메뉴 건너뛰기




Volumn 287, Issue 17, 2012, Pages 13510-13517

Metal transport across biomembranes: Emerging models for a distinct chemistry

Author keywords

[No Author keywords available]

Indexed keywords

ALKALI EARTH; BIOMEMBRANES; COORDINATION GEOMETRY; DISTINCTIVE FEATURES; DISTRIBUTION OF METAL; ESSENTIAL COMPONENT; KEY ELEMENTS; LIFE PROCESS; METAL TRANSFERS; METAL TRANSPORT; STRUCTURAL INFORMATION; TRANSITION ELEMENT; TRANSMEMBRANE TRANSPORT; TRANSMEMBRANES;

EID: 84859972108     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.R111.319343     Document Type: Short Survey
Times cited : (88)

References (83)
  • 2
    • 70350637580 scopus 로고    scopus 로고
    • Coordination chemistry of bacterial metal transport and sensing
    • Ma, Z., Jacobsen, F. E., and Giedroc, D. P. (2009) Coordination chemistry of bacterial metal transport and sensing. Chem. Rev. 109, 4644-4681
    • (2009) Chem. Rev. , vol.109 , pp. 4644-4681
    • Ma, Z.1    Jacobsen, F.E.2    Giedroc, D.P.3
  • 4
    • 56149117733 scopus 로고    scopus 로고
    • Copper homeostasis in bacteria
    • Osman, D., and Cavet, J. S. (2008) Copper homeostasis in bacteria. Adv.Appl. Microbiol. 65, 217-247
    • (2008) Adv.Appl. Microbiol. , vol.65 , pp. 217-247
    • Osman, D.1    Cavet, J.S.2
  • 5
    • 0035968001 scopus 로고    scopus 로고
    • Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis
    • DOI 10.1126/science.1060331
    • Outten, C. E., and O'Halloran, T. V. (2001) Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis. Science 292, 2488-2492 (Pubitemid 32605687)
    • (2001) Science , vol.292 , Issue.5526 , pp. 2488-2492
    • Outten, C.E.1    O'Halloran, T.V.2
  • 6
    • 0037565061 scopus 로고    scopus 로고
    • Efflux-mediated heavy metal resistance in prokaryotes
    • Nies, D. H. (2003) Efflux-mediated heavy metal resistance in prokaryotes. FEMS Microbiol. Rev. 27, 313-339
    • (2003) FEMS Microbiol. Rev. , vol.27 , pp. 313-339
    • Nies, D.H.1
  • 8
    • 9244234392 scopus 로고    scopus 로고
    • Bacterial iron sources: From siderophores to hemophores
    • DOI 10.1146/annurev.micro.58.030603.123811
    • Wandersman, C., and Delepelaire, P. (2004) Bacterial iron sources: from siderophores to hemophores. Annu. Rev. Microbiol. 58, 611-647 (Pubitemid 39551999)
    • (2004) Annual Review of Microbiology , vol.58 , pp. 611-647
    • Wandersman, C.1    Delepelaire, P.2
  • 9
    • 3843101432 scopus 로고    scopus 로고
    • Arabidopsis Yellow Stripe-Like2 (YSL2): A metal-regulated gene encoding a plasma membrane transporter of nicotianamine-metal complexes
    • DOI 10.1111/j.1365-313X.2004.02128.x
    • DiDonato, R. J., Jr., Roberts, L. A., Sanderson, T., Eisley, R. B., and Walker, E. L. (2004) Arabidopsis Yellow Stripe-Like2 (YSL2): a metal-regulated gene encoding a plasma membrane transporter of nicotinamine-metal complexes. Plant J. 39, 403-414 (Pubitemid 39040145)
    • (2004) Plant Journal , vol.39 , Issue.3 , pp. 403-414
    • DiDonato Jr., R.J.1    Roberts, L.A.2    Sanderson, T.3    Eisley, R.B.4    Walker, E.L.5
  • 11
    • 33646128945 scopus 로고    scopus 로고
    • Put the metal to the petal: Metal uptake and transport throughout plants
    • Colangelo, E. P., and Guerinot, M. L. (2006) Put the metal to the petal: metal uptake and transport throughout plants. Curr. Opin. Plant Biol. 9, 322-330
    • (2006) Curr. Opin. Plant Biol. , vol.9 , pp. 322-330
    • Colangelo, E.P.1    Guerinot, M.L.2
  • 15
    • 34648833810 scopus 로고    scopus 로고
    • Structure of the zinc transporter YiiP
    • DOI 10.1126/science.1143748
    • Lu, M., and Fu, D. (2007) Structure of the zinc transporter YiiP. Science 317, 1746-1748 (Pubitemid 47461838)
    • (2007) Science , vol.317 , Issue.5845 , pp. 1746-1748
    • Lu, M.1    Fu, D.2
  • 19
    • 33644867700 scopus 로고    scopus 로고
    • Projection structure of the human copper transporter CTR1 at 6-Å resolution reveals a compact trimer with a novel channel-like architecture
    • DOI 10.1073/pnas.0509929103
    • Aller, S. G., and Unger, V. M. (2006) Projection structure of the human copper transporter CTR1 at 6-Å resolution reveals a compact trimer with a novel channel-like architecture. Proc. Natl. Acad. Sci. U.S.A. 103, 3627-3632 (Pubitemid 43376606)
    • (2006) Proceedings of the National Academy of Sciences of the United States of America , vol.103 , Issue.10 , pp. 3627-3632
    • Aller, S.G.1    Unger, V.M.2
  • 20
    • 31044446123 scopus 로고    scopus 로고
    • Metal-binding affinity of the transmembrane site in ZntA: Implications for metal selectivity
    • DOI 10.1021/bi051836n
    • Liu, J., Dutta, S. J., Stemmler, A. J., and Mitra, B. (2006) Metal-binding affinity of the transmembrane site in ZntA: implications for metal selectivity. Biochemistry 45, 763-772 (Pubitemid 43122241)
    • (2006) Biochemistry , vol.45 , Issue.3 , pp. 763-772
    • Liu, J.1    Dutta, S.J.2    Stemmler, A.J.3    Mitra, B.4
  • 22
    • 0345114077 scopus 로고
    • Hard and soft acids and bases
    • Pearson, R. G. (1963) Hard and soft acids and bases. J. Am. Chem. Soc. 85, 3533-3539
    • (1963) J. Am. Chem. Soc. , vol.85 , pp. 3533-3539
    • Pearson, R.G.1
  • 23
    • 33747706168 scopus 로고    scopus 로고
    • Binding and transport of metal ions at the dimer interface of the Escherichia coli metal transporter YiiP
    • DOI 10.1074/jbc.M602254200
    • Wei, Y., and Fu, D. (2006) Binding and transport of metal ions at the dimer interface of the Escherichia coli metal transporter YiiP. J. Biol. Chem. 281, 23492-23502 (Pubitemid 44274124)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.33 , pp. 23492-23502
    • Wei, Y.1    Fu, D.2
  • 24
    • 0011509370 scopus 로고    scopus 로고
    • Structural and functional aspects of metal sites in biology
    • Holm, R. H., Kennepohl, P., and Solomon, E. I. (1996) Structural and functional aspects of metal sites in biology. Chem. Rev. 96, 2239-2314 (Pubitemid 126641104)
    • (1996) Chemical Reviews , vol.96 , Issue.7 , pp. 2239-2314
    • Holm, R.H.1    Kennepohl, P.2    Solomon, E.I.3
  • 27
    • 0042208193 scopus 로고    scopus 로고
    • The metal specificity and selectivity of ZntA from Escherichia coli using the acylphosphate intermediate
    • DOI 10.1074/jbc.M301415200
    • Hou, Z., and Mitra, B. (2003) The metal specificity and selectivity of ZntA from Escherichia coli using the acylphosphate intermediate. J. Biol. Chem. 278, 28455-28461 (Pubitemid 36935747)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.31 , pp. 28455-28461
    • Hou, Z.1    Mitra, B.2
  • 28
    • 1842530384 scopus 로고    scopus 로고
    • Kinetic Study of the Antiport Mechanism of an Escherichia coli Zinc Transporter, ZitB
    • DOI 10.1074/jbc.M313510200
    • Chao, Y., and Fu, D. (2004) Kinetic study of the antiport mechanism of an Escherichia coli zinc transporter, ZitB. J. Biol. Chem. 279, 12043-12050 (Pubitemid 38445766)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.13 , pp. 12043-12050
    • Chao, Y.1    Fu, D.2
  • 29
    • 34948819713 scopus 로고    scopus 로고
    • Dissecting the Salmonella response to copper
    • DOI 10.1099/mic.0.2007/006536-0
    • Espariz, M., Checa, S. K., Audero, M. E., Pontel, L. B., and Soncini, F. C. (2007) Dissecting the Salmonella response to copper. Microbiology 153, 2989-2997 (Pubitemid 47517060)
    • (2007) Microbiology , vol.153 , Issue.9 , pp. 2989-2997
    • Espariz, M.1    Checa, S.K.2    Audero, M.E.P.3    Pontel, L.B.4    Soncini, F.C.5
  • 33
    • 0034635468 scopus 로고    scopus 로고
    • The ATP hydrolytic activity of purified ZntA, a Pb(II)/Cd(II)/Zn(II)- translocating ATPase from Escherichia coli
    • Sharma, R., Rensing, C., Rosen, B. P., and Mitra, B. (2000) The ATP hydrolytic activity of purified ZntA, a Pb(II)/Cd(II)/Zn(II)-translocating ATPase from Escherichia coli. J. Biol. Chem. 275, 3873-3978
    • (2000) J. Biol. Chem. , vol.275 , pp. 3873-3978
    • Sharma, R.1    Rensing, C.2    Rosen, B.P.3    Mitra, B.4
  • 35
    • 34447103789 scopus 로고    scopus 로고
    • Trafficking of the copper-ATPases, ATP7A and ATP7B: Role in copper homeostasis
    • DOI 10.1016/j.abb.2007.04.021, PII S000398610700210X
    • La Fontaine, S., and Mercer, J. F. (2007) Trafficking of the copper-ATPases, ATP7A and ATP7B: role in copper homeostasis. Arch. Biochem. Biophys. 463, 149-167 (Pubitemid 47030343)
    • (2007) Archives of Biochemistry and Biophysics , vol.463 , Issue.2 , pp. 149-167
    • La, F.S.1    Mercer, J.F.B.2
  • 36
    • 0037781037 scopus 로고    scopus 로고
    • PAA1, a P-type ATPase of arabidopsis, functions in copper transport in chloroplasts
    • Shikanai, T., Müller-Moulé, P., Munekage, Y., Niyogi, K. K., and Pilon, M. (2003) PAA1, a P-type ATPase of Arabidopsis, functions in copper transport in chloroplasts. Plant Cell 15, 1333-1346 (Pubitemid 36715176)
    • (2003) Plant Cell , vol.15 , Issue.6 , pp. 1333-1346
    • Shikanai, T.1    Muller-Moule, P.2    Munekage, Y.3    Niyogi, K.K.4    Pilon, M.5
  • 38
    • 0028916909 scopus 로고
    • The Menkes/Wilson disease gene homolog in yeast provides copper to a ceruloplasmin-like oxidase required for iron uptake
    • Yuan, D. S., Stearman, R., Dancis, A., Dunn, T., Beeler, T., and Klausner, R. D. (1995) The Menkes/Wilson disease gene homolog in yeast provides copper to a ceruloplasmin-like oxidase required for iron uptake. Proc. Natl. Acad. Sci. U.S.A. 92, 2632-2636
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 2632-2636
    • Yuan, D.S.1    Stearman, R.2    Dancis, A.3    Dunn, T.4    Beeler, T.5    Klausner, R.D.6
  • 40
    • 37249043376 scopus 로고    scopus 로고
    • The structural basis of calcium transport by the calcium pump
    • DOI 10.1038/nature06418, PII NATURE06418
    • Olesen, C., Picard, M., Winther, A. M., Gyrup, C., Morth, J. P., Oxvig, C., Møller, J. V., and Nissen, P. (2007) The structural basis of calcium transport by the calcium pump. Nature 450, 1036-1042 (Pubitemid 350273617)
    • (2007) Nature , vol.450 , Issue.7172 , pp. 1036-1042
    • Olesen, C.1    Picard, M.2    Winther, A.-M.L.3    Gyrup, C.4    Morth, J.P.5    Oxvig, C.6    Moller, J.V.7    Nissen, P.8
  • 41
    • 0035997378 scopus 로고    scopus 로고
    • Biochemistry of Na,K-ATPase
    • Kaplan, J. H. (2002) Biochemistry of Na,K-ATPase. Annu. Rev. Biochem. 71, 511-535
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 511-535
    • Kaplan, J.H.1
  • 42
    • 68749085059 scopus 로고    scopus 로고
    • Dissecting the role of the N-terminal metal-binding domains in activating the yeast copper ATPase in vivo
    • Morin, I., Gudin, S., Mintz, E., and Cuillel, M. (2009) Dissecting the role of the N-terminal metal-binding domains in activating the yeast copper ATPase in vivo. FEBS J. 276, 4483-4495
    • (2009) FEBS J. , vol.276 , pp. 4483-4495
    • Morin, I.1    Gudin, S.2    Mintz, E.3    Cuillel, M.4
  • 43
    • 0036175362 scopus 로고    scopus 로고
    • Metallochaperones and metal-transporting ATPases: A comparative analysis of sequences and structures
    • DOI 10.1101/gr.196802
    • Arnesano, F., Banci, L., Bertini, I., Ciofi-Baffoni, S., Molteni, E., Huffman, D. L., and O'Halloran, T. V. (2002) Metallochaperones and metal-transporting ATPases: a comparative analysis of sequences and structures. Genome Res. 12, 255-271 (Pubitemid 34162992)
    • (2002) Genome Research , vol.12 , Issue.2 , pp. 255-271
    • Arnesano, F.1    Banci, L.2    Bertini, I.3    Ciofi-Baffoni, S.4    Molteni, E.5    Huffman, D.L.6    O'Halloran, T.V.7
  • 45
    • 0141431021 scopus 로고    scopus 로고
    • +-ATPase CopA
    • DOI 10.1021/bi034806y
    • Mandal, A. K., and Argüello, J. M. (2003) Functional roles of metal-binding domains of the Archaeoglobus fulgidus Cu+-ATPase CopA. Biochemistry 42, 11040-11047 (Pubitemid 37174396)
    • (2003) Biochemistry , vol.42 , Issue.37 , pp. 11040-11047
    • Mandal, A.K.1    Arguello, J.M.2
  • 47
    • 0033813548 scopus 로고    scopus 로고
    • Structural basis for copper transfer by the metallochaperone for the Menkes/Wilson disease proteins
    • Wernimont, A. K., Huffman, D. L., Lamb, A. L., O'Halloran, T. V., and Rosenzweig, A. C. (2000) Structural basis for copper transfer by the metallochaperone for the Menkes/Wilson disease proteins. Nat. Struct. Mol. Biol. 7, 766-771
    • (2000) Nat. Struct. Mol. Biol. , vol.7 , pp. 766-771
    • Wernimont, A.K.1    Huffman, D.L.2    Lamb, A.L.3    O'Halloran, T.V.4    Rosenzweig, A.C.5
  • 50
    • 57649207910 scopus 로고    scopus 로고
    • How do bacterial cells ensure that metalloproteins get the correct metal?
    • Waldron, K. J., and Robinson, N. J. (2009) How do bacterial cells ensure that metalloproteins get the correct metal? Nat. Rev. Microbiol. 7, 25-35
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 25-35
    • Waldron, K.J.1    Robinson, N.J.2
  • 51
    • 0033543578 scopus 로고    scopus 로고
    • Energetics and topology of CzcA, a cation/proton antiporter of the resistance-nodulation-cell division protein family
    • Goldberg, M., Pribyl, T., Juhnke, S., and Nies, D. H. (1999) Energetics and topology of CzcA, a cation/proton antiporter of the resistance-nodulation- cell division protein family. J. Biol. Chem. 274, 26065-26070
    • (1999) J. Biol. Chem. , vol.274 , pp. 26065-26070
    • Goldberg, M.1    Pribyl, T.2    Juhnke, S.3    Nies, D.H.4
  • 54
    • 77957141422 scopus 로고    scopus 로고
    • Crystal structures of the CusA efflux pump suggest methionine-mediated metal transport
    • Long, F., Su, C. C., Zimmermann, M. T., Boyken, S. E., Rajashankar, K. R., Jernigan, R. L., and Yu, E. W. (2010) Crystal structures of the CusA efflux pump suggest methionine-mediated metal transport. Nature 467, 484-488
    • (2010) Nature , vol.467 , pp. 484-488
    • Long, F.1    Su, C.C.2    Zimmermann, M.T.3    Boyken, S.E.4    Rajashankar, K.R.5    Jernigan, R.L.6    Yu, E.W.7
  • 55
    • 79952145187 scopus 로고    scopus 로고
    • Crystal structure of the CusBA heavy metal efflux complex of Escherichia coli
    • Su, C. C., Long, F., Zimmermann, M. T., Rajashankar, K. R., Jernigan, R. L., and Yu, E. W. (2011) Crystal structure of the CusBA heavy metal efflux complex of Escherichia coli. Nature 470, 558-562
    • (2011) Nature , vol.470 , pp. 558-562
    • Su, C.C.1    Long, F.2    Zimmermann, M.T.3    Rajashankar, K.R.4    Jernigan, R.L.5    Yu, E.W.6
  • 56
    • 79251563176 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli CusC, the outer membrane component of a heavy metal efflux pump
    • Kulathila, R., Kulathila, R., Indic, M., and van den Berg, B. (2011) Crystal structure of Escherichia coli CusC, the outer membrane component of a heavy metal efflux pump. PLoS ONE 6, e15610
    • (2011) PLoS ONE , vol.6
    • Kulathila, R.1    Kulathila, R.2    Indic, M.3    Van Den Berg, B.4
  • 57
    • 79956087446 scopus 로고    scopus 로고
    • Switch or funnel: How RND-type transport systems control periplasmic metal homeostasis
    • Kim, E. H., Nies, D. H., McEvoy, M. M., and Rensing, C. (2011) Switch or funnel: how RND-type transport systems control periplasmic metal homeostasis. J. Bacteriol. 193, 2381-2387
    • (2011) J. Bacteriol. , vol.193 , pp. 2381-2387
    • Kim, E.H.1    Nies, D.H.2    McEvoy, M.M.3    Rensing, C.4
  • 59
    • 0034718523 scopus 로고    scopus 로고
    • The zinc metalloregulatory protein Synechococcus PCC7942 SmtB binds a single zinc ion per monomer with high affinity in a tetrahedral coordination geometry
    • VanZile, M. L., Cosper, N. J., Scott, R. A., and Giedroc, D. P. (2000) The zinc metalloregulatory protein Synechococcus PCC7942 SmtB binds a single zinc ion per monomer with high affinity in a tetrahedral coordination geometry. Biochemistry 39, 11818-11829
    • (2000) Biochemistry , vol.39 , pp. 11818-11829
    • VanZile, M.L.1    Cosper, N.J.2    Scott, R.A.3    Giedroc, D.P.4
  • 60
    • 37249081439 scopus 로고    scopus 로고
    • Substrate-linked conformational change in the periplasmic component of a Cu(I)/Ag(I) efflux system
    • DOI 10.1074/jbc.M703937200
    • Bagai, I., Liu, W., Rensing, C., Blackburn, N. J., and McEvoy, M. M. (2007) Substrate-linked conformational change in the periplasmic component of a Cu(I)/Ag(I) efflux system. J. Biol. Chem. 282, 35695-35702 (Pubitemid 350277135)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.49 , pp. 35695-35702
    • Bagai, I.1    Liu, W.2    Rensing, C.3    Blackburn, N.J.4    McEvoy, M.M.5
  • 61
    • 55249109759 scopus 로고    scopus 로고
    • Direct metal transfer between periplasmic proteins identifies a bacterial copper chaperone
    • Bagai, I., Rensing, C., Blackburn, N. J., and McEvoy, M. M. (2008) Direct metal transfer between periplasmic proteins identifies a bacterial copper chaperone. Biochemistry 47, 11408-11414
    • (2008) Biochemistry , vol.47 , pp. 11408-11414
    • Bagai, I.1    Rensing, C.2    Blackburn, N.J.3    McEvoy, M.M.4
  • 62
    • 79952967236 scopus 로고    scopus 로고
    • Structural and metal binding characterization of the C-terminal metallochaperone domain of membrane fusion protein SilB from Cupriavidus metallidurans CH34
    • Bersch, B., Derfoufi, K. M., De Angelis, F., Auquier, V., Ekendé, E. N., Mergeay, M., Ruysschaert, J. M., and Vandenbussche, G. (2011) Structural and metal binding characterization of the C-terminal metallochaperone domain of membrane fusion protein SilB from Cupriavidus metallidurans CH34. Biochemistry 50, 2194-2204
    • (2011) Biochemistry , vol.50 , pp. 2194-2204
    • Bersch, B.1    Derfoufi, K.M.2    De Angelis, F.3    Auquier, V.4    Ekendé, E.N.5    Mergeay, M.6    Ruysschaert, J.M.7    Vandenbussche, G.8
  • 63
    • 78650791250 scopus 로고    scopus 로고
    • The Cus efflux system removes toxic ions via a methionine shuttle
    • Su, C. C., Long, F., and Yu, E. W. (2011) The Cus efflux system removes toxic ions via a methionine shuttle. Protein Sci. 20, 6-18
    • (2011) Protein Sci. , vol.20 , pp. 6-18
    • Su, C.C.1    Long, F.2    Yu, E.W.3
  • 64
    • 70350029582 scopus 로고    scopus 로고
    • Copper transport in mammalian cells: Special care for a metal with special needs
    • Kaplan, J. H., and Lutsenko, S. (2009) Copper transport in mammalian cells: special care for a metal with special needs. J. Biol. Chem. 284, 25461-25465
    • (2009) J. Biol. Chem. , vol.284 , pp. 25461-25465
    • Kaplan, J.H.1    Lutsenko, S.2
  • 66
    • 15744400088 scopus 로고    scopus 로고
    • Stable plasma membrane levels of hCTR1 mediate cellular copper uptake
    • DOI 10.1074/jbc.M500116200
    • Eisses, J. F., Chi, Y., and Kaplan, J. H. (2005) Stable plasma membrane levels of hCTR1 mediate cellular copper uptake. J. Biol. Chem. 280, 9635-9639 (Pubitemid 40409660)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.10 , pp. 9635-9639
    • Eisses, J.F.1    Chi, Y.2    Kaplan, J.H.3
  • 67
    • 34848820957 scopus 로고    scopus 로고
    • Distinct mechanisms for Ctr1-mediated copper and cisplatin transport
    • DOI 10.1074/jbc.M703973200
    • Sinani, D., Adle, D. J., Kim, H., and Lee, J. (2007) Distinct mechanisms for Ctr1-mediated copper and cisplatin transport. J. Biol. Chem. 282, 26775-26785 (Pubitemid 47501950)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.37 , pp. 26775-26785
    • Sinani, D.1    Adle, D.J.2    Kim, H.3    Lee, J.4
  • 68
    • 0037047283 scopus 로고    scopus 로고
    • Molecular characterization of hCTR1, the human copper uptake protein
    • Eisses, J. F., and Kaplan, J. H. (2002) Molecular characterization of hCTR1, the human copper uptake protein. J. Biol. Chem. 277, 29162-29171
    • (2002) J. Biol. Chem. , vol.277 , pp. 29162-29171
    • Eisses, J.F.1    Kaplan, J.H.2
  • 69
    • 77954629362 scopus 로고    scopus 로고
    • Cα trace model of the transmembrane domain of human copper transporter 1, motion and functional implications
    • Schushan, M., Barkan, Y., Haliloglu, T., and Ben-Tal, N. (2010) Cα trace model of the transmembrane domain of human copper transporter 1, motion and functional implications. Proc. Natl. Acad. Sci. U.S.A. 107, 10908-10913
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 10908-10913
    • Schushan, M.1    Barkan, Y.2    Haliloglu, T.3    Ben-Tal, N.4
  • 70
    • 1642404510 scopus 로고    scopus 로고
    • C-Terminal Domain of the Membrane Copper Transporter Ctr1 from Saccharomyces cerevisiae Binds Four Cu(I) Ions as a Cuprous-Thiolate Polynuclear Cluster: Sub-femtomolar Cu(I) Affinity of Three Proteins Involved in Copper Trafficking
    • DOI 10.1021/ja0390350
    • Xiao, Z., Loughlin, F., George, G. N., Howlett, G. J., and Wedd, A. G. (2004) C-terminal domain of the membrane copper transporter Ctr1 from Saccharomyces cerevisiae binds four Cu(I) ions as a cuprous-thiolate polynuclear cluster: subfemtomolar Cu(I) affinity of three proteins involved in copper trafficking. J. Am. Chem. Soc. 126, 3081-3090 (Pubitemid 38380713)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.10 , pp. 3081-3090
    • Xiao, Z.1    Loughlin, F.2    George, G.N.3    Howlett, G.J.4    Wedd, A.G.5
  • 71
    • 0030953624 scopus 로고    scopus 로고
    • A novel family of ubiquitous heavy metal ion transport proteins
    • DOI 10.1007/s002329900192
    • 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 (Pubitemid 27146309)
    • (1997) Journal of Membrane Biology , vol.156 , Issue.2 , pp. 99-103
    • Paulsen, I.T.1    Saier Jr., M.H.2
  • 72
    • 0037131363 scopus 로고    scopus 로고
    • Biochemical properties of vacuolar zinc transport systems of saccharomyces cerevisiae
    • DOI 10.1074/jbc.M205052200
    • 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 (Pubitemid 35190887)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.42 , pp. 39187-39194
    • MacDiarmid, C.W.1    Milanick, M.A.2    Eide, D.J.3
  • 73
    • 3543109122 scopus 로고    scopus 로고
    • Zinc and the Msc2 zinc transporter protein are required for endoplasmic reticulum function
    • DOI 10.1083/jcb.200401157
    • Ellis, C. D., Wang, F., MacDiarmid, C. W., Clark, S., Lyons, T., and Eide, D. J. (2004) Zinc and the Msc2 zinc transporter protein are required for endoplasmic reticulum function. J. Cell Biol. 166, 325-335 (Pubitemid 39031236)
    • (2004) Journal of Cell Biology , vol.166 , Issue.3 , pp. 325-335
    • Ellis, C.D.1    Wang, F.2    MacDiarmid, C.W.3    Clark, S.4    Lyons, T.5    Eide, D.J.6
  • 74
    • 0037423203 scopus 로고    scopus 로고
    • ZnT7, a novel mammalian zinc transporter, accumulates zinc in the Golgi apparatus
    • DOI 10.1074/jbc.M207644200
    • 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 (Pubitemid 36801145)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.6 , pp. 4096-4102
    • Kirschke, C.P.1    Huang, L.2
  • 75
    • 34248204401 scopus 로고    scopus 로고
    • A novel major facilitator superfamily protein at the tonoplast influences zinc tolerance and accumulation in Arabidopsis
    • DOI 10.1104/pp.106.092015
    • Haydon, M. J., and Cobbett, C. S. (2007) A novel major facilitator superfamily protein at the tonoplast influences zinc tolerance and accumulation in Arabidopsis. Plant Physiol. 143, 1705-1719 (Pubitemid 46849481)
    • (2007) Plant Physiology , vol.143 , Issue.4 , pp. 1705-1719
    • Haydon, M.J.1    Cobbett, C.S.2
  • 76
    • 23344440858 scopus 로고    scopus 로고
    • Heteromeric protein complexes mediate zinc transport into the secretory pathway of eukaryotic cells
    • DOI 10.1074/jbc.M505500200
    • Ellis, C. D., MacDiarmid, C. W., and Eide, D. J. (2005) Heteromeric protein complexes mediate zinc transport into the secretory pathway of eukaryotic cells. J. Biol. Chem. 280, 28811-28818 (Pubitemid 41105783)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.31 , pp. 28811-28818
    • Ellis, C.D.1    MacDiarmid, C.W.2    Eide, D.J.3
  • 77
    • 67650050211 scopus 로고    scopus 로고
    • Mammalian zinc transporters: Nutritional and physiologic regulation
    • Lichten, L. A., and Cousins, R. J. (2009) Mammalian zinc transporters: nutritional and physiologic regulation. Annu. Rev. Nutr. 29, 153-176
    • (2009) Annu. Rev. Nutr. , vol.29 , pp. 153-176
    • Lichten, L.A.1    Cousins, R.J.2
  • 78
    • 0346120020 scopus 로고    scopus 로고
    • Poplar Metal Tolerance Protein 1 Confers Zinc Tolerance and Is an Oligomeric Vacuolar Zinc Transporter with an Essential Leucine Zipper Motif
    • DOI 10.1105/tpc.017541
    • Blaudez, D., Kohler, A., Martin, F., Sanders, D., and Chalot, M. (2003) Poplar metal tolerance protein 1 confers zinc tolerance and is an oligomeric vacuolar zinc transporter with an essential leucine zipper motif. Plant Cell 15, 2911-2928 (Pubitemid 37546260)
    • (2003) Plant Cell , vol.15 , Issue.12 , pp. 2911-2928
    • Blaudez, D.1    Kohler, A.2    Martin, F.3    Sanders, D.4    Chalot, M.5
  • 79
    • 4544338200 scopus 로고    scopus 로고
    • Oligomeric state of the Escherichia coli metal transporter YiiP
    • DOI 10.1074/jbc.M407044200
    • Wei, Y., Li, H., and Fu, D. (2004) Oligomeric state of the Escherichia coli metal transporter YiiP. J. Biol. Chem. 279, 39251-39259 (Pubitemid 39258186)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.38 , pp. 39251-39259
    • Wei, Y.1    Li, H.2    Fu, D.3
  • 80
    • 70349789244 scopus 로고    scopus 로고
    • Structural basis for autoregulation of the zinc transporter YiiP
    • Lu, M., Chai, J., and Fu, D. (2009) Structural basis for autoregulation of the zinc transporter YiiP. Nat. Struct. Mol. Biol. 16, 1063-1067
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 1063-1067
    • Lu, M.1    Chai, J.2    Fu, D.3
  • 81
    • 26644450950 scopus 로고    scopus 로고
    • Selective metal binding to a membrane-embedded aspartate in the Escherichia coli metal transporter YiiP (FieF)
    • DOI 10.1074/jbc.M506107200
    • Wei, Y., and Fu, D. (2005) Selective metal binding to a membrane-embedded aspartate in the Escherichia coli metal transporter YiiP (FieF). J. Biol. Chem. 280, 33716-33724 (Pubitemid 41443089)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.40 , pp. 33716-33724
    • Wei, Y.1    Fu, D.2
  • 82
    • 7744220357 scopus 로고    scopus 로고
    • Characteristics of zinc transport by two bacterial cation diffusion facilitators from Ralstonia metallidurans CH34 and Escherichia coli
    • DOI 10.1128/JB.186.22.7499-7507.2004
    • Anton, A., Weltrowski, A., Haney, C. J., Franke, S., Grass, G., Rensing, C., and Nies, D. H. (2004) Characteristics of zinc transport by two bacterial cation diffusion facilitators from Ralstonia metallidurans CH34 and Escherichia coli. J. Bacteriol. 186, 7499-7507 (Pubitemid 39463713)
    • (2004) Journal of Bacteriology , vol.186 , Issue.22 , pp. 7499-7507
    • Anton, A.1    Weltrowski, A.2    Haney, C.J.3    Franke, S.4    Grass, G.5    Rensing, C.6    Nies, D.H.7
  • 83
    • 77957963055 scopus 로고    scopus 로고
    • Achieving reliability and high accuracy in automated protein docking: ClusPro, PIPER, SDU, and stability analysis in CAPRI rounds 13-19
    • Kozakov, D., Hall, D. R., Beglov, D., Brenke, R., Comeau, S. R., Shen, Y., Li, K., Zheng, J., Vakili, P., Paschalidis, I. Ch., and Vajda, S. (2010) Achieving reliability and high accuracy in automated protein docking: ClusPro, PIPER, SDU, and stability analysis in CAPRI rounds 13-19. Proteins 78, 3124-3130
    • (2010) Proteins , vol.78 , pp. 3124-3130
    • Kozakov, D.1    Hall, D.R.2    Beglov, D.3    Brenke, R.4    Comeau, S.R.5    Shen, Y.6    Li, K.7    Zheng, J.8    Vakili, P.9    Paschalidis, I.Ch.10    Vajda, S.11


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.