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Volumn 7, Issue 10, 2012, Pages 1636-1640

New sensors for quantitative measurement of mitochondrial Zn 2+sup

Author keywords

[No Author keywords available]

Indexed keywords

ZINC; CYTOCHROME C OXIDASE;

EID: 84867812919     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb300171p     Document Type: Article
Times cited : (87)

References (32)
  • 1
    • 0034056797 scopus 로고    scopus 로고
    • Human zinc deficiency
    • Hambidge, M. (2000) Human zinc deficiency J. Nutr. 130, 1344S-1349S
    • (2000) J. Nutr. , vol.130
    • Hambidge, M.1
  • 2
    • 67650050211 scopus 로고    scopus 로고
    • Mammalian zinc transporters: Nutritional and physiologic regulation
    • Lichten, L. A. and Cousins, R. (2009) Mammalian zinc transporters: Nutritional and physiologic regulation Annu. Rev. Nutr. 29, 153-176
    • (2009) Annu. Rev. Nutr. , vol.29 , pp. 153-176
    • Lichten, L.A.1    Cousins, R.2
  • 3
    • 77952566927 scopus 로고    scopus 로고
    • Cytosolic zinc buffering and muffling: Their role in intracellular zinc homeostasis
    • Colvin, R., Holmes, W., Fontaine, C., and Maret, W. (2010) Cytosolic zinc buffering and muffling: Their role in intracellular zinc homeostasis Metallomics 2, 306
    • (2010) Metallomics , vol.2 , pp. 306
    • Colvin, R.1    Holmes, W.2    Fontaine, C.3    Maret, W.4
  • 4
    • 33751223540 scopus 로고    scopus 로고
    • Zinc-buffering capacity of a eukaryotic cell at physiological pZn
    • Krezel, A. and Maret, W. (2006) Zinc-buffering capacity of a eukaryotic cell at physiological pZn J. Biol. Inorg. Chem. 11, 1049-1062
    • (2006) J. Biol. Inorg. Chem. , vol.11 , pp. 1049-1062
    • Krezel, A.1    Maret, W.2
  • 6
    • 0033788519 scopus 로고    scopus 로고
    • Induction of neuronal apoptosis by thiol oxidation: Putative role of intracellular zinc release
    • Aizenman, E., Stout, A. K., Hartnett, K. A., Dineley, K. E., McLaughlin, B., and Reynolds, I. J. (2000) Induction of neuronal apoptosis by thiol oxidation: putative role of intracellular zinc release J. Neurochem. 75, 1878-1888
    • (2000) J. Neurochem. , vol.75 , pp. 1878-1888
    • Aizenman, E.1    Stout, A.K.2    Hartnett, K.A.3    Dineley, K.E.4    McLaughlin, B.5    Reynolds, I.J.6
  • 8
    • 0035861677 scopus 로고    scopus 로고
    • Zn(2+) induces permeability transition pore opening and release of pro-apoptotic peptides from neuronal mitochondria
    • Jiang, D., Sullivan, P. G., Sensi, S. L., Steward, O., and Weiss, J. H. (2001) Zn(2+) induces permeability transition pore opening and release of pro-apoptotic peptides from neuronal mitochondria J. Biol. Chem. 276, 47524-47529
    • (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
  • 9
    • 0038637993 scopus 로고    scopus 로고
    • Zinc inhibition of cellular energy production: Implications for mitochondria and neurodegeneration
    • Dineley, K., Votyakova, T., and Reynolds, I. (2003) Zinc inhibition of cellular energy production: implications for mitochondria and neurodegeneration J. Neurochem. 85, 563-570
    • (2003) J. Neurochem. , vol.85 , pp. 563-570
    • Dineley, K.1    Votyakova, T.2    Reynolds, I.3
  • 10
    • 13344259905 scopus 로고    scopus 로고
    • Zinc causes loss of membrane potential and elevates reactive oxygen species in rat brain mitochondria
    • Dineley, K., Richards, L. L., Votyakova, T., and Reynolds, I. (2005) Zinc causes loss of membrane potential and elevates reactive oxygen species in rat brain mitochondria Mitochondrion 5, 55-65
    • (2005) Mitochondrion , vol.5 , pp. 55-65
    • Dineley, K.1    Richards, L.L.2    Votyakova, T.3    Reynolds, I.4
  • 11
    • 26844509261 scopus 로고    scopus 로고
    • Zn2+ inhibits mitochondrial movement in neurons by phosphatidylinositol 3-kinase activation
    • Malaiyandi, L., Honick, A. S., Rintoul, G., Wang, Q. J., and Reynolds, I. (2005) Zn2+ inhibits mitochondrial movement in neurons by phosphatidylinositol 3-kinase activation J. Neurosci. 25, 9507-9514
    • (2005) J. Neurosci. , vol.25 , pp. 9507-9514
    • Malaiyandi, L.1    Honick, A.S.2    Rintoul, G.3    Wang, Q.J.4    Reynolds, I.5
  • 12
    • 59649092943 scopus 로고    scopus 로고
    • Intracellular Zn2+ accumulation contributes to synaptic failure, mitochondrial depolarization, and cell death in an acute slice oxygen-glucose deprivation model of ischemia
    • Medvedeva, Y., Lin, B., Shuttleworth, C., and Weiss, J. (2009) Intracellular Zn2+ accumulation contributes to synaptic failure, mitochondrial depolarization, and cell death in an acute slice oxygen-glucose deprivation model of ischemia J. Neurosci. 29, 1105-1114
    • (2009) J. Neurosci. , vol.29 , pp. 1105-1114
    • Medvedeva, Y.1    Lin, B.2    Shuttleworth, C.3    Weiss, J.4
  • 13
    • 33745952665 scopus 로고    scopus 로고
    • Mitochondrial trafficking to synapses in cultured primary cortical neurons
    • Chang, D. T., Honick, A. S., and Reynolds, I. J. (2006) Mitochondrial trafficking to synapses in cultured primary cortical neurons J. Neurosci. 26, 7035-7045
    • (2006) J. Neurosci. , vol.26 , pp. 7035-7045
    • Chang, D.T.1    Honick, A.S.2    Reynolds, I.J.3
  • 14
    • 67650257938 scopus 로고    scopus 로고
    • Genetically encoded sensors to elucidate spatial distribution of cellular zinc
    • Dittmer, P., Miranda, J., Gorski, J., and Palmer, A. (2009) Genetically encoded sensors to elucidate spatial distribution of cellular zinc J. Biol. Chem. 284, 16289-16297
    • (2009) J. Biol. Chem. , vol.284 , pp. 16289-16297
    • Dittmer, P.1    Miranda, J.2    Gorski, J.3    Palmer, A.4
  • 18
    • 20144370934 scopus 로고    scopus 로고
    • Direct visualization of mitochondrial zinc accumulation reveals uniporter-dependent and -independent transport mechanisms
    • Malaiyandi, L., Vergun, O., Dineley, K., and Reynolds, I. (2005) Direct visualization of mitochondrial zinc accumulation reveals uniporter-dependent and -independent transport mechanisms J. Neurochem. 93, 1242-1250
    • (2005) J. Neurochem. , vol.93 , pp. 1242-1250
    • Malaiyandi, L.1    Vergun, O.2    Dineley, K.3    Reynolds, I.4
  • 20
    • 56749177293 scopus 로고    scopus 로고
    • Organelle-specific zinc detection using zinpyr-labeled fusion proteins in live cells
    • Tomat, E., Nolan, E. M., Jaworski, J., and Lippard, S. J. (2008) Organelle-specific zinc detection using zinpyr-labeled fusion proteins in live cells J. Am. Chem. Soc. 130, 15776-15777
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 15776-15777
    • Tomat, E.1    Nolan, E.M.2    Jaworski, J.3    Lippard, S.J.4
  • 23
    • 79956297378 scopus 로고    scopus 로고
    • Measuring steady-state and dynamic endoplasmic reticulum and Golgi Zn2+ with genetically encoded sensors
    • Qin, Y., Dittmer, P. J., Park, J. G., Jansen, K. B., and Palmer, A. (2011) Measuring steady-state and dynamic endoplasmic reticulum and Golgi Zn2+ with genetically encoded sensors Proc. Natl. Acad. Sci. U.S.A. 108, 7351-7356
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 7351-7356
    • Qin, Y.1    Dittmer, P.J.2    Park, J.G.3    Jansen, K.B.4    Palmer, A.5
  • 24
    • 3242706582 scopus 로고    scopus 로고
    • Expanded dynamic range of fluorescent indicators for Ca(2+) by circularly permuted yellow fluorescent proteins
    • Nagai, T., Yamada, S., Tominaga, T., Ichikawa, M., and Miyawaki, A. (2004) Expanded dynamic range of fluorescent indicators for Ca(2+) by circularly permuted yellow fluorescent proteins Proc. Natl. Acad. Sci. U.S.A. 101, 10554-10559
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 10554-10559
    • Nagai, T.1    Yamada, S.2    Tominaga, T.3    Ichikawa, M.4    Miyawaki, A.5
  • 26
  • 27
    • 79959870658 scopus 로고    scopus 로고
    • Imaging intracellular pH in live cells with a genetically encoded red fluorescent protein sensor
    • Tantama, M., Hung, Y. P., and Yellen, G. (2011) Imaging intracellular pH in live cells with a genetically encoded red fluorescent protein sensor J. Am. Chem. Soc. 133, 10034-10037
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 10034-10037
    • Tantama, M.1    Hung, Y.P.2    Yellen, G.3
  • 28
    • 0037328645 scopus 로고    scopus 로고
    • In situ assay of the intramitochondrial enzymes: Use of alamethicin for permeabilization of mitochondria
    • Gostimskaya, I. S., Grivennikova, V. G., Zharova, T. V., Bakeeva, L. E., and Vinogradov, A. D. (2003) In situ assay of the intramitochondrial enzymes: use of alamethicin for permeabilization of mitochondria Anal. Biochem. 313, 46-52
    • (2003) Anal. Biochem. , vol.313 , pp. 46-52
    • Gostimskaya, I.S.1    Grivennikova, V.G.2    Zharova, T.V.3    Bakeeva, L.E.4    Vinogradov, A.D.5
  • 29
    • 84855724443 scopus 로고    scopus 로고
    • Mapping the zinc-transporting system in mammary cells: Molecular analysis reveals a phenotype-dependent zinc-transporting network during lactation
    • Kelleher, S., Velasquez, V., Croxford, T. P., McCormick, N. H., Lopez, V., and MacDavid, J. (2012) Mapping the zinc-transporting system in mammary cells: molecular analysis reveals a phenotype-dependent zinc-transporting network during lactation J. Cell Physiol. 227, 1761-1770
    • (2012) J. Cell Physiol. , vol.227 , pp. 1761-1770
    • Kelleher, S.1    Velasquez, V.2    Croxford, T.P.3    McCormick, N.H.4    Lopez, V.5    MacDavid, J.6
  • 30
    • 77956214419 scopus 로고    scopus 로고
    • X-Ray fluorescence microscopy reveals accumulation and secretion of discrete intracellular zinc pools in the lactating mouse mammary gland
    • Mccormick, N., Velasquez, V., Finney, L., Vogt, S., and Kelleher, S. (2010) X-Ray fluorescence microscopy reveals accumulation and secretion of discrete intracellular zinc pools in the lactating mouse mammary gland PLoS ONE 5, e11078
    • (2010) PLoS ONE , vol.5 , pp. 11078
    • McCormick, N.1    Velasquez, V.2    Finney, L.3    Vogt, S.4    Kelleher, S.5
  • 31
    • 0036765589 scopus 로고    scopus 로고
    • A reevaluation of neuronal zinc measurements: Artifacts associated with high intracellular dye concentration
    • Dineley, K., Malaiyandi, L., and Reynolds, I. (2002) A reevaluation of neuronal zinc measurements: artifacts associated with high intracellular dye concentration Mol. Pharmacol. 62, 618-627
    • (2002) Mol. Pharmacol. , vol.62 , pp. 618-627
    • Dineley, K.1    Malaiyandi, L.2    Reynolds, I.3
  • 32
    • 48949104251 scopus 로고    scopus 로고
    • The integration of glutathione homeostasis and redox signaling
    • Meyer, A. J. (2008) The integration of glutathione homeostasis and redox signaling J. Plant Physiol. 165, 1390-1403
    • (2008) J. Plant Physiol. , vol.165 , pp. 1390-1403
    • Meyer, A.J.1


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