.4    Choi, D.W.5
  • 180
    • 0021077610 scopus 로고
    • Senile dementia of the Alzheimer type
    • Terry, R. D. & Katzman, R. Senile dementia of the Alzheimer type. Ann. Neurol. 14, 497-506 (1983).
    • (1983) Ann. Neurol. , vol.14 , pp. 497-506
    • Terry, R.D.1    Katzman, R.2
  • 181
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner, G. G. & Wong, C. W. Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem. Biophys. Res. Commun. 120, 885-890 (1984).
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 182
    • 0012510759 scopus 로고
    • Amyloid plaque core protein in Alzheimer disease and Down syndrome
    • Masters, C. L. et al. Amyloid plaque core protein in Alzheimer disease and Down syndrome. Proc. Natl Acad. Sci. USA 82, 4245-449 (1985).
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 4245-4449
    • Masters, C.L.1
  • 183
    • 0028180196 scopus 로고
    • Modulation of A β adhesiveness and secretase site cleavage by zinc
    • Bush, A. I., Pettingell, W. H. Jr, Paradis, M. D. & Tanzi, R. E. Modulation of A β adhesiveness and secretase site cleavage by zinc. J. Biol. Chem. 269, 12152-12158 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 12152-12158
    • Bush, A.I.1    Pettingell Jr., W.H.2    Paradis, M.D.3    Tanzi, R.E.4
  • 184
    • 0027980901 scopus 로고
    • Rapid induction of Alzheimer A β amyloid formation by zinc
    • Bush, A. I. et al. Rapid induction of Alzheimer A β amyloid formation by zinc. Science 265, 1464-1467 (1994). First report that amyloid-β specifically and saturably binds and is precipitated by zinc.
    • (1994) Science , vol.265 , pp. 1464-1467
    • Bush, A.I.1
  • 185
    • 18444399243 scopus 로고    scopus 로고
    • Treatment of Alzheimer's disease with clioquinol
    • Regland, B. et al. Treatment of Alzheimer's disease with clioquinol. Dement. Geriatr. Cogn. Disord. 12, 408-414 (2001).
    • (2001) Dement. Geriatr. Cogn. Disord. , vol.12 , pp. 408-414
    • Regland, B.1
  • 186
    • 10744224267 scopus 로고    scopus 로고
    • Metal-protein attenuation win iodochlorhydroxyquin (clioquinol) targeting Aβ amyloid deposition and toxicity in Alzheimer disease: A pilot phase 2 clinical trial
    • Ritchie, C. W. et al. Metal-protein attenuation win iodochlorhydroxyquin (clioquinol) targeting Aβ amyloid deposition and toxicity in Alzheimer disease: a pilot phase 2 clinical trial. Arch. Neurci. 60, 1685-1691 (2003).
    • (2003) Arch. Neurci. , vol.60 , pp. 1685-1691
    • Ritchie, C.W.1
  • 187
    • 0028171064 scopus 로고
    • The amyloid β-protein precursor and its mammalian homologues. Evidence for a zinc-modulated heparin-binding superfamily
    • Bush, A. I., Pettingell, W. H. Jr, de Paradis, M., Tanzi, R. E. & Wasco, W. The amyloid β-protein precursor and its mammalian homologues. Evidence for a zinc-modulated heparin-binding superfamily. J. Biol. Chem. 269, 26618-26621 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 26618-26621
    • Bush, A.I.1    Pettingell Jr., W.H.2    De Paradis, M.3    Tanzi, R.E.4    Wasco, W.5
  • 188
    • 0027220686 scopus 로고
    • A novel zinc(II) binding site modulates the function of the β A4 amyloid protein precursor of Alzheimer's disease
    • Bush, A. I. et al. A novel zinc(II) binding site modulates the function of the β A4 amyloid protein precursor of Alzheimer's disease. J. Biol. Chem. 268, 16109-16112 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 16109-16112
    • Bush, A.I.1
  • 189
    • 0027984643 scopus 로고
    • Interaction between the zinc (II) and the heparin binding site of the Alzheimer's disease β A4 amyloid precursor protein (APP)
    • Multhaup, G., Bush, A. I., Pollwein, P. & Masters, C. L. Interaction between the zinc (II) and the heparin binding site of the Alzheimer's disease β A4 amyloid precursor protein (APP). FEBS Lett. 355, 151-154 (1994).
    • (1994) FEBS Lett. , vol.355 , pp. 151-154
    • Multhaup, G.1    Bush, A.I.2    Pollwein, P.3    Masters, C.L.4
  • 190
    • 0032546577 scopus 로고    scopus 로고
    • Copper-binding amyloid precursor protein undergoes a site-specific fragmentation in the reduction of hydrogen peroxide
    • Multhaup, G. et al. Copper-binding amyloid precursor protein undergoes a site-specific fragmentation in the reduction of hydrogen peroxide. Biochemistry 37, 7224-7230 (1998).
    • (1998) Biochemistry , vol.37 , pp. 7224-7230
    • Multhaup, G.1
  • 191
    • 0033587478 scopus 로고    scopus 로고
    • Histidine-13 is a crucial residue in the zinc ion-induced aggregation of the A β peptide of Alzheimer's disease
    • Liu, S. T., Howlett, G. & Barrow, C. J. Histidine-13 is a crucial residue in the zinc ion-induced aggregation of the A β peptide of Alzheimer's disease. Biochemistry 38, 9373-9378 (1999).
    • (1999) Biochemistry , vol.38 , pp. 9373-9378
    • Liu, S.T.1    Howlett, G.2    Barrow, C.J.3
  • 192
    • 0025295039 scopus 로고
    • Cleavage of amyloid β peptide during constitutive processing of its precursor
    • Esch, F. S. et al. Cleavage of amyloid β peptide during constitutive processing of its precursor. Science 248, 1122-1124 (1990).
    • (1990) Science , vol.248 , pp. 1122-1124
    • Esch, F.S.1
  • 193
    • 0030704680 scopus 로고    scopus 로고
    • Zinc-induced Alzheimer's Aβ1-40 aggregation is mediated by conformational factors
    • Huang, X. et al. Zinc-induced Alzheimer's Aβ1-40 aggregation is mediated by conformational factors. J. Biol. Chem. 272, 26464-26470 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 26464-26470
    • Huang, X.1
  • 194
    • 0032557425 scopus 로고    scopus 로고
    • Dramatic aggregation of Alzheimer Aβ by Cu(II) is induced by conditions representing physiological acidosis
    • Atwood, C. S. et al. Dramatic aggregation of Alzheimer Aβ by Cu(II) is induced by conditions representing physiological acidosis. J. Biol. Chem. 273, 12817-12826 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 12817-12826
    • Atwood, C.S.1
  • 197
    • 0346106076 scopus 로고    scopus 로고
    • Metal binding and oxidation of amyloid-β within isolated senile plaque cores: Raman microscopic evidence
    • Dong, J. et al. Metal binding and oxidation of amyloid-β within isolated senile plaque cores: Raman microscopic evidence. Biochemistry 42, 2768-2773 (2003).
    • (2003) Biochemistry , vol.42 , pp. 2768-2773
    • Dong, J.1
  • 198
    • 0033844944 scopus 로고    scopus 로고
    • Characterization of copper interactions with Alzheimer amyloid β peptides: Identification of an attomolar-affinity copper binding site on amyloid β1-42
    • Atwood, C. S. et al. Characterization of copper interactions with Alzheimer amyloid β peptides: identification of an attomolar-affinity copper binding site on amyloid β1-42. J. Neurochem. 75, 1219-1233 (2000).
    • (2000) J. Neurochem. , vol.75 , pp. 1219-1233
    • Atwood, C.S.1
  • 199
    • 0033232709 scopus 로고    scopus 로고
    • The Alzheimer's disease amyloid precursor protein modulates copper-induced toxicity and oxidative stress in primary neuronal cultures
    • White, A. R. et al. The Alzheimer's disease amyloid precursor protein modulates copper-induced toxicity and oxidative stress in primary neuronal cultures. J. Neurosci. 19, 9170-9179 (1999).
    • (1999) J. Neurosci. , vol.19 , pp. 9170-9179
    • White, A.R.1
  • 200
    • 0031981072 scopus 로고    scopus 로고
    • Amyloid-β deposition in Alzheimer transgenic mice is associated with oxidative stress
    • Smith, M. A. et al. Amyloid-β deposition in Alzheimer transgenic mice is associated with oxidative stress. J. Neurochem. 70, 2212-2215 (1998).
    • (1998) J. Neurochem. , vol.70 , pp. 2212-2215
    • Smith, M.A.1
  • 202
    • 5444235015 scopus 로고    scopus 로고
    • Gene knockout of amyloid precursor protein and amyloid precursor-like protein-2 increases cellular copper levels in primary mouse cortical neurons and embryonic flbroblasts
    • Bellingham, S. A. et al. Gene knockout of amyloid precursor protein and amyloid precursor-like protein-2 increases cellular copper levels in primary mouse cortical neurons and embryonic flbroblasts. J. Neurochem. 91, 423-428 (2004).
    • (2004) J. Neurochem. , vol.91 , pp. 423-428
    • Bellingham, S.A.1
  • 203
    • 0037160028 scopus 로고    scopus 로고
    • Overexpression of Alzheimer's disease amyloid-β opposes the age-dependent elevations of brain copper and iron
    • Maynard, C. J. et al. Overexpression of Alzheimer's disease amyloid-β opposes the age-dependent elevations of brain copper and iron. J. Biol. Chem. 277, 44670-44676 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 44670-44676
    • Maynard, C.J.1
  • 204
    • 0037386086 scopus 로고    scopus 로고
    • The metallobiology of Alzheimer's disease
    • Bush, A. I. The metallobiology of Alzheimer's disease. Trends Neurosci. 26, 207-214 (2003).
    • (2003) Trends Neurosci. , vol.26 , pp. 207-214
    • Bush, A.I.1
  • 205
    • 0033601338 scopus 로고    scopus 로고
    • Cu(II) potentiation of Alzheimer Aβ neurotoxidty. Correlation with cell-free hydrogen peroxide production and metal reduction
    • Huang, X. et al. Cu(II) potentiation of Alzheimer Aβ neurotoxidty. Correlation with cell-free hydrogen peroxide production and metal reduction. J. Biol. Chem. 274, 37111-37116 (1999). Genetic ablation of ZnT3 decreases vessel wall amyloid-β deposition in an APP transgenic mouse model of Alzheimer's disease.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37111-37116
    • Huang, X.1
  • 206
    • 18344414746 scopus 로고    scopus 로고
    • The A β peptide of Alzheimer's disease directly produces hydrogen peroxide through metal ion reduction
    • Huang, X. et al. The A β peptide of Alzheimer's disease directly produces hydrogen peroxide through metal ion reduction. Biochemistry 38, 7609-7616 (1999).
    • (1999) Biochemistry , vol.38 , pp. 7609-7616
    • Huang, X.1
  • 207
    • 0035865905 scopus 로고    scopus 로고
    • Redox-active iron mediates amyloid-β toxicity
    • Rottkamp, C. A. et al. Redox-active iron mediates amyloid-β toxicity. Free Radic. Biol. Med. 30, 447-450 (2001).
    • (2001) Free Radic. Biol. Med. , vol.30 , pp. 447-450
    • Rottkamp, C.A.1
  • 208
    • 0001052504 scopus 로고    scopus 로고
    • Copper catalyzed oxidation of Alzheimer Aβ
    • Atwood, C. S. et al. Copper catalyzed oxidation of Alzheimer Aβ. Cell Mol. Biol. (Noisy-le-grand) 46, 777-783 (2000).
    • (2000) Cell Mol. Biol. (Noisy-le-grand) , vol.46 , pp. 777-783
    • Atwood, C.S.1
  • 209
    • 9144235443 scopus 로고    scopus 로고
    • Copper mediates dityrosine cross-linking of Alzheimer's amyloid-β
    • Atwood, C. S. et al. Copper mediates dityrosine cross-linking of Alzheimer's amyloid-β. Biochemistry 43, 560-568 (2004).
    • (2004) Biochemistry , vol.43 , pp. 560-568
    • Atwood, C.S.1
  • 210
    • 0242290357 scopus 로고    scopus 로고
    • Neurotoxic, redox-competent Alzheimer's β-amyloid is released from lipid membrane by methionine oxidation
    • Barnham, K. J. et al. Neurotoxic, redox-competent Alzheimer's β-amyloid is released from lipid membrane by methionine oxidation. J. Biol. Chem. 278, 42959-42965 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 42959-42965
    • Barnham, K.J.1
  • 211
    • 0032590054 scopus 로고    scopus 로고
    • Soluble pool of Aβ amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease
    • McLean, C. A. et al. Soluble pool of Aβ amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease. Ann. Neurol. 46, 860-866 (1996).
    • (1996) Ann. Neurol. , vol.46 , pp. 860-866
    • McLean, C.A.1
  • 212
    • 0033551782 scopus 로고    scopus 로고
    • Aqueous dissolution of Alzheimer's disease Aβ amyloid deposits by biometal depletion
    • Cherny, R. A. et al. Aqueous dissolution of Alzheimer's disease Aβ amyloid deposits by biometal depletion. J. Biol. Chem. 274, 23223-23228 (1999). Amyloid-β causes toxicity by producing hydrogen peroxide catalytically on binding copper ions.
    • (1999) J. Biol. Chem. , vol.274 , pp. 23223-23228
    • Cherny, R.A.1
  • 213
    • 0034746895 scopus 로고    scopus 로고
    • Oxidation of Aβ and plaque biogenesis in Alzheimer's disease and Down syndrome
    • Head, E. et al. Oxidation of Aβ and plaque biogenesis in Alzheimer's disease and Down syndrome. Neurobiol. Dis. 8, 792-806 (2001).
    • (2001) Neurobiol. Dis. , vol.8 , pp. 792-806
    • Head, E.1
  • 214
    • 0035874024 scopus 로고    scopus 로고
    • New evidence that the Alzheimer β-amyloid peptide does not spontaneously form free radicals: An ESR study using a series of spin-traps
    • Turnbull, S., Tabner, B. J., El Agnaf, O. M., Twyman, L. J. & Allsop, D. New evidence that the Alzheimer β-amyloid peptide does not spontaneously form free radicals: an ESR study using a series of spin-traps. Free Radic. Biol. Med. 30, 1154-1162 (2001).
    • (2001) Free Radic. Biol. Med. , vol.30 , pp. 1154-1162
    • Turnbull, S.1    Tabner, B.J.2    El Agnaf, O.M.3    Twyman, L.J.4    Allsop, D.5
  • 215
    • 0028807137 scopus 로고
    • Brain regional correspondence between Alzheimer's disease histopathology and biomarkers of protein oxidation
    • Hensley, K. et al. Brain regional correspondence between Alzheimer's disease histopathology and biomarkers of protein oxidation. J. Neurochem. 65, 2146-2156 (1995).
    • (1995) J. Neurochem. , vol.65 , pp. 2146-2156
    • Hensley, K.1
  • 216
    • 0037188530 scopus 로고    scopus 로고
    • Contribution by synaptic zinc to the gender-disparate plaque formation in human Swedish mutant APP transgenic mice
    • Lee, J. Y., Cole, T. B., Palmiter, R. D., Suh, S. W. & Koh, J. Y. Contribution by synaptic zinc to the gender-disparate plaque formation in human Swedish mutant APP transgenic mice. Proc. Natl Acad. Sci. USA 99, 7705-7710 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7705-7710
    • Lee, J.Y.1    Cole, T.B.2    Palmiter, R.D.3    Suh, S.W.4    Koh, J.Y.5
  • 217
    • 1842506368 scopus 로고    scopus 로고
    • Neuronal zinc exchange with the blood vessel wall promotes cerebral amyloid angiopathy in an animal model of Alzheimer's disease
    • Friedlich, A. L. et al. Neuronal zinc exchange with the blood vessel wall promotes cerebral amyloid angiopathy in an animal model of Alzheimer's disease. J. Neurosci. 24, 3453-3459 (2004). The precipitation of amyloid-β in the post-mortem brain tissue of patients with Alzheimer's disease is reversible with zinc chelation.
    • (2004) J. Neurosci. , vol.24 , pp. 3453-3459
    • Friedlich, A.L.1
  • 218
    • 0028138473 scopus 로고
    • Metallothionein in amyotrophic lateral sclerosis
    • Sillevis Smitt, P. A. et al. Metallothionein in amyotrophic lateral sclerosis. Biol. Signals 3, 193-197 (1994).
    • (1994) Biol. Signals , vol.3 , pp. 193-197
    • Sillevis Smitt, P.A.1
  • 219
    • 0026781415 scopus 로고
    • Metallothionein immunoreactivity is increased in the spinal cord of patients with amyotrophic lateral sclerosis
    • Sillevis Smitt, P. A., Blaauwgeers, H. G., Troost, D. & de Jong, J. M. Metallothionein immunoreactivity is increased in the spinal cord of patients with amyotrophic lateral sclerosis. Neurosci. Lett. 144, 107-110 (1992).
    • (1992) Neurosci. Lett. , vol.144 , pp. 107-110
    • Sillevis Smitt, P.A.1    Blaauwgeers, H.G.2    Troost, D.3    De Jong, J.M.4
  • 220
    • 15844393658 scopus 로고    scopus 로고
    • Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury
    • Reaume, A. G. et al. Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury. Nature Genet. 13, 43-47 (1996).
    • (1996) Nature Genet. , vol.13 , pp. 43-47
    • Reaume, A.G.1
  • 221
    • 0031572869 scopus 로고    scopus 로고
    • Superoxide-dependent peroxidase activity of H48Q: A auperoxide dismutase variant associated with familial amyotrophic lateral sclerosis
    • Liochev, S. I., Chen, L. L., Hallewell, R. A. & Fridovich, I. Superoxide-dependent peroxidase activity of H48Q: a auperoxide dismutase variant associated with familial amyotrophic lateral sclerosis. Arch. Biochem. Biophys. 346, 263-268 (1997).
    • (1997) Arch. Biochem. Biophys. , vol.346 , pp. 263-268
    • Liochev, S.I.1    Chen, L.L.2    Hallewell, R.A.3    Fridovich, I.4
  • 223
    • 0037081444 scopus 로고    scopus 로고
    • In vivo peroxidative activity of FALS-mutant human CuZnSODs expressed in yeast
    • Roe, J. A. et al. In vivo peroxidative activity of FALS-mutant human CuZnSODs expressed in yeast. Free Radic. Biol. Med. 32, 169-174 (2002).
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 169-174
    • Roe, J.A.1
  • 224
    • 0039251419 scopus 로고    scopus 로고
    • Induction of nitric oxide-dependent apoptosis in motor neurons by zinc-deficient superoxide dismutase
    • Estevez, A. G. et al. Induction of nitric oxide-dependent apoptosis in motor neurons by zinc-deficient superoxide dismutase. Science 286, 2498-2500 (1999).
    • (1999) Science , vol.286 , pp. 2498-2500
    • Estevez, A.G.1
  • 225
    • 0011392304 scopus 로고    scopus 로고
    • Metallothionein expression is altered in a transgenic murine model of familial amyotrophic lateral sclerosis
    • Gong, Y. H. & Elliott, J. L. Metallothionein expression is altered in a transgenic murine model of familial amyotrophic lateral sclerosis. Exp. Neurol. 162, 27-36 (2000).
    • (2000) Exp. Neurol. , vol.162 , pp. 27-36
    • Gong, Y.H.1    Elliott, J.L.2
  • 226
    • 0035058876 scopus 로고    scopus 로고
    • Reduction of metallothioneins promotes the disease expression of familial amyotrophic lateral sclerosis mice in a dose-dependent manner
    • Nagano, S. et al. Reduction of metallothioneins promotes the disease expression of familial amyotrophic lateral sclerosis mice in a dose-dependent manner. Eur. J. Neurosci. 13, 1363-1370 (2001).
    • (2001) Eur. J. Neurosci. , vol.13 , pp. 1363-1370
    • Nagano, S.1
  • 227
    • 0037109771 scopus 로고    scopus 로고
    • Disease progression in a transgenic model of familial amyotrophic lateral sclerosis is dependent on both neuronal and non-neuronal zinc binding proteins
    • Puttaparthi, K. et al. Disease progression in a transgenic model of familial amyotrophic lateral sclerosis is dependent on both neuronal and non-neuronal zinc binding proteins. J. Neurosci. 22, 8790-8796 (2002).
    • (2002) J. Neurosci. , vol.22 , pp. 8790-8796
    • Puttaparthi, K.1
  • 229
    • 4644238758 scopus 로고    scopus 로고
    • The lipophilic metal chelator DP-109 reduces amyloid pathology in brains of human β-amyloid precursor protein transgenic mice
    • Lee, J. Y., Friedman, J. E., Angel, I., Kozak, A. & Koh, J. Y. The lipophilic metal chelator DP-109 reduces amyloid pathology in brains of human β-amyloid precursor protein transgenic mice. Neurobiol. Aging 25, 1315-1321 (2004).
    • (2004) Neurobiol. Aging , vol.25 , pp. 1315-1321
    • Lee, J.Y.1    Friedman, J.E.2    Angel, I.3    Kozak, A.4    Koh, J.Y.5
  • 230
    • 2442596245 scopus 로고    scopus 로고
    • Evaluation of safety and changes in the NIH stroke scale, Rankin, and Barthel scores following DP-b99 administration in acute stroke patients
    • Rosenberg, G., Angel, I., Kozak, A., Rehovot, I. & Schneider, D. Evaluation of safety and changes in the NIH stroke scale, Rankin, and Barthel scores following DP-b99 administration in acute stroke patients. Stroke 35, 338 (2004).
    • (2004) Stroke , vol.35 , pp. 338
    • Rosenberg, G.1    Angel, I.2    Kozak, A.3    Rehovot, I.4    Schneider, D.5
  • 231
    • 0036015024 scopus 로고    scopus 로고
    • Pyruvate blocks zinc-induced neurotoxicity in immortalized hypothalamic neurons
    • Kawahara, M., Kato-Negishi, M. & Kuroda, Y. Pyruvate blocks zinc-induced neurotoxicity in immortalized hypothalamic neurons. Cell. Mol. Neurobiol. 22, 87-93 (2002).
    • (2002) Cell. Mol. Neurobiol. , vol.22 , pp. 87-93
    • Kawahara, M.1    Kato-Negishi, M.2    Kuroda, Y.3
  • 232
    • 0842325221 scopus 로고    scopus 로고
    • Pyruvate limits zinc-induced rat oligodendrocyte progenitor cell death
    • Kelland, E. E., Kelly, M. D. & Toms, N. J. Pyruvate limits zinc-induced rat oligodendrocyte progenitor cell death. Eur. J. Neurosci. 19, 287-294 (2004).
    • (2004) Eur. J. Neurosci. , vol.19 , pp. 287-294
    • Kelland, E.E.1    Kelly, M.D.2    Toms, N.J.3
  • 233
    • 0035888871 scopus 로고    scopus 로고
    • Protection by pyruvate against transient forebrain ischemia in rats
    • Lee, J. Y., Kim, Y. H. & Koh, J. Y. Protection by pyruvate against transient forebrain ischemia in rats. J. Neurosci. 21, RC171 (2001).
    • (2001) J. Neurosci. , vol.21
    • Lee, J.Y.1    Kim, Y.H.2    Koh, J.Y.3
  • 234
    • 0032738998 scopus 로고    scopus 로고
    • Antioxidative properties of pyruvate and protection of the ischemic rat heart during cardioplegia
    • Dobsak, P. & Courderot-Masuyer, C. Antioxidative properties of pyruvate and protection of the ischemic rat heart during cardioplegia. J. Cardiovasc. Pharmacol. 34, 651-659 (1999).
    • (1999) J. Cardiovasc. Pharmacol. , vol.34 , pp. 651-659
    • Dobsak, P.1    Courderot-Masuyer, C.2
  • 236
    • 0035845652 scopus 로고    scopus 로고
    • Advances in intravenous thrombolytic therapy for treatment of acute stroke
    • Albers, G. W. Advances in intravenous thrombolytic therapy for treatment of acute stroke. Neurology 57, S77-S81 (2001).
    • (2001) Neurology , vol.57
    • Albers, G.W.1
  • 237
    • 0029857469 scopus 로고    scopus 로고
    • Neuronal cell death and tPA63
    • Tsirka, S. E., Rogove, A. D. & Strickland, S. Neuronal cell death and tPA63. Nature 384, 123-124 (1996).
    • (1996) Nature , vol.384 , pp. 123-124
    • Tsirka, S.E.1    Rogove, A.D.2    Strickland, S.3
  • 238
    • 0033597411 scopus 로고    scopus 로고
    • Nonproteolytic neuroprotection by human recombinant tissue plasminogen actwator
    • Kim, Y. H., Park, J. H., Hong, S. H. & Koh, J. Y. Nonproteolytic neuroprotection by human recombinant tissue plasminogen actwator. Science 284, 647-650 (1999).
    • (1999) Science , vol.284 , pp. 647-650
    • Kim, Y.H.1    Park, J.H.2    Hong, S.H.3    Koh, J.Y.4
  • 239
    • 1242271323 scopus 로고    scopus 로고
    • Modulation of zinc toxicity by tissue plasminogen actuator
    • Siddiq, M. M. & Tsirka, S. E. Modulation of zinc toxicity by tissue plasminogen actuator. Mol. Cell. Neurosci. 25, 162-171 (2004).
    • (2004) Mol. Cell. Neurosci. , vol.25 , pp. 162-171
    • Siddiq, M.M.1    Tsirka, S.E.2
  • 240
    • 0033981982 scopus 로고    scopus 로고
    • The concept of transmitter receptors: 100 Years on
    • Bennett, M. R. The concept of transmitter receptors: 100 years on. Neuropharmacology 39, 523-546 (2000).
    • (2000) Neuropharmacology , vol.39 , pp. 523-546
    • Bennett, M.R.1
  • 241
    • 77049149364 scopus 로고
    • The effect of inhibitory nerve impulses on a crustacean muscle fibre
    • Fatt, P. & Katz, B. The effect of inhibitory nerve impulses on a crustacean muscle fibre. J. Physiol. (Lond.) 121, 374-389 (1953).
    • (1953) J. Physiol. (Lond.) , vol.121 , pp. 374-389
    • Fatt, P.1    Katz, B.2
  • 242
    • 0026460797 scopus 로고
    • A new twist in the brain-gut axis
    • Whitcomb, D. C. & Taylor, I. L. A new twist in the brain-gut axis. Am. J. Med. Sci. 304, 334-338 (1992).
    • (1992) Am. J. Med. Sci. , vol.304 , pp. 334-338
    • Whitcomb, D.C.1    Taylor, I.L.2
  • 243
    • 0007535551 scopus 로고
    • Action catalytique des venins des serpents sur les acids nucleiques
    • Delezenne, C. & Morel, H. Action catalytique des venins des serpents sur les acids nucleiques. Cr. Acad. Sci. 244-246 (1919).
    • (1919) Cr. Acad. Sci. , pp. 244-246
    • Delezenne, C.1    Morel, H.2
  • 244
    • 0023105267 scopus 로고
    • Zinc-containing 7S-NGF complex. Evidence from zinc histochemistry for localization in salivary secretory granules
    • Frederickson, C. J., Perez-Clausell, J. & Danscher, G. Zinc-containing 7S-NGF complex. Evidence from zinc histochemistry for localization in salivary secretory granules. J. Histochem. Cytochem. 35, 579-583 (1987).
    • (1987) J. Histochem. Cytochem. , vol.35 , pp. 579-583
    • Frederickson, C.J.1    Perez-Clausell, J.2    Danscher, G.3
  • 246
    • 0030989421 scopus 로고    scopus 로고
    • Ultrastructural localization of zinc ions in the rat prostate: An autometallographic study
    • Sorensen, M. B., Stoltenberg, M., Juhl, S., Danscher, G. & Ernst, E. Ultrastructural localization of zinc ions in the rat prostate: an autometallographic study. Prostate 31, 125-130 (1997).
    • (1997) Prostate , vol.31 , pp. 125-130
    • Sorensen, M.B.1    Stoltenberg, M.2    Juhl, S.3    Danscher, G.4    Ernst, E.5
  • 247
    • 0014461463 scopus 로고
    • Submicroscopic heavy metal localization in the prosecreta of the Paneth cells of the mouse
    • Translation
    • Muller, A. & Geyer, G. Submicroscopic heavy metal localization in the prosecreta of the Paneth cells of the mouse. (Translation) Gegenbaurs. Morphol. Jahrb. 113, 70-77 (1969).
    • (1969) Gegenbaurs. Morphol. Jahrb. , vol.113 , pp. 70-77
    • Muller, A.1    Geyer, G.2
  • 248
    • 0014184654 scopus 로고
    • Heavy metals in rat mast cell granules
    • Gustafson, G. T. Heavy metals in rat mast cell granules. Lab. Invest. 17, 588-598 (1967).
    • (1967) Lab. Invest. , vol.17 , pp. 588-598
    • Gustafson, G.T.1
  • 249
    • 18144438401 scopus 로고
    • Diagnostic value of selective cytochemical reaction to zinc in peripheral blood granulocytes
    • Translation
    • Gol'dberg, E. D., Bovt, V. D. & Eshchenko, V. A. Diagnostic value of selective cytochemical reaction to zinc in peripheral blood granulocytes. (Translation) Klin. Lab Diagn. 25-27 (1993).
    • (1993) Klin. Lab Diagn. , pp. 25-27
    • Gol'dberg, E.D.1    Bovt, V.D.2    Eshchenko, V.A.3
  • 250
    • 0028506240 scopus 로고
    • The cytochemical dithizone reaction of the blood granulocytes in zinc-deficient states
    • Translation
    • Ieshchenko, V. A., Bovt, V. D., Skoliboh, S. O. & Volovyk, M. V. The cytochemical dithizone reaction of the blood granulocytes in zinc-deficient states. (Translation) Lik. Sprava. 86-88 (1994).
    • (1994) Lik. Sprava. , pp. 86-88
    • Ieshchenko, V.A.1    Bovt, V.D.2    Skoliboh, S.O.3    Volovyk, M.V.4
  • 251
    • 0023149918 scopus 로고
    • Zinc in the anterior pituitary of rat: A histochemical and analytical work
    • Thorlacius-Ussing, O. Zinc in the anterior pituitary of rat: a histochemical and analytical work. Neuroendocrinology 45, 233-242 (1987).
    • (1987) Neuroendocrinology , vol.45 , pp. 233-242
    • Thorlacius-Ussing, O.1
  • 252
    • 0014163030 scopus 로고
    • Electron microscopical localization of the zinc in hippocampal mossy fibre synapses by a modified sulfide silver procedure
    • Haug, F. M. Electron microscopical localization of the zinc in hippocampal mossy fibre synapses by a modified sulfide silver procedure. Histochemie 8, 355-368 (1967).
    • (1967) Histochemie , vol.8 , pp. 355-368
    • Haug, F.M.1
  • 253
    • 4444358048 scopus 로고    scopus 로고
    • Method for identifying neuronal cells suffering zinc toxicity by use of a novel fluorescent sensor
    • Frederickson, C. J. et al. Method for identifying neuronal cells suffering zinc toxicity by use of a novel fluorescent sensor. J. Neurosci. Methods 139, 79-89 (2004).
    • (2004) J. Neurosci. Methods , vol.139 , pp. 79-89
    • Frederickson, C.J.1
  • 254
    • 0033556370 scopus 로고    scopus 로고
    • Zinc modulation of AMPA receptors may be relevant to splice variants in carp retina
    • Shen, Y. & Yang, X. L. Zinc modulation of AMPA receptors may be relevant to splice variants in carp retina. Neurosci. Lett. 259, 177-180 (1999).
    • (1999) Neurosci. Lett. , vol.259 , pp. 177-180
    • Shen, Y.1    Yang, X.L.2
  • 255
    • 0035839170 scopus 로고    scopus 로고
    • Synaptically-released zinc inhibits N-methyl-D-aspartate receptor activation at recurrent mossy fiber synapses
    • Molnar, P. & Nadler, J. V. Synaptically-released zinc inhibits N-methyl-D-aspartate receptor activation at recurrent mossy fiber synapses. Brain Res. 910, 205-207 (2001).
    • (2001) Brain Res. , vol.910 , pp. 205-207
    • Molnar, P.1    Nadler, J.V.2
  • 256
    • 0034945186 scopus 로고    scopus 로고
    • Zinc inhibition of group I mGluR-mediated calcium homeostasis in auditory neurons
    • Zirpel, L. & Parks, T. N. Zinc inhibition of group I mGluR-mediated calcium homeostasis in auditory neurons. J. Assoc. Res. Otolaryngol. 2, 180-187 (2001).
    • (2001) J. Assoc. Res. Otolaryngol. , vol.2 , pp. 180-187
    • Zirpel, L.1    Parks, T.N.2
  • 259
    • 0027071673 scopus 로고
    • Ionic zinc may function as an endogenous ligand for the haloperidol-sensitive sigma 2 receptor in rat brain
    • Connor, M. A. & Chavkin, C. Ionic zinc may function as an endogenous ligand for the haloperidol-sensitive sigma 2 receptor in rat brain. Mol. Pharmacol. 42, 471-479 (1992).
    • (1992) Mol. Pharmacol. , vol.42 , pp. 471-479
    • Connor, M.A.1    Chavkin, C.2
  • 260
    • 0027971908 scopus 로고
    • Oocytes from Xenopus laevis contain an intrinsic sigma 2-like binding site
    • Patterson, T. A., Connor, M., Appleyard, S. M. & Chavkin, C. Oocytes from Xenopus laevis contain an intrinsic sigma 2-like binding site. Neurosci. Lett. 180, 159-162 (1994).
    • (1994) Neurosci. Lett. , vol.180 , pp. 159-162
    • Patterson, T.A.1    Connor, M.2    Appleyard, S.M.3    Chavkin, C.4
  • 261
  • 262
    • 0346259943 scopus 로고    scopus 로고
    • Metal ion-mediated agonism and agonist enhancement in melanocortin MC1 and MC4 receptors
    • Holst, B., Elling, C. E. & Schwartz, T. W. Metal ion-mediated agonism and agonist enhancement in melanocortin MC1 and MC4 receptors. J. Biol. Chem. 277, 47662-47670 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 47662-47670
    • Holst, B.1    Elling, C.E.2    Schwartz, T.W.3
  • 263
    • 0025356149 scopus 로고
    • Modulation of mu, delta and kappa opioid receptors in rat brain by metal ions and histidine
    • Tejwani, G. A. & Hanissian, S. H. Modulation of mu, delta and kappa opioid receptors in rat brain by metal ions and histidine. Neuropharmacology 29, 445-452 (1990).
    • (1990) Neuropharmacology , vol.29 , pp. 445-452
    • Tejwani, G.A.1    Hanissian, S.H.2
  • 265
    • 0032875714 scopus 로고    scopus 로고
    • Zinc modulation of ionic currents in the horizontal limb of the diagonal band of Broca
    • Easaw, J. C., Jassar, B. S., Harris, K. H. & Jhamandas, J. H. Zinc modulation of ionic currents in the horizontal limb of the diagonal band of Broca. Neuroscience 94, 785-795 (1999).
    • (1999) Neuroscience , vol.94 , pp. 785-795
    • Easaw, J.C.1    Jassar, B.S.2    Harris, K.H.3    Jhamandas, J.H.4
  • 266
    • 0023269150 scopus 로고
    • Batrachotoxin-modified sodium channels in planar lipid bilayers. Characterization of saxitoxin- and tetrodotoxin-induced channel closures
    • Green, W. N., Weiss, L. B. & Andersen, O. S. Batrachotoxin-modified sodium channels in planar lipid bilayers. Characterization of saxitoxin- and tetrodotoxin-induced channel closures. J. Gen. Physiol. 89, 873-903 (1987).
    • (1987) J. Gen. Physiol. , vol.89 , pp. 873-903
    • Green, W.N.1    Weiss, L.B.2    Andersen, O.S.3
  • 267
    • 0033825706 scopus 로고    scopus 로고
    • - channel in rat choroid plexus: Regulation by intra cellular messengers and inhibition by divalent cations
    • - channel in rat choroid plexus: regulation by intracellular messengers and inhibition by divalent cations. Pflugers Arch. 440, 933-940 (2000).
    • (2000) Pflugers Arch. , vol.440 , pp. 933-940
    • Kajita, H.1    Whitwell, C.2    Brown, P.D.3
  • 268
    • 0033600590 scopus 로고    scopus 로고
    • 2+-sensitive channel in reconstituted lipid vesicles
    • 2+-sensitive channel in reconstituted lipid vesicles. Biochemistry 38, 11189-11196 (1999).
    • (1999) Biochemistry , vol.38 , pp. 11189-11196
    • Lin, H.1    Zhu, Y.J.2    Lal, R.3
  • 269
    • 0032518972 scopus 로고    scopus 로고
    • Modulation by zinc of the glutamate transporters in glial cells and cones isolated from the tiger salamander retina
    • Spiridon, M., Kamm, D., Billups, B., Mobbs, P. & Attwell, D. Modulation by zinc of the glutamate transporters in glial cells and cones isolated from the tiger salamander retina. J. Physiol. (Lond.) 506, 363-376 (1998).
    • (1998) J. Physiol. (Lond.) , vol.506 , pp. 363-376
    • Spiridon, M.1    Kamm, D.2    Billups, B.3    Mobbs, P.4    Attwell, D.5
  • 270
    • 0030611085 scopus 로고    scopus 로고
    • 3H]WIN 35,428 binding to the human dopamine transporter in a similar fashion
    • 3H]WIN 35,428 binding to the human dopamine transporter in a similar fashion. J. Neurochem. 69, 1106-1118 (1997).
    • (1997) J. Neurochem. , vol.69 , pp. 1106-1118
    • Wu, Q.1    Coffey, L.L.2    Reith, M.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.