메뉴 건너뛰기




Volumn 61, Issue 1, 2004, Pages 49-68

Overview of mammalian zinc transporters

Author keywords

CDF; Efflux; Mammalian zinc transporter; Uptake; Zinc homeostasis; ZIP; Znt

Indexed keywords

ANTIBIOTIC AGENT; CLIOQUINOL; MEMBRANE PROTEIN; PROTEIN SUBUNIT; UNCLASSIFIED DRUG; ZINC; ZINC TRANSPORTER;

EID: 1642580782     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00018-003-3148-y     Document Type: Review
Times cited : (354)

References (167)
  • 1
    • 0027394031 scopus 로고
    • The biochemical basis of zinc physiology
    • Vallee B. L. and Falchuk K. H. (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
    • 0029866646 scopus 로고    scopus 로고
    • The galvanization of biology: A growing appreciation for the roles of zinc
    • Berg J. M. and Shi Y. (1996) The galvanization of biology: a growing appreciation for the roles of zinc. Science 271: 1081-1085
    • (1996) Science , vol.271 , pp. 1081-1085
    • Berg, J.M.1    Shi, Y.2
  • 3
    • 0025303335 scopus 로고
    • Zinc coordination, function and structure of zinc enzymes and other proteins
    • Vallee B. L. and Auld D. S. (1990) Zinc coordination, function and structure of zinc enzymes and other proteins. Biochemistry 29: 5647-5659
    • (1990) Biochemistry , vol.29 , pp. 5647-5659
    • Vallee, B.L.1    Auld, D.S.2
  • 5
    • 0035696301 scopus 로고    scopus 로고
    • Functions of zinc in signaling, proliferation and differentiation of mammalian cells
    • Beyersmann D. and Haase H. (2001) Functions of zinc in signaling, proliferation and differentiation of mammalian cells. Biometals 14: 331-341
    • (2001) Biometals , vol.14 , pp. 331-341
    • Beyersmann, D.1    Haase, H.2
  • 6
    • 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
  • 7
    • 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. and Choi D. W. (1996) The role of zinc in selective neuronal death after transient global cerebral ischemia. Science 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
  • 8
    • 0034011588 scopus 로고    scopus 로고
    • Overview of zinc absorption and excretion in the human gastrointestinal tract
    • Krebs N. F. (2000) Overview of zinc absorption and excretion in the human gastrointestinal tract. J. Nutr. 130: 1374S-1377S
    • (2000) J. Nutr. , vol.130
    • Krebs, N.F.1
  • 10
    • 0029971595 scopus 로고    scopus 로고
    • Zinc transport in mammalian cells
    • Reyes J. G. (1996) Zinc transport in mammalian cells. Am. J. Physiol. 270: 0401-410
    • (1996) Am. J. Physiol. , vol.270 , pp. 401-410
    • Reyes, J.G.1
  • 12
    • 0021866385 scopus 로고
    • Intravesicular localization of zinc in rat telencephalic boutons. A histochemical study
    • Perez-Clausell J. and Danscher G. (1985) Intravesicular localization of zinc in rat telencephalic boutons. A histochemical study. Brain Res. 337: 91-98
    • (1985) Brain Res. , vol.337 , pp. 91-98
    • Perez-Clausell, J.1    Danscher, G.2
  • 13
    • 0026688299 scopus 로고
    • Enrichment of glutamate in zinc-containing terminals of the cat visual cortex
    • Beaulieu C., Dyck R. and Cynader M. (1992) Enrichment of glutamate in zinc-containing terminals of the cat visual cortex. Neuroreport 3: 861-864
    • (1992) Neuroreport , vol.3 , pp. 861-864
    • Beaulieu, C.1    Dyck, R.2    Cynader, M.3
  • 14
    • 0028246488 scopus 로고
    • Video image analysis of labile zinc in viable pancreatic islet cells using a specific fluorescent probe for zinc
    • Zalewski P. D., Millard S. H., Forbes I. J., Kapaniris O., Slavotinek A., Betts W. H. et al. (1994) Video image analysis of labile zinc in viable pancreatic islet cells using a specific fluorescent probe for zinc. J. Histochem. Cytochem. 42: 877-884
    • (1994) J. Histochem. Cytochem. , vol.42 , pp. 877-884
    • Zalewski, P.D.1    Millard, S.H.2    Forbes, I.J.3    Kapaniris, O.4    Slavotinek, A.5    Betts, W.H.6
  • 15
    • 0002607644 scopus 로고
    • An introduction to the biochemistry of zinc
    • Mills, C. F. (ed), Springer-Verlag, New York
    • Williams R. J. P. (1989) An introduction to the biochemistry of zinc. In: Zinc in Human Biology, pp. 15-31, Mills, C. F. (ed), Springer-Verlag, New York
    • (1989) Zinc in Human Biology , pp. 15-31
    • Williams, R.J.P.1
  • 16
    • 0033551106 scopus 로고    scopus 로고
    • Unidirectional transport from apical to basolateral compartment of cobalt ion in polarized Madin-Darby canine kidney cells
    • Nagao M., Sugaru E., Kambe T. and Sasaki R. (1999) Unidirectional transport from apical to basolateral compartment of cobalt ion in polarized Madin-Darby canine kidney cells. Biochem. Biophys. Res. Commun. 257: 289-294
    • (1999) Biochem. Biophys. Res. Commun. , vol.257 , pp. 289-294
    • Nagao, M.1    Sugaru, E.2    Kambe, T.3    Sasaki, R.4
  • 17
    • 0030755366 scopus 로고    scopus 로고
    • Cloning and characterization of a mammalian proton-coupled metal-ion transporter
    • Gunshin H., Mackenzie B., Berger U. V., Gunshin Y., Romero M. F., Boron W. F. et al. (1997) Cloning and characterization of a mammalian proton-coupled metal-ion transporter. Nature 388: 482-488
    • (1997) Nature , vol.388 , pp. 482-488
    • Gunshin, H.1    Mackenzie, B.2    Berger, U.V.3    Gunshin, Y.4    Romero, M.F.5    Boron, W.F.6
  • 18
    • 0035744950 scopus 로고    scopus 로고
    • Properties of the mammalian and yeast metal-ion transporters DCT1 and Smf1p expressed in Xenopus laevis oocytes
    • Sacher A., Cohen A. and Nelson N. (2001) Properties of the mammalian and yeast metal-ion transporters DCT1 and Smf1p expressed in Xenopus laevis oocytes. J. Exp. Biol. 204: 1053-1061
    • (2001) J. Exp. Biol. , vol.204 , pp. 1053-1061
    • Sacher, A.1    Cohen, A.2    Nelson, N.3
  • 19
    • 0033984237 scopus 로고    scopus 로고
    • Nramp2 expression is associated with pH-dependent iron uptake across the apical membrane of human intestinal Caco-2 cells
    • Tandy S., Williams M., Leggett A., Lopez-Jimenez M., Dedes M., Ramesh B. et al. (2000) Nramp2 expression is associated with pH-dependent iron uptake across the apical membrane of human intestinal Caco-2 cells. J. Biol. Chem. 275: 1023-1029
    • (2000) J. Biol. Chem. , vol.275 , pp. 1023-1029
    • Tandy, S.1    Williams, M.2    Leggett, A.3    Lopez-Jimenez, M.4    Dedes, M.5    Ramesh, B.6
  • 20
    • 0033564656 scopus 로고    scopus 로고
    • Cellular and subcellular localization of the Nramp2 iron transporter in the intestinal brush border and regulation by dietary iron
    • Canonne-Hergaux F., Gruenheid S., Ponka P. and Gros P. (1999) Cellular and subcellular localization of the Nramp2 iron transporter in the intestinal brush border and regulation by dietary iron. Blood 93: 4406-4417
    • (1999) Blood , vol.93 , pp. 4406-4417
    • Canonne-Hergaux, F.1    Gruenheid, S.2    Ponka, P.3    Gros, P.4
  • 21
    • 0000438237 scopus 로고    scopus 로고
    • Metal ion uptake in eukaryotes
    • Eide D. and Guerinot M. L. (1997) Metal ion uptake in eukaryotes. ASM News 63: 199-205
    • (1997) ASM News , vol.63 , pp. 199-205
    • Eide, D.1    Guerinot, M.L.2
  • 22
    • 0030791257 scopus 로고    scopus 로고
    • Molecular biology of iron and zinc uptake in eukaryotes
    • Eide D. (1997) Molecular biology of iron and zinc uptake in eukaryotes. Curr. Opin. Cell Biol. 9: 573-577
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 573-577
    • Eide, D.1
  • 23
    • 0031794474 scopus 로고    scopus 로고
    • Sequence analyses and phylogenetic characterization of the ZIP family of metal ion transport proteins
    • Eng B. H., Guerinot M. L., Eide D. and Saier M. H. Jr. (1998) Sequence analyses and phylogenetic characterization of the ZIP family of metal ion transport proteins. J. Membr. Biol. 166: 1-7
    • (1998) J. Membr. Biol. , vol.166 , pp. 1-7
    • Eng, B.H.1    Guerinot, M.L.2    Eide, D.3    Saier Jr., M.H.4
  • 24
    • 0030953624 scopus 로고    scopus 로고
    • A novel family of ubiquitous heavy metal ion transport proteins
    • Paulsen I. T. and Saier M. H. Jr. (1997) A novel family of ubiquitous heavy metal ion transport proteins. J. Membr. Biol. 156: 99-103
    • (1997) J. Membr. Biol. , vol.156 , pp. 99-103
    • Paulsen, I.T.1    Saier Jr., M.H.2
  • 25
    • 0033151564 scopus 로고    scopus 로고
    • Zeroing in on zinc uptake in yeast and plants
    • Guerinot M. L. and Eide D. (1999) Zeroing in on zinc uptake in yeast and plants. Curr. Opin. Plant Biol. 2: 244-249
    • (1999) Curr. Opin. Plant Biol. , vol.2 , pp. 244-249
    • Guerinot, M.L.1    Eide, D.2
  • 26
    • 0031953430 scopus 로고    scopus 로고
    • Mammalian zinc transporters
    • McMahon R. J. and Cousins R. J. (1998) Mammalian zinc transporters. J. Nutr. 128: 667-670
    • (1998) J. Nutr. , vol.128 , pp. 667-670
    • McMahon, R.J.1    Cousins, R.J.2
  • 27
    • 0034011237 scopus 로고    scopus 로고
    • Integrative aspects of zinc transporters
    • Cousins R. J. and McMahon R. J. (2000) Integrative aspects of zinc transporters. J. Nutr. 130: 1384S0-1387S
    • (2000) J. Nutr. , vol.130
    • Cousins, R.J.1    McMahon, R.J.2
  • 28
    • 0034192475 scopus 로고    scopus 로고
    • The ZIP family of metal transporters
    • Guerinot M. L. (2000) The ZIP family of metal transporters. Biochim. Biophys. Acta. 1465: 190-198
    • (2000) Biochim. Biophys. Acta. , vol.1465 , pp. 190-198
    • Guerinot, M.L.1
  • 29
    • 0035693722 scopus 로고    scopus 로고
    • Eukaryotic zinc transporters and their regulation
    • Gaither L. A. and Eide D. J. (2001) Eukaryotic zinc transporters and their regulation. Biometals 14: 251-270
    • (2001) Biometals , vol.14 , pp. 251-270
    • Gaither, L.A.1    Eide, D.J.2
  • 30
    • 0035696323 scopus 로고    scopus 로고
    • Bacterial zinc transporters and regulators
    • Hantke K. (2001) Bacterial zinc transporters and regulators. Biometals 14: 239-249
    • (2001) Biometals , vol.14 , pp. 239-249
    • Hantke, K.1
  • 31
    • 0037853748 scopus 로고    scopus 로고
    • Phylogenetic relationships within cation transporter families of Arabidopsis
    • Maser P., Thomine S., Schroeder J. I., Ward J. M., Hirschi K., Sze H. et al. (2001) Phylogenetic relationships within cation transporter families of Arabidopsis. Plant Physiol. 126: 1646-1667
    • (2001) Plant Physiol. , vol.126 , pp. 1646-1667
    • Maser, P.1    Thomine, S.2    Schroeder, J.I.3    Ward, J.M.4    Hirschi, K.5    Sze, H.6
  • 32
    • 0036223732 scopus 로고    scopus 로고
    • Cellular transporters for zinc
    • Harris E. D. (2002) Cellular transporters for zinc. Nutr. Rev. 60: 121-124
    • (2002) Nutr. Rev. , vol.60 , pp. 121-124
    • Harris, E.D.1
  • 33
    • 0344177605 scopus 로고    scopus 로고
    • Localization of zinc in the rat submandibular gland and the effect of its deficiency on salivary secretion
    • Ishii K., Sato M., Akita M. and Tomita H. (1999) Localization of zinc in the rat submandibular gland and the effect of its deficiency on salivary secretion. Ann. Otol. Rhinol. Laryngol. 108: 300-308
    • (1999) Ann. Otol. Rhinol. Laryngol. , vol.108 , pp. 300-308
    • Ishii, K.1    Sato, M.2    Akita, M.3    Tomita, H.4
  • 34
    • 0028886687 scopus 로고
    • Characterization of N-(6-methoxy-8-quinolyl)-p-toluenesulfonamide for the detection of zinc in living sperm cells
    • Andrews J. C., Nolan J. P., Hammerstedt R. H. and Bavister B. D. (1995) Characterization of N-(6-methoxy-8-quinolyl)-p-toluenesulfonamide for the detection of zinc in living sperm cells. Cytometry 21: 153-159
    • (1995) Cytometry , vol.21 , pp. 153-159
    • Andrews, J.C.1    Nolan, J.P.2    Hammerstedt, R.H.3    Bavister, B.D.4
  • 35
    • 0017797285 scopus 로고
    • An improved Timm sulphide silver method for light and electron microscopic localization of heavy metals in biological tissues
    • Danscher G. and Zimmer J. (1978) An improved Timm sulphide silver method for light and electron microscopic localization of heavy metals in biological tissues. Histochemistry 55: 27-40
    • (1978) Histochemistry , vol.55 , pp. 27-40
    • Danscher, G.1    Zimmer, J.2
  • 36
    • 0035177564 scopus 로고    scopus 로고
    • Differential subcellular localization of zinc in the rat retina
    • Akagi T., Kaneda M., Ishii K. and Hashikawa T. (2001) Differential subcellular localization of zinc in the rat retina. J. Histochem. Cytochem. 49: 87-96
    • (2001) J. Histochem. Cytochem. , vol.49 , pp. 87-96
    • Akagi, T.1    Kaneda, M.2    Ishii, K.3    Hashikawa, T.4
  • 37
    • 0023149918 scopus 로고
    • Zinc in the anterior pituitary of rat: A histochemical and analytical work
    • Thorlacius-Ussing O. (1987) Zinc in the anterior pituitary of rat: a histochemical and analytical work. Neuroendocrinology 45: 233-242
    • (1987) Neuroendocrinology , vol.45 , pp. 233-242
    • Thorlacius-Ussing, O.1
  • 38
    • 0023105267 scopus 로고
    • Zinc-containing 7S-NGF complex. Evidence from zinc histochemistry for localization in salivary secretory granules
    • Frederickson C. J., Perez-Clausell J. and Danscher G. (1987) Zinc-containing 7S-NGF complex. Evidence from zinc histochemistry for localization in salivary secretory granules. J. Histochem. Cytochem. 35: 579-583
    • (1987) J. Histochem. Cytochem. , vol.35 , pp. 579-583
    • Frederickson, C.J.1    Perez-Clausell, J.2    Danscher, G.3
  • 39
    • 0004608219 scopus 로고    scopus 로고
    • Importance of zinc in the central nervous system: The zinc-containing neuron
    • Frederickson C. J., Suh S. W., Silva D. and Thompson R. B. (2000) Importance of zinc in the central nervous system: the zinc-containing neuron. J. Nutr. 130: 1471S-1483S
    • (2000) J. Nutr. , vol.130
    • Frederickson, C.J.1    Suh, S.W.2    Silva, D.3    Thompson, R.B.4
  • 40
    • 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. and Ernst E. (1997) Ultrastructural localization of zinc ions in the rat prostate: an autometallographic study. Prostate 31: 125-130
    • (1997) Prostate , vol.31 , pp. 125-130
    • Sorensen, M.B.1    Stoltenberg, M.2    Juhl, S.3    Danscher, G.4    Ernst, E.5
  • 41
    • 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. and Palmiter R. D. (1999) Elimination of zinc from synaptic vesicles in the intact mouse brain by disruption of the ZnT3 gene. Proc. Natl. Acad. Sci. USA 96: 1716-1721
    • (1999) Proc. Natl. Acad. Sci. USA , 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
  • 42
    • 0029911793 scopus 로고    scopus 로고
    • The yeast ZRT1 gene encodes the zinc transporter protein of a high-affinity uptake system induced by zinc limitation
    • Zhao H. and Eide D. (1996) The yeast ZRT1 gene encodes the zinc transporter protein of a high-affinity uptake system induced by zinc limitation. Proc. Natl. Acad. Sci. USA 93: 2454-2458
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2454-2458
    • Zhao, H.1    Eide, D.2
  • 43
    • 0029841951 scopus 로고    scopus 로고
    • The ZRT2 gene encodes the low affinity zinc transporter in Saccharomyces cerevisiae
    • Zhao H. and Eide D. (1996) The ZRT2 gene encodes the low affinity zinc transporter in Saccharomyces cerevisiae. J. Biol. Chem. 271: 23203-23210
    • (1996) J. Biol. Chem. , vol.271 , pp. 23203-23210
    • Zhao, H.1    Eide, D.2
  • 44
    • 0032499739 scopus 로고    scopus 로고
    • Identification of a family of zinc transporter genes from Arabidopsis that respond to zinc deficiency
    • Grotz N., Fox T., Connolly E., Park W., Guerinot M. L. and Eide D. (1998) Identification of a family of zinc transporter genes from Arabidopsis that respond to zinc deficiency. Proc. Natl. Acad. Sci. USA 95: 7220-7224
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7220-7224
    • Grotz, N.1    Fox, T.2    Connolly, E.3    Park, W.4    Guerinot, M.L.5    Eide, D.6
  • 45
    • 0035933885 scopus 로고    scopus 로고
    • The human ZIP1 transporter mediates zinc uptake in human K562 erythroleukemia cells
    • Gaither L. A. and Eide D. J. (2001) The human ZIP1 transporter mediates zinc uptake in human K562 erythroleukemia cells. J. Biol. Chem. 276: 22258-22264
    • (2001) J. Biol. Chem. , vol.276 , pp. 22258-22264
    • Gaither, L.A.1    Eide, D.J.2
  • 46
    • 0034051667 scopus 로고    scopus 로고
    • Functional expression of the human hZIP2 zinc transporter
    • Gaither L. A. and Eide D. J. (2000) Functional expression of the human hZIP2 zinc transporter. J. Biol. Chem. 275: 5560-5564
    • (2000) J. Biol. Chem. , vol.275 , pp. 5560-5564
    • Gaither, L.A.1    Eide, D.J.2
  • 47
    • 0034161957 scopus 로고    scopus 로고
    • Zinc-regulated ubiquitin conjugation signals endocytosis of the yeast ZRT1 zinc transporter
    • Gitan R. S. and Eide D. J. (2000) Zinc-regulated ubiquitin conjugation signals endocytosis of the yeast ZRT1 zinc transporter. Biochem. J. 346 Pt. 2: 329-336
    • (2000) Biochem. J. , vol.346 , Issue.2 PART , pp. 329-336
    • Gitan, R.S.1    Eide, D.J.2
  • 48
    • 0034710975 scopus 로고    scopus 로고
    • Altered selectivity in an Arabidopsis metal transporter
    • Rogers E. E., Eide D. J. and Guerinot M. L. (2000) Altered selectivity in an Arabidopsis metal transporter. Proc. Natl. Acad. Sci. USA 97: 12356-12360
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12356-12360
    • Rogers, E.E.1    Eide, D.J.2    Guerinot, M.L.3
  • 49
    • 0033931310 scopus 로고    scopus 로고
    • 2+ homeostasis
    • 2+ homeostasis. IUBMB Life 49: 249-253
    • (2000) IUBMB Life , vol.49 , pp. 249-253
    • Taylor, K.M.1
  • 50
    • 0028360127 scopus 로고
    • Oestrogen-regulated genes in breast cancer: Association of pLIV1 with lymph node involvement
    • Manning D. L., Robertson J. F., Ellis I. O., Elston C. W., McClelland R. A., Gee J. M. et al. (1994) Oestrogen-regulated genes in breast cancer: association of pLIV1 with lymph node involvement. Eur. J. Cancer 30 A: 675-678
    • (1994) Eur. J. Cancer , vol.30 A , pp. 675-678
    • Manning, D.L.1    Robertson, J.F.2    Ellis, I.O.3    Elston, C.W.4    McClelland, R.A.5    Gee, J.M.6
  • 52
    • 0036939017 scopus 로고    scopus 로고
    • Mycobacterium bovis BCG cell wall and lipopolysaccharide induce a novel gene, BIGM103, encoding a 7-TM protein: Identification of a new protein family having Zn-transporter and Zn-metalloprotease signatures
    • Begum N. A., Kobayashi M., Moriwaki Y., Matsumoto M., Toyoshima K. and Seya T. (2002) Mycobacterium bovis BCG cell wall and lipopolysaccharide induce a novel gene, BIGM103, encoding a 7-TM protein: identification of a new protein family having Zn-transporter and Zn-metalloprotease signatures. Genomics 80: 630-645
    • (2002) Genomics , vol.80 , pp. 630-645
    • Begum, N.A.1    Kobayashi, M.2    Moriwaki, Y.3    Matsumoto, M.4    Toyoshima, K.5    Seya, T.6
  • 53
    • 0029095760 scopus 로고
    • Structural features of a superfamily of zinc-endopeptidases: The metzincins
    • Stocker W. and Bode W. (1995) Structural features of a superfamily of zinc-endopeptidases: the metzincins. Curr. Opin. Struct. Biol. 5: 383-390
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 383-390
    • Stocker, W.1    Bode, W.2
  • 54
    • 0036308552 scopus 로고    scopus 로고
    • A novel member of a zinc transporter family is defective in acrodermatitis enteropathica
    • Wang K., Zhou B., Kuo Y. M., Zemansky J. and Gitschier J. (2002) A novel member of a zinc transporter family is defective in acrodermatitis enteropathica. Am. J. Hum. Genet. 71: 66-73
    • (2002) Am. J. Hum. Genet. , vol.71 , pp. 66-73
    • Wang, K.1    Zhou, B.2    Kuo, Y.M.3    Zemansky, J.4    Gitschier, J.5
  • 55
    • 0034488054 scopus 로고    scopus 로고
    • Cloning and characterization of IAR1, a gene required for auxin conjugate sensitivity in Arabidopsis
    • Lasswell J., Rogg L. E., Nelson D. C., Rongey C. and Bartel B. (2000) Cloning and characterization of IAR1, a gene required for auxin conjugate sensitivity in Arabidopsis. Plant Cell 12: 2395-2408
    • (2000) Plant Cell , vol.12 , pp. 2395-2408
    • Lasswell, J.1    Rogg, L.E.2    Nelson, D.C.3    Rongey, C.4    Bartel, B.5
  • 56
    • 0033581008 scopus 로고    scopus 로고
    • Evidence for a zinc uptake transporter in human prostate cancer cells which is regulated by prolactin and testosterone
    • Costello L. C., Liu Y, Zou J. and Franklin R. B. (1999) Evidence for a zinc uptake transporter in human prostate cancer cells which is regulated by prolactin and testosterone. J. Biol. Chem. 274: 17499-17504
    • (1999) J. Biol. Chem. , vol.274 , pp. 17499-17504
    • Costello, L.C.1    Liu, Y.2    Zou, J.3    Franklin, R.B.4
  • 57
    • 0034792801 scopus 로고    scopus 로고
    • Effects of intracellular zinc depletion on metallothionein and ZIP2 transporter expression and apoptosis
    • Cao J., Bobo J. A., Liuzzi J. P. and Cousins R. J. (2001) Effects of intracellular zinc depletion on metallothionein and ZIP2 transporter expression and apoptosis. J. Leukoc. Biol. 70: 559-566
    • (2001) J. Leukoc. Biol. , vol.70 , pp. 559-566
    • Cao, J.1    Bobo, J.A.2    Liuzzi, J.P.3    Cousins, R.J.4
  • 58
    • 0037229776 scopus 로고    scopus 로고
    • Pancreatic metallothionein-I may play a role in zinc homeostasis during maternal dietary zinc deficiency in mice
    • Lee D. K., Geiser J., Dufner-Beattie J. and Andrews G. K. (2003) Pancreatic metallothionein-I may play a role in zinc homeostasis during maternal dietary zinc deficiency in mice. J. Nutr. 133: 45-50
    • (2003) J. Nutr. , vol.133 , pp. 45-50
    • Lee, D.K.1    Geiser, J.2    Dufner-Beattie, J.3    Andrews, G.K.4
  • 59
    • 0032582651 scopus 로고    scopus 로고
    • Regulation of zinc homeostasis in yeast by binding of the ZAP1 transcriptional activator to zinc-responsive promoter elements
    • Zhao H., Butler E., Rodgers J., Spizzo T., Duesterhoeft S. and Eide D. (1998) Regulation of zinc homeostasis in yeast by binding of the ZAP1 transcriptional activator to zinc-responsive promoter elements. J. Biol. Chem. 273: 28713-28720
    • (1998) J. Biol. Chem. , vol.273 , pp. 28713-28720
    • Zhao, H.1    Butler, E.2    Rodgers, J.3    Spizzo, T.4    Duesterhoeft, S.5    Eide, D.6
  • 60
    • 0032582814 scopus 로고    scopus 로고
    • Zinc-induced inactivation of the yeast ZRT1 zinc transporter occurs through endocytosis and vacuolar degradation
    • Gitan R. S., Luo H., Rodgers J., Broderius M. and Eide D. (1998) Zinc-induced inactivation of the yeast ZRT1 zinc transporter occurs through endocytosis and vacuolar degradation. J. Biol. Chem. 273: 28617-28624
    • (1998) J. Biol. Chem. , vol.273 , pp. 28617-28624
    • Gitan, R.S.1    Luo, H.2    Rodgers, J.3    Broderius, M.4    Eide, D.5
  • 61
    • 0035798192 scopus 로고    scopus 로고
    • Differential subcellular localization of hZip1 in adherent and non-adherent cells
    • Milon B., Dhermy D., Pountney D., Bourgeois M. and Beaumont C. (2001) Differential subcellular localization of hZip1 in adherent and non-adherent cells. FEBS Lett. 507: 241-246
    • (2001) FEBS Lett. , vol.507 , pp. 241-246
    • Milon, B.1    Dhermy, D.2    Pountney, D.3    Bourgeois, M.4    Beaumont, C.5
  • 62
    • 0034660257 scopus 로고    scopus 로고
    • Zinc transporters that regulate vacuolar zinc storage in Saccharomyces cerevisiae
    • MacDiarmid C. W., Gaither L. A. and Eide D. (2000) Zinc transporters that regulate vacuolar zinc storage in Saccharomyces cerevisiae. Embo J. 19: 2845-2855
    • (2000) Embo J. , vol.19 , pp. 2845-2855
    • MacDiarmid, C.W.1    Gaither, L.A.2    Eide, D.3
  • 63
    • 0033393582 scopus 로고    scopus 로고
    • Isolation and characterization of human and mouse ZIRTL, a member of the IRT1 family of transporters, mapping within the epidermal differentiation complex
    • Lioumi M., Ferguson C. A., Sharpe P. T., Freeman T., Marenholz I., Mischke D. et al. (1999) Isolation and characterization of human and mouse ZIRTL, a member of the IRT1 family of transporters, mapping within the epidermal differentiation complex. Genomics 62: 272-280
    • (1999) Genomics , vol.62 , pp. 272-280
    • Lioumi, M.1    Ferguson, C.A.2    Sharpe, P.T.3    Freeman, T.4    Marenholz, I.5    Mischke, D.6
  • 64
    • 0029262430 scopus 로고
    • Subtraction cloning of growth arrest inducible genes in normal human epithelial cells
    • Yamaguchi S. (1995) [Subtraction cloning of growth arrest inducible genes in normal human epithelial cells]. Kokubyo Gakkai Zasshi 62: 78-93
    • (1995) Kokubyo Gakkai Zasshi , vol.62 , pp. 78-93
    • Yamaguchi, S.1
  • 65
    • 0024433859 scopus 로고
    • Clinical and laboratory diagnosis of acrodermatitis enteropathica
    • Van Wouwe J. P. (1989) Clinical and laboratory diagnosis of acrodermatitis enteropathica. Eur. J. Pediatr. 149: 2-8
    • (1989) Eur. J. Pediatr. , vol.149 , pp. 2-8
    • Van Wouwe, J.P.1
  • 67
    • 0018608176 scopus 로고
    • A defect in zinc uptake by jejunal biopsies in acrodermatitis enteropathica
    • Lond
    • Atherton D. J., Muller D. P., Aggett P. J. and Harries J. T. (1979) A defect in zinc uptake by jejunal biopsies in acrodermatitis enteropathica. Clin. Sci, (Lond) 56: 505-507
    • (1979) Clin. Sci. , vol.56 , pp. 505-507
    • Atherton, D.J.1    Muller, D.P.2    Aggett, P.J.3    Harries, J.T.4
  • 68
    • 0016395653 scopus 로고
    • Letter: Acrodermatitis enteropathica: A lethal inherited human zinc-deficiency disorder
    • Moynahan E. J. (1974) Letter: Acrodermatitis enteropathica: a lethal inherited human zinc-deficiency disorder. Lancet 2: 399-400
    • (1974) Lancet , vol.2 , pp. 399-400
    • Moynahan, E.J.1
  • 69
    • 0035074296 scopus 로고    scopus 로고
    • Homozygosity mapping places the acrodermatitis enteropathica gene on chromosomal region 8q24.3
    • Wang K., Pugh E. W., Griffen S., Doheny K. F., Mostafa W. Z., al-Aboosi M. M. et al. (2001) Homozygosity mapping places the acrodermatitis enteropathica gene on chromosomal region 8q24.3. Am. J. Hum. Genet. 68: 1055-1060
    • (2001) Am. J. Hum. Genet. , vol.68 , pp. 1055-1060
    • Wang, K.1    Pugh, E.W.2    Griffen, S.3    Doheny, K.F.4    Mostafa, W.Z.5    Al-Aboosi, M.M.6
  • 70
    • 0036648254 scopus 로고    scopus 로고
    • Identification of SLC39A4, a gene involved in acrodermatitis enteropathica
    • Kury S., Dreno B., Bezieau S., Giraudet S., Kharfi M., Kamoun R. et al. (2002) Identification of SLC39A4, a gene involved in acrodermatitis enteropathica. Nat. Genet. 31: 239-240
    • (2002) Nat. Genet. , vol.31 , pp. 239-240
    • Kury, S.1    Dreno, B.2    Bezieau, S.3    Giraudet, S.4    Kharfi, M.5    Kamoun, R.6
  • 71
    • 0031968380 scopus 로고    scopus 로고
    • Metallothionein knockout and transgenic mice exhibit altered intestinal processing of zinc with uniform zinc-dependent zinc transporter-1 expression
    • Davis S. R., McMahon R. J. and Cousins R. J. (1998) Metallothionein knockout and transgenic mice exhibit altered intestinal processing of zinc with uniform zinc-dependent zinc transporter-1 expression. J. Nutr. 128: 825-831
    • (1998) J. Nutr. , vol.128 , pp. 825-831
    • Davis, S.R.1    McMahon, R.J.2    Cousins, R.J.3
  • 72
    • 0035696465 scopus 로고    scopus 로고
    • Extracellular and immunological actions of zinc
    • Rink L. and Gabriel P. (2001) Extracellular and immunological actions of zinc. Biometals 14: 367-383
    • (2001) Biometals , vol.14 , pp. 367-383
    • Rink, L.1    Gabriel, P.2
  • 73
    • 0023723087 scopus 로고
    • Effects of oestrogen on the expression of a 4.4 kb mRNA in the ZR-75-1 human breast cancer cell line
    • Manning D. L., Daly R. J., Lord P. G., Kelly K. F. and Green C. D. (1988) Effects of oestrogen on the expression of a 4.4 kb mRNA in the ZR-75-1 human breast cancer cell line. Mol. Cell. Endocrinol. 59: 205-212
    • (1988) Mol. Cell. Endocrinol. , vol.59 , pp. 205-212
    • Manning, D.L.1    Daly, R.J.2    Lord, P.G.3    Kelly, K.F.4    Green, C.D.5
  • 74
    • 0030998467 scopus 로고    scopus 로고
    • Interaction between estradiol and growth factors in the regulation of specific gene expression in MCF-7 human breast cancer cells
    • El-Tanani M. K. and Green C. D. (1997) Interaction between estradiol and growth factors in the regulation of specific gene expression in MCF-7 human breast cancer cells. J. Steroid Biochem. Mol. Biol. 60: 269-276
    • (1997) J. Steroid Biochem. Mol. Biol. , vol.60 , pp. 269-276
    • El-Tanani, M.K.1    Green, C.D.2
  • 75
    • 0037028486 scopus 로고    scopus 로고
    • Ermelin, an endoplasmic reticulum transmembrane protein, contains the novel HELP domain conserved in eukaryotes
    • Suzuki A. and Endo T. (2002) Ermelin, an endoplasmic reticulum transmembrane protein, contains the novel HELP domain conserved in eukaryotes. Gene 284: 31-40
    • (2002) Gene , vol.284 , pp. 31-40
    • Suzuki, A.1    Endo, T.2
  • 77
    • 0024114619 scopus 로고
    • Searching for coding sequences in the mammalian genome: The H-2K region of the mouse MHC is replete with genes expressed in embryos
    • Abe K., Wei J. F., Wei F. S., Hsu Y. C., Uehara H., Artzt K. et al. (1988) Searching for coding sequences in the mammalian genome: the H-2K region of the mouse MHC is replete with genes expressed in embryos. Embo J. 7: 3441-3449
    • (1988) Embo J. , vol.7 , pp. 3441-3449
    • Abe, K.1    Wei, J.F.2    Wei, F.S.3    Hsu, Y.C.4    Uehara, H.5    Artzt, K.6
  • 78
    • 0030219462 scopus 로고    scopus 로고
    • cDNA cloning of the human homologues of the mouse Ke4 and Ke6 genes at the centromeric end of the human MHC region
    • Ando A., Kikuti Y. Y., Shigenari A., Kawata H., Okamoto N., Shiina T. et al. (1996) cDNA cloning of the human homologues of the mouse Ke4 and Ke6 genes at the centromeric end of the human MHC region. Genomics 35: 600-602
    • (1996) Genomics , vol.35 , pp. 600-602
    • Ando, A.1    Kikuti, Y.Y.2    Shigenari, A.3    Kawata, H.4    Okamoto, N.5    Shiina, T.6
  • 79
    • 0025174214 scopus 로고
    • A putative transmembrane protein with histidine-rich charge clusters encoded in the H-2K/tw5 region of mice
    • St-Jacques B., Han T. H., MacMurray A. and Shin H. S. (1990) A putative transmembrane protein with histidine-rich charge clusters encoded in the H-2K/tw5 region of mice. Mol. Cell. Biol. 10: 138-145
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 138-145
    • St-Jacques, B.1    Han, T.H.2    MacMurray, A.3    Shin, H.S.4
  • 80
    • 0032829708 scopus 로고    scopus 로고
    • The catecholamines up (Catsup) protein of Drosophila melanogaster functions as a negative regulator of tyrosine hydroxylase activity
    • Stathakis D. G., Burton D. Y., McIvor W. E., Krishnakumar S., Wright T. R. and O'Donnell J. M. (1999) The catecholamines up (Catsup) protein of Drosophila melanogaster functions as a negative regulator of tyrosine hydroxylase activity. Genetics 153: 361-382
    • (1999) Genetics , vol.153 , pp. 361-382
    • Stathakis, D.G.1    Burton, D.Y.2    McIvor, W.E.3    Krishnakumar, S.4    Wright, T.R.5    O'Donnell, J.M.6
  • 81
    • 12444276104 scopus 로고
    • Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1
    • Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S. et al. (1994) Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 1: 223-229
    • (1994) DNA Res. , vol.1 , pp. 223-229
    • Nomura, N.1    Nagase, T.2    Miyajima, N.3    Sazuka, T.4    Tanaka, A.5    Sato, S.6
  • 82
    • 0033615363 scopus 로고    scopus 로고
    • Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro
    • Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N. and Ohara O. (1999) Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 6: 337-345
    • (1999) DNA Res. , vol.6 , pp. 337-345
    • Nagase, T.1    Ishikawa, K.2    Kikuno, R.3    Hirosawa, M.4    Nomura, N.5    Ohara, O.6
  • 83
    • 0029071561 scopus 로고
    • Ion efflux systems involved in bacterial metal resistances
    • Nies D. H. and Silver S. (1995) Ion efflux systems involved in bacterial metal resistances. J. Ind. Microbiol. 14: 186-199
    • (1995) J. Ind. Microbiol. , vol.14 , pp. 186-199
    • Nies, D.H.1    Silver, S.2
  • 84
    • 0026732140 scopus 로고
    • CzcR and CzcD, gene products affecting regulation of resistance to cobalt, zinc and cadmium (czc system) in Alcaligenes eutrophus
    • Nies D. H. (1992) CzcR and CzcD, gene products affecting regulation of resistance to cobalt, zinc and cadmium (czc system) in Alcaligenes eutrophus. J. Bacteriol. 174: 8102-8110
    • (1992) J. Bacteriol. , vol.174 , pp. 8102-8110
    • Nies, D.H.1
  • 85
    • 0024741152 scopus 로고
    • Identification of a gene conferring resistance to zinc and cadmium ions in the yeast Saccharomyces cerevisiae
    • Kamizono A., Nishizawa M., Teranishi Y., Murata K. and Kimura A. (1989) Identification of a gene conferring resistance to zinc and cadmium ions in the yeast Saccharomyces cerevisiae. Mol. Gen. Genet. 219: 161-167
    • (1989) Mol. Gen. Genet. , vol.219 , pp. 161-167
    • Kamizono, A.1    Nishizawa, M.2    Teranishi, Y.3    Murata, K.4    Kimura, A.5
  • 86
    • 0026707878 scopus 로고
    • COT1, a gene involved in cobalt accumulation in Saccharomyces cerevisiae
    • Conklin D. S., McMaster J. A., Culbertson M. R. and Kung C. (1992) COT1, a gene involved in cobalt accumulation in Saccharomyces cerevisiae. Mol. Cell. Biol. 12: 3678-3688
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3678-3688
    • Conklin, D.S.1    McMaster, J.A.2    Culbertson, M.R.3    Kung, C.4
  • 87
    • 0028948696 scopus 로고
    • Cloning and functional characterization of a mammalian zinc transporter that confers resistance to zinc
    • Palmiter R. D. and Findley S. D. (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
  • 88
    • 0344578041 scopus 로고    scopus 로고
    • CzcD is a heavy metal ion transporter involved in regulation of heavy metal resistance in Ralstonia sp. strain CH34
    • Anton A., Grosse C., Reissmann J., Pribyl T. and Nies D. H. (1999) CzcD is a heavy metal ion transporter involved in regulation of heavy metal resistance in Ralstonia sp. strain CH34. J. Bacteriol. 181: 6876-6881
    • (1999) J. Bacteriol. , vol.181 , pp. 6876-6881
    • Anton, A.1    Grosse, C.2    Reissmann, J.3    Pribyl, T.4    Nies, D.H.5
  • 90
    • 0033369167 scopus 로고    scopus 로고
    • Cloning, expression and vesicular localization of zinc transporter Dri 27/ZnT4 in intestinal tissue and cells
    • Murgia C., Vespignani I., Cerase J., Nobili F. and Perozzi G. (1999) Cloning, expression and vesicular localization of zinc transporter Dri 27/ZnT4 in intestinal tissue and cells. Am. J. Physiol. 277: G1231-1239
    • (1999) Am. J. Physiol. , vol.277
    • Murgia, C.1    Vespignani, I.2    Cerase, J.3    Nobili, F.4    Perozzi, G.5
  • 91
    • 0346634896 scopus 로고    scopus 로고
    • Characterization of the ZAT1p zinc transporter from Arabidopsis thaliana in microbial model organisms and reconstituted proteoliposomes
    • Bloss T., Clemens S. and Nies D. H. (2002) Characterization of the ZAT1p zinc transporter from Arabidopsis thaliana in microbial model organisms and reconstituted proteoliposomes. Planta 214: 783-791
    • (2002) Planta , vol.214 , pp. 783-791
    • Bloss, T.1    Clemens, S.2    Nies, D.H.3
  • 92
    • 0035859817 scopus 로고    scopus 로고
    • Functional activity and role of cation-efflux family members in Ni hyperaccumulation in Thlaspi goesingense
    • Persans M. W., Nieman K. and Salt D. E. (2001) Functional activity and role of cation-efflux family members in Ni hyperaccumulation in Thlaspi goesingense. Proc. Natl. Acad. Sci. USA 98: 9995-10000
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 9995-10000
    • Persans, M.W.1    Nieman, K.2    Salt, D.E.3
  • 94
    • 0037131363 scopus 로고    scopus 로고
    • Biochemical properties of vacuolar zinc transport systems of Saccharomyces cerevisiae
    • MacDiarmid C. W., Milanick M. A. and Eide D. J. (2002) Biochemical properties of vacuolar zinc transport systems of Saccharomyces cerevisiae. J. Biol. Chem. 277: 39187-39194
    • (2002) J. Biol. Chem. , vol.277 , pp. 39187-39194
    • MacDiarmid, C.W.1    Milanick, M.A.2    Eide, D.J.3
  • 95
    • 0030724951 scopus 로고    scopus 로고
    • A novel gene involved in zinc transport is deficient in the lethal milk mouse
    • Huang L. and Gitschier J. (1997) A novel gene involved in zinc transport is deficient in the lethal milk mouse. Nat. Genet. 17: 292-297
    • (1997) Nat. Genet. , vol.17 , pp. 292-297
    • Huang, L.1    Gitschier, J.2
  • 96
    • 0029873677 scopus 로고    scopus 로고
    • ZnT-2, a mammalian protein that confers resistance to zinc by facilitating vesicular sequestration
    • Palmiter R. D., Cole T. B. and Findley S. D. (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
  • 97
    • 0030839480 scopus 로고    scopus 로고
    • Expression of zinc transporter gene, ZnT-1, is induced after transient forebrain ischemia in the gerbil
    • Tsuda M., Imaizumi K., Katayama T., Kitagawa K., Wanaka A., Tohyama M. et al. (1997) Expression of zinc transporter gene, ZnT-1, is induced after transient forebrain ischemia in the gerbil. J. Neurosci. 17: 6678-6684
    • (1997) J. Neurosci. , vol.17 , pp. 6678-6684
    • Tsuda, M.1    Imaizumi, K.2    Katayama, T.3    Kitagawa, K.4    Wanaka, A.5    Tohyama, M.6
  • 98
    • 0032574826 scopus 로고    scopus 로고
    • Regulation of the zinc transporter ZnT-1 by dietary zinc
    • McMahon R. J. and Cousins R. J. (1998) Regulation of the zinc transporter ZnT-1 by dietary zinc. Proc. Natl. Acad. Sci. USA 95: 4841-4846
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4841-4846
    • McMahon, R.J.1    Cousins, R.J.2
  • 99
    • 0034602175 scopus 로고    scopus 로고
    • The transcription factor MTF-1 mediates metal regulation of the mouse ZnT1 gene
    • Langmade S. J., Ravindra R., Daniels P. J. and Andrews G. K. (2000) The transcription factor MTF-1 mediates metal regulation of the mouse ZnT1 gene. J. Biol. Chem. 275: 34803-34809
    • (2000) J. Biol. Chem. , vol.275 , pp. 34803-34809
    • Langmade, S.J.1    Ravindra, R.2    Daniels, P.J.3    Andrews, G.K.4
  • 100
    • 0035181875 scopus 로고    scopus 로고
    • Differential regulation of zinc transporter 1, 2 and 4 mRNA expression by dietary zinc in rats
    • Liuzzi J. P., Blanchard R. K. and Cousins R. J. (2001) Differential regulation of zinc transporter 1, 2 and 4 mRNA expression by dietary zinc in rats. J. Nutr. 131: 46-52
    • (2001) J. Nutr. , vol.131 , pp. 46-52
    • Liuzzi, J.P.1    Blanchard, R.K.2    Cousins, R.J.3
  • 102
    • 0037135606 scopus 로고    scopus 로고
    • Functional characterization of a novel mammalian zinc transporter, ZnT6
    • Huang L., Kirschke C. P., and Gitschier J. (2002) Functional characterization of a novel mammalian zinc transporter, ZnT6. J. Biol. Chem. 277: 26389-26395
    • (2002) J. Biol. Chem. , vol.277 , pp. 26389-26395
    • Huang, L.1    Kirschke, C.P.2    Gitschier, J.3
  • 103
    • 0032819199 scopus 로고    scopus 로고
    • A local, high-density, single-nucleotide polymorphism map used to clone Caenorhabditis elegans cdf-1
    • Jakubowski J. and Kornfeld K. (1999) A local, high-density, single-nucleotide polymorphism map used to clone Caenorhabditis elegans cdf-1. Genetics 153: 743-752
    • (1999) Genetics , vol.153 , pp. 743-752
    • Jakubowski, J.1    Kornfeld, K.2
  • 104
    • 0036102081 scopus 로고    scopus 로고
    • Zinc ions and cation diffusion facilitator proteins regulate Ras-mediated signaling
    • Bruinsma J. J., Jirakulaporn T., MuslinA. J., and Kornfeld K. (2002) Zinc ions and cation diffusion facilitator proteins regulate Ras-mediated signaling. Dev. Cell 2: 567-578
    • (2002) Dev. Cell , vol.2 , pp. 567-578
    • Bruinsma, J.J.1    Jirakulaporn, T.2    Muslin, A.J.3    Kornfeld, K.4
  • 105
    • 0036279149 scopus 로고    scopus 로고
    • 2+) makes the difference
    • 2+) makes the difference. Mol. Cell. 9: 927-928
    • (2002) Mol. Cell. , vol.9 , pp. 927-928
    • Hajnal, A.1
  • 106
    • 0035696187 scopus 로고    scopus 로고
    • Cellular zinc sensors: MTF-1 regulation of gene expression
    • Andrews G. K. (2001) Cellular zinc sensors: MTF-1 regulation of gene expression. Biometals 14: 223-237
    • (2001) Biometals , vol.14 , pp. 223-237
    • Andrews, G.K.1
  • 108
    • 0037013710 scopus 로고    scopus 로고
    • Distribution of the zinc transporter ZnT-1 in comparison with chelatable zinc in the mouse brain
    • Sekler I., Moran A., Hershfinkel M., Dori A., Margulis A., Birenzweig N. et al. (2002) Distribution of the zinc transporter ZnT-1 in comparison with chelatable zinc in the mouse brain. J. Comp. Neurol. 447: 201-209
    • (2002) J. Comp. Neurol. , vol.447 , pp. 201-209
    • Sekler, I.1    Moran, A.2    Hershfinkel, M.3    Dori, A.4    Margulis, A.5    Birenzweig, N.6
  • 109
  • 110
    • 0036845298 scopus 로고    scopus 로고
    • Zinc transporters in the rat mammary gland respond to marginal zinc and vitamin a intakes during lactation
    • Kelleher S. L. and Lonnerdal B. (2002) Zinc transporters in the rat mammary gland respond to marginal zinc and vitamin A intakes during lactation. J. Nutr. 132: 3280-3285
    • (2002) J. Nutr. , vol.132 , pp. 3280-3285
    • Kelleher, S.L.1    Lonnerdal, B.2
  • 111
    • 0037315905 scopus 로고    scopus 로고
    • Zinc transporters 1, 2 and 4 are differentially expressed and localized in rats during pregnancy and lactation
    • Liuzzi J. P., Bobo J. A., Cui L., McMahon R. J. and Cousins R. J. (2003) Zinc transporters 1, 2 and 4 are differentially expressed and localized in rats during pregnancy and lactation. J. Nutr. 133: 342-351
    • (2003) J. Nutr. , vol.133 , pp. 342-351
    • Liuzzi, J.P.1    Bobo, J.A.2    Cui, L.3    McMahon, R.J.4    Cousins, R.J.5
  • 112
    • 0036868477 scopus 로고    scopus 로고
    • High-level expression of zinc transporter-2 in the rat lateral and dorsal prostate
    • Iguchi K., Usui S., Inoue T., Sugimura Y., Tatematsu M. and Hirano K. (2002) High-level expression of zinc transporter-2 in the rat lateral and dorsal prostate. J. Androl. 23: 819-824
    • (2002) J. Androl. , vol.23 , pp. 819-824
    • Iguchi, K.1    Usui, S.2    Inoue, T.3    Sugimura, Y.4    Tatematsu, M.5    Hirano, K.6
  • 113
    • 0015833040 scopus 로고
    • Prenatal and postnatal development after transitory gestational zinc deficiency in rats
    • Hurley L. S. and Mutch P. B. (1973) Prenatal and postnatal development after transitory gestational zinc deficiency in rats. J. Nutr. 103: 649-656
    • (1973) J. Nutr. , vol.103 , pp. 649-656
    • Hurley, L.S.1    Mutch, P.B.2
  • 114
    • 0024595958 scopus 로고
    • Zinc and cadmium concentrations in indigenous blacks with normal, hypertrophic and malignant prostate
    • Ogunlewe J. O. and Osegbe D. N. (1989) Zinc and cadmium concentrations in indigenous blacks with normal, hypertrophic and malignant prostate. Cancer 63: 1388-1392
    • (1989) Cancer , vol.63 , pp. 1388-1392
    • Ogunlewe, J.O.1    Osegbe, D.N.2
  • 115
    • 0037123746 scopus 로고    scopus 로고
    • Relationship between zinc and neurotransmitters released into the amygdalar extracellular space
    • Minami A., Takeda A., Yamaide R. and Oku N. (2002) Relationship between zinc and neurotransmitters released into the amygdalar extracellular space. Brain Res. 936: 91-94
    • (2002) Brain Res. , vol.936 , pp. 91-94
    • Minami, A.1    Takeda, A.2    Yamaide, R.3    Oku, N.4
  • 117
    • 0030731726 scopus 로고    scopus 로고
    • Ultrastructural localization of zinc transporter-3 (ZnT-3) to synaptic vesicle membranes within mossy fiber boutons in the hippocampus of mouse and monkey
    • Wenzel H. J., Cole T. B., Born D. E., Schwartzkroin P. A. and Palmiter R. D. (1997) Ultrastructural localization of zinc transporter-3 (ZnT-3) to synaptic vesicle membranes within mossy fiber boutons in the hippocampus of mouse and monkey. Proc. Natl. Acad. Sci. USA 94: 12676-12681
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12676-12681
    • Wenzel, H.J.1    Cole, T.B.2    Born, D.E.3    Schwartzkroin, P.A.4    Palmiter, R.D.5
  • 118
    • 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. and Koh J. Y. (2002) 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) 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
  • 119
    • 0004586594 scopus 로고    scopus 로고
    • Zinc-enriched (ZEN) terminals in mouse spinal cord: Immunohistochemistry and autometallography
    • Jo S. M., Danscher G., Daa Schroder H., Won M. H. and Cole T. B. (2000) Zinc-enriched (ZEN) terminals in mouse spinal cord: immunohistochemistry and autometallography. Brain Res. 870: 163-169
    • (2000) Brain Res. , vol.870 , pp. 163-169
    • Jo, S.M.1    Danscher, G.2    Daa Schroder, H.3    Won, M.H.4    Cole, T.B.5
  • 121
    • 0035824283 scopus 로고    scopus 로고
    • Zinc-enriched GABAergic terminals in mouse spinal cord
    • Wang Z., Li J. Y., Dahlstrom A. and Danscher G. (2001) Zinc-enriched GABAergic terminals in mouse spinal cord. Brain Res. 921: 165-172
    • (2001) Brain Res. , vol.921 , pp. 165-172
    • Wang, Z.1    Li, J.Y.2    Dahlstrom, A.3    Danscher, G.4
  • 122
    • 0037087217 scopus 로고    scopus 로고
    • Inhibitory zinc-enriched terminals in the mouse cerebellum: Double-immunohistochemistry for zinc transporter 3 and glutamate decarboxylase
    • Wang Z., Danscher G., Kim Y. K., Dahlstrom A. and Mook Jo S. (2002) Inhibitory zinc-enriched terminals in the mouse cerebellum: double- immunohistochemistry for zinc transporter 3 and glutamate decarboxylase. Neurosci. Lett. 321: 37-40
    • (2002) Neurosci. Lett. , vol.321 , pp. 37-40
    • Wang, Z.1    Danscher, G.2    Kim, Y.K.3    Dahlstrom, A.4    Mook Jo, S.5
  • 123
    • 0021287299 scopus 로고
    • 2+ from brain tissue during activity
    • 2+ from brain tissue during activity. Nature 308: 734-736
    • (1984) Nature , vol.308 , pp. 734-736
    • Assaf, S.Y.1    Chung, S.H.2
  • 124
    • 0031456815 scopus 로고    scopus 로고
    • Metal ions and synaptic transmission: Think zinc
    • Huang E. P. (1997) Metal ions and synaptic transmission: think zinc. Proc. Natl. Acad. Sci. USA 94: 13386-13387
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13386-13387
    • Huang, E.P.1
  • 125
    • 0028170444 scopus 로고
    • 2-: An endogenous modulator of ligand- and voltage-gated ion channels
    • 2-: an endogenous modulator of ligand- and voltage-gated ion channels. Neuropharmacology 33: 935-952
    • (1994) Neuropharmacology , vol.33 , pp. 935-952
    • Harrison, N.L.1    Gibbons, S.J.2
  • 126
    • 0028354969 scopus 로고
    • Modulation of inhibitory and excitatory amino acid receptor ion channels by zinc
    • Smart T. G., Xie X. and Krishek B. J. (1994) Modulation of inhibitory and excitatory amino acid receptor ion channels by zinc. Prog. Neurobiol. 42: 393-341
    • (1994) Prog. Neurobiol. , vol.42 , pp. 393-1341
    • Smart, T.G.1    Xie, X.2    Krishek, B.J.3
  • 127
    • 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. and Palmiter R. D. (2001) Removing zinc from synaptic vesicles does not impair spatial learning, memory or sensorimotor functions in the mouse. Brain Res. 891: 253-265
    • (2001) Brain Res. , vol.891 , pp. 253-265
    • Cole, T.B.1    Martyanova, A.2    Palmiter, R.D.3
  • 128
    • 0037439069 scopus 로고    scopus 로고
    • Lack of vesicular zinc in mossy fibers does not affect synaptic excitability of CA3 pyramidal cells in zinc transporter 3 knockout mice
    • Lopantsev V., Wenzel H. J., Cole T. B., Palmiter R. D. and Schwartzkroin P. A. (2003) Lack of vesicular zinc in mossy fibers does not affect synaptic excitability of CA3 pyramidal cells in zinc transporter 3 knockout mice. Neuroscience 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
  • 130
    • 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. and Koh J. Y. (2000) Accumulation of zinc in degenerating hippocampal neurons of ZnT3-null mice after seizures: evidence against synaptic vesicle origin. J. Neurosci. 20: RC79
    • (2000) J. Neurosci. , vol.20
    • Lee, J.Y.1    Cole, T.B.2    Palmiter, R.D.3    Koh, J.Y.4
  • 132
    • 0037188472 scopus 로고    scopus 로고
    • The galvanization of beta-amyloid in Alzheimer's disease
    • Bush A. I. and Tanzi R. E. (2002) The galvanization of beta-amyloid in Alzheimer's disease. Proc. Natl. Acad. Sci. USA 99: 7317-7319
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7317-7319
    • Bush, A.I.1    Tanzi, R.E.2
  • 133
    • 0032557425 scopus 로고    scopus 로고
    • Dramatic aggregation of Alzheimer abeta by Cu(II) is induced by conditions representing physiological acidosis
    • Atwood C. S., Moir R. D., Huang X., Scarpa R. C., Bacarra N. M., Romano D. M. et al. (1998) Dramatic aggregation of Alzheimer abeta by Cu(II) is induced by conditions representing physiological acidosis. J. Biol. Chem. 273: 12817-12826
    • (1998) J. Biol. Chem. , vol.273 , pp. 12817-12826
    • Atwood, C.S.1    Moir, R.D.2    Huang, X.3    Scarpa, R.C.4    Bacarra, N.M.5    Romano, D.M.6
  • 134
    • 0029742199 scopus 로고    scopus 로고
    • Correlative memory deficits, Abeta elevation and amyloid plaques in transgenic mice
    • Hsiao K., Chapman P., Nilsen S., Eckman C., Harigaya Y., Younkin S. et al. (1996) Correlative memory deficits, Abeta elevation and amyloid plaques in transgenic mice. Science 274: 99-102
    • (1996) Science , vol.274 , pp. 99-102
    • Hsiao, K.1    Chapman, P.2    Nilsen, S.3    Eckman, C.4    Harigaya, Y.5    Younkin, S.6
  • 136
    • 0034964390 scopus 로고    scopus 로고
    • Treatment with a copper-zinc chelator markedly and rapidly inhibits beta-amyloid accumulation in Alzheimer's disease transgenic mice
    • Cherny R. A., Atwood C. S., Xilinas M. E., Gray D. N., Jones W. D., McLean C. A. et al. (2001) Treatment with a copper-zinc chelator markedly and rapidly inhibits beta-amyloid accumulation in Alzheimer's disease transgenic mice. Neuron 30: 665-676
    • (2001) Neuron , vol.30 , pp. 665-676
    • Cherny, R.A.1    Atwood, C.S.2    Xilinas, M.E.3    Gray, D.N.4    Jones, W.D.5    McLean, C.A.6
  • 137
    • 0017870725 scopus 로고
    • Zinc deficiency in murine milk underlies expression of the lethal milk (lm) mutation
    • Piletz J. E. and Ganschow R. E. (1978) Zinc deficiency in murine milk underlies expression of the lethal milk (lm) mutation. Science 199: 181-183
    • (1978) Science , vol.199 , pp. 181-183
    • Piletz, J.E.1    Ganschow, R.E.2
  • 138
    • 0021814726 scopus 로고
    • Studies in human lactation: Zinc, copper, manganese and chromium in human milk in the first month of lactation
    • Casey C. E., Hambidge K. M. and Neville M. C. (1985) Studies in human lactation: zinc, copper, manganese and chromium in human milk in the first month of lactation. Am. J. Clin. Nutr. 41: 1193-1200
    • (1985) Am. J. Clin. Nutr. , vol.41 , pp. 1193-1200
    • Casey, C.E.1    Hambidge, K.M.2    Neville, M.C.3
  • 139
    • 0037093455 scopus 로고    scopus 로고
    • Constitutive expression of hZnT4 zinc transporter in human breast epithelial cells
    • Michalczyk A. A., Allen J., Blomeley R. C. and Ackland M. L. (2002) Constitutive expression of hZnT4 zinc transporter in human breast epithelial cells. Biochem. J. 364: 105-113
    • (2002) Biochem. J. , vol.364 , pp. 105-113
    • Michalczyk, A.A.1    Allen, J.2    Blomeley, R.C.3    Ackland, M.L.4
  • 140
    • 0020569082 scopus 로고
    • Toxic milk, a new mutation affecting cooper metabolism in the mouse
    • Rauch H. (1983) Toxic milk, a new mutation affecting cooper metabolism in the mouse. J. Hered. 74: 141-144
    • (1983) J. Hered. , vol.74 , pp. 141-144
    • Rauch, H.1
  • 141
    • 0034535614 scopus 로고    scopus 로고
    • Defective localization of the Wilson disease protein (ATP7B) in the mammary gland of the toxic milk mouse and the effects of copper supplementation
    • Michalczyk A. A., Rieger J., Allen K. J., Mercer J. F. and Ackland M. L. (2000) Defective localization of the Wilson disease protein (ATP7B) in the mammary gland of the toxic milk mouse and the effects of copper supplementation. Biochem. J. 352 Pt 2: 565-571
    • (2000) Biochem. J. , vol.352 , Issue.2 PART , pp. 565-571
    • Michalczyk, A.A.1    Rieger, J.2    Allen, K.J.3    Mercer, J.F.4    Ackland, M.L.5
  • 142
    • 0030803730 scopus 로고    scopus 로고
    • Biochemical characterization of the Wilson disease protein and functional expression in the yeast Saccharomyces cerevisiae
    • Hung I. H., Suzuki M., Yamaguchi Y., Yuan D. S., Klausner R. D. and Gitlin J. D. (1997) Biochemical characterization of the Wilson disease protein and functional expression in the yeast Saccharomyces cerevisiae. J. Biol. Chem. 272: 21461-21466
    • (1997) J. Biol. Chem. , vol.272 , pp. 21461-21466
    • Hung, I.H.1    Suzuki, M.2    Yamaguchi, Y.3    Yuan, D.S.4    Klausner, R.D.5    Gitlin, J.D.6
  • 143
    • 0028108574 scopus 로고
    • Subtractive hybridization cloning of novel genes differentially expressed during intestinal development
    • Barila D., Murgia C., Nobili F., Gaetani S. and Perozzi G. (1994) Subtractive hybridization cloning of novel genes differentially expressed during intestinal development. Eur. J. Biochem. 223: 701-709
    • (1994) Eur. J. Biochem. , vol.223 , pp. 701-709
    • Barila, D.1    Murgia, C.2    Nobili, F.3    Gaetani, S.4    Perozzi, G.5
  • 144
    • 0036890215 scopus 로고    scopus 로고
    • Intracellular distribution of labile Zn(II) and zinc transporter expression in the kidney and in MDCK cells
    • Ranaldi G., Perozzi G., Truong-Tran A., Zalewski P. and Murgia C. (2002) Intracellular distribution of labile Zn(II) and zinc transporter expression in the kidney and in MDCK cells. Am. J. Physiol. Renal Physiol. 283: F1365-1375
    • (2002) Am. J. Physiol. Renal Physiol. , vol.283
    • Ranaldi, G.1    Perozzi, G.2    Truong-Tran, A.3    Zalewski, P.4    Murgia, C.5
  • 145
    • 0021751131 scopus 로고
    • Zinc metabolism in lethal-milk mice. Otolith, lactation and aging effects
    • Erway L. C. and Grider A. Jr. (1984) Zinc metabolism in lethal-milk mice. Otolith, lactation and aging effects. J. Hered. 75: 480-484
    • (1984) J. Hered. , vol.75 , pp. 480-484
    • Erway, L.C.1    Grider Jr., A.2
  • 146
    • 0034839157 scopus 로고    scopus 로고
    • Expression pattern, genomic structure and evaluation of the human SLC30A4 gene as a candidate for acrodermatitis enteropathica
    • Kury S., Devilder M. C., Avet-Loiseau H., Dreno B. and Moisan J. P. (2001) Expression pattern, genomic structure and evaluation of the human SLC30A4 gene as a candidate for acrodermatitis enteropathica. Hum. Genet. 109: 178-185
    • (2001) Hum. Genet. , vol.109 , pp. 178-185
    • Kury, S.1    Devilder, M.C.2    Avet-Loiseau, H.3    Dreno, B.4    Moisan, J.P.5
  • 147
    • 0034798254 scopus 로고    scopus 로고
    • Genomic localization, organization and amplification of the human zinc transporter protein gene, ZNT4, and exclusion as a candidate gene in different clinical variants of acrodermatitis enteropathica
    • Bleck O., Ashton G. H., Mallipeddi R., South A. P., Whittock N. V., McLean W. H. et al. (2001) Genomic localization, organization and amplification of the human zinc transporter protein gene, ZNT4, and exclusion as a candidate gene in different clinical variants of acrodermatitis enteropathica. Arch. Dermatol. Res. 293: 392-396
    • (2001) Arch. Dermatol. Res. , vol.293 , pp. 392-396
    • Bleck, O.1    Ashton, G.H.2    Mallipeddi, R.3    South, A.P.4    Whittock, N.V.5    McLean, W.H.6
  • 148
    • 0036488035 scopus 로고    scopus 로고
    • ZNT4 gene is not responsible for acrodermatitis enteropathica in Japanese families
    • Nakano A., Nakano H., Hanada K., Nomura K. and Uitto J. (2002) ZNT4 gene is not responsible for acrodermatitis enteropathica in Japanese families. Hum. Genet. 110: 201-202
    • (2002) Hum. Genet. , vol.110 , pp. 201-202
    • Nakano, A.1    Nakano, H.2    Hanada, K.3    Nomura, K.4    Uitto, J.5
  • 149
    • 0026354372 scopus 로고
    • Effects of carbonic anhydrase inhibitor on the otolithic organs of developing chick embryos
    • Kido T., Sekitani T., Yamashita H., Endo S., Masumitsu Y. and Shimogori H. (1991) Effects of carbonic anhydrase inhibitor on the otolithic organs of developing chick embryos. Am. J. Otolaryngol. 12: 191-195
    • (1991) Am. J. Otolaryngol. , vol.12 , pp. 191-195
    • Kido, T.1    Sekitani, T.2    Yamashita, H.3    Endo, S.4    Masumitsu, Y.5    Shimogori, H.6
  • 150
    • 0037166325 scopus 로고    scopus 로고
    • Cloning and characterization of a novel mammalian zinc transporter, zinc transporter 5, abundantly expressed in pancreatic beta cells
    • Kambe T., Narita H., Yamaguchi-Iwai Y., Hirose J., Amano T., Sugiura N. et al. (2002) Cloning and characterization of a novel mammalian zinc transporter, zinc transporter 5, abundantly expressed in pancreatic beta cells. J. Biol. Chem. 277: 19049-19055
    • (2002) J. Biol. Chem. , vol.277 , pp. 19049-19055
    • Kambe, T.1    Narita, H.2    Yamaguchi-Iwai, Y.3    Hirose, J.4    Amano, T.5    Sugiura, N.6
  • 151
    • 0037151036 scopus 로고    scopus 로고
    • A novel zinc-regulated human zinc transporter, hZTL1, is localized to the enterocyte apical membrane
    • Cragg R. A., Christie G. R., Phillips S. R., Russi R. M., Kury S., Mathers J. C. et al. (2002) A novel zinc-regulated human zinc transporter, hZTL1, is localized to the enterocyte apical membrane. J. Biol. Chem. 277: 22789-22797
    • (2002) J. Biol. Chem. , vol.277 , pp. 22789-22797
    • Cragg, R.A.1    Christie, G.R.2    Phillips, S.R.3    Russi, R.M.4    Kury, S.5    Mathers, J.C.6
  • 152
    • 0037098959 scopus 로고    scopus 로고
    • Osteopenia and male-specific sudden cardiac death in mice lacking a zinc transporter gene, Znt5
    • Inoue K., Matsuda K., Itoh M., Kawaguchi H., Tomoike H., Aoyagi T. et al. (2002) Osteopenia and male-specific sudden cardiac death in mice lacking a zinc transporter gene, Znt5. Hum. Mol. Genet. 11: 1775-1784
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1775-1784
    • Inoue, K.1    Matsuda, K.2    Itoh, M.3    Kawaguchi, H.4    Tomoike, H.5    Aoyagi, T.6
  • 153
    • 0035895955 scopus 로고    scopus 로고
    • The yeast gene MSC2, a member of the cation diffusion facilitator family, affects the cellular distribution of zinc
    • Li L. and Kaplan J. (2001) The yeast gene MSC2, a member of the cation diffusion facilitator family, affects the cellular distribution of zinc. J. Biol. Chem. 276: 5036-5043
    • (2001) J. Biol. Chem. , vol.276 , pp. 5036-5043
    • Li, L.1    Kaplan, J.2
  • 154
    • 0032054714 scopus 로고    scopus 로고
    • The role of assembly in insulin's biosynthesis
    • Dodson G. and Steiner D. (1998) The role of assembly in insulin's biosynthesis. Curr. Opin. Struct. Biol. 8: 189-194
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 189-194
    • Dodson, G.1    Steiner, D.2
  • 155
    • 0033839040 scopus 로고    scopus 로고
    • Survey of mRNAs encoding zinc transporters and other metal complexing proteins in pancreatic islets of rats from birth to adulthood: Similar patterns in the Sprague-Dawley and Wistar BB strains
    • Clifford K. S. and MacDonald M. J. (2000) Survey of mRNAs encoding zinc transporters and other metal complexing proteins in pancreatic islets of rats from birth to adulthood: similar patterns in the Sprague-Dawley and Wistar BB strains. Diabetes Res. Clin. Pract. 49: 77-85
    • (2000) Diabetes Res. Clin. Pract. , vol.49 , pp. 77-85
    • Clifford, K.S.1    MacDonald, M.J.2
  • 156
    • 0021839667 scopus 로고
    • Properties of membrane-bound and solubilized forms of alkaline phosphatase from human liver
    • Chakrabartty A. and Stinson R. A. (1985) Properties of membrane-bound and solubilized forms of alkaline phosphatase from human liver. Biochim. Biophys. Acta 839: 174-180
    • (1985) Biochim. Biophys. Acta , vol.839 , pp. 174-180
    • Chakrabartty, A.1    Stinson, R.A.2
  • 157
    • 0033386205 scopus 로고    scopus 로고
    • Alkaline phosphatase knock-out mice recapitulate the metabolic and skeletal defects of infantile hypophosphatasia
    • Fedde K. N., Blair L., Silverstein J., Coburn S. P., Ryan L. M., Weinstein R. S. et al. (1999) Alkaline phosphatase knock-out mice recapitulate the metabolic and skeletal defects of infantile hypophosphatasia. J. Bone Miner. Res. 14: 2015-2026
    • (1999) J. Bone Miner. Res. , vol.14 , pp. 2015-2026
    • Fedde, K.N.1    Blair, L.2    Silverstein, J.3    Coburn, S.P.4    Ryan, L.M.5    Weinstein, R.S.6
  • 158
    • 0027930471 scopus 로고
    • Hypophosphatasia and the role of alkaline phosphatase in skeletal mineralization
    • Whyte M. P. (1994) Hypophosphatasia and the role of alkaline phosphatase in skeletal mineralization. Endocr. Rev. 15: 439-461
    • (1994) Endocr. Rev. , vol.15 , pp. 439-461
    • Whyte, M.P.1
  • 159
    • 0029909937 scopus 로고    scopus 로고
    • Ligand-regulated transport of the Menkes copper P-type ATPase efflux pump from the Golgi apparatus to the plasma membrane: A novel mechanism of regulated trafficking
    • Petris M. J., Mercer J. F., Culvenor J. G., Lockhart P, Gleeson P. A. and Camakaris J. (1996) Ligand-regulated transport of the Menkes copper P-type ATPase efflux pump from the Golgi apparatus to the plasma membrane: a novel mechanism of regulated trafficking. Embo J. 15: 6084-6095
    • (1996) Embo J. , vol.15 , pp. 6084-6095
    • Petris, M.J.1    Mercer, J.F.2    Culvenor, J.G.3    Lockhart, P.4    Gleeson, P.A.5    Camakaris, J.6
  • 160
    • 0037423203 scopus 로고    scopus 로고
    • ZnT7, a novel mammalian zinc transporter, accumulates zinc in the Golgi apparatus
    • Kirschke C. P. and Huang L. (2003) ZnT7, a novel mammalian zinc transporter, accumulates zinc in the Golgi apparatus. J. Biol. Chem. 278: 4096-4102
    • (2003) J. Biol. Chem. , vol.278 , pp. 4096-4102
    • Kirschke, C.P.1    Huang, L.2
  • 162
    • 0032126699 scopus 로고    scopus 로고
    • Mutation in AP-3 delta in the mocha mouse links endosomal transport to storage deficiency in platelets, melanosomes and synaptic vesicles
    • Kantheti P., Qiao X., Diaz M. E., Peden A. A., Meyer G. E., Carskadon S. L. et al. (1998) Mutation in AP-3 delta in the mocha mouse links endosomal transport to storage deficiency in platelets, melanosomes and synaptic vesicles. Neuron 21: 111-122
    • (1998) Neuron , vol.21 , pp. 111-122
    • Kantheti, P.1    Qiao, X.2    Diaz, M.E.3    Peden, A.A.4    Meyer, G.E.5    Carskadon, S.L.6
  • 163
    • 0021433332 scopus 로고
    • Trace metals and otolith defects in mocha mice
    • Rolfsen R. M. and Erway L. C. (1984) Trace metals and otolith defects in mocha mice. J. Hered. 75: 159-162
    • (1984) J. Hered. , vol.75 , pp. 159-162
    • Rolfsen, R.M.1    Erway, L.C.2
  • 164
    • 0032587547 scopus 로고    scopus 로고
    • The beta3a subunit gene (Ap3b1) of the AP-3 adaptor complex is altered in the mouse hypopigmentation mutant pear1, a model for Hermansky-Pudlak syndrome and night blindness
    • Feng L., Seymour A. B., Jiang S., To A., Peden A. A., Novak E. K. et al. (1999) The beta3A subunit gene (Ap3b1) of the AP-3 adaptor complex is altered in the mouse hypopigmentation mutant pear1, a model for Hermansky-Pudlak syndrome and night blindness. Hum. Mol. Genet. 8: 323-330
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 323-330
    • Feng, L.1    Seymour, A.B.2    Jiang, S.3    To, A.4    Peden, A.A.5    Novak, E.K.6
  • 165
    • 0034471359 scopus 로고    scopus 로고
    • Defective organellar membrane protein trafficking in Ap3b1-deficient cells
    • Yang W, Li C., Ward D. M., Kaplan J. and Mansour S. L. (2000) Defective organellar membrane protein trafficking in Ap3b1-deficient cells. J. Cell Sci. 113 ( Pt 22): 4077-4086
    • (2000) J. Cell Sci. , vol.113 , Issue.22 PART , pp. 4077-4086
    • Yang, W.1    Li, C.2    Ward, D.M.3    Kaplan, J.4    Mansour, S.L.5
  • 166
    • 0037008731 scopus 로고    scopus 로고
    • BLOC-1, a novel complex containing the pallidin and muted proteins involved in the biogenesis of melanosomes and platelet-dense granules
    • Falcon-Perez J. M., Starcevic M., Gautam R. and Dell'Angelica E. C. (2002) BLOC-1, a novel complex containing the pallidin and muted proteins involved in the biogenesis of melanosomes and platelet-dense granules. J. Biol. Chem. 277: 28191-28199
    • (2002) J. Biol. Chem. , vol.277 , pp. 28191-28199
    • Falcon-Perez, J.M.1    Starcevic, M.2    Gautam, R.3    Dell'Angelica, E.C.4
  • 167
    • 0032743997 scopus 로고    scopus 로고
    • The pallid gene encodes a novel, syntaxin 13-interacting protein involved in platelet storage pool deficiency
    • Huang L., Kuo Y. M. and Gitschier J. (1999) The pallid gene encodes a novel, syntaxin 13-interacting protein involved in platelet storage pool deficiency. Nat. Genet. 23: 329-332
    • (1999) Nat. Genet. , vol.23 , pp. 329-332
    • Huang, L.1    Kuo, Y.M.2    Gitschier, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.