메뉴 건너뛰기




Volumn 8, Issue 10, 2013, Pages

Cooperative Functions of ZnT1, Metallothionein and ZnT4 in the Cytoplasm Are Required for Full Activation of TNAP in the Early Secretory Pathway

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINE PHOSPHATASE; METALLOTHIONEIN; TISSUE NONSPECIFIC ALKALINE PHOSPHATASE; UNCLASSIFIED DRUG; ZINC; ZINC TRANSPORTER; ZINC TRANSPORTER 4; ZINC TRANSPORTER 5;

EID: 84885738104     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0077445     Document Type: Article
Times cited : (33)

References (51)
  • 1
    • 0027394031 scopus 로고
    • The biochemical basis of zinc physiology
    • Vallee BL, Falchuk KH, (1993) The biochemical basis of zinc physiology. Physiol Rev 73: 79-118.
    • (1993) Physiol Rev , vol.73 , pp. 79-118
    • Vallee, B.L.1    Falchuk, K.H.2
  • 2
    • 84861979200 scopus 로고    scopus 로고
    • New perspectives of zinc coordination environments in proteins
    • Maret W, (2012) New perspectives of zinc coordination environments in proteins. J Inorg Biochem 111: 110-116.
    • (2012) J Inorg Biochem , vol.111 , pp. 110-116
    • Maret, W.1
  • 3
    • 30744471169 scopus 로고    scopus 로고
    • Counting the zinc-proteins encoded in the human genome
    • Andreini C, Banci L, Bertini I, Rosato A, (2006) Counting the zinc-proteins encoded in the human genome. J Proteome Res 5: 196-201.
    • (2006) J Proteome Res , vol.5 , pp. 196-201
    • Andreini, C.1    Banci, L.2    Bertini, I.3    Rosato, A.4
  • 4
    • 80054737086 scopus 로고    scopus 로고
    • Minimal functional sites allow a classification of zinc sites in proteins
    • Andreini C, Bertini I, Cavallaro G, (2011) Minimal functional sites allow a classification of zinc sites in proteins. PLoS One 6: e26325.
    • (2011) PLoS One , vol.6
    • Andreini, C.1    Bertini, I.2    Cavallaro, G.3
  • 5
    • 70350680995 scopus 로고    scopus 로고
    • Coordination dynamics of zinc in proteins
    • Maret W, Li Y, (2009) Coordination dynamics of zinc in proteins. Chem Rev 109: 4682-4707.
    • (2009) Chem Rev , vol.109 , pp. 4682-4707
    • Maret, W.1    Li, Y.2
  • 6
    • 80755153625 scopus 로고    scopus 로고
    • Redox biochemistry of mammalian metallothioneins
    • Maret W, (2011) Redox biochemistry of mammalian metallothioneins. J Biol Inorg Chem 16: 1079-1086.
    • (2011) J Biol Inorg Chem , vol.16 , pp. 1079-1086
    • Maret, W.1
  • 7
    • 79952992995 scopus 로고    scopus 로고
    • Evidence for operation of the direct zinc ligand exchange mechanism for trafficking, transport, and reactivity of zinc in mammalian cells
    • Costello LC, Fenselau CC, Franklin RB, (2011) Evidence for operation of the direct zinc ligand exchange mechanism for trafficking, transport, and reactivity of zinc in mammalian cells. J Inorg Biochem 105: 589-599.
    • (2011) J Inorg Biochem , vol.105 , pp. 589-599
    • Costello, L.C.1    Fenselau, C.C.2    Franklin, R.B.3
  • 8
    • 79960156125 scopus 로고    scopus 로고
    • Molecular and genetic features of zinc transporters in physiology and pathogenesis
    • Fukada T, Kambe T, (2011) Molecular and genetic features of zinc transporters in physiology and pathogenesis. Metallomics 3: 662-674.
    • (2011) Metallomics , vol.3 , pp. 662-674
    • Fukada, T.1    Kambe, T.2
  • 9
    • 79959564958 scopus 로고    scopus 로고
    • An overview of a wide range of functions of znt and zip zinc transporters in the secretory pathway
    • Kambe T, (2011) An overview of a wide range of functions of znt and zip zinc transporters in the secretory pathway. Biosci Biotechnol Biochem 75: 1036-1043.
    • (2011) Biosci Biotechnol Biochem , vol.75 , pp. 1036-1043
    • Kambe, T.1
  • 10
    • 0036716282 scopus 로고    scopus 로고
    • Strategies for mmp inhibition in cancer: Innovations for the post-trial era
    • Overall CM, Lopez-Otin C, (2002) Strategies for mmp inhibition in cancer: Innovations for the post-trial era. Nat Rev Cancer 2: 657-672.
    • (2002) Nat Rev Cancer , vol.2 , pp. 657-672
    • Overall, C.M.1    Lopez-Otin, C.2
  • 11
    • 0037224740 scopus 로고    scopus 로고
    • The adams family of metalloproteases: Multidomain proteins with multiple functions
    • Seals DF, Courtneidge SA, (2003) The adams family of metalloproteases: Multidomain proteins with multiple functions. Genes Dev 17: 7-30.
    • (2003) Genes Dev , vol.17 , pp. 7-30
    • Seals, D.F.1    Courtneidge, S.A.2
  • 12
    • 0028918706 scopus 로고
    • Biology of human alkaline phosphatases with special reference to cancer
    • Millan JL, Fishman WH, (1995) Biology of human alkaline phosphatases with special reference to cancer. Crit Rev Clin Lab Sci 32: 1-39.
    • (1995) Crit Rev Clin Lab Sci , vol.32 , pp. 1-39
    • Millan, J.L.1    Fishman, W.H.2
  • 13
    • 34447510930 scopus 로고    scopus 로고
    • Function and regulation of human copper-transporting atpases
    • Lutsenko S, Barnes NL, Bartee MY, Dmitriev OY, (2007) Function and regulation of human copper-transporting atpases. Physiol Rev 87: 1011-1046.
    • (2007) Physiol Rev , vol.87 , pp. 1011-1046
    • Lutsenko, S.1    Barnes, N.L.2    Bartee, M.Y.3    Dmitriev, O.Y.4
  • 14
    • 84861927586 scopus 로고    scopus 로고
    • Advances in the understanding of mammalian copper transporters
    • Wang Y, Hodgkinson V, Zhu S, Weisman GA, Petris MJ, (2011) Advances in the understanding of mammalian copper transporters. Adv Nutr 2: 129-137.
    • (2011) Adv Nutr , vol.2 , pp. 129-137
    • Wang, Y.1    Hodgkinson, V.2    Zhu, S.3    Weisman, G.A.4    Petris, M.J.5
  • 15
    • 43949133356 scopus 로고    scopus 로고
    • The genetics of essential metal homeostasis during development
    • Kambe T, Weaver BP, Andrews GK, (2008) The genetics of essential metal homeostasis during development. Genesis 46: 214-228.
    • (2008) Genesis , vol.46 , pp. 214-228
    • Kambe, T.1    Weaver, B.P.2    Andrews, G.K.3
  • 16
    • 24744456569 scopus 로고    scopus 로고
    • Two different zinc transport complexes of cation diffusion facilitator proteins localized in the secretory pathway operate to activate alkaline phosphatases in vertebrate cells
    • Suzuki T, Ishihara K, Migaki H, Nagao M, Yamaguchi-Iwai Y, et al. (2005) Two different zinc transport complexes of cation diffusion facilitator proteins localized in the secretory pathway operate to activate alkaline phosphatases in vertebrate cells. J Biol Chem 280: 30956-30962.
    • (2005) J Biol Chem , vol.280 , pp. 30956-30962
    • Suzuki, T.1    Ishihara, K.2    Migaki, H.3    Nagao, M.4    Yamaguchi-Iwai, Y.5
  • 17
    • 71449098469 scopus 로고    scopus 로고
    • Demonstration and characterization of the heterodimerization of ZnT5 and ZnT6 in the early secretory pathway
    • Fukunaka A, Suzuki T, Kurokawa Y, Yamazaki T, Fujiwara N, et al. (2009) Demonstration and characterization of the heterodimerization of ZnT5 and ZnT6 in the early secretory pathway. J Biol Chem 284: 30798-30806.
    • (2009) J Biol Chem , vol.284 , pp. 30798-30806
    • Fukunaka, A.1    Suzuki, T.2    Kurokawa, Y.3    Yamazaki, T.4    Fujiwara, N.5
  • 18
    • 79955529543 scopus 로고    scopus 로고
    • Tissue nonspecific alkaline phosphatase is activated via a two-step mechanism by zinc transport complexes in the early secretory pathway
    • Fukunaka A, Kurokawa Y, Teranishi F, Sekler I, Oda K, et al. (2011) Tissue nonspecific alkaline phosphatase is activated via a two-step mechanism by zinc transport complexes in the early secretory pathway. J Biol Chem 286: 16363-16373.
    • (2011) J Biol Chem , vol.286 , pp. 16363-16373
    • Fukunaka, A.1    Kurokawa, Y.2    Teranishi, F.3    Sekler, I.4    Oda, K.5
  • 19
    • 84867152630 scopus 로고    scopus 로고
    • Molecular architecture and function of znt transporters
    • Kambe T, (2012) Molecular architecture and function of znt transporters. Curr Top Membr 69: 199-220.
    • (2012) Curr Top Membr , vol.69 , pp. 199-220
    • Kambe, T.1
  • 20
    • 1242295160 scopus 로고    scopus 로고
    • Efflux and compartmentalization of zinc by members of the slc30 family of solute carriers
    • Palmiter RD, Huang L, (2004) Efflux and compartmentalization of zinc by members of the slc30 family of solute carriers. Pflugers Arch 447: 744-751.
    • (2004) Pflugers Arch , vol.447 , pp. 744-751
    • Palmiter, R.D.1    Huang, L.2
  • 21
    • 77952566927 scopus 로고    scopus 로고
    • Cytosolic zinc buffering and muffling: Their role in intracellular zinc homeostasis
    • Colvin RA, Holmes WR, Fontaine CP, Maret W, (2010) Cytosolic zinc buffering and muffling: Their role in intracellular zinc homeostasis. Metallomics 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
  • 22
    • 79959997623 scopus 로고    scopus 로고
    • Metals on the move: Zinc ions in cellular regulation and in the coordination dynamics of zinc proteins
    • Maret W, (2011) Metals on the move: Zinc ions in cellular regulation and in the coordination dynamics of zinc proteins. Biometals 24: 411-418.
    • (2011) Biometals , vol.24 , pp. 411-418
    • Maret, W.1
  • 23
    • 12844265345 scopus 로고    scopus 로고
    • Zinc transporters, ZnT5 and ZnT7, are required for the activation of alkaline phosphatases, zinc-requiring enzymes that are glycosylphosphatidylinositol-anchored to the cytoplasmic membrane
    • Suzuki T, Ishihara K, Migaki H, Matsuura W, Kohda A, et al. (2005) Zinc transporters, ZnT5 and ZnT7, are required for the activation of alkaline phosphatases, zinc-requiring enzymes that are glycosylphosphatidylinositol-anchored to the cytoplasmic membrane. J Biol Chem 280: 637-643.
    • (2005) J Biol Chem , vol.280 , pp. 637-643
    • Suzuki, T.1    Ishihara, K.2    Migaki, H.3    Matsuura, W.4    Kohda, A.5
  • 24
    • 58149460415 scopus 로고    scopus 로고
    • Novel proteolytic processing of the ectodomain of the zinc transporter ZIP4 (SLC39A4) during zinc deficiency is inhibited by acrodermatitis enteropathica mutations
    • Kambe T, Andrews GK, (2009) Novel proteolytic processing of the ectodomain of the zinc transporter ZIP4 (SLC39A4) during zinc deficiency is inhibited by acrodermatitis enteropathica mutations. Mol Cell Biol 29: 129-139.
    • (2009) Mol Cell Biol , vol.29 , pp. 129-139
    • Kambe, T.1    Andrews, G.K.2
  • 25
    • 84878579262 scopus 로고    scopus 로고
    • Compound heterozygous mutations in slc30a2/znt2 results in low milk zinc concentrations: A novel mechanism for zinc deficiency in a breast-fed infant
    • Itsumura N, Inamo Y, Okazaki F, Teranishi F, Narita H, et al. (2013) Compound heterozygous mutations in slc30a2/znt2 results in low milk zinc concentrations: A novel mechanism for zinc deficiency in a breast-fed infant. PLoS One 8: e64045.
    • (2013) PLoS One , vol.8
    • Itsumura, N.1    Inamo, Y.2    Okazaki, F.3    Teranishi, F.4    Narita, H.5
  • 26
    • 33745842537 scopus 로고    scopus 로고
    • Zinc transport complexes contribute to the homeostatic maintenance of secretory pathway function in vertebrate cells
    • Ishihara K, Yamazaki T, Ishida Y, Suzuki T, Oda K, et al. (2006) Zinc transport complexes contribute to the homeostatic maintenance of secretory pathway function in vertebrate cells. J Biol Chem 281: 17743-17750.
    • (2006) J Biol Chem , vol.281 , pp. 17743-17750
    • Ishihara, K.1    Yamazaki, T.2    Ishida, Y.3    Suzuki, T.4    Oda, K.5
  • 27
    • 33947600099 scopus 로고    scopus 로고
    • Molecular characterization of two metallothionein isoforms in avian species: Evolutionary history, tissue distribution profile, and expression associated with metal accumulation
    • Nam DH, Kim EY, Iwata H, Tanabe S, (2007) Molecular characterization of two metallothionein isoforms in avian species: Evolutionary history, tissue distribution profile, and expression associated with metal accumulation. Comp Biochem Physiol C Toxicol Pharmacol 145: 295-305.
    • (2007) Comp Biochem Physiol C Toxicol Pharmacol , vol.145 , pp. 295-305
    • Nam, D.H.1    Kim, E.Y.2    Iwata, H.3    Tanabe, S.4
  • 28
    • 58149152752 scopus 로고    scopus 로고
    • Chromium(vi) inhibits mouse metallothionein-i gene transcription by preventing the zinc-dependent formation of an mtf-1-p300 complex
    • Kimura T, Li Y, Okumura F, Itoh N, Nakanishi T, et al. (2008) Chromium(vi) inhibits mouse metallothionein-i gene transcription by preventing the zinc-dependent formation of an mtf-1-p300 complex. Biochem J 415: 477-482.
    • (2008) Biochem J , vol.415 , pp. 477-482
    • Kimura, T.1    Li, Y.2    Okumura, F.3    Itoh, N.4    Nakanishi, T.5
  • 29
    • 77954477140 scopus 로고    scopus 로고
    • Roles of comm-domain-containing 1 in stability and recruitment of the copper-transporting atpase in a mouse hepatoma cell line
    • Miyayama T, Hiraoka D, Kawaji F, Nakamura E, Suzuki N, et al. (2010) Roles of comm-domain-containing 1 in stability and recruitment of the copper-transporting atpase in a mouse hepatoma cell line. Biochem J 429: 53-61.
    • (2010) Biochem J , vol.429 , pp. 53-61
    • Miyayama, T.1    Hiraoka, D.2    Kawaji, F.3    Nakamura, E.4    Suzuki, N.5
  • 30
    • 77649185941 scopus 로고    scopus 로고
    • Cell-density-dependent methylmercury susceptibility of cultured human brain microvascular pericytes
    • Hirooka T, Fujiwara Y, Minami Y, Ishii A, Ishigooka M, et al. (2010) Cell-density-dependent methylmercury susceptibility of cultured human brain microvascular pericytes. Toxicol In Vitro 24: 835-841.
    • (2010) Toxicol In Vitro , vol.24 , pp. 835-841
    • Hirooka, T.1    Fujiwara, Y.2    Minami, Y.3    Ishii, A.4    Ishigooka, M.5
  • 31
    • 0028948696 scopus 로고
    • Cloning and functional characterization of a mammalian zinc transporter that confers resistance to zinc
    • Palmiter RD, Findley SD, (1995) Cloning and functional characterization of a mammalian zinc transporter that confers resistance to zinc. EMBO J 14: 639-649.
    • (1995) EMBO J , vol.14 , pp. 639-649
    • Palmiter, R.D.1    Findley, S.D.2
  • 32
    • 0029873677 scopus 로고    scopus 로고
    • ZnT-2, a mammalian protein that confers resistance to zinc by facilitating vesicular sequestration
    • Palmiter RD, Cole TB, Findley SD, (1996) ZnT-2, a mammalian protein that confers resistance to zinc by facilitating vesicular sequestration. EMBO J 15: 1784-1791.
    • (1996) EMBO J , vol.15 , pp. 1784-1791
    • Palmiter, R.D.1    Cole, T.B.2    Findley, S.D.3
  • 33
    • 33947727880 scopus 로고    scopus 로고
    • Zinc transporter 2 (slc30a2) can suppress the vesicular zinc defect of adaptor protein 3-depleted fibroblasts by promoting zinc accumulation in lysosomes
    • Falcon-Perez JM, Dell'Angelica EC, (2007) Zinc transporter 2 (slc30a2) can suppress the vesicular zinc defect of adaptor protein 3-depleted fibroblasts by promoting zinc accumulation in lysosomes. Exp Cell Res 313: 1473-1483.
    • (2007) Exp Cell Res , vol.313 , pp. 1473-1483
    • Falcon-Perez, J.M.1    Dell'Angelica, E.C.2
  • 34
    • 0035811058 scopus 로고    scopus 로고
    • The metallochaperone atox1 plays a critical role in perinatal copper homeostasis
    • Hamza I, Faisst A, Prohaska J, Chen J, Gruss P, et al. (2001) The metallochaperone atox1 plays a critical role in perinatal copper homeostasis. Proc Natl Acad Sci U S A 98: 6848-6852.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 6848-6852
    • Hamza, I.1    Faisst, A.2    Prohaska, J.3    Chen, J.4    Gruss, P.5
  • 35
    • 67349118440 scopus 로고    scopus 로고
    • Copper accumulation and compartmentalization in mouse fibroblast lacking metallothionein and copper chaperone, atox1
    • Miyayama T, Suzuki KT, Ogra Y, (2009) Copper accumulation and compartmentalization in mouse fibroblast lacking metallothionein and copper chaperone, atox1. Toxicol Appl Pharmacol 237: 205-213.
    • (2009) Toxicol Appl Pharmacol , vol.237 , pp. 205-213
    • Miyayama, T.1    Suzuki, K.T.2    Ogra, Y.3
  • 36
    • 17644375510 scopus 로고    scopus 로고
    • Role of antioxidant-1 in extracellular superoxide dismutase function and expression
    • Jeney V, Itoh S, Wendt M, Gradek Q, Ushio-Fukai M, et al. (2005) Role of antioxidant-1 in extracellular superoxide dismutase function and expression. Circ Res 96: 723-729.
    • (2005) Circ Res , vol.96 , pp. 723-729
    • Jeney, V.1    Itoh, S.2    Wendt, M.3    Gradek, Q.4    Ushio-Fukai, M.5
  • 37
    • 0038323978 scopus 로고    scopus 로고
    • Supplying copper to the cuproenzyme peptidylglycine alpha-amidating monooxygenase
    • El Meskini R, Culotta VC, Mains RE, Eipper BA, (2003) Supplying copper to the cuproenzyme peptidylglycine alpha-amidating monooxygenase. J Biol Chem 278: 12278-12284.
    • (2003) J Biol Chem , vol.278 , pp. 12278-12284
    • El Meskini, R.1    Culotta, V.C.2    Mains, R.E.3    Eipper, B.A.4
  • 38
    • 67650540770 scopus 로고    scopus 로고
    • Identification of the zn2+ binding site and mode of operation of a mammalian zn2+ transporter
    • Ohana E, Hoch E, Keasar C, Kambe T, Yifrach O, et al. (2009) Identification of the zn2+ binding site and mode of operation of a mammalian zn2+ transporter. J Biol Chem 284: 17677-17686.
    • (2009) J Biol Chem , vol.284 , pp. 17677-17686
    • Ohana, E.1    Hoch, E.2    Keasar, C.3    Kambe, T.4    Yifrach, O.5
  • 39
    • 38749086503 scopus 로고    scopus 로고
    • Regulation of cellular zinc balance as a potential mechanism of ever-mediated protection against pathogenesis by cutaneous oncogenic human papillomaviruses
    • Lazarczyk M, Pons C, Mendoza JA, Cassonnet P, Jacob Y, et al. (2008) Regulation of cellular zinc balance as a potential mechanism of ever-mediated protection against pathogenesis by cutaneous oncogenic human papillomaviruses. J Exp Med 205: 35-42.
    • (2008) J Exp Med , vol.205 , pp. 35-42
    • Lazarczyk, M.1    Pons, C.2    Mendoza, J.A.3    Cassonnet, P.4    Jacob, Y.5
  • 40
    • 79957705205 scopus 로고    scopus 로고
    • Rapid homeostatic response of h4iie cells to diethylenetriaminepentaacetic acid is not due to changes in the amount or localization of znt-1 protein
    • Dutta A, Sankavaram K, Chong L, Palermo A, Michel RG, et al. (2011) Rapid homeostatic response of h4iie cells to diethylenetriaminepentaacetic acid is not due to changes in the amount or localization of znt-1 protein. Nutr Res 31: 404-411.
    • (2011) Nutr Res , vol.31 , pp. 404-411
    • Dutta, A.1    Sankavaram, K.2    Chong, L.3    Palermo, A.4    Michel, R.G.5
  • 41
    • 0036854425 scopus 로고    scopus 로고
    • A novel phenoxazine derivative suppresses surface igm expression in dt40 b cell line
    • Gao S, Takano T, Sada K, He J, Noda C, et al. (2002) A novel phenoxazine derivative suppresses surface igm expression in dt40 b cell line. Br J Pharmacol 137: 749-755.
    • (2002) Br J Pharmacol , vol.137 , pp. 749-755
    • Gao, S.1    Takano, T.2    Sada, K.3    He, J.4    Noda, C.5
  • 43
    • 67650050211 scopus 로고    scopus 로고
    • Mammalian zinc transporters: Nutritional and physiologic regulation
    • Lichten LA, Cousins RJ, (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.J.2
  • 45
    • 56649111126 scopus 로고    scopus 로고
    • The zinc transporter slc39a13/zip13 is required for connective tissue development; its involvement in bmp/tgf-beta signaling pathways
    • Fukada T, Civic N, Furuichi T, Shimoda S, Mishima K, et al. (2008) The zinc transporter slc39a13/zip13 is required for connective tissue development; its involvement in bmp/tgf-beta signaling pathways. PLoS ONE 3: e3642.
    • (2008) PLoS ONE , vol.3
    • Fukada, T.1    Civic, N.2    Furuichi, T.3    Shimoda, S.4    Mishima, K.5
  • 46
    • 67650050212 scopus 로고    scopus 로고
    • Zinc transporter zip8 (slc39a8) and zinc influence ifn-gamma expression in activated human t cells
    • Aydemir TB, Liuzzi J, McClellan S, Cousins RJ, (2009) Zinc transporter zip8 (slc39a8) and zinc influence ifn-gamma expression in activated human t cells. J Leukoc Biol 86: 337-348.
    • (2009) J Leukoc Biol , vol.86 , pp. 337-348
    • Aydemir, T.B.1    Liuzzi, J.2    McClellan, S.3    Cousins, R.J.4
  • 47
    • 78049405392 scopus 로고    scopus 로고
    • Zinc dyshomeostasis is linked with the loss of mucolipidosis iv-associated trpml1 ion channel
    • Eichelsdoerfer JL, Evans JA, Slaugenhaupt SA, Cuajungco MP, (2010) Zinc dyshomeostasis is linked with the loss of mucolipidosis iv-associated trpml1 ion channel. J Biol Chem 285: 34304-34308.
    • (2010) J Biol Chem , vol.285 , pp. 34304-34308
    • Eichelsdoerfer, J.L.1    Evans, J.A.2    Slaugenhaupt, S.A.3    Cuajungco, M.P.4
  • 48
    • 84862691112 scopus 로고    scopus 로고
    • A novel role of the l-type calcium channel alpha(1d) subunit as a gatekeeper for intracellular zinc signaling: Zinc wave
    • Yamasaki S, Hasegawa A, Hojyo S, Ohashi W, Fukada T, et al. (2012) A novel role of the l-type calcium channel alpha(1d) subunit as a gatekeeper for intracellular zinc signaling: Zinc wave. PLoS One 7: e39654.
    • (2012) PLoS One , vol.7
    • Yamasaki, S.1    Hasegawa, A.2    Hojyo, S.3    Ohashi, W.4    Fukada, T.5
  • 49
    • 84856998257 scopus 로고    scopus 로고
    • Protein kinase ck2 triggers cytosolic zinc signaling pathways by phosphorylation of zinc channel zip7
    • Taylor KM, Hiscox S, Nicholson RI, Hogstrand C, Kille P, (2012) Protein kinase ck2 triggers cytosolic zinc signaling pathways by phosphorylation of zinc channel zip7. Sci Signal 5: ra11.
    • (2012) Sci Signal , vol.5
    • Taylor, K.M.1    Hiscox, S.2    Nicholson, R.I.3    Hogstrand, C.4    Kille, P.5
  • 50
    • 84874718742 scopus 로고    scopus 로고
    • Essential role of the zinc transporter zip9/slc39a9 in regulating the activations of akt and erk in b-cell receptor signaling pathway in dt40 cells
    • Taniguchi M, Fukunaka A, Hagihara M, Watanabe K, Kamino S, et al. (2013) Essential role of the zinc transporter zip9/slc39a9 in regulating the activations of akt and erk in b-cell receptor signaling pathway in dt40 cells. PLoS One 8: e58022.
    • (2013) PLoS One , vol.8
    • Taniguchi, M.1    Fukunaka, A.2    Hagihara, M.3    Watanabe, K.4    Kamino, S.5
  • 51
    • 84871396523 scopus 로고    scopus 로고
    • Promotion of vesicular zinc efflux by zip13 and its implications for spondylocheiro dysplastic ehlers-danlos syndrome
    • Jeong J, Walker JM, Wang F, Park JG, Palmer AE, et al. (2012) Promotion of vesicular zinc efflux by zip13 and its implications for spondylocheiro dysplastic ehlers-danlos syndrome. Proc Natl Acad Sci U S A 109: E3530-3538.
    • (2012) Proc Natl Acad Sci U S A , vol.109
    • Jeong, J.1    Walker, J.M.2    Wang, F.3    Park, J.G.4    Palmer, A.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.