메뉴 건너뛰기




Volumn 17, Issue 2, 2013, Pages 129-136

Chelators for investigating zinc metalloneurochemistry

Author keywords

[No Author keywords available]

Indexed keywords

4 [[2 (BIS PYRIDIN 2 YLMETHYLAMINO)ETHYLAMINO]METHYL]PHENYL]METHANESULFONIC ACID; AMPA RECEPTOR; CHELATING AGENT; EDETIC ACID; EGTAZIC ACID; ETHYLENE GLYCOL 1,2 BIS(2 AMINOPHENYL) ETHER N,N,N',N' TETRAACETIC ACID; ETHYLENEDIAMINE N,N' DIACETIC N,N' DI BETA PROPIONIC ACID; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE PHOSPHATASE; N,N,N',N' TETRAKIS(2 PYRIDYLMETHYL) ETHYLENEDIAMINE; UNCLASSIFIED DRUG; ZINC ION;

EID: 84876716446     PISSN: 13675931     EISSN: 18790402     Source Type: Journal    
DOI: 10.1016/j.cbpa.2013.01.009     Document Type: Review
Times cited : (71)

References (59)
  • 2
    • 79959404630 scopus 로고    scopus 로고
    • Biochemistry of mobile zinc and nitric oxide revealed by fluorescent sensors
    • Pluth M.D., Tomat E., Lippard S.J. Biochemistry of mobile zinc and nitric oxide revealed by fluorescent sensors. Annu Rev Biochem 2011, 80:333-355.
    • (2011) Annu Rev Biochem , vol.80 , pp. 333-355
    • Pluth, M.D.1    Tomat, E.2    Lippard, S.J.3
  • 3
    • 79951557273 scopus 로고    scopus 로고
    • Zinc is decreased in prostate cancer: an established relationship of prostate cancer!
    • Costello L.C., Franklin R.B. Zinc is decreased in prostate cancer: an established relationship of prostate cancer!. J Biol Inorg Chem 2011, 16:3-8.
    • (2011) J Biol Inorg Chem , vol.16 , pp. 3-8
    • Costello, L.C.1    Franklin, R.B.2
  • 4
    • 84862306310 scopus 로고    scopus 로고
    • Zinc in specialized secretory tissues: roles in the pancreas, prostate, and mammary gland
    • Kelleher S.L., McCormick N.H., Velasquez V., Lopez V. Zinc in specialized secretory tissues: roles in the pancreas, prostate, and mammary gland. Adv Nutr 2011, 2:101-111.
    • (2011) Adv Nutr , vol.2 , pp. 101-111
    • Kelleher, S.L.1    McCormick, N.H.2    Velasquez, V.3    Lopez, V.4
  • 5
    • 77952566927 scopus 로고    scopus 로고
    • Cytosolic zinc buffering and muffling: their role in intracellular zinc homeostasis
    • Colvin R.A., Holmes W.R., Fontaine C.P., Maret W. Cytosolic zinc buffering and muffling: their role in intracellular zinc homeostasis. Metallomics 2010, 2:306-317.
    • (2010) Metallomics , vol.2 , pp. 306-317
    • Colvin, R.A.1    Holmes, W.R.2    Fontaine, C.P.3    Maret, W.4
  • 7
    • 84864310728 scopus 로고    scopus 로고
    • Visualizing metal ions in cells: an overview of analytical techniques, approaches, and probes
    • Dean K.M., Qin Y., Palmer A.E. Visualizing metal ions in cells: an overview of analytical techniques, approaches, and probes. Biochim Biophys Acta 2012, 1823:1406-1415.
    • (2012) Biochim Biophys Acta , vol.1823 , pp. 1406-1415
    • Dean, K.M.1    Qin, Y.2    Palmer, A.E.3
  • 8
    • 48849094488 scopus 로고    scopus 로고
    • Is zinc a neuromodulator?
    • Kay A.R., Toth K. Is zinc a neuromodulator?. Sci Signal 2008, 1:re3.
    • (2008) Sci Signal , vol.1
    • Kay, A.R.1    Toth, K.2
  • 10
    • 0037388116 scopus 로고    scopus 로고
    • Meeting of the minds: metalloneurochemistry
    • Burdette S.C., Lippard S.J. Meeting of the minds: metalloneurochemistry. Proc Natl Acad Sci U S A 2003, 100:3605-3610.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 3605-3610
    • Burdette, S.C.1    Lippard, S.J.2
  • 11
    • 79960504449 scopus 로고    scopus 로고
    • Zinc in neurotransmission
    • Toth K. Zinc in neurotransmission. Annu Rev Nutr 2011, 31:139-153.
    • (2011) Annu Rev Nutr , vol.31 , pp. 139-153
    • Toth, K.1
  • 12
    • 27644593831 scopus 로고    scopus 로고
    • Synaptic plasticity at hippocampal mossy fibre synapses
    • Nicoll R.A., Schmitz D. Synaptic plasticity at hippocampal mossy fibre synapses. Nat Rev Neurosci 2005, 6:863-876.
    • (2005) Nat Rev Neurosci , vol.6 , pp. 863-876
    • Nicoll, R.A.1    Schmitz, D.2
  • 13
    • 0021866385 scopus 로고
    • Intravesicular localization of zinc in rat telencephalic boutons. A histochemical study
    • Perez-Clausell J., Danscher G. Intravesicular localization of zinc in rat telencephalic boutons. A histochemical study. Brain Res 1985, 337:91-98.
    • (1985) Brain Res , vol.337 , pp. 91-98
    • Perez-Clausell, J.1    Danscher, G.2
  • 15
    • 0033574071 scopus 로고    scopus 로고
    • Elimination of zinc from synaptic vesicles in the intact mouse brain by disruption of the ZnT3 gene
    • Cole T.B., Wenzel H.J., Kafer K.E., Schwartzkroin P.A., Palmiter R.D. Elimination of zinc from synaptic vesicles in the intact mouse brain by disruption of the ZnT3 gene. Proc Natl Acad Sci U S A 1999, 96:1716-1721.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 1716-1721
    • Cole, T.B.1    Wenzel, H.J.2    Kafer, K.E.3    Schwartzkroin, P.A.4    Palmiter, R.D.5
  • 16
    • 19444371698 scopus 로고    scopus 로고
    • Vglut1 and ZnT3 co-targeting mechanisms regulate vesicular zinc stores in PC12 cells
    • Salazar G., Craige B., Love R., Kalman D., Faundez V. Vglut1 and ZnT3 co-targeting mechanisms regulate vesicular zinc stores in PC12 cells. J Cell Sci 2005, 118:1911-1921.
    • (2005) J Cell Sci , vol.118 , pp. 1911-1921
    • Salazar, G.1    Craige, B.2    Love, R.3    Kalman, D.4    Faundez, V.5
  • 17
    • 0033578855 scopus 로고    scopus 로고
    • Long-term potentiation - a decade of progress?
    • Malenka R.C., Nicoll R.A. Long-term potentiation - a decade of progress?. Science 1999, 285:1870-1874.
    • (1999) Science , vol.285 , pp. 1870-1874
    • Malenka, R.C.1    Nicoll, R.A.2
  • 18
    • 0035830711 scopus 로고    scopus 로고
    • Removing zinc from synaptic vesicles does not impair spatial learning, memory, or sensorimotor functions in the mouse
    • Cole T.B., Martyanova A., Palmiter R.D. Removing zinc from synaptic vesicles does not impair spatial learning, memory, or sensorimotor functions in the mouse. Brain Res 2001, 891:253-265.
    • (2001) Brain Res , vol.891 , pp. 253-265
    • Cole, T.B.1    Martyanova, A.2    Palmiter, R.D.3
  • 19
    • 0037439069 scopus 로고    scopus 로고
    • Lack of vesicular zinc in synaptic excitability of mossy fibers does not affect CA3 pyramidal cells in zinc transporter 3 knockout mice
    • Lopantsev V., Wenzel H.J., Cole T.B., Palmiter R.D., Schwartzkroin P.A. Lack of vesicular zinc in synaptic excitability of mossy fibers does not affect CA3 pyramidal cells in zinc transporter 3 knockout mice. Neuroscience 2003, 116:237-248.
    • (2003) Neuroscience , vol.116 , pp. 237-248
    • Lopantsev, V.1    Wenzel, H.J.2    Cole, T.B.3    Palmiter, R.D.4    Schwartzkroin, P.A.5
  • 21
    • 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 2003, 23:6847-6855.
    • (2003) J Neurosci , vol.23 , pp. 6847-6855
    • Kay, A.R.1
  • 22
    • 78649482651 scopus 로고    scopus 로고
    • Zinc is externalized rather than released during synaptic transmission
    • Nydegger I., Rumschik S.M., Kay A.R. Zinc is externalized rather than released during synaptic transmission. ACS Chem Neurosci 2010, 1:728-736.
    • (2010) ACS Chem Neurosci , vol.1 , pp. 728-736
    • Nydegger, I.1    Rumschik, S.M.2    Kay, A.R.3
  • 23
    • 84867628280 scopus 로고    scopus 로고
    • Evidence for an extracellular zinc-veneer in rodent brains from experiments with Zn-ionophores and ZnT3 knockouts
    • Nydegger I., Rumschik S.M., Zhao J.F., Kay A.R. Evidence for an extracellular zinc-veneer in rodent brains from experiments with Zn-ionophores and ZnT3 knockouts. ACS Chem Neurosci 2012, 3:761-766.
    • (2012) ACS Chem Neurosci , vol.3 , pp. 761-766
    • Nydegger, I.1    Rumschik, S.M.2    Zhao, J.F.3    Kay, A.R.4
  • 24
    • 78649547075 scopus 로고    scopus 로고
    • Zinc transporter 3 is involved in learned fear and extinction, but not in innate fear
    • Martel G., Hevi C., Friebely O., Baybutt T., Shumyatsky G.P. Zinc transporter 3 is involved in learned fear and extinction, but not in innate fear. Learn Mem 2010, 17:582-590.
    • (2010) Learn Mem , vol.17 , pp. 582-590
    • Martel, G.1    Hevi, C.2    Friebely, O.3    Baybutt, T.4    Shumyatsky, G.P.5
  • 25
    • 76149093866 scopus 로고    scopus 로고
    • Cognitive loss in zinc transporter-3 knock-out mice: a phenocopy for the synaptic and memory deficits of Alzheimer's disease?
    • Adlard P.A., Parncutt J.M., Finkelstein D.I., Bush A.I. Cognitive loss in zinc transporter-3 knock-out mice: a phenocopy for the synaptic and memory deficits of Alzheimer's disease?. J Neurosci 2010, 30:1631-1636.
    • (2010) J Neurosci , vol.30 , pp. 1631-1636
    • Adlard, P.A.1    Parncutt, J.M.2    Finkelstein, D.I.3    Bush, A.I.4
  • 26
    • 79958005264 scopus 로고    scopus 로고
    • Zinc transporter ZnT3 is involved in memory dependent on the hippocampus and perirhinal cortex
    • Martel G., Hevi C., Kane-Goldsmith N., Shumyatsky G.P. Zinc transporter ZnT3 is involved in memory dependent on the hippocampus and perirhinal cortex. Behav Brain Res 2011, 223:233-238.
    • (2011) Behav Brain Res , vol.223 , pp. 233-238
    • Martel, G.1    Hevi, C.2    Kane-Goldsmith, N.3    Shumyatsky, G.P.4
  • 28
    • 84863393278 scopus 로고    scopus 로고
    • Picomolar concentrations of free zinc(II) ions regulate receptor protein-tyrosine phosphatase beta activity
    • Wilson M., Hogstrand C., Maret W. Picomolar concentrations of free zinc(II) ions regulate receptor protein-tyrosine phosphatase beta activity. J Biol Chem 2012, 287:9322-9326.
    • (2012) J Biol Chem , vol.287 , pp. 9322-9326
    • Wilson, M.1    Hogstrand, C.2    Maret, W.3
  • 29
    • 0034517709 scopus 로고    scopus 로고
    • Molecular organization of a zinc binding N-terminal modulatory domain in a NMDA receptor subunit
    • Paoletti P., Perin-Dureau F., Fayyazuddin A., Le Goff A., Callebaut I., Neyton J. Molecular organization of a zinc binding N-terminal modulatory domain in a NMDA receptor subunit. Neuron 2000, 28:911-925.
    • (2000) Neuron , vol.28 , pp. 911-925
    • Paoletti, P.1    Perin-Dureau, F.2    Fayyazuddin, A.3    Le Goff, A.4    Callebaut, I.5    Neyton, J.6
  • 30
    • 72449151659 scopus 로고    scopus 로고
    • Structure of the zinc-bound amino-terminal domain of the NMDA receptor NR2B subunit
    • Karakas E., Simorowski N., Furukawa H. Structure of the zinc-bound amino-terminal domain of the NMDA receptor NR2B subunit. EMBO J 2009, 28:3910-3920.
    • (2009) EMBO J , vol.28 , pp. 3910-3920
    • Karakas, E.1    Simorowski, N.2    Furukawa, H.3
  • 31
    • 39449099067 scopus 로고    scopus 로고
    • Zinc-mediated transactivation of TrkB potentiates the hippocampal mossy fiber-CA3 pyramid synapse
    • Huang Y.Z., Pan E., Xiong Z.Q., McNamara J.O. Zinc-mediated transactivation of TrkB potentiates the hippocampal mossy fiber-CA3 pyramid synapse. Neuron 2008, 57:546-558.
    • (2008) Neuron , vol.57 , pp. 546-558
    • Huang, Y.Z.1    Pan, E.2    Xiong, Z.Q.3    McNamara, J.O.4
  • 32
    • 84868117570 scopus 로고    scopus 로고
    • Neuroprotective effects of reactive oxygen species mediated by BDNF-independent activation of TrkB
    • Huang Y.Z., McNamara J.O. Neuroprotective effects of reactive oxygen species mediated by BDNF-independent activation of TrkB. J Neurosci 2012, 32:15521-15532.
    • (2012) J Neurosci , vol.32 , pp. 15521-15532
    • Huang, Y.Z.1    McNamara, J.O.2
  • 33
    • 84868660479 scopus 로고    scopus 로고
    • Zinc potentiates GluK3 glutamate receptor function by stabilizing the ligand binding domain dimer interface
    • Veran J., Kumar J., Pinheiro P.S., Athane A., Mayer M.L., Perrais D., Mulle C. Zinc potentiates GluK3 glutamate receptor function by stabilizing the ligand binding domain dimer interface. Neuron 2012, 76:565-578.
    • (2012) Neuron , vol.76 , pp. 565-578
    • Veran, J.1    Kumar, J.2    Pinheiro, P.S.3    Athane, A.4    Mayer, M.L.5    Perrais, D.6    Mulle, C.7
  • 37
    • 63849207439 scopus 로고    scopus 로고
    • Synaptically released zinc triggers metabotropic signaling via a zinc-sensing receptor in the hippocampus
    • Besser L., Chorin E., Sekler I., Silverman W.F., Atkin S., Russell J.T., Hershfinkel M. Synaptically released zinc triggers metabotropic signaling via a zinc-sensing receptor in the hippocampus. J Neurosci 2009, 29:2890-2901.
    • (2009) J Neurosci , vol.29 , pp. 2890-2901
    • Besser, L.1    Chorin, E.2    Sekler, I.3    Silverman, W.F.4    Atkin, S.5    Russell, J.T.6    Hershfinkel, M.7
  • 38
    • 79952744484 scopus 로고    scopus 로고
    • Zinc transporter ZnT-3 regulates presynaptic Erk1/2 signaling and hippocampus-dependent memory
    • Sindreu C., Palmiter R.D., Storm D.R. Zinc transporter ZnT-3 regulates presynaptic Erk1/2 signaling and hippocampus-dependent memory. Proc Natl Acad Sci U S A 2011, 108:3366-3370.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 3366-3370
    • Sindreu, C.1    Palmiter, R.D.2    Storm, D.R.3
  • 39
    • 80053111747 scopus 로고    scopus 로고
    • Vesicular zinc promotes presynaptic and inhibits postsynaptic long-term potentiation of mossy fiber-CA3 synapse
    • Pan E., Zhang X.A., Huang Z., Krezel A., Zhao M., Tinberg C.E., Lippard S.J., McNamara J.O. Vesicular zinc promotes presynaptic and inhibits postsynaptic long-term potentiation of mossy fiber-CA3 synapse. Neuron 2011, 71:1116-1126.
    • (2011) Neuron , vol.71 , pp. 1116-1126
    • Pan, E.1    Zhang, X.A.2    Huang, Z.3    Krezel, A.4    Zhao, M.5    Tinberg, C.E.6    Lippard, S.J.7    McNamara, J.O.8
  • 40
    • 33845287306 scopus 로고    scopus 로고
    • Zinspy sensors with enhanced dynamic range for imaging neuronal cell zinc uptake and mobilization
    • Nolan E.M., Ryu J.W., Jaworski J., Feazell R.P., Sheng M., Lippard S.J. Zinspy sensors with enhanced dynamic range for imaging neuronal cell zinc uptake and mobilization. J Am Chem Soc 2006, 128:15517-15528.
    • (2006) J Am Chem Soc , vol.128 , pp. 15517-15528
    • Nolan, E.M.1    Ryu, J.W.2    Jaworski, J.3    Feazell, R.P.4    Sheng, M.5    Lippard, S.J.6
  • 41
    • 0345114077 scopus 로고
    • Hard and soft acids and bases
    • Pearson R.G. Hard and soft acids and bases. J Am Chem Soc 1963, 85:3533.
    • (1963) J Am Chem Soc , vol.85 , pp. 3533
    • Pearson, R.G.1
  • 42
    • 0034688987 scopus 로고    scopus 로고
    • Kinetics and mechanism of copper(II) complex formation with tripodal aminopolythiaether and aminopolypyridyl ligands in aqueous solution
    • Ambundo E.A., Deydier M.V., Ochrymowycz L.A., Rorabacher D.B. Kinetics and mechanism of copper(II) complex formation with tripodal aminopolythiaether and aminopolypyridyl ligands in aqueous solution. Inorg Chem 2000, 39:1171-1179.
    • (2000) Inorg Chem , vol.39 , pp. 1171-1179
    • Ambundo, E.A.1    Deydier, M.V.2    Ochrymowycz, L.A.3    Rorabacher, D.B.4
  • 45
    • 0033617578 scopus 로고    scopus 로고
    • 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., O'Halloran T.V. Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase. Science 1999, 284:805-808.
    • (1999) Science , vol.284 , pp. 805-808
    • Rae, T.D.1    Schmidt, P.J.2    Pufahl, R.A.3    Culotta, V.C.4    O'Halloran, T.V.5
  • 46
    • 34948868783 scopus 로고    scopus 로고
    • 2+ chelators cause " dying-back" neurite degeneration associated with energy impairment
    • 2+ chelators cause " dying-back" neurite degeneration associated with energy impairment. J Neurosci Res 2007, 85:2844-2855.
    • (2007) J Neurosci Res , vol.85 , pp. 2844-2855
    • Yang, Y.1    Kawataki, T.2    Fukui, K.3    Koike, T.4
  • 47
    • 84858671513 scopus 로고    scopus 로고
    • Reaction of metal-binding ligands with the zinc proteome: zinc sensors and N,N,N',N'-tetrakis(2-pyridylmethyl)ethylenediamine
    • Meeusen J.W., Nowakowski A., Petering D.H. Reaction of metal-binding ligands with the zinc proteome: zinc sensors and N,N,N',N'-tetrakis(2-pyridylmethyl)ethylenediamine. Inorg Chem 2012, 51:3625-3632.
    • (2012) Inorg Chem , vol.51 , pp. 3625-3632
    • Meeusen, J.W.1    Nowakowski, A.2    Petering, D.H.3
  • 49
    • 54049144212 scopus 로고    scopus 로고
    • Zinc chelation induces rapid depletion of the X-linked inhibitor of apoptosis and sensitizes prostate cancer cells to TRAIL-mediated apoptosis
    • Makhov P., Golovine K., Uzzo R.G., Rothman J., Crispen P.L., Shaw T., Scoll B.J., Kolenko V.M. Zinc chelation induces rapid depletion of the X-linked inhibitor of apoptosis and sensitizes prostate cancer cells to TRAIL-mediated apoptosis. Cell Death Differ 2008, 15:1745-1751.
    • (2008) Cell Death Differ , vol.15 , pp. 1745-1751
    • Makhov, P.1    Golovine, K.2    Uzzo, R.G.3    Rothman, J.4    Crispen, P.L.5    Shaw, T.6    Scoll, B.J.7    Kolenko, V.M.8
  • 50
    • 84855805416 scopus 로고    scopus 로고
    • Zinc pyrithione induces ERK- and PKC-dependent necrosis distinct from TPEN-induced apoptosis in prostate cancer cells
    • Carraway R.E., Dobner P.R. Zinc pyrithione induces ERK- and PKC-dependent necrosis distinct from TPEN-induced apoptosis in prostate cancer cells. Biochim Biophys Acta 2012, 1823:544-557.
    • (2012) Biochim Biophys Acta , vol.1823 , pp. 544-557
    • Carraway, R.E.1    Dobner, P.R.2
  • 51
    • 77149144132 scopus 로고    scopus 로고
    • Minding metals: tailoring multifunctional chelating agents for neurodegenerative disease
    • Perez L.R., Franz K.J. Minding metals: tailoring multifunctional chelating agents for neurodegenerative disease. Dalton Trans 2010, 39:2177-2187.
    • (2010) Dalton Trans , vol.39 , pp. 2177-2187
    • Perez, L.R.1    Franz, K.J.2
  • 53
    • 57649130599 scopus 로고    scopus 로고
    • Sequestration of copper from beta-amyloid promotes selective lysis by cyclen-hybrid cleavage agents
    • Wu W.H., Lei P., Liu Q., Hu J., Gunn A.P., Chen M.S., Rui Y.F., Su X.Y., Xie Z.P., Zhao Y.F., et al. Sequestration of copper from beta-amyloid promotes selective lysis by cyclen-hybrid cleavage agents. J Biol Chem 2008, 283:31657-31664.
    • (2008) J Biol Chem , vol.283 , pp. 31657-31664
    • Wu, W.H.1    Lei, P.2    Liu, Q.3    Hu, J.4    Gunn, A.P.5    Chen, M.S.6    Rui, Y.F.7    Su, X.Y.8    Xie, Z.P.9    Zhao, Y.F.10
  • 55
    • 12444311699 scopus 로고    scopus 로고
    • Design and synthesis of zinc-selective chelators for extracellular applications
    • Kawabata E., Kikuchi K., Urano Y., Kojima H., Odani A., Nagano T. Design and synthesis of zinc-selective chelators for extracellular applications. J Am Chem Soc 2005, 127:818-819.
    • (2005) J Am Chem Soc , vol.127 , pp. 818-819
    • Kawabata, E.1    Kikuchi, K.2    Urano, Y.3    Kojima, H.4    Odani, A.5    Nagano, T.6
  • 56
    • 0029777299 scopus 로고    scopus 로고
    • 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. The role of zinc in selective neuronal death after transient global cerebral ischemia. Science 1996, 272:1013-1016.
    • (1996) Science , vol.272 , pp. 1013-1016
    • Koh, J.Y.1    Suh, S.W.2    Gwag, B.J.3    He, Y.Y.4    Hsu, C.Y.5    Choi, D.W.6
  • 57
    • 40949143947 scopus 로고    scopus 로고
    • A reversible pH-dependent intramolecular pyridine-aldehyde cyclization
    • Zhang X.A., Song D., Lippard S.J. A reversible pH-dependent intramolecular pyridine-aldehyde cyclization. J Org Chem 2008, 73:734-737.
    • (2008) J Org Chem , vol.73 , pp. 734-737
    • Zhang, X.A.1    Song, D.2    Lippard, S.J.3
  • 58
    • 44849102395 scopus 로고    scopus 로고
    • Metals in neurobiology: probing their chemistry and biology with molecular imaging
    • Que E.L., Domaille D.W., Chang C.J. Metals in neurobiology: probing their chemistry and biology with molecular imaging. Chem Rev 2008, 108:1517-1549.
    • (2008) Chem Rev , vol.108 , pp. 1517-1549
    • Que, E.L.1    Domaille, D.W.2    Chang, C.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.