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Volumn 93, Issue 3, 2011, Pages 405-420

Family reunion - The ZIP/prion gene family

Author keywords

Evolution; Function; Prion proteins; Zinc; ZIP proteins

Indexed keywords

PRION PROTEIN; UNCLASSIFIED DRUG; ZINC TRANSPORTER; ZIP PROTEIN;

EID: 79351469258     PISSN: 03010082     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pneurobio.2010.12.001     Document Type: Review
Times cited : (32)

References (225)
  • 3
    • 15244341973 scopus 로고    scopus 로고
    • Gene expression profiling in chronic copper overload reveals upregulation of Prnp and App
    • Armendariz A.D., Gonzalez M., Loguinov A.V., Vulpe C.D. Gene expression profiling in chronic copper overload reveals upregulation of Prnp and App. Physiol. Genomics 2004, 20:45-54.
    • (2004) Physiol. Genomics , vol.20 , pp. 45-54
    • Armendariz, A.D.1    Gonzalez, M.2    Loguinov, A.V.3    Vulpe, C.D.4
  • 7
    • 0028085838 scopus 로고
    • Cytoplasmic tail deletion of T cell receptor (TCR) β-chain results in its surface expression as glycosylphosphatidylinositol-anchored polypeptide on mature T cells in the absence of TCR-α
    • Bell L.M., Solomon K.R., Gold J.P., Tan K.-N. Cytoplasmic tail deletion of T cell receptor (TCR) β-chain results in its surface expression as glycosylphosphatidylinositol-anchored polypeptide on mature T cells in the absence of TCR-α. J. Biol. Chem. 1994, 269:22758-22763.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22758-22763
    • Bell, L.M.1    Solomon, K.R.2    Gold, J.P.3    Tan, K.-N.4
  • 8
    • 59449087527 scopus 로고    scopus 로고
    • Regulation of prion gene expression by transcription factors SP1 and metal transcription factor-1
    • Bellingham S.A., Coleman L.A., Masters C.L., Camakaris J., Hill A.F. Regulation of prion gene expression by transcription factors SP1 and metal transcription factor-1. J. Biol. Chem. 2009, 284:1291-1301.
    • (2009) J. Biol. Chem. , vol.284 , pp. 1291-1301
    • Bellingham, S.A.1    Coleman, L.A.2    Masters, C.L.3    Camakaris, J.4    Hill, A.F.5
  • 10
    • 0027291065 scopus 로고
    • Release of the cellular prion protein from cultured cells after loss of its glycoinositol phospholipid anchor
    • Borchelt D.R., Rogers M., Stahl N., Telling G., Prusiner S.B. Release of the cellular prion protein from cultured cells after loss of its glycoinositol phospholipid anchor. Glycobiology 1993, 3:319-329.
    • (1993) Glycobiology , vol.3 , pp. 319-329
    • Borchelt, D.R.1    Rogers, M.2    Stahl, N.3    Telling, G.4    Prusiner, S.B.5
  • 13
    • 65949111521 scopus 로고    scopus 로고
    • Brain proteins that mind metals: a neurodegenerative perspective
    • Brown D.R. Brain proteins that mind metals: a neurodegenerative perspective. Dalton Trans. 2009, 4069-4076.
    • (2009) Dalton Trans. , pp. 4069-4076
    • Brown, D.R.1
  • 14
    • 67749133518 scopus 로고    scopus 로고
    • Structural features of the Zn(2+) complex with the single repeat region of "prion related protein" (PrP-rel-2) of zebrafish zPrP63-70 fragment
    • Camponeschi F., Gaggelli E., Kozlowski H., Valensin D., Valensin G. Structural features of the Zn(2+) complex with the single repeat region of "prion related protein" (PrP-rel-2) of zebrafish zPrP63-70 fragment. Dalton Trans. 2009, 24:4643-4645.
    • (2009) Dalton Trans. , vol.24 , pp. 4643-4645
    • Camponeschi, F.1    Gaggelli, E.2    Kozlowski, H.3    Valensin, D.4    Valensin, G.5
  • 16
    • 0023860332 scopus 로고
    • Detection of prion protein mRNA in normal and scrapie-infected tissues and cell lines
    • Caughey B., Race R.E., Chesebro B. Detection of prion protein mRNA in normal and scrapie-infected tissues and cell lines. J. Gen. Virol. 1988, 69(Pt 3):711-716.
    • (1988) J. Gen. Virol. , vol.69 , Issue.PART 3 , pp. 711-716
    • Caughey, B.1    Race, R.E.2    Chesebro, B.3
  • 17
    • 4344590587 scopus 로고    scopus 로고
    • Copper(II) binding to the human Doppel protein may mark its functional diversity from the prion protein
    • Cereghetti G.M., Negro A., Vinck E., Massimino M.L., Sorgato M.C., Van Doorslaer S. Copper(II) binding to the human Doppel protein may mark its functional diversity from the prion protein. J. Biol. Chem. 2004, 279:36497-36503.
    • (2004) J. Biol. Chem. , vol.279 , pp. 36497-36503
    • Cereghetti, G.M.1    Negro, A.2    Vinck, E.3    Massimino, M.L.4    Sorgato, M.C.5    Van Doorslaer, S.6
  • 18
    • 2342660750 scopus 로고    scopus 로고
    • Integration site selection by retroviruses
    • Cereseto A., Giacca M. Integration site selection by retroviruses. AIDS Rev. 2004, 6:13-21.
    • (2004) AIDS Rev. , vol.6 , pp. 13-21
    • Cereseto, A.1    Giacca, M.2
  • 19
    • 2342429689 scopus 로고    scopus 로고
    • Thermodynamic studies of the mechanism of metal binding to the Escherichia coli zinc transporter YiiP
    • Chao Y., Fu D. Thermodynamic studies of the mechanism of metal binding to the Escherichia coli zinc transporter YiiP. J. Biol. Chem. 2004, 279:17173-17180.
    • (2004) J. Biol. Chem. , vol.279 , pp. 17173-17180
    • Chao, Y.1    Fu, D.2
  • 22
    • 33747164172 scopus 로고    scopus 로고
    • Interaction of metals with prion protein: possible role of divalent cations in the pathogenesis of prion diseases
    • Choi C.J., Kanthasamy A., Anantharam V., Kanthasamy A.G. Interaction of metals with prion protein: possible role of divalent cations in the pathogenesis of prion diseases. Neurotoxicology 2006, 27:777-787.
    • (2006) Neurotoxicology , vol.27 , pp. 777-787
    • Choi, C.J.1    Kanthasamy, A.2    Anantharam, V.3    Kanthasamy, A.G.4
  • 23
    • 18344381293 scopus 로고    scopus 로고
    • Zinc deficiency is associated with increased brain zinc import and LIV-1 expression and decreased ZnT-1 expression in neonatal rats
    • Chowanadisai W., Kelleher S.L., Lonnerdal B. Zinc deficiency is associated with increased brain zinc import and LIV-1 expression and decreased ZnT-1 expression in neonatal rats. J. Nutr. 2005, 135:1002-1007.
    • (2005) J. Nutr. , vol.135 , pp. 1002-1007
    • Chowanadisai, W.1    Kelleher, S.L.2    Lonnerdal, B.3
  • 24
    • 28844433559 scopus 로고    scopus 로고
    • The disintegrin ADAM9 indirectly contributes to the physiological processing of cellular prion by modulating ADAM10 activity
    • Cisse M.A., Sunyach C., Lefranc-Jullien S., Postina R., Vincent B., Checler F. The disintegrin ADAM9 indirectly contributes to the physiological processing of cellular prion by modulating ADAM10 activity. J. Biol. Chem. 2005, 280:40624-40631.
    • (2005) J. Biol. Chem. , vol.280 , pp. 40624-40631
    • Cisse, M.A.1    Sunyach, C.2    Lefranc-Jullien, S.3    Postina, R.4    Vincent, B.5    Checler, F.6
  • 25
    • 0034916581 scopus 로고    scopus 로고
    • Prion diseases of humans and animals: their causes and molecular basis
    • Collinge J. Prion diseases of humans and animals: their causes and molecular basis. Annu. Rev. Neurosci. 2001, 24:519-550.
    • (2001) Annu. Rev. Neurosci. , vol.24 , pp. 519-550
    • Collinge, J.1
  • 26
    • 36049020231 scopus 로고    scopus 로고
    • A general model of prion strains and their pathogenicity
    • Collinge J., Clarke A.R. A general model of prion strains and their pathogenicity. Science 2007, 318:930-936.
    • (2007) Science , vol.318 , pp. 930-936
    • Collinge, J.1    Clarke, A.R.2
  • 27
    • 12544259444 scopus 로고    scopus 로고
    • Molecular characterization, phylogenetic relationships, and developmental expression patterns of prion genes in zebrafish (Danio rerio)
    • Cotto E., Andre M., Forgue J., Fleury H.J., Babin P.J. Molecular characterization, phylogenetic relationships, and developmental expression patterns of prion genes in zebrafish (Danio rerio). FEBS J. 2005, 272:500-513.
    • (2005) FEBS J. , vol.272 , pp. 500-513
    • Cotto, E.1    Andre, M.2    Forgue, J.3    Fleury, H.J.4    Babin, P.J.5
  • 28
    • 33845982198 scopus 로고    scopus 로고
    • Characterization of intron loss events in mammals
    • Coulombe-Huntington J., Majewski J. Characterization of intron loss events in mammals. Genome Res. 2007, 17:23-32.
    • (2007) Genome Res. , vol.17 , pp. 23-32
    • Coulombe-Huntington, J.1    Majewski, J.2
  • 29
    • 33747723380 scopus 로고    scopus 로고
    • Mammalian zinc transport, trafficking, and signals
    • Cousins R.J., Liuzzi J.P., Lichten L.A. Mammalian zinc transport, trafficking, and signals. J. Biol. Chem. 2006, 281:24085-24089.
    • (2006) J. Biol. Chem. , vol.281 , pp. 24085-24089
    • Cousins, R.J.1    Liuzzi, J.P.2    Lichten, L.A.3
  • 31
    • 34250687105 scopus 로고    scopus 로고
    • HZip2 and hZip3 zinc transporters are down regulated in human prostate adenocarcinomatous glands
    • Desouki M.M., Geradts J., Milon B., Franklin R.B., Costello L.C. hZip2 and hZip3 zinc transporters are down regulated in human prostate adenocarcinomatous glands. Mol. Cancer 2007, 6:37.
    • (2007) Mol. Cancer , vol.6 , pp. 37
    • Desouki, M.M.1    Geradts, J.2    Milon, B.3    Franklin, R.B.4    Costello, L.C.5
  • 32
  • 33
    • 77951217018 scopus 로고    scopus 로고
    • Endogenous proteolytic cleavage of disease-associated prion protein to produce C2 fragments is strongly cell- and tissue-dependent
    • Dron M., Moudjou M., Chapuis J., Salamat M.K., Bernard J., Cronier S., Langevin C., Laude H. Endogenous proteolytic cleavage of disease-associated prion protein to produce C2 fragments is strongly cell- and tissue-dependent. J. Biol. Chem. 2010, 285:10252-10264.
    • (2010) J. Biol. Chem. , vol.285 , pp. 10252-10264
    • Dron, M.1    Moudjou, M.2    Chapuis, J.3    Salamat, M.K.4    Bernard, J.5    Cronier, S.6    Langevin, C.7    Laude, H.8
  • 34
    • 33745040492 scopus 로고    scopus 로고
    • Mouse ZIP1 and ZIP3 genes together are essential for adaptation to dietary zinc deficiency during pregnancy
    • Dufner-Beattie J., Huang Z.L., Geiser J., Xu W., Andrews G.K. Mouse ZIP1 and ZIP3 genes together are essential for adaptation to dietary zinc deficiency during pregnancy. Genesis 2006, 44:239-251.
    • (2006) Genesis , vol.44 , pp. 239-251
    • Dufner-Beattie, J.1    Huang, Z.L.2    Geiser, J.3    Xu, W.4    Andrews, G.K.5
  • 35
    • 10344248917 scopus 로고    scopus 로고
    • The adaptive response to dietary zinc in mice involves the differential cellular localization and zinc regulation of the zinc transporters ZIP4 and ZIP5
    • Dufner-Beattie J., Kuo Y.M., Gitschier J., Andrews G.K. The adaptive response to dietary zinc in mice involves the differential cellular localization and zinc regulation of the zinc transporters ZIP4 and ZIP5. J. Biol. Chem. 2004, 279:49082-49090.
    • (2004) J. Biol. Chem. , vol.279 , pp. 49082-49090
    • Dufner-Beattie, J.1    Kuo, Y.M.2    Gitschier, J.3    Andrews, G.K.4
  • 36
    • 34347352057 scopus 로고    scopus 로고
    • The mouse acrodermatitis enteropathica gene Slc39a4 (Zip4) is essential for early development and heterozygosity causes hypersensitivity to zinc deficiency
    • Dufner-Beattie J., Weaver B.P., Geiser J., Bilgen M., Larson M., Xu W., Andrews G.K. The mouse acrodermatitis enteropathica gene Slc39a4 (Zip4) is essential for early development and heterozygosity causes hypersensitivity to zinc deficiency. Hum. Mol. Genet. 2007, 16:1391-1399.
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 1391-1399
    • Dufner-Beattie, J.1    Weaver, B.P.2    Geiser, J.3    Bilgen, M.4    Larson, M.5    Xu, W.6    Andrews, G.K.7
  • 37
  • 38
    • 0029891827 scopus 로고    scopus 로고
    • A novel iron-regulated metal transporter from plants identified by functional expression in yeast
    • Eide D., Broderius M., Fett J., Guerinot M.L. A novel iron-regulated metal transporter from plants identified by functional expression in yeast. Proc. Natl. Acad. Sci. U.S.A. 1996, 93:5624-5628.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 5624-5628
    • Eide, D.1    Broderius, M.2    Fett, J.3    Guerinot, M.L.4
  • 39
    • 1342344814 scopus 로고    scopus 로고
    • The SLC39 family of metal ion transporters
    • Eide D.J. The SLC39 family of metal ion transporters. Pflugers Arch. 2004, 447:796-800.
    • (2004) Pflugers Arch. , vol.447 , pp. 796-800
    • Eide, D.J.1
  • 40
    • 33746929895 scopus 로고    scopus 로고
    • Zinc transporters and the cellular trafficking of zinc
    • Eide D.J. Zinc transporters and the cellular trafficking of zinc. Biochim. Biophys. Acta 2006, 1763:711-722.
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 711-722
    • Eide, D.J.1
  • 41
    • 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., Saier M.H. Sequence analyses and phylogenetic characterization of the ZIP family of metal ion transport proteins. J. Membr. Biol. 1998, 166:1-7.
    • (1998) J. Membr. Biol. , vol.166 , pp. 1-7
    • Eng, B.H.1    Guerinot, M.L.2    Eide, D.3    Saier, M.H.4
  • 42
    • 33750576527 scopus 로고    scopus 로고
    • Prions: protein only or something more? Overview of potential prion cofactors
    • Fasano C., Campana V., Zurzolo C. Prions: protein only or something more? Overview of potential prion cofactors. J. Mol. Neurosci. 2006, 29:195-214.
    • (2006) J. Mol. Neurosci. , vol.29 , pp. 195-214
    • Fasano, C.1    Campana, V.2    Zurzolo, C.3
  • 43
    • 33144470760 scopus 로고    scopus 로고
    • The phylogeny of teleost ZIP and ZnT zinc transporters and their tissue specific expression and response to zinc in zebrafish
    • Feeney G.P., Zheng D., Kille P., Hogstrand C. The phylogeny of teleost ZIP and ZnT zinc transporters and their tissue specific expression and response to zinc in zebrafish. Biochim. Biophys. Acta 2005, 1732:88-95.
    • (2005) Biochim. Biophys. Acta , vol.1732 , pp. 88-95
    • Feeney, G.P.1    Zheng, D.2    Kille, P.3    Hogstrand, C.4
  • 44
    • 36849037428 scopus 로고    scopus 로고
    • Structure of a site-2 protease family intramembrane metalloprotease
    • Feng L., Yan H., Wu Z., Yan N., Wang Z., Jeffrey P.D., Shi Y. Structure of a site-2 protease family intramembrane metalloprotease. Science 2007, 318:1608-1612.
    • (2007) Science , vol.318 , pp. 1608-1612
    • Feng, L.1    Yan, H.2    Wu, Z.3    Yan, N.4    Wang, Z.5    Jeffrey, P.D.6    Shi, Y.7
  • 45
    • 2942720836 scopus 로고    scopus 로고
    • The role of PrP in health and disease
    • Flechsig E., Weissmann C. The role of PrP in health and disease. Curr. Mol. Med. 2004, 4:337-353.
    • (2004) Curr. Mol. Med. , vol.4 , pp. 337-353
    • Flechsig, E.1    Weissmann, C.2
  • 46
    • 53449102571 scopus 로고    scopus 로고
    • NCAM is at the heart of reciprocal regulation of E-cadherin- and integrin-mediated adhesions via signaling modulation
    • Frame M.C., Inman G.J. NCAM is at the heart of reciprocal regulation of E-cadherin- and integrin-mediated adhesions via signaling modulation. Dev. Cell 2008, 15:494-496.
    • (2008) Dev. Cell , vol.15 , pp. 494-496
    • Frame, M.C.1    Inman, G.J.2
  • 49
    • 84954358022 scopus 로고    scopus 로고
    • The solute carrier (SLC) complement of the human genome: phylogenetic classification reveals four major families
    • Fredriksson R., Nordstrom K.J., Stephansson O., Hagglund M.G., Schioth H.B. The solute carrier (SLC) complement of the human genome: phylogenetic classification reveals four major families. FEBS Lett. 2008, 582:3811-3816.
    • (2008) FEBS Lett. , vol.582 , pp. 3811-3816
    • Fredriksson, R.1    Nordstrom, K.J.2    Stephansson, O.3    Hagglund, M.G.4    Schioth, H.B.5
  • 50
    • 0031647381 scopus 로고    scopus 로고
    • Vertebrate Tinman homologues XNkx2-3 and XNkx2-5 are required for heart formation in a functionally redundant manner
    • Fu Y., Yan W., Mohun T.J., Evans S.M. Vertebrate Tinman homologues XNkx2-3 and XNkx2-5 are required for heart formation in a functionally redundant manner. Development 1998, 125:4439-4449.
    • (1998) Development , vol.125 , pp. 4439-4449
    • Fu, Y.1    Yan, W.2    Mohun, T.J.3    Evans, S.M.4
  • 53
    • 0035693722 scopus 로고    scopus 로고
    • Eukaryotic zinc transporters and their regulation
    • Gaither L.A., Eide D.J. Eukaryotic zinc transporters and their regulation. Biometals 2001, 14:251-270.
    • (2001) Biometals , vol.14 , pp. 251-270
    • Gaither, L.A.1    Eide, D.J.2
  • 55
    • 0034161957 scopus 로고    scopus 로고
    • Zinc-regulated ubiquitin conjugation signals endocytosis of the yeast ZRT1 zinc transporter
    • Gitan R.S., Eide D.J. Zinc-regulated ubiquitin conjugation signals endocytosis of the yeast ZRT1 zinc transporter. Biochem. J. 2000, 346(Pt 2):329-336.
    • (2000) Biochem. J. , vol.346 , Issue.PART 2 , pp. 329-336
    • Gitan, R.S.1    Eide, D.J.2
  • 56
    • 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., Eide D. Zinc-induced inactivation of the yeast ZRT1 zinc transporter occurs through endocytosis and vacuolar degradation. J. Biol. Chem. 1998, 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
  • 57
    • 36949011636 scopus 로고    scopus 로고
    • The G protein-coupled receptor subset of the rat genome
    • Gloriam D.E., Fredriksson R., Schioth H.B. The G protein-coupled receptor subset of the rat genome. BMC Genomics 2007, 8:338.
    • (2007) BMC Genomics , vol.8 , pp. 338
    • Gloriam, D.E.1    Fredriksson, R.2    Schioth, H.B.3
  • 58
    • 68349145078 scopus 로고    scopus 로고
    • Next-generation gene targeting in the mouse for functional genomics
    • Gondo Y., Fukumura R., Murata T., Makino S. Next-generation gene targeting in the mouse for functional genomics. BMB Rep. 2009, 42:315-323.
    • (2009) BMB Rep. , vol.42 , pp. 315-323
    • Gondo, Y.1    Fukumura, R.2    Murata, T.3    Makino, S.4
  • 60
    • 12444299959 scopus 로고    scopus 로고
    • FieF (YiiP) from Escherichia coli mediates decreased cellular accumulation of iron and relieves iron stress
    • Grass G., Otto M., Fricke B., Haney C.J., Rensing C., Nies D.H., Munkelt D. FieF (YiiP) from Escherichia coli mediates decreased cellular accumulation of iron and relieves iron stress. Arch. Microbiol. 2005, 183:9-18.
    • (2005) Arch. Microbiol. , vol.183 , pp. 9-18
    • Grass, G.1    Otto, M.2    Fricke, B.3    Haney, C.J.4    Rensing, C.5    Nies, D.H.6    Munkelt, D.7
  • 61
    • 52949096859 scopus 로고    scopus 로고
    • The function of Stat3 in tumor cells and their microenvironment
    • Groner B., Lucks P., Borghouts C. The function of Stat3 in tumor cells and their microenvironment. Semin. Cell Dev. Biol. 2008, 19:341-350.
    • (2008) Semin. Cell Dev. Biol. , vol.19 , pp. 341-350
    • Groner, B.1    Lucks, P.2    Borghouts, C.3
  • 62
    • 0034192475 scopus 로고    scopus 로고
    • The ZIP family of metal transporters
    • Guerinot M.L. The ZIP family of metal transporters. Biochim. Biophys. Acta 2000, 1465:190-198.
    • (2000) Biochim. Biophys. Acta , vol.1465 , pp. 190-198
    • Guerinot, M.L.1
  • 63
    • 72149127389 scopus 로고    scopus 로고
    • The alpha-secretase-derived N-terminal product of cellular prion, N1, displays neuroprotective function in vitro and in vivo
    • Guillot-Sestier M.V., Sunyach C., Druon C., Scarzello S., Checler F. The alpha-secretase-derived N-terminal product of cellular prion, N1, displays neuroprotective function in vitro and in vivo. J. Biol. Chem. 2009, 284:35973-35986.
    • (2009) J. Biol. Chem. , vol.284 , pp. 35973-35986
    • Guillot-Sestier, M.V.1    Sunyach, C.2    Druon, C.3    Scarzello, S.4    Checler, F.5
  • 64
    • 69949131244 scopus 로고    scopus 로고
    • PrPC-related signal transduction is influenced by copper, membrane integrity and the alpha cleavage site
    • Haigh C.L., Lewis V.A., Vella L.J., Masters C.L., Hill A.F., Lawson V.A., Collins S.J. PrPC-related signal transduction is influenced by copper, membrane integrity and the alpha cleavage site. Cell Res. 2009, 19:1062-1078.
    • (2009) Cell Res. , vol.19 , pp. 1062-1078
    • Haigh, C.L.1    Lewis, V.A.2    Vella, L.J.3    Masters, C.L.4    Hill, A.F.5    Lawson, V.A.6    Collins, S.J.7
  • 65
    • 0027405573 scopus 로고
    • Processing of a cellular prion protein: identification of N- and C-terminal cleavage sites
    • Harris D.A., Huber M.T., van Dijken P., Shyng S.L., Chait B.T., Wang R. Processing of a cellular prion protein: identification of N- and C-terminal cleavage sites. Biochemistry 1993, 32:1009-1016.
    • (1993) Biochemistry , vol.32 , pp. 1009-1016
    • Harris, D.A.1    Huber, M.T.2    van Dijken, P.3    Shyng, S.L.4    Chait, B.T.5    Wang, R.6
  • 66
    • 33745249951 scopus 로고    scopus 로고
    • ZIP8, member of the solute-carrier-39 (SLC39) metal-transporter family: characterization of transporter properties
    • He L., Girijashanker K., Dalton T.P., Reed J., Li H., Soleimani M., Nebert D.W. ZIP8, member of the solute-carrier-39 (SLC39) metal-transporter family: characterization of transporter properties. Mol. Pharmacol. 2006, 70:171-180.
    • (2006) Mol. Pharmacol. , vol.70 , pp. 171-180
    • He, L.1    Girijashanker, K.2    Dalton, T.P.3    Reed, J.4    Li, H.5    Soleimani, M.6    Nebert, D.W.7
  • 67
    • 67649663950 scopus 로고    scopus 로고
    • Discovery of ZIP transporters that participate in cadmium damage to testis and kidney
    • He L., Wang B., Hay E.B., Nebert D.W. Discovery of ZIP transporters that participate in cadmium damage to testis and kidney. Toxicol. Appl. Pharmacol. 2009, 238:250-257.
    • (2009) Toxicol. Appl. Pharmacol. , vol.238 , pp. 250-257
    • He, L.1    Wang, B.2    Hay, E.B.3    Nebert, D.W.4
  • 68
    • 1242340323 scopus 로고    scopus 로고
    • The ABCs of solute carriers: physiological, pathological and therapeutic implications of human membrane transport proteins. Introduction
    • Hediger M.A., Romero M.F., Peng J.B., Rolfs A., Takanaga H., Bruford E.A. The ABCs of solute carriers: physiological, pathological and therapeutic implications of human membrane transport proteins. Introduction. Pflugers Arch. 2004, 447:465-468.
    • (2004) Pflugers Arch. , vol.447 , pp. 465-468
    • Hediger, M.A.1    Romero, M.F.2    Peng, J.B.3    Rolfs, A.4    Takanaga, H.5    Bruford, E.A.6
  • 69
    • 69749121831 scopus 로고    scopus 로고
    • The role of zinc transporters in cadmium and manganese transport in mammalian cells
    • Himeno S., Yanagiya T., Fujishiro H. The role of zinc transporters in cadmium and manganese transport in mammalian cells. Biochimie 2009, 91:1218-1222.
    • (2009) Biochimie , vol.91 , pp. 1218-1222
    • Himeno, S.1    Yanagiya, T.2    Fujishiro, H.3
  • 71
    • 61849121844 scopus 로고    scopus 로고
    • Zinc transporters and cancer: a potential role for ZIP7 as a hub for tyrosine kinase activation
    • Hogstrand C., Kille P., Nicholson R.I., Taylor K.M. Zinc transporters and cancer: a potential role for ZIP7 as a hub for tyrosine kinase activation. Trends Mol. Med. 2009, 15:101-111.
    • (2009) Trends Mol. Med. , vol.15 , pp. 101-111
    • Hogstrand, C.1    Kille, P.2    Nicholson, R.I.3    Taylor, K.M.4
  • 73
    • 34547475050 scopus 로고    scopus 로고
    • Prion proteins: a biological role beyond prion diseases
    • Hu W., Rosenberg R.N., Stuve O. Prion proteins: a biological role beyond prion diseases. Acta Neurol. Scand. 2007, 116:75-82.
    • (2007) Acta Neurol. Scand. , vol.116 , pp. 75-82
    • Hu, W.1    Rosenberg, R.N.2    Stuve, O.3
  • 74
    • 17644400171 scopus 로고    scopus 로고
    • The ZIP7 gene (Slc39a7) encodes a zinc transporter involved in zinc homeostasis of the Golgi apparatus
    • Huang L., Kirschke C.P., Zhang Y., Yu Y.Y. The ZIP7 gene (Slc39a7) encodes a zinc transporter involved in zinc homeostasis of the Golgi apparatus. J. Biol. Chem. 2005, 280:15456-15463.
    • (2005) J. Biol. Chem. , vol.280 , pp. 15456-15463
    • Huang, L.1    Kirschke, C.P.2    Zhang, Y.3    Yu, Y.Y.4
  • 75
    • 25444454543 scopus 로고    scopus 로고
    • New and old functions of STAT3: a pivotal target for individualized treatment of cancer
    • Inghirami G., Chiarle R., Simmons W.J., Piva R., Schlessinger K., Levy D.E. New and old functions of STAT3: a pivotal target for individualized treatment of cancer. Cell Cycle 2005, 4:1131-1133.
    • (2005) Cell Cycle , vol.4 , pp. 1131-1133
    • Inghirami, G.1    Chiarle, R.2    Simmons, W.J.3    Piva, R.4    Schlessinger, K.5    Levy, D.E.6
  • 76
    • 27244447041 scopus 로고    scopus 로고
    • Polymorphism at 3' UTR+28 of the prion-like protein gene is associated with sporadic Creutzfeldt-Jakob disease
    • Jeong B.H., Kim N.H., Choi E.K., Lee C., Song Y.H., Kim J.I., Carp R.I., Kim Y.S. Polymorphism at 3' UTR+28 of the prion-like protein gene is associated with sporadic Creutzfeldt-Jakob disease. Eur. J. Hum. Genet. 2005, 13:1094-1097.
    • (2005) Eur. J. Hum. Genet. , vol.13 , pp. 1094-1097
    • Jeong, B.H.1    Kim, N.H.2    Choi, E.K.3    Lee, C.4    Song, Y.H.5    Kim, J.I.6    Carp, R.I.7    Kim, Y.S.8
  • 78
    • 0031765769 scopus 로고    scopus 로고
    • Endogenous proteolytic cleavage of normal and disease-associated isoforms of the human prion protein in neural and non-neural tissues
    • Jimenez-Huete A., Lievens P.M., Vidal R., Piccardo P., Ghetti B., Tagliavini F., Frangione B., Prelli F. Endogenous proteolytic cleavage of normal and disease-associated isoforms of the human prion protein in neural and non-neural tissues. Am. J. Pathol. 1998, 153:1561-1572.
    • (1998) Am. J. Pathol. , vol.153 , pp. 1561-1572
    • Jimenez-Huete, A.1    Lievens, P.M.2    Vidal, R.3    Piccardo, P.4    Ghetti, B.5    Tagliavini, F.6    Frangione, B.7    Prelli, F.8
  • 79
    • 0024559146 scopus 로고
    • A unique signature identifies a family of zinc-dependent metallopeptidases
    • Jongeneel C.V., Bouvier J., Bairoch A. A unique signature identifies a family of zinc-dependent metallopeptidases. FEBS Lett. 1989, 242:211-214.
    • (1989) FEBS Lett. , vol.242 , pp. 211-214
    • Jongeneel, C.V.1    Bouvier, J.2    Bairoch, A.3
  • 80
    • 57749177443 scopus 로고    scopus 로고
    • RNA-based gene duplication: mechanistic and evolutionary insights
    • Kaessmann H., Vinckenbosch N., Long M. RNA-based gene duplication: mechanistic and evolutionary insights. Nat. Rev. Genet. 2009, 10:19-31.
    • (2009) Nat. Rev. Genet. , vol.10 , pp. 19-31
    • Kaessmann, H.1    Vinckenbosch, N.2    Long, M.3
  • 81
    • 34147126803 scopus 로고    scopus 로고
    • Zinc and its transporter ZIP10 are involved in invasive behavior of breast cancer cells
    • Kagara N., Tanaka N., Noguchi S., Hirano T. Zinc and its transporter ZIP10 are involved in invasive behavior of breast cancer cells. Cancer Sci. 2007, 98:692-697.
    • (2007) Cancer Sci. , vol.98 , pp. 692-697
    • Kagara, N.1    Tanaka, N.2    Noguchi, S.3    Hirano, T.4
  • 82
    • 33846186838 scopus 로고    scopus 로고
    • Molecular cloning and functional characterization of novel zinc transporter rZip10 (Slc39a10) involved in zinc uptake across rat renal brush-border membrane
    • Kaler P., Prasad R. Molecular cloning and functional characterization of novel zinc transporter rZip10 (Slc39a10) involved in zinc uptake across rat renal brush-border membrane. Am. J. Physiol. Renal Physiol. 2007, 292:F217-229.
    • (2007) Am. J. Physiol. Renal Physiol. , vol.292
    • Kaler, P.1    Prasad, R.2
  • 83
    • 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 G.K. Novel proteolytic processing of the ectodomain of the zinc transporter ZIP4 (SLC39A4) during zinc deficiency is inhibited by acrodermatitis enteropathica mutations. Mol. Cell. Biol. 2009, 29:129-139.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 129-139
    • Kambe, T.1    Andrews, G.K.2
  • 84
    • 45549087856 scopus 로고    scopus 로고
    • Slc39a1 to 3 (subfamily II) Zip genes in mice have unique cell-specific functions during adaptation to zinc deficiency
    • Kambe T., Geiser J., Lahner B., Salt D.E., Andrews G.K. Slc39a1 to 3 (subfamily II) Zip genes in mice have unique cell-specific functions during adaptation to zinc deficiency. Am. J. Physiol. Regul. Integr. Comp. Physiol. 2008, 294:R1474-1481.
    • (2008) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.294
    • Kambe, T.1    Geiser, J.2    Lahner, B.3    Salt, D.E.4    Andrews, G.K.5
  • 85
    • 33645724195 scopus 로고    scopus 로고
    • Sequence similarity and functional relationship among eukaryotic ZIP and CDF transporters
    • Kambe T., Suzuki T., Nagao M., Yamaguchi-Iwai Y. Sequence similarity and functional relationship among eukaryotic ZIP and CDF transporters. Genom. Proteom. Bioinform. 2006, 4:1-9.
    • (2006) Genom. Proteom. Bioinform. , vol.4 , pp. 1-9
    • Kambe, T.1    Suzuki, T.2    Nagao, M.3    Yamaguchi-Iwai, Y.4
  • 87
    • 34147112306 scopus 로고    scopus 로고
    • Copper and zinc promote interactions between membrane-anchored peptides of the metal binding domain of the prion protein
    • Kenward A.G., Bartolotti L.J., Burns C.S. Copper and zinc promote interactions between membrane-anchored peptides of the metal binding domain of the prion protein. Biochemistry 2007, 46:4261-4271.
    • (2007) Biochemistry , vol.46 , pp. 4261-4271
    • Kenward, A.G.1    Bartolotti, L.J.2    Burns, C.S.3
  • 88
    • 38849125000 scopus 로고    scopus 로고
    • In silico comparative analysis of DNA and amino acid sequences for prion protein gene
    • Kim Y., Lee J., Lee C. In silico comparative analysis of DNA and amino acid sequences for prion protein gene. Transbound Emerg. Dis. 2008, 55:105-114.
    • (2008) Transbound Emerg. Dis. , vol.55 , pp. 105-114
    • Kim, Y.1    Lee, J.2    Lee, C.3
  • 89
    • 29344444795 scopus 로고    scopus 로고
    • Site-2 protease regulated intramembrane proteolysis: sequence homologs suggest an ancient signaling cascade
    • Kinch L.N., Ginalski K., Grishin N.V. Site-2 protease regulated intramembrane proteolysis: sequence homologs suggest an ancient signaling cascade. Protein Sci. 2006, 15:84-93.
    • (2006) Protein Sci. , vol.15 , pp. 84-93
    • Kinch, L.N.1    Ginalski, K.2    Grishin, N.V.3
  • 91
    • 33747360185 scopus 로고    scopus 로고
    • YKE4 (YIL023C) encodes a bidirectional zinc transporter in the endoplasmic reticulum of Saccharomyces cerevisiae
    • Kumanovics A., Poruk K.E., Osborn K.A., Ward D.M., Kaplan J. YKE4 (YIL023C) encodes a bidirectional zinc transporter in the endoplasmic reticulum of Saccharomyces cerevisiae. J. Biol. Chem. 2006, 281:22566-22574.
    • (2006) J. Biol. Chem. , vol.281 , pp. 22566-22574
    • Kumanovics, A.1    Poruk, K.E.2    Osborn, K.A.3    Ward, D.M.4    Kaplan, J.5
  • 93
    • 0024841156 scopus 로고
    • Membrane anchoring of a human IgG Fc receptor (CD16) determined by a single amino acid
    • Lanier L., Cwirla S., Yu G., Testi R., Phillips J.H. Membrane anchoring of a human IgG Fc receptor (CD16) determined by a single amino acid. Science 1989, 246:1611-1613.
    • (1989) Science , vol.246 , pp. 1611-1613
    • Lanier, L.1    Cwirla, S.2    Yu, G.3    Testi, R.4    Phillips, J.H.5
  • 94
    • 0141515196 scopus 로고    scopus 로고
    • Putative functions of PrP(C)
    • Lasmezas C.I. Putative functions of PrP(C). Br. Med. Bull. 2003, 66:61-70.
    • (2003) Br. Med. Bull. , vol.66 , pp. 61-70
    • Lasmezas, C.I.1
  • 98
    • 34249995984 scopus 로고    scopus 로고
    • Prion protein with an octapeptide insertion has impaired neuroprotective activity in transgenic mice
    • Li A., Piccardo P., Barmada S.J., Ghetti B., Harris D.A. Prion protein with an octapeptide insertion has impaired neuroprotective activity in transgenic mice. EMBO J. 2007, 26:2777-2785.
    • (2007) EMBO J. , vol.26 , pp. 2777-2785
    • Li, A.1    Piccardo, P.2    Barmada, S.J.3    Ghetti, B.4    Harris, D.A.5
  • 99
    • 0029806025 scopus 로고    scopus 로고
    • Suppression of oxidative damage by Saccharomyces cerevisiae ATX2, which encodes a manganese-trafficking protein that localizes to Golgi-like vesicles
    • Lin S.J., Culotta V.C. Suppression of oxidative damage by Saccharomyces cerevisiae ATX2, which encodes a manganese-trafficking protein that localizes to Golgi-like vesicles. Mol. Cell. Biol. 1996, 16:6303-6312.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6303-6312
    • Lin, S.J.1    Culotta, V.C.2
  • 100
    • 78649863705 scopus 로고    scopus 로고
    • Selective electrodiffusion of zinc ions in a Zrt-, Irt-like protein, ZIPB
    • Lin W., Chai J., Love J., Fu D. Selective electrodiffusion of zinc ions in a Zrt-, Irt-like protein, ZIPB. J. Biol. Chem. 2010.
    • (2010) J. Biol. Chem.
    • Lin, W.1    Chai, J.2    Love, J.3    Fu, D.4
  • 104
    • 72149086674 scopus 로고    scopus 로고
    • Zip6- attenuation promotes epithelial-to-mesenchymal transition in ductal breast tumor (T47D) cells
    • Lopez V., Kelleher S.L. Zip6- attenuation promotes epithelial-to-mesenchymal transition in ductal breast tumor (T47D) cells. Exp. Cell Res. 2010, 316:366-375.
    • (2010) Exp. Cell Res. , vol.316 , pp. 366-375
    • Lopez, V.1    Kelleher, S.L.2
  • 105
    • 70349789244 scopus 로고    scopus 로고
    • Structural basis for autoregulation of the zinc transporter YiiP
    • Lu M., Chai J., Fu D. Structural basis for autoregulation of the zinc transporter YiiP. Nat. Struct. Mol. Biol. 2009, 16:1063-1067.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 1063-1067
    • Lu, M.1    Chai, J.2    Fu, D.3
  • 106
    • 34648833810 scopus 로고    scopus 로고
    • Structure of the zinc transporter YiiP
    • Lu M., Fu D. Structure of the zinc transporter YiiP. Science 2007, 317:1746-1748.
    • (2007) Science , vol.317 , pp. 1746-1748
    • Lu, M.1    Fu, D.2
  • 108
    • 0034660257 scopus 로고    scopus 로고
    • Zinc transporters that regulate vacuolar zinc storage in Saccharomyces cerevisiae
    • MacDiarmid C.W., Gaither L.A., Eide D. Zinc transporters that regulate vacuolar zinc storage in Saccharomyces cerevisiae. EMBO J. 2000, 19:2845-2855.
    • (2000) EMBO J. , vol.19 , pp. 2845-2855
    • MacDiarmid, C.W.1    Gaither, L.A.2    Eide, D.3
  • 109
    • 0035795677 scopus 로고    scopus 로고
    • Isolation and functional characterisation of the promoter region of the human prion protein gene
    • Mahal S.P., Asante E.A., Antoniou M., Collinge J. Isolation and functional characterisation of the promoter region of the human prion protein gene. Gene 2001, 268:105-114.
    • (2001) Gene , vol.268 , pp. 105-114
    • Mahal, S.P.1    Asante, E.A.2    Antoniou, M.3    Collinge, J.4
  • 110
    • 0036925662 scopus 로고    scopus 로고
    • Genomic characterization of the human prion protein (PrP) gene locus
    • Makrinou E., Collinge J., Antoniou M. Genomic characterization of the human prion protein (PrP) gene locus. Mamm. Genome 2002, 13:696-703.
    • (2002) Mamm. Genome , vol.13 , pp. 696-703
    • Makrinou, E.1    Collinge, J.2    Antoniou, M.3
  • 112
    • 1642410070 scopus 로고    scopus 로고
    • Alpha- and beta- cleavages of the amino-terminus of the cellular prion protein
    • Mange A., Beranger F., Peoc'h K., Onodera T., Frobert Y., Lehmann S. Alpha- and beta- cleavages of the amino-terminus of the cellular prion protein. Biol. Cell. 2004, 96:125-132.
    • (2004) Biol. Cell. , vol.96 , pp. 125-132
    • Mange, A.1    Beranger, F.2    Peoc'h, K.3    Onodera, T.4    Frobert, Y.5    Lehmann, S.6
  • 114
    • 34147120549 scopus 로고    scopus 로고
    • A histidine-rich cluster mediates the ubiquitination and degradation of the human zinc transporter, hZIP4, and protects against zinc cytotoxicity
    • Mao X., Kim B.E., Wang F., Eide D.J., Petris M.J. A histidine-rich cluster mediates the ubiquitination and degradation of the human zinc transporter, hZIP4, and protects against zinc cytotoxicity. J. Biol. Chem. 2007, 282:6992-7000.
    • (2007) J. Biol. Chem. , vol.282 , pp. 6992-7000
    • Mao, X.1    Kim, B.E.2    Wang, F.3    Eide, D.J.4    Petris, M.J.5
  • 116
    • 0020488029 scopus 로고
    • Cloning of cDNA sequences of hormone-regulated genes from the MCF-7 human breast cancer cell line
    • Masiakowski P., Breathnach R., Bloch J., Gannon F., Krust A., Chambon P. Cloning of cDNA sequences of hormone-regulated genes from the MCF-7 human breast cancer cell line. Nucleic Acids Res. 1982, 10:7895-7903.
    • (1982) Nucleic Acids Res. , vol.10 , pp. 7895-7903
    • Masiakowski, P.1    Breathnach, R.2    Bloch, J.3    Gannon, F.4    Krust, A.5    Chambon, P.6
  • 117
    • 0035812297 scopus 로고    scopus 로고
    • The prion gene complex encoding PrP(C) and Doppel: insights from mutational analysis
    • Mastrangelo P., Westaway D. The prion gene complex encoding PrP(C) and Doppel: insights from mutational analysis. Gene 2001, 275:1-18.
    • (2001) Gene , vol.275 , pp. 1-18
    • Mastrangelo, P.1    Westaway, D.2
  • 118
    • 33645750291 scopus 로고    scopus 로고
    • Zinc transport activity of Fear of Intimacy is essential for proper gonad morphogenesis and DE-cadherin expression
    • Mathews W.R., Ong D., Milutinovich A.B., Van Doren M. Zinc transport activity of Fear of Intimacy is essential for proper gonad morphogenesis and DE-cadherin expression. Development 2006, 133:1143-1153.
    • (2006) Development , vol.133 , pp. 1143-1153
    • Mathews, W.R.1    Ong, D.2    Milutinovich, A.B.3    Van Doren, M.4
  • 119
    • 12844253099 scopus 로고    scopus 로고
    • Drosophila fear of intimacy encodes a Zrt/IRT-like protein (ZIP) family zinc transporter functionally related to mammalian ZIP proteins
    • Mathews W.R., Wang F., Eide D.J., Van Doren M. Drosophila fear of intimacy encodes a Zrt/IRT-like protein (ZIP) family zinc transporter functionally related to mammalian ZIP proteins. J. Biol. Chem. 2005, 280:787-795.
    • (2005) J. Biol. Chem. , vol.280 , pp. 787-795
    • Mathews, W.R.1    Wang, F.2    Eide, D.J.3    Van Doren, M.4
  • 120
    • 67049099121 scopus 로고    scopus 로고
    • SLC39A9 (ZIP9) regulates zinc homeostasis in the secretory pathway: characterization of the ZIP subfamily I protein in vertebrate cells
    • Matsuura W., Yamazaki T., Yamaguchi-Iwai Y., Masuda S., Nagao M., Andrews G.K., Kambe T. SLC39A9 (ZIP9) regulates zinc homeostasis in the secretory pathway: characterization of the ZIP subfamily I protein in vertebrate cells. Biosci. Biotechnol. Biochem. 2009, 73:1142-1148.
    • (2009) Biosci. Biotechnol. Biochem. , vol.73 , pp. 1142-1148
    • Matsuura, W.1    Yamazaki, T.2    Yamaguchi-Iwai, Y.3    Masuda, S.4    Nagao, M.5    Andrews, G.K.6    Kambe, T.7
  • 122
    • 0034714488 scopus 로고    scopus 로고
    • Examination of the human prion protein-like gene doppel for genetic susceptibility to sporadic and variant Creutzfeldt-Jakob disease
    • Mead S., Beck J., Dickinson A., Fisher E.M., Collinge J. Examination of the human prion protein-like gene doppel for genetic susceptibility to sporadic and variant Creutzfeldt-Jakob disease. Neurosci. Lett. 2000, 290:117-120.
    • (2000) Neurosci. Lett. , vol.290 , pp. 117-120
    • Mead, S.1    Beck, J.2    Dickinson, A.3    Fisher, E.M.4    Collinge, J.5
  • 123
    • 75649086115 scopus 로고    scopus 로고
    • Epithelial-mesenchymal transition in development and cancer
    • Micalizzi D.S., Ford H.L. Epithelial-mesenchymal transition in development and cancer. Future Oncol. 2009, 5:1129-1143.
    • (2009) Future Oncol. , vol.5 , pp. 1129-1143
    • Micalizzi, D.S.1    Ford, H.L.2
  • 124
    • 34249941302 scopus 로고    scopus 로고
    • Copper and the prion protein: methods, structures, function, and disease
    • Millhauser G.L. Copper and the prion protein: methods, structures, function, and disease. Annu. Rev. Phys. Chem. 2007, 58:299-320.
    • (2007) Annu. Rev. Phys. Chem. , vol.58 , pp. 299-320
    • Millhauser, G.L.1
  • 125
    • 52949091163 scopus 로고    scopus 로고
    • Zinc signalling and subcellular distribution: emerging targets in type 2 diabetes
    • Mocchegiani E., Giacconi R., Malavolta M. Zinc signalling and subcellular distribution: emerging targets in type 2 diabetes. Trends Mol. Med. 2008, 14:419-428.
    • (2008) Trends Mol. Med. , vol.14 , pp. 419-428
    • Mocchegiani, E.1    Giacconi, R.2    Malavolta, M.3
  • 126
    • 0031884894 scopus 로고    scopus 로고
    • Identification of genes controlling germ cell migration and embryonic gonad formation in Drosophila
    • Moore L.A., Broihier H.T., Van Doren M., Lunsford L.B., Lehmann R. Identification of genes controlling germ cell migration and embryonic gonad formation in Drosophila. Development 1998, 125:667-678.
    • (1998) Development , vol.125 , pp. 667-678
    • Moore, L.A.1    Broihier, H.T.2    Van Doren, M.3    Lunsford, L.B.4    Lehmann, R.5
  • 127
    • 1642523682 scopus 로고    scopus 로고
    • Inter- and intra-octarepeat Cu(II) site geometries in the prion protein: implications in Cu(II) binding cooperativity and Cu(II)-mediated assemblies
    • Morante S., Gonzalez-Iglesias R., Potrich C., Meneghini C., Meyer-Klaucke W., Menestrina G., Gasset M. Inter- and intra-octarepeat Cu(II) site geometries in the prion protein: implications in Cu(II) binding cooperativity and Cu(II)-mediated assemblies. J. Biol. Chem. 2004, 279:11753-11759.
    • (2004) J. Biol. Chem. , vol.279 , pp. 11753-11759
    • Morante, S.1    Gonzalez-Iglesias, R.2    Potrich, C.3    Meneghini, C.4    Meyer-Klaucke, W.5    Menestrina, G.6    Gasset, M.7
  • 128
    • 0016395653 scopus 로고
    • Letter: Acrodermatitis enteropathica: a lethal inherited human zinc-deficiency disorder
    • Moynahan E.J. Letter: Acrodermatitis enteropathica: a lethal inherited human zinc-deficiency disorder. Lancet 1974, 2:399-400.
    • (1974) Lancet , vol.2 , pp. 399-400
    • Moynahan, E.J.1
  • 129
    • 1342347557 scopus 로고    scopus 로고
    • Minimal mutations are required to effect a radical change in function in CEA family members of the Ig superfamily
    • Naghibalhossaini F., Stanners C.P. Minimal mutations are required to effect a radical change in function in CEA family members of the Ig superfamily. J. Cell Sci. 2004, 117:761-769.
    • (2004) J. Cell Sci. , vol.117 , pp. 761-769
    • Naghibalhossaini, F.1    Stanners, C.P.2
  • 130
    • 0036513626 scopus 로고    scopus 로고
    • The snail superfamily of zinc-finger transcription factors
    • Nieto M.A. The snail superfamily of zinc-finger transcription factors. Nat. Rev. Mol. Cell Biol. 2002, 3:155-166.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 155-166
    • Nieto, M.A.1
  • 132
    • 0027074458 scopus 로고
    • Purification and properties of the cellular prion protein from Syrian hamster brain
    • Pan K.M., Stahl N., Prusiner S.B. Purification and properties of the cellular prion protein from Syrian hamster brain. Protein Sci. 1992, 1:1343-1352.
    • (1992) Protein Sci. , vol.1 , pp. 1343-1352
    • Pan, K.M.1    Stahl, N.2    Prusiner, S.B.3
  • 133
    • 1642524321 scopus 로고    scopus 로고
    • Dual mechanisms for shedding of the cellular prion protein
    • Parkin E.T., Watt N.T., Turner A.J., Hooper N.M. Dual mechanisms for shedding of the cellular prion protein. J. Biol. Chem. 2004, 279:11170-11178.
    • (2004) J. Biol. Chem. , vol.279 , pp. 11170-11178
    • Parkin, E.T.1    Watt, N.T.2    Turner, A.J.3    Hooper, N.M.4
  • 134
    • 0032509499 scopus 로고    scopus 로고
    • Copper stimulates endocytosis of the prion protein
    • Pauly P.C., Harris D.A. Copper stimulates endocytosis of the prion protein. J. Biol. Chem. 1998, 273:33107-33110.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33107-33110
    • Pauly, P.C.1    Harris, D.A.2
  • 135
    • 0342858819 scopus 로고    scopus 로고
    • First report of polymorphisms in the prion-like protein gene (PRND): implications for human prion diseases
    • Peoc'h K., Guerin C., Brandel J.P., Launay J.M., Laplanche J.L. First report of polymorphisms in the prion-like protein gene (PRND): implications for human prion diseases. Neurosci. Lett. 2000, 286:144-148.
    • (2000) Neurosci. Lett. , vol.286 , pp. 144-148
    • Peoc'h, K.1    Guerin, C.2    Brandel, J.P.3    Launay, J.M.4    Laplanche, J.L.5
  • 136
    • 0035799312 scopus 로고    scopus 로고
    • Ablation of the metal ion-induced endocytosis of the prion protein by disease-associated mutation of the octarepeat region
    • Perera W.S., Hooper N.M. Ablation of the metal ion-induced endocytosis of the prion protein by disease-associated mutation of the octarepeat region. Curr. Biol. 2001, 11:519-523.
    • (2001) Curr. Biol. , vol.11 , pp. 519-523
    • Perera, W.S.1    Hooper, N.M.2
  • 137
    • 34347328067 scopus 로고    scopus 로고
    • Targeting of the mouse Slc39a2 (Zip2) gene reveals highly cell-specific patterns of expression, and unique functions in zinc, iron, and calcium homeostasis
    • Peters J.L., Dufner-Beattie J., Xu W., Geiser J., Lahner B., Salt D.E., Andrews G.K. Targeting of the mouse Slc39a2 (Zip2) gene reveals highly cell-specific patterns of expression, and unique functions in zinc, iron, and calcium homeostasis. Genesis 2007, 45:339-352.
    • (2007) Genesis , vol.45 , pp. 339-352
    • Peters, J.L.1    Dufner-Beattie, J.2    Xu, W.3    Geiser, J.4    Lahner, B.5    Salt, D.E.6    Andrews, G.K.7
  • 139
    • 33846844874 scopus 로고    scopus 로고
    • Comparative genomic analysis of prion genes
    • Premzl M., Gamulin V. Comparative genomic analysis of prion genes. BMC Genomics 2007, 8:1.
    • (2007) BMC Genomics , vol.8 , pp. 1
    • Premzl, M.1    Gamulin, V.2
  • 140
    • 8444247483 scopus 로고    scopus 로고
    • Evolution of vertebrate genes related to prion and shadoo proteins - clues from comparative genomic analysis
    • Premzl M., Gready J.E., Jermin L.S., Simonic T., Marshall Graves J.A. Evolution of vertebrate genes related to prion and shadoo proteins - clues from comparative genomic analysis. Mol. Biol. Evol. 2004, 21:2210-2231.
    • (2004) Mol. Biol. Evol. , vol.21 , pp. 2210-2231
    • Premzl, M.1    Gready, J.E.2    Jermin, L.S.3    Simonic, T.4    Marshall Graves, J.A.5
  • 141
    • 0141760321 scopus 로고    scopus 로고
    • Shadoo, a new protein highly conserved from fish to mammals and with similarity to prion protein
    • Premzl M., Sangiorgio L., Strumbo B., Marshall Graves J.A., Simonic T., Gready J.E. Shadoo, a new protein highly conserved from fish to mammals and with similarity to prion protein. Gene 2003, 314:89-102.
    • (2003) Gene , vol.314 , pp. 89-102
    • Premzl, M.1    Sangiorgio, L.2    Strumbo, B.3    Marshall Graves, J.A.4    Simonic, T.5    Gready, J.E.6
  • 142
    • 0028874320 scopus 로고
    • A 60-kDa prion protein (PrP) with properties of both the normal and scrapie-associated forms of PrP
    • Priola S.A., Caughey B., Wehrly K., Chesebro B. A 60-kDa prion protein (PrP) with properties of both the normal and scrapie-associated forms of PrP. J. Biol. Chem. 1995, 270:3299-3305.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3299-3305
    • Priola, S.A.1    Caughey, B.2    Wehrly, K.3    Chesebro, B.4
  • 145
    • 63249096637 scopus 로고    scopus 로고
    • ATM-mediated transcriptional elevation of prion in response to copper-induced oxidative stress
    • Qin K., Zhao L., Ash R.D., McDonough W.F., Zhao R.Y. ATM-mediated transcriptional elevation of prion in response to copper-induced oxidative stress. J. Biol. Chem. 2009, 284:4582-4593.
    • (2009) J. Biol. Chem. , vol.284 , pp. 4582-4593
    • Qin, K.1    Zhao, L.2    Ash, R.D.3    McDonough, W.F.4    Zhao, R.Y.5
  • 146
    • 33746417936 scopus 로고    scopus 로고
    • Doppel-induced apoptosis and counteraction by cellular prion protein in neuroblastoma and astrocytes
    • Qin K., Zhao L., Tang Y., Bhatta S., Simard J.M., Zhao R.Y. Doppel-induced apoptosis and counteraction by cellular prion protein in neuroblastoma and astrocytes. Neuroscience 2006, 141:1375-1388.
    • (2006) Neuroscience , vol.141 , pp. 1375-1388
    • Qin, K.1    Zhao, L.2    Tang, Y.3    Bhatta, S.4    Simard, J.M.5    Zhao, R.Y.6
  • 147
    • 47949104726 scopus 로고    scopus 로고
    • Stress-protective signalling of prion protein is corrupted by scrapie prions
    • Rambold A.S., Muller V., Ron U., Ben-Tal N., Winklhofer K.F., Tatzelt J. Stress-protective signalling of prion protein is corrupted by scrapie prions. EMBO J. 2008, 27:1974-1984.
    • (2008) EMBO J. , vol.27 , pp. 1974-1984
    • Rambold, A.S.1    Muller, V.2    Ron, U.3    Ben-Tal, N.4    Winklhofer, K.F.5    Tatzelt, J.6
  • 148
    • 70249140847 scopus 로고    scopus 로고
    • Prion metal interaction: is prion pathogenesis a cause or a consequence of metal imbalance?
    • Rana A., Gnaneswari D., Bansal S., Kundu B. Prion metal interaction: is prion pathogenesis a cause or a consequence of metal imbalance?. Chem. Biol. Interact. 2009, 181:282-291.
    • (2009) Chem. Biol. Interact. , vol.181 , pp. 282-291
    • Rana, A.1    Gnaneswari, D.2    Bansal, S.3    Kundu, B.4
  • 149
    • 0029036451 scopus 로고
    • Evolutionary families of metallopeptidases
    • Rawlings N.D., Barrett A.J. Evolutionary families of metallopeptidases. Methods Enzymol. 1995, 248:183-228.
    • (1995) Methods Enzymol. , vol.248 , pp. 183-228
    • Rawlings, N.D.1    Barrett, A.J.2
  • 150
    • 0031883399 scopus 로고    scopus 로고
    • The genetic control of the distinction between fat body and gonadal mesoderm in Drosophila
    • Riechmann V., Rehorn K.P., Reuter R., Leptin M. The genetic control of the distinction between fat body and gonadal mesoderm in Drosophila. Development 1998, 125:713-723.
    • (1998) Development , vol.125 , pp. 713-723
    • Riechmann, V.1    Rehorn, K.P.2    Reuter, R.3    Leptin, M.4
  • 152
    • 0037301562 scopus 로고    scopus 로고
    • An evolutionary basis for scrapie disease: identification of a fish prion mRNA
    • Rivera-Milla E., Stuermer C.A.O., Malaga-Trillo E. An evolutionary basis for scrapie disease: identification of a fish prion mRNA. Trends Genetics 2003, 19:72-75.
    • (2003) Trends Genetics , vol.19 , pp. 72-75
    • Rivera-Milla, E.1    Stuermer, C.A.O.2    Malaga-Trillo, E.3
  • 154
    • 33749377870 scopus 로고    scopus 로고
    • Large-scale intron conservation and order-of-magnitude variation in intron loss/gain rates in apicomplexan evolution
    • Roy S.W., Penny D. Large-scale intron conservation and order-of-magnitude variation in intron loss/gain rates in apicomplexan evolution. Genome Res. 2006, 16:1270-1275.
    • (2006) Genome Res. , vol.16 , pp. 1270-1275
    • Roy, S.W.1    Penny, D.2
  • 155
    • 55949095393 scopus 로고    scopus 로고
    • Zinc transporters ZnT1 (Slc30a1) Zip8 (Slc39a8), and Zip10 (Slc39a10) in mouse red blood cells are differentially regulated during erythroid development and by dietary zinc deficiency
    • Ryu M.S., Lichten L.A., Liuzzi J.P., Cousins R.J. Zinc transporters ZnT1 (Slc30a1) Zip8 (Slc39a8), and Zip10 (Slc39a10) in mouse red blood cells are differentially regulated during erythroid development and by dietary zinc deficiency. J. Nutr. 2008, 138:2076-2083.
    • (2008) J. Nutr. , vol.138 , pp. 2076-2083
    • Ryu, M.S.1    Lichten, L.A.2    Liuzzi, J.P.3    Cousins, R.J.4
  • 156
    • 0029760949 scopus 로고    scopus 로고
    • Three-exon structure of the gene encoding the rat prion protein and its expression in tissues
    • Saeki K., Matsumoto Y., Hirota Y., Onodera T. Three-exon structure of the gene encoding the rat prion protein and its expression in tissues. Virus Genes 1996, 12:15-20.
    • (1996) Virus Genes , vol.12 , pp. 15-20
    • Saeki, K.1    Matsumoto, Y.2    Hirota, Y.3    Onodera, T.4
  • 157
    • 33646571843 scopus 로고    scopus 로고
    • Recent advances in clarifying prion protein functions using knockout mice and derived cell lines
    • Sakudo A., Onodera T., Suganuma Y., Kobayashi T., Saeki K., Ikuta K. Recent advances in clarifying prion protein functions using knockout mice and derived cell lines. Mini Rev. Med. Chem. 2006, 6:589-601.
    • (2006) Mini Rev. Med. Chem. , vol.6 , pp. 589-601
    • Sakudo, A.1    Onodera, T.2    Suganuma, Y.3    Kobayashi, T.4    Saeki, K.5    Ikuta, K.6
  • 158
    • 0025674324 scopus 로고
    • Integration specificity of retrotransposons and retroviruses
    • Sandmeyer S.B., Hansen L.J., Chalker D.L. Integration specificity of retrotransposons and retroviruses. Annu. Rev. Genet. 1990, 24:491-518.
    • (1990) Annu. Rev. Genet. , vol.24 , pp. 491-518
    • Sandmeyer, S.B.1    Hansen, L.J.2    Chalker, D.L.3
  • 159
    • 18544376071 scopus 로고    scopus 로고
    • Prion protein recruits its neuronal receptor NCAM to lipid rafts to activate p59fyn and to enhance neurite outgrowth
    • Santuccione A., Sytnyk V., Leshchyns'ka I., Schachner M. Prion protein recruits its neuronal receptor NCAM to lipid rafts to activate p59fyn and to enhance neurite outgrowth. J. Cell Biol. 2005, 169:341-354.
    • (2005) J. Cell Biol. , vol.169 , pp. 341-354
    • Santuccione, A.1    Sytnyk, V.2    Leshchyns'ka, I.3    Schachner, M.4
  • 161
    • 70349669073 scopus 로고    scopus 로고
    • Evolutionary descent of prion genes from the ZIP family of metal ion transporters
    • Schmitt-Ulms G., Ehsani S., Watts J.C., Westaway D., Wille H. Evolutionary descent of prion genes from the ZIP family of metal ion transporters. PLoS One 2009, 4:e7208.
    • (2009) PLoS One , vol.4
    • Schmitt-Ulms, G.1    Ehsani, S.2    Watts, J.C.3    Westaway, D.4    Wille, H.5
  • 164
    • 61549101845 scopus 로고    scopus 로고
    • Concordant correlation of LIV-1 and E-cadherin expression in human breast cancer cell MCF-7
    • Shen H., Qin H., Guo J. Concordant correlation of LIV-1 and E-cadherin expression in human breast cancer cell MCF-7. Mol. Biol. Rep. 2009, 36:653-659.
    • (2009) Mol. Biol. Rep. , vol.36 , pp. 653-659
    • Shen, H.1    Qin, H.2    Guo, J.3
  • 165
    • 0027204276 scopus 로고
    • A prion protein cycles between the cell surface and an endocytic compartment in cultured neuroblastoma cells
    • Shyng S.L., Huber M.T., Harris D.A. A prion protein cycles between the cell surface and an endocytic compartment in cultured neuroblastoma cells. J. Biol. Chem. 1993, 268:15922-15928.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15922-15928
    • Shyng, S.L.1    Huber, M.T.2    Harris, D.A.3
  • 166
    • 0034282872 scopus 로고    scopus 로고
    • Doppel is an N-glycosylated, glycosylphosphatidylinositol-anchored protein Expression in testis and ectopic production in the brains of Prnp(0/0) mice predisposed to Purkinje cell loss
    • Silverman G.L., Qin K., Moore R.C., Yang Y., Mastrangelo P., Tremblay P., Prusiner S.B., Cohen F.E., Westaway D. Doppel is an N-glycosylated, glycosylphosphatidylinositol-anchored protein Expression in testis and ectopic production in the brains of Prnp(0/0) mice predisposed to Purkinje cell loss. J. Biol. Chem. 2000, 275:26834-26841.
    • (2000) J. Biol. Chem. , vol.275 , pp. 26834-26841
    • Silverman, G.L.1    Qin, K.2    Moore, R.C.3    Yang, Y.4    Mastrangelo, P.5    Tremblay, P.6    Prusiner, S.B.7    Cohen, F.E.8    Westaway, D.9
  • 168
    • 33644766915 scopus 로고    scopus 로고
    • Prion protein (PrPc) positively regulates neural precursor proliferation during developmental and adult mammalian neurogenesis
    • Steele A.D., Emsley J.G., Ozdinler P.H., Lindquist S., Macklis J.D. Prion protein (PrPc) positively regulates neural precursor proliferation during developmental and adult mammalian neurogenesis. Proc. Natl. Acad. Sci. U.S.A. 2006, 103:3416-3421.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 3416-3421
    • Steele, A.D.1    Emsley, J.G.2    Ozdinler, P.H.3    Lindquist, S.4    Macklis, J.D.5
  • 169
    • 0037028486 scopus 로고    scopus 로고
    • Ermelin, an endoplasmic reticulum transmembrane protein, contains the novel HELP domain conserved in eukaryotes
    • Suzuki A., Endo T. Ermelin, an endoplasmic reticulum transmembrane protein, contains the novel HELP domain conserved in eukaryotes. Gene 2002, 284:31-40.
    • (2002) Gene , vol.284 , pp. 31-40
    • Suzuki, A.1    Endo, T.2
  • 170
    • 0036298793 scopus 로고    scopus 로고
    • CDNA sequence and tissue expression of Fugu rubripes prion protein-like: a candidate for the teleost orthologue of tetrapod PrPs
    • Suzuki T., Kurokawa T., Hashimoto H., Sugiyama M. cDNA sequence and tissue expression of Fugu rubripes prion protein-like: a candidate for the teleost orthologue of tetrapod PrPs. Biochem. Biophys. Res. Commun. 2002, 294:912-917.
    • (2002) Biochem. Biophys. Res. Commun. , vol.294 , pp. 912-917
    • Suzuki, T.1    Kurokawa, T.2    Hashimoto, H.3    Sugiyama, M.4
  • 171
    • 55349130350 scopus 로고    scopus 로고
    • Zn(II) ions bind very efficiently to tandem repeat region of "prion related protein" (PrP-rel-2) of zebra-fish MS and potentiometric evidence
    • Szyrwiel L., Jankowska E., Janicka-Klos A., Szewczuk Z., Valensin D., Kozlowski H. Zn(II) ions bind very efficiently to tandem repeat region of "prion related protein" (PrP-rel-2) of zebra-fish MS and potentiometric evidence. Dalton Trans. 2008, 44:6117-6120.
    • (2008) Dalton Trans. , vol.44 , pp. 6117-6120
    • Szyrwiel, L.1    Jankowska, E.2    Janicka-Klos, A.3    Szewczuk, Z.4    Valensin, D.5    Kozlowski, H.6
  • 172
    • 0030468932 scopus 로고    scopus 로고
    • Cadherin-mediated cell adhesion and cell motility in Drosophila trachea regulated by the transcription factor Escargot
    • Tanaka-Matakatsu M., Uemura T., Oda H., Takeichi M., Hayashi S. Cadherin-mediated cell adhesion and cell motility in Drosophila trachea regulated by the transcription factor Escargot. Development 1996, 122:3697-3705.
    • (1996) Development , vol.122 , pp. 3697-3705
    • Tanaka-Matakatsu, M.1    Uemura, T.2    Oda, H.3    Takeichi, M.4    Hayashi, S.5
  • 174
    • 33748774652 scopus 로고    scopus 로고
    • Fear of intimacy-a close LIV-1 acquaintancy?
    • Taylor K., Nicholson R.I. Fear of intimacy-a close LIV-1 acquaintancy?. Development 2006, 133:3053.
    • (2006) Development , vol.133 , pp. 3053
    • Taylor, K.1    Nicholson, R.I.2
  • 175
    • 0033931310 scopus 로고    scopus 로고
    • LIV-1 breast cancer protein belongs to new family of histidine-rich membrane proteins with potential to control intracellular Zn2+ homeostasis
    • Taylor K.M. LIV-1 breast cancer protein belongs to new family of histidine-rich membrane proteins with potential to control intracellular Zn2+ homeostasis. IUBMB Life 2000, 49:249-253.
    • (2000) IUBMB Life , vol.49 , pp. 249-253
    • Taylor, K.M.1
  • 176
    • 59149096668 scopus 로고    scopus 로고
    • A distinct role in breast cancer for two LIV-1 family zinc transporters
    • Taylor K.M. A distinct role in breast cancer for two LIV-1 family zinc transporters. Biochem. Soc. Trans. 2008, 36:1247-1251.
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 1247-1251
    • Taylor, K.M.1
  • 177
    • 8444226084 scopus 로고    scopus 로고
    • Zinc transporter LIV-1: a link between cellular development and cancer progression
    • Taylor K.M., Hiscox S., Nicholson R.I. Zinc transporter LIV-1: a link between cellular development and cancer progression. Trends Endocrinol. Metab. 2004, 15:461-463.
    • (2004) Trends Endocrinol. Metab. , vol.15 , pp. 461-463
    • Taylor, K.M.1    Hiscox, S.2    Nicholson, R.I.3
  • 178
    • 0142009677 scopus 로고    scopus 로고
    • Structure-function analysis of LIV-1, the breast cancer-associated protein that belongs to a new subfamily of zinc transporters
    • Taylor K.M., Morgan H.E., Johnson A., Hadley L.J., Nicholson R.I. Structure-function analysis of LIV-1, the breast cancer-associated protein that belongs to a new subfamily of zinc transporters. Biochem. J. 2003, 375:51-59.
    • (2003) Biochem. J. , vol.375 , pp. 51-59
    • Taylor, K.M.1    Morgan, H.E.2    Johnson, A.3    Hadley, L.J.4    Nicholson, R.I.5
  • 179
    • 11844279752 scopus 로고    scopus 로고
    • Structure-function analysis of a novel member of the LIV-1 subfamily of zinc transporters, ZIP14
    • Taylor K.M., Morgan H.E., Johnson A., Nicholson R.I. Structure-function analysis of a novel member of the LIV-1 subfamily of zinc transporters, ZIP14. FEBS Lett. 2005, 579:427-432.
    • (2005) FEBS Lett. , vol.579 , pp. 427-432
    • Taylor, K.M.1    Morgan, H.E.2    Johnson, A.3    Nicholson, R.I.4
  • 181
    • 0037379164 scopus 로고    scopus 로고
    • The LZT proteins; the LIV-1 subfamily of zinc transporters
    • Taylor K.M., Nicholson R.I. The LZT proteins; the LIV-1 subfamily of zinc transporters. Biochim. Biophys. Acta 2003, 1611:16-30.
    • (2003) Biochim. Biophys. Acta , vol.1611 , pp. 16-30
    • Taylor, K.M.1    Nicholson, R.I.2
  • 182
    • 70450198396 scopus 로고    scopus 로고
    • Epithelial-mesenchymal transitions in development and disease
    • Thiery J.P., Acloque H., Huang R.Y., Nieto M.A. Epithelial-mesenchymal transitions in development and disease. Cell 2009, 139:871-890.
    • (2009) Cell , vol.139 , pp. 871-890
    • Thiery, J.P.1    Acloque, H.2    Huang, R.Y.3    Nieto, M.A.4
  • 184
  • 185
    • 12744263653 scopus 로고    scopus 로고
    • Extracellular copper ions regulate cellular prion protein (PrPC) expression and metabolism in neuronal cells
    • Toni M., Massimino M.L., Griffoni C., Salvato B., Tomasi V., Spisni E. Extracellular copper ions regulate cellular prion protein (PrPC) expression and metabolism in neuronal cells. FEBS Lett. 2005, 579:741-744.
    • (2005) FEBS Lett. , vol.579 , pp. 741-744
    • Toni, M.1    Massimino, M.L.2    Griffoni, C.3    Salvato, B.4    Tomasi, V.5    Spisni, E.6
  • 186
    • 33846815516 scopus 로고    scopus 로고
    • Identification of novel genes that co-cluster with estrogen receptor alpha in breast tumor biopsy specimens, using a large-scale real-time reverse transcription-PCR approach
    • Tozlu S., Girault I., Vacher S., Vendrell J., Andrieu C., Spyratos F., Cohen P., Lidereau R., Bieche I. Identification of novel genes that co-cluster with estrogen receptor alpha in breast tumor biopsy specimens, using a large-scale real-time reverse transcription-PCR approach. Endocr. Relat. Cancer 2006, 13:1109-1120.
    • (2006) Endocr. Relat. Cancer , vol.13 , pp. 1109-1120
    • Tozlu, S.1    Girault, I.2    Vacher, S.3    Vendrell, J.4    Andrieu, C.5    Spyratos, F.6    Cohen, P.7    Lidereau, R.8    Bieche, I.9
  • 189
    • 0038348380 scopus 로고    scopus 로고
    • Fear of intimacy encodes a novel transmembrane protein required for gonad morphogenesis in Drosophila
    • Van Doren M., Mathews W.R., Samuels M., Moore L.A., Broihier H.T., Lehmann R. fear of intimacy encodes a novel transmembrane protein required for gonad morphogenesis in Drosophila. Development 2003, 130:2355-2364.
    • (2003) Development , vol.130 , pp. 2355-2364
    • Van Doren, M.1    Mathews, W.R.2    Samuels, M.3    Moore, L.A.4    Broihier, H.T.5    Lehmann, R.6
  • 191
    • 33846476657 scopus 로고    scopus 로고
    • Novel aspects of prions, their receptor molecules, and innovative approaches for TSE therapy
    • Vana K., Zuber C., Nikles D., Weiss S. Novel aspects of prions, their receptor molecules, and innovative approaches for TSE therapy. Cell. Mol. Neurobiol. 2007, 27:107-128.
    • (2007) Cell. Mol. Neurobiol. , vol.27 , pp. 107-128
    • Vana, K.1    Zuber, C.2    Nikles, D.3    Weiss, S.4
  • 193
    • 0028788207 scopus 로고
    • The effect of the acrodermatitis enteropathica mutation on zinc uptake in human fibroblasts
    • Vazquez F., Grider A. The effect of the acrodermatitis enteropathica mutation on zinc uptake in human fibroblasts. Biol. Trace Elem. Res. 1995, 50:109-117.
    • (1995) Biol. Trace Elem. Res. , vol.50 , pp. 109-117
    • Vazquez, F.1    Grider, A.2
  • 194
    • 0034634655 scopus 로고    scopus 로고
    • Phorbol ester-regulated cleavage of normal prion protein in HEK293 human cells and murine neurons
    • Vincent B., Paitel E., Frobert Y., Lehmann S., Grassi J., Checler F. Phorbol ester-regulated cleavage of normal prion protein in HEK293 human cells and murine neurons. J. Biol. Chem. 2000, 275:35612-35616.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35612-35616
    • Vincent, B.1    Paitel, E.2    Frobert, Y.3    Lehmann, S.4    Grassi, J.5    Checler, F.6
  • 195
    • 0035851151 scopus 로고    scopus 로고
    • The disintegrins ADAM10 and TACE contribute to the constitutive and phorbol ester-regulated normal cleavage of the cellular prion protein
    • Vincent B., Paitel E., Saftig P., Frobert Y., Hartmann D., De Strooper B., Grassi J., Lopez-Perez E., Checler F. The disintegrins ADAM10 and TACE contribute to the constitutive and phorbol ester-regulated normal cleavage of the cellular prion protein. J. Biol. Chem. 2001, 276:37743-37746.
    • (2001) J. Biol. Chem. , vol.276 , pp. 37743-37746
    • Vincent, B.1    Paitel, E.2    Saftig, P.3    Frobert, Y.4    Hartmann, D.5    De Strooper, B.6    Grassi, J.7    Lopez-Perez, E.8    Checler, F.9
  • 197
    • 59349099006 scopus 로고    scopus 로고
    • Alpha-cleavage of the prion protein occurs in a late compartment of the secretory pathway and is independent of lipid rafts
    • Walmsley A.R., Watt N.T., Taylor D.R., Perera W.S., Hooper N.M. alpha-cleavage of the prion protein occurs in a late compartment of the secretory pathway and is independent of lipid rafts. Mol. Cell. Neurosci. 2009, 40:242-248.
    • (2009) Mol. Cell. Neurosci. , vol.40 , pp. 242-248
    • Walmsley, A.R.1    Watt, N.T.2    Taylor, D.R.3    Perera, W.S.4    Hooper, N.M.5
  • 198
    • 37849042540 scopus 로고    scopus 로고
    • The prion protein is a combined zinc and copper binding protein: Zn2+ alters the distribution of Cu2+ coordination modes
    • Walter E.D., Stevens D.J., Visconte M.P., Millhauser G.L. The prion protein is a combined zinc and copper binding protein: Zn2+ alters the distribution of Cu2+ coordination modes. J. Am. Chem. Soc. 2007, 129:15440-15441.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 15440-15441
    • Walter, E.D.1    Stevens, D.J.2    Visconte, M.P.3    Millhauser, G.L.4
  • 199
    • 2642587498 scopus 로고    scopus 로고
    • Zinc-stimulated endocytosis controls activity of the mouse ZIP1 and ZIP3 zinc uptake transporters
    • Wang F., Dufner-Beattie J., Kim B.E., Petris M.J., Andrews G., Eide D.J. Zinc-stimulated endocytosis controls activity of the mouse ZIP1 and ZIP3 zinc uptake transporters. J. Biol. Chem. 2004, 279:24631-24639.
    • (2004) J. Biol. Chem. , vol.279 , pp. 24631-24639
    • Wang, F.1    Dufner-Beattie, J.2    Kim, B.E.3    Petris, M.J.4    Andrews, G.5    Eide, D.J.6
  • 200
    • 1542376716 scopus 로고    scopus 로고
    • Acrodermatitis enteropathica mutations affect transport activity, localization and zinc-responsive trafficking of the mouse ZIP4 zinc transporter
    • Wang F., Kim B.E., Dufner-Beattie J., Petris M.J., Andrews G., Eide D.J. Acrodermatitis enteropathica mutations affect transport activity, localization and zinc-responsive trafficking of the mouse ZIP4 zinc transporter. Hum. Mol. Genet. 2004, 13:563-571.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 563-571
    • Wang, F.1    Kim, B.E.2    Dufner-Beattie, J.3    Petris, M.J.4    Andrews, G.5    Eide, D.J.6
  • 201
    • 10944273358 scopus 로고    scopus 로고
    • The mammalian Zip5 protein is a zinc transporter that localizes to the basolateral surface of polarized cells
    • Wang F., Kim B.E., Petris M.J., Eide D.J. The mammalian Zip5 protein is a zinc transporter that localizes to the basolateral surface of polarized cells. J. Biol. Chem. 2004, 279:51433-51441.
    • (2004) J. Biol. Chem. , vol.279 , pp. 51433-51441
    • Wang, F.1    Kim, B.E.2    Petris, M.J.3    Eide, D.J.4
  • 202
    • 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., Gitschier J. A novel member of a zinc transporter family is defective in acrodermatitis enteropathica. Am. J. Hum. Genet. 2002, 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
  • 203
    • 0042658237 scopus 로고    scopus 로고
    • The prion protein and neuronal zinc homeostasis
    • Watt N.T., Hooper N.M. The prion protein and neuronal zinc homeostasis. Trends Biochem. Sci. 2003, 28:406-410.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 406-410
    • Watt, N.T.1    Hooper, N.M.2
  • 204
    • 27744547982 scopus 로고    scopus 로고
    • Reactive oxygen species-mediated beta-cleavage of the prion protein in the cellular response to oxidative stress
    • Watt N.T., Taylor D.R., Gillott A., Thomas D.A., Perera W.S., Hooper N.M. Reactive oxygen species-mediated beta-cleavage of the prion protein in the cellular response to oxidative stress. J. Biol. Chem. 2005, 280:35914-35921.
    • (2005) J. Biol. Chem. , vol.280 , pp. 35914-35921
    • Watt, N.T.1    Taylor, D.R.2    Gillott, A.3    Thomas, D.A.4    Perera, W.S.5    Hooper, N.M.6
  • 207
    • 34249937435 scopus 로고    scopus 로고
    • The prion protein family: diversity, rivalry, and dysfunction
    • Watts J.C., Westaway D. The prion protein family: diversity, rivalry, and dysfunction. Biochim. Biophys. Acta 2007, 1772:654-672.
    • (2007) Biochim. Biophys. Acta , vol.1772 , pp. 654-672
    • Watts, J.C.1    Westaway, D.2
  • 209
    • 36248960703 scopus 로고    scopus 로고
    • Novel zinc-responsive post-transcriptional mechanisms reciprocally regulate expression of the mouse Slc39a4 and Slc39a5 zinc transporters (Zip4 and Zip5)
    • Weaver B.P., Dufner-Beattie J., Kambe T., Andrews G.K. Novel zinc-responsive post-transcriptional mechanisms reciprocally regulate expression of the mouse Slc39a4 and Slc39a5 zinc transporters (Zip4 and Zip5). Biol. Chem. 2007, 388:1301-1312.
    • (2007) Biol. Chem. , vol.388 , pp. 1301-1312
    • Weaver, B.P.1    Dufner-Beattie, J.2    Kambe, T.3    Andrews, G.K.4
  • 210
    • 78049316349 scopus 로고    scopus 로고
    • Zip4 (Slc39a4) expression is activated in hepatocellular carcinomas and functions to repress apoptosis, enhance cell cycle and increase migration
    • Weaver B.P., Zhang Y., Hiscox S., Guo G.L., Apte U., Taylor K.M., Sheline C.T., Wang L., Andrews G.K. Zip4 (Slc39a4) expression is activated in hepatocellular carcinomas and functions to repress apoptosis, enhance cell cycle and increase migration. PLoS One 2010, 5.
    • (2010) PLoS One , pp. 5
    • Weaver, B.P.1    Zhang, Y.2    Hiscox, S.3    Guo, G.L.4    Apte, U.5    Taylor, K.M.6    Sheline, C.T.7    Wang, L.8    Andrews, G.K.9
  • 212
    • 26944485546 scopus 로고    scopus 로고
    • Two major branches of anti-cadmium defense in the mouse: MTF-1/metallothioneins and glutathione
    • Wimmer U., Wang Y., Georgiev O., Schaffner W. Two major branches of anti-cadmium defense in the mouse: MTF-1/metallothioneins and glutathione. Nucleic Acids Res. 2005, 33:5715-5727.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 5715-5727
    • Wimmer, U.1    Wang, Y.2    Georgiev, O.3    Schaffner, W.4
  • 213
    • 0034931126 scopus 로고    scopus 로고
    • Three-dimensional structures of prion proteins
    • Wuthrich K., Riek R. Three-dimensional structures of prion proteins. Adv. Protein Chem. 2001, 57:55-82.
    • (2001) Adv. Protein Chem. , vol.57 , pp. 55-82
    • Wuthrich, K.1    Riek, R.2
  • 216
    • 2442674220 scopus 로고    scopus 로고
    • Zinc transporter LIVI controls epithelial-mesenchymal transition in zebrafish gastrula organizer
    • Yamashita S., Miyagi C., Fukada T., Kagara N., Che Y.S., Hirano T. Zinc transporter LIVI controls epithelial-mesenchymal transition in zebrafish gastrula organizer. Nature 2004, 429:298-302.
    • (2004) Nature , vol.429 , pp. 298-302
    • Yamashita, S.1    Miyagi, C.2    Fukada, T.3    Kagara, N.4    Che, Y.S.5    Hirano, T.6
  • 217
    • 0242662244 scopus 로고    scopus 로고
    • The octapeptide repeats in mammalian prion protein constitute a pH-dependent folding and aggregation site
    • Zahn R. The octapeptide repeats in mammalian prion protein constitute a pH-dependent folding and aggregation site. J. Mol. Biol. 2003, 334:477-488.
    • (2003) J. Mol. Biol. , vol.334 , pp. 477-488
    • Zahn, R.1
  • 218
    • 0037423709 scopus 로고    scopus 로고
    • NMR structure of a variant human prion protein with two disulfide bridges
    • Zahn R., Guntert P., von Schroetter C., Wuthrich K. NMR structure of a variant human prion protein with two disulfide bridges. J. Mol. Biol. 2003, 326:225-234.
    • (2003) J. Mol. Biol. , vol.326 , pp. 225-234
    • Zahn, R.1    Guntert, P.2    von Schroetter, C.3    Wuthrich, K.4
  • 219
    • 33144456321 scopus 로고    scopus 로고
    • Prion protein is expressed on long-term repopulating hematopoietic stem cells and is important for their self-renewal
    • Zhang C.C., Steele A.D., Lindquist S., Lodish H.F. Prion protein is expressed on long-term repopulating hematopoietic stem cells and is important for their self-renewal. Proc. Natl. Acad. Sci. U.S.A. 2006, 103:2184-2189.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 2184-2189
    • Zhang, C.C.1    Steele, A.D.2    Lindquist, S.3    Lodish, H.F.4
  • 220
    • 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., Eide D. The yeast ZRT1 gene encodes the zinc transporter protein of a high-affinity uptake system induced by zinc limitation. Proc. Natl. Acad. Sci. U.S.A. 1996, 93:2454-2458.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 2454-2458
    • Zhao, H.1    Eide, D.2
  • 221
    • 0029841951 scopus 로고    scopus 로고
    • The ZRT2 gene encodes the low affinity zinc transporter in Saccharomyces cerevisiae
    • Zhao H., Eide D. The ZRT2 gene encodes the low affinity zinc transporter in Saccharomyces cerevisiae. J. Biol. Chem. 1996, 271:23203-23210.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23203-23210
    • Zhao, H.1    Eide, D.2
  • 222
    • 34548723312 scopus 로고    scopus 로고
    • LIV-1 suppression inhibits HeLa cell invasion by targeting ERK1/2-Snail/Slug pathway
    • Zhao L., Chen W., Taylor K.M., Cai B., Li X. LIV-1 suppression inhibits HeLa cell invasion by targeting ERK1/2-Snail/Slug pathway. Biochem. Biophys. Res. Commun. 2007, 363:82-88.
    • (2007) Biochem. Biophys. Res. Commun. , vol.363 , pp. 82-88
    • Zhao, L.1    Chen, W.2    Taylor, K.M.3    Cai, B.4    Li, X.5
  • 223
    • 77957783944 scopus 로고    scopus 로고
    • ZRT/IRT-like protein 14 (ZIP14) promotes the cellular assimilation of iron from transferrin
    • Zhao N., Gao J., Enns C.A., Knutson M.D. ZRT/IRT-like protein 14 (ZIP14) promotes the cellular assimilation of iron from transferrin. J. Biol. Chem. 2010, 285:32141-32150.
    • (2010) J. Biol. Chem. , vol.285 , pp. 32141-32150
    • Zhao, N.1    Gao, J.2    Enns, C.A.3    Knutson, M.D.4
  • 225
    • 49049109504 scopus 로고    scopus 로고
    • Regulation of ZIP and ZnT zinc transporters in zebrafish gill: zinc repression of ZIP10 transcription by an intronic MRE cluster
    • Zheng D., Feeney G.P., Kille P., Hogstrand C. Regulation of ZIP and ZnT zinc transporters in zebrafish gill: zinc repression of ZIP10 transcription by an intronic MRE cluster. Physiol. Genomics 2008, 34:205-214.
    • (2008) Physiol. Genomics , vol.34 , pp. 205-214
    • Zheng, D.1    Feeney, G.P.2    Kille, P.3    Hogstrand, C.4


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