메뉴 건너뛰기




Volumn 463, Issue 2, 2014, Pages 167-176

Biochemical characterization of P-type copper ATPases

Author keywords

Bacterial copper ATPase; Cellular trafficking; Cisplatin; Copper displacement; Mammalian copper ATPase interaction; Serine phosphorylation

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CALCIUM; CISPLATIN; COPPER; COPPER EXPORTING ADENOSINE TRIPHOSPHATASE; HISTIDINE; LYSINE; MENKES PROTEIN; PROTEASOME; SERINE; SODIUM; WILSON DISEASE PROTEIN; CATION TRANSPORT PROTEIN;

EID: 84907199826     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20140741     Document Type: Review
Times cited : (47)

References (77)
  • 1
    • 0028866670 scopus 로고
    • Organization of P-type ATPases: Significance of structural diversity
    • Lutsenko, S. and Kaplan, J. H. (1995) Organization of P-type ATPases: significance of structural diversity. Biochemistry 34, 15607-15613.
    • (1995) Biochemistry , vol.34 , pp. 15607-15613
    • Lutsenko, S.1    Kaplan, J.H.2
  • 2
    • 0031964372 scopus 로고    scopus 로고
    • Evolution of substrate specificities in the P-type ATPase superfamily
    • Axelsen, K. B. and Palmgren, M. G. (1998) Evolution of substrate specificities in the P-type ATPase superfamily. J. Mol. Evol. 46, 84-101 CrossRef PubMed.
    • (1998) J. Mol. Evol. , vol.46 , pp. 84-101
    • Axelsen, K.B.1    Palmgren, M.G.2
  • 3
    • 3242701547 scopus 로고    scopus 로고
    • Biology, structure and mechanism of P-type ATPases
    • Kühlbrandt, W. (2004) Biology, structure and mechanism of P-type ATPases. Nat. Rev. Mol. Cell Biol. 5, 282-295 CrossRef PubMed.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 282-295
    • Kühlbrandt, W.1
  • 5
    • 0018401053 scopus 로고
    • +dependent ATPase of the sarcoplasmic reticulum
    • +dependent ATPase of the sarcoplasmic reticulum. Annu. Rev. Biochem. 48, 275-292 CrossRef PubMed.
    • (1979) Annu. Rev. Biochem. , vol.48 , pp. 275-292
    • De Meis, L.1    Vianna, A.L.2
  • 6
    • 0021894467 scopus 로고
    • Mechanism of calcium transport
    • Inesi, G. (1985) Mechanism of calcium transport. Annu. Rev. Physiol. 47, 573-601 CrossRef PubMed.
    • (1985) Annu. Rev. Physiol. , vol.47 , pp. 573-601
    • Inesi, G.1
  • 7
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6Å resolution
    • Toyoshima, C., Nakasako, M., Nomura, H. and Ogawa, H. (2000) Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6Å resolution. Nature 405, 647-655 CrossRef PubMed.
    • (2000) Nature , vol.405 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 8
    • 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 CrossRef PubMed.
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 511-535
    • Kaplan, J.H.1
  • 9
    • 2942668632 scopus 로고    scopus 로고
    • Phosphoryl transfer and calcium ion occlusion in the calcium pump
    • Sørensen, T. L., Møller, J. V. and Nissen, P. (2004) Phosphoryl transfer and calcium ion occlusion in the calcium pump. Science 304, 1672-1675 CrossRef PubMed.
    • (2004) Science , vol.304 , pp. 1672-1675
    • Sørensen, T.L.1    Møller, J.V.2    Nissen, P.3
  • 11
    • 66249147196 scopus 로고    scopus 로고
    • Crystal structure of the sodium-potassium pump at 2.4Å resolution
    • Shinoda, T., Ogawa, H., Cornelius, F. and Toyoshima, C. (2009) Crystal structure of the sodium-potassium pump at 2.4Å resolution. Nature 459, 446-450 CrossRef PubMed.
    • (2009) Nature , vol.459 , pp. 446-450
    • Shinoda, T.1    Ogawa, H.2    Cornelius, F.3    Toyoshima, C.4
  • 12
    • 0030199612 scopus 로고    scopus 로고
    • CPx-type ATPases: A class of P-type ATPases that pump heavy metals
    • Solioz, M. and Vulpe, C. (1996) CPx-type ATPases: a class of P-type ATPases that pump heavy metals. Trends Biochem. Sci. 21, 237-241 CrossRef PubMed.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 237-241
    • Solioz, M.1    Vulpe, C.2
  • 13
    • 0036175362 scopus 로고    scopus 로고
    • Metallochaperones and metal-transporting ATPases: A comparative analysis of sequences and structures
    • 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 CrossRef PubMed.
    • (2002) Genome Res , vol.12 , 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
  • 14
    • 0141987910 scopus 로고    scopus 로고
    • Identification of ion selectivity determinants in heavy metal transport P1B-type ATPases
    • Argüello, J. M. (2003) Identification of ion selectivity determinants in heavy metal transport P1B-type ATPases. J. Membr. Biol. 195, 93-108 CrossRef PubMed.
    • (2003) J. Membr. Biol. , vol.195 , pp. 93-108
    • Argüello, J.M.1
  • 15
    • 34248633103 scopus 로고    scopus 로고
    • The structure and function of heavy metal transport P1B-ATPases
    • Argüello, J. M., Eren, E. and González-Guerrero, M. (2007) The structure and function of heavy metal transport P1B-ATPases. Biometals 20, 233-248 CrossRef PubMed.
    • (2007) Biometals , vol.20 , pp. 233-248
    • Argüello, J.M.1    Eren, E.2    González-Guerrero, M.3
  • 16
    • 34447103789 scopus 로고    scopus 로고
    • Trafficking of the copper-ATPases ATP7A and ATP7B: Role in copper homeostasis
    • 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 CrossRef PubMed.
    • (2007) Arch. Biochem. Biophys. , vol.463 , pp. 149-167
    • La Fontaine, S.1    Mercer, J.F.2
  • 18
    • 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 CrossRef PubMed.
    • (2009) J. Biol. Chem. , vol.284 , pp. 25461-25465
    • Kaplan, J.H.1    Lutsenko, S.2
  • 22
    • 44649182134 scopus 로고    scopus 로고
    • Structure of a copper pump suggests a regulatory role for its metal-binding domain
    • Wu, C. C., Rice, W. J. and Stokes, D. L. (2008) Structure of a copper pump suggests a regulatory role for its metal-binding domain. Structure 16, 976-985 CrossRef PubMed.
    • (2008) Structure , vol.16 , pp. 976-985
    • Wu, C.C.1    Rice, W.J.2    Stokes, D.L.3
  • 25
    • 67649509594 scopus 로고    scopus 로고
    • +-transporting P-type ATPase
    • +-transporting P-type ATPase. EMBO J. 28, 1782-1791 CrossRef PubMed.
    • (2009) EMBO J. , vol.28 , pp. 1782-1791
    • Tsuda, T.1    Toyoshima, C.2
  • 26
    • 42449127446 scopus 로고    scopus 로고
    • Membrane structure of CtrA3, a copper-transporting P-type-ATPase from Aquifex aeolicus
    • Chintalapati, S., Al Kurdi, R., van Scheltinga, A. C. and Kühlbrandt, W. (2008) Membrane structure of CtrA3, a copper-transporting P-type-ATPase from Aquifex aeolicus. J. Mol. Biol. 378, 581-595 CrossRef PubMed.
    • (2008) J. Mol. Biol. , vol.378 , pp. 581-595
    • Chintalapati, S.1    Al Kurdi, R.2    Van Scheltinga, A.C.3    Kühlbrandt, W.4
  • 29
    • 53049099060 scopus 로고    scopus 로고
    • Intermediate phosphorylation reactions in the mechanism of ATP utilization by the copper ATPase (CopA) of Thermotoga maritima
    • Hatori, Y., Hirata, A., Toyoshima, C., Lewis, D., Pilankatta, R. and Inesi, G. (2008) Intermediate phosphorylation reactions in the mechanism of ATP utilization by the copper ATPase (CopA) of Thermotoga maritima . J. Biol. Chem. 283, 22541-22549 CrossRef PubMed.
    • (2008) J. Biol. Chem. , vol.283 , pp. 22541-22549
    • Hatori, Y.1    Hirata, A.2    Toyoshima, C.3    Lewis, D.4    Pilankatta, R.5    Inesi, G.6
  • 34
    • 66649083458 scopus 로고    scopus 로고
    • Reaction cycle of Thermotoga maritima copper ATPase and conformational characterization of catalytically deficient mutants
    • Hatori, Y., Lewis, D., Toyoshima, C. and Inesi, G. (2009) Reaction cycle of Thermotoga maritima copper ATPase and conformational characterization of catalytically deficient mutants. Biochemistry 48, 4871-4880 CrossRef PubMed.
    • (2009) Biochemistry , vol.48 , pp. 4871-4880
    • Hatori, Y.1    Lewis, D.2    Toyoshima, C.3    Inesi, G.4
  • 36
    • 38049138584 scopus 로고    scopus 로고
    • How processing of aspartylphosphate is coupled to lumenal gating of the ion pathway in the calcium pump
    • Toyoshima, C., Norimatsu, Y., Iwasawa, S., Tsuda, T. and Ogawa, H. (2007) How processing of aspartylphosphate is coupled to lumenal gating of the ion pathway in the calcium pump. Proc. Natl. Acad. Sci. U.S.A. 104, 19831-19836 CrossRef PubMed.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 19831-19836
    • Toyoshima, C.1    Norimatsu, Y.2    Iwasawa, S.3    Tsuda, T.4    Ogawa, H.5
  • 37
    • 84859972108 scopus 로고    scopus 로고
    • Metal transport across biomembranes: Emerging models for a distinct chemistry
    • Argüello, J. M., Raimunda, D. and González-Guerrero, M. (2012) Metal transport across. biomembranes: emerging models for a distinct chemistry. J. Biol. Chem. 287, 13510-13517 CrossRef PubMed.
    • (2012) J. Biol. Chem. , vol.287 , pp. 13510-13517
    • Argüello, J.M.1    Raimunda, D.2    González-Guerrero, M.3
  • 38
    • 0027446365 scopus 로고
    • Isolation of a candidate gene for Menkes disease and evidence that it encodes a copper-transporting ATPase
    • Vulpe, C., Levinson, B., Whitney, S., Packman, S. and Gitschier, J. (1993) Isolation of a candidate gene for Menkes disease and evidence that it encodes a copper-transporting ATPase. Nat. Genet. 3, 7-13 CrossRef PubMed.
    • (1993) Nat. Genet. , vol.3 , pp. 7-13
    • Vulpe, C.1    Levinson, B.2    Whitney, S.3    Packman, S.4    Gitschier, J.5
  • 40
    • 0027452091 scopus 로고
    • The Wilson disease gene is a putative copper transporting P-type ATPase similar to the Menkes gene
    • Bull, P. C., Thomas, G. R., Rommens, J. M., Forbes, J. R. and Cox, D. W. (1993) The Wilson disease gene is a putative copper transporting P-type ATPase similar to the Menkes gene. Nat. Genet. 5, 327-337 CrossRef PubMed.
    • (1993) Nat. Genet. , vol.5 , pp. 327-337
    • Bull, P.C.1    Thomas, G.R.2    Rommens, J.M.3    Forbes, J.R.4    Cox, D.W.5
  • 41
    • 0028040512 scopus 로고
    • Characterization of the Wilson disease gene encoding a P-type copper transporting ATPase: Genomic organization, alternative splicing, and structure/function predictions
    • Petrukhin, K., Lutsenko, S., Chernov, I., Ross, B. M., Kaplan, J. H. and Gilliam, T. C. (1994) Characterization of the Wilson disease gene encoding a P-type copper transporting ATPase: genomic organization, alternative splicing, and structure/function predictions. Hum. Mol. Genet. 3, 1647-1656 CrossRef PubMed.
    • (1994) Hum. Mol. Genet. , vol.3 , pp. 1647-1656
    • Petrukhin, K.1    Lutsenko, S.2    Chernov, I.3    Ross, B.M.4    Kaplan, J.H.5    Gilliam, T.C.6
  • 42
    • 34447510930 scopus 로고    scopus 로고
    • Function and regulation of human copper-transporting ATPases
    • Lutsenko, S., Barnes, N. L., Bartee, M. Y. and Dmitriev, O. Y. (2007) Function and regulation of human copper-transporting ATPases. Physiol. Rev. 87, 1011-1046 CrossRef PubMed.
    • (2007) Physiol. Rev. , vol.87 , pp. 1011-1046
    • Lutsenko, S.1    Barnes, N.L.2    Bartee, M.Y.3    Dmitriev, O.Y.4
  • 43
    • 59449086382 scopus 로고    scopus 로고
    • The multi-layered regulation of copper translocating P-type ATPases
    • Veldhuis, N. A., Gaeth, A. P., Pearson, R. B., Gabriel, K. and Camakaris, J. (2009) The multi-layered regulation of copper translocating P-type ATPases. Biometals 22, 177-190 CrossRef PubMed.
    • (2009) Biometals , vol.22 , pp. 177-190
    • Veldhuis, N.A.1    Gaeth, A.P.2    Pearson, R.B.3    Gabriel, K.4    Camakaris, J.5
  • 44
    • 0029909937 scopus 로고    scopus 로고
    • Ligand-regulated transport of the Menkes copper P-type ATPase efflux pump from the Golgi apparatus to the plasma membrane: A novel mechanism of regulated trafficking
    • Petris, M. J., Mercer, J. F., Culvenor, J. G., Lockhart, P., Gleeson, P. A. and Camakaris, J. (1996) Ligand-regulated transport of the Menkes copper P-type ATPase efflux pump from the Golgi apparatus to the plasma membrane: a novel mechanism of regulated trafficking. EMBO J. 15, 6084-6095 PubMed.
    • (1996) EMBO J. , vol.15 , pp. 6084-6095
    • Petris, M.J.1    Mercer, J.F.2    Culvenor, J.G.3    Lockhart, P.4    Gleeson, P.A.5    Camakaris, J.6
  • 46
    • 0030839796 scopus 로고    scopus 로고
    • N-terminal domains of human copper-transporting adenosine triphosphatases (the Wilson's and Menkes disease proteins) bind copper selectively in vivo and in vitro with stoichiometry of one copper per metal-binding repeat
    • Lutsenko, S., Petrukhin, K., Cooper, M. J., Gilliam, C. T. and Kaplan, J. H. (1997) N-terminal domains of human copper-transporting adenosine triphosphatases (the Wilson's and Menkes disease proteins) bind copper selectively in vivo and in vitro with stoichiometry of one copper per metal-binding repeat. J. Biol. Chem. 272, 18939-18944 CrossRef PubMed.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18939-18944
    • Lutsenko, S.1    Petrukhin, K.2    Cooper, M.J.3    Gilliam, C.T.4    Kaplan, J.H.5
  • 47
    • 0031455381 scopus 로고    scopus 로고
    • Expression, purification, and metal binding properties of the N-terminal domain from the Wilson disease putative copper-transporting ATPase (ATP7B)
    • DiDonato, M., Narindrasorasak, S., Forbes, J. R., Cox, D. W. and Sarkar, B. (1997) Expression, purification, and metal binding properties of the N-terminal domain from the Wilson disease putative copper-transporting ATPase (ATP7B). J. Biol. Chem. 272, 33279-33282 CrossRef PubMed.
    • (1997) J. Biol. Chem. , vol.272 , pp. 33279-33282
    • Didonato, M.1    Narindrasorasak, S.2    Forbes, J.R.3    Cox, D.W.4    Sarkar, B.5
  • 48
    • 0033617198 scopus 로고    scopus 로고
    • Role of the copper-binding domain in the copper transport function of ATP7B, the P-type ATPase defective in Wilson disease
    • Forbes, J. R., Hsi, G. and Cox, D. W. (1999) Role of the copper-binding domain in the copper transport function of ATP7B, the P-type ATPase defective in Wilson disease. J. Biol. Chem. 274, 12408-12413 CrossRef PubMed.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12408-12413
    • Forbes, J.R.1    Hsi, G.2    Cox, D.W.3
  • 49
    • 0041856098 scopus 로고    scopus 로고
    • The distinct roles of the N-terminal copper-binding sites in regulation of catalytic activity of the Wilson's disease protein
    • Huster, D. and Lutsenko, S. (2003) The distinct roles of the N-terminal copper-binding sites in regulation of catalytic activity of the Wilson's disease protein. J. Biol. Chem. 78, 32212-32218 CrossRef.
    • (2003) J. Biol. Chem. , vol.78 , pp. 32212-32218
    • Huster, D.1    Lutsenko, S.2
  • 50
    • 66149157256 scopus 로고    scopus 로고
    • An NMR study of the interaction of the N-terminal cytoplasmic tail of the Wilson disease protein with copper(I)-HAH1
    • Banci, L., Bertini, I., Cantini, F., Massagni, C., Migliardi, M. and Rosato, A. (2009) An NMR study of the interaction of the N-terminal cytoplasmic tail of the Wilson disease protein with copper(I)-HAH1. J. Biol. Chem. 284, 9354-9360 CrossRef PubMed.
    • (2009) J. Biol. Chem. , vol.284 , pp. 9354-9360
    • Banci, L.1    Bertini, I.2    Cantini, F.3    Massagni, C.4    Migliardi, M.5    Rosato, A.6
  • 51
    • 69049100197 scopus 로고    scopus 로고
    • Solution structures of the actuator domain of ATP7A and ATP7B, the Menkes and Wilson disease proteins
    • Banci, L., Bertini, I., Cantini, F., Migliardi, M., Natile, G., Nushi, F. and Rosato, A. (2009) Solution structures of the actuator domain of ATP7A and ATP7B, the Menkes and Wilson disease proteins. Biochemistry 48, 7849-7855 CrossRef PubMed.
    • (2009) Biochemistry , vol.48 , pp. 7849-7855
    • Banci, L.1    Bertini, I.2    Cantini, F.3    Migliardi, M.4    Natile, G.5    Nushi, F.6    Rosato, A.7
  • 52
    • 33645754710 scopus 로고    scopus 로고
    • Solution structure of the N-domain of Wilson disease protein: Distinct nucleotide-binding environment and effects of disease mutations
    • Dmitriev, O., Tsivkovskii, R., Abildgaard, F., Morgan, C. T., Markley, J. L. and Lutsenko, S. (2006) Solution structure of the N-domain of Wilson disease protein: distinct nucleotide-binding environment and effects of disease mutations. Proc. Natl. Acad. Sci. U.S.A. 103, 5302-5307 CrossRef PubMed.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 5302-5307
    • Dmitriev, O.1    Tsivkovskii, R.2    Abildgaard, F.3    Morgan, C.T.4    Markley, J.L.5    Lutsenko, S.6
  • 53
    • 0035958909 scopus 로고    scopus 로고
    • The regulation of catalytic activity of the Menkes copper-translocating P-type ATPase. Role of high affinity copper-binding sites
    • Voskoboinik, I., Mar, J., Strausak, D. and Camakaris, J. (2001) The regulation of catalytic activity of the Menkes copper-translocating P-type ATPase. Role of high affinity copper-binding sites. J. Biol. Chem. 276, 28620-28627 CrossRef PubMed.
    • (2001) J. Biol. Chem. , vol.276 , pp. 28620-28627
    • Voskoboinik, I.1    Mar, J.2    Strausak, D.3    Camakaris, J.4
  • 54
    • 0037059855 scopus 로고    scopus 로고
    • Functional properties of the copper-transporting ATPase ATP7B (the Wilson's disease protein) expressed in insect cells
    • Tsivkovskii, R., Eisses, J. F., Kaplan, J. H. and Lutsenko, S. (2002) Functional properties of the copper-transporting ATPase ATP7B (the Wilson's disease protein) expressed in insect cells. J. Biol. Chem. 277, 976-983 CrossRef PubMed.
    • (2002) J. Biol. Chem. , vol.277 , pp. 976-983
    • Tsivkovskii, R.1    Eisses, J.F.2    Kaplan, J.H.3    Lutsenko, S.4
  • 55
    • 69249092561 scopus 로고    scopus 로고
    • +-ATPase (ATP7B, Wilson disease protein) for functional characterization of catalytic activity and serine residues undergoing copper-dependent phosphorylation
    • +-ATPase (ATP7B, Wilson disease protein) for functional characterization of catalytic activity and serine residues undergoing copper-dependent phosphorylation. J. Biol. Chem. 284, 21307-21316 CrossRef PubMed.
    • (2009) J. Biol. Chem. , vol.284 , pp. 21307-21316
    • Pilankatta, R.1    Lewis, D.2    Adams, C.M.3    Inesi, G.4
  • 57
    • 0033021364 scopus 로고    scopus 로고
    • +/K+ -ATPase investigated on solid supported membranes: Rapid solution exchange with a new technique
    • +/K+ -ATPase investigated on solid supported membranes: rapid solution exchange with a new technique. Biophys. J. 76, 814-826 CrossRef PubMed.
    • (1999) Biophys. J. , vol.76 , pp. 814-826
    • Pintschovius, J.1    Fendler, K.2
  • 60
    • 79953186625 scopus 로고    scopus 로고
    • Involvement of protein kinase D in expression and trafficking of ATP7B (copper ATPase)
    • Pilankatta, R., Lewis, D. and Inesi, G. (2011) Involvement of protein kinase D in expression and trafficking of ATP7B (copper ATPase). J. Biol. Chem. 286, 7389-7396 CrossRef PubMed.
    • (2011) J. Biol. Chem. , vol.286 , pp. 7389-7396
    • Pilankatta, R.1    Lewis, D.2    Inesi, G.3
  • 61
    • 78649279746 scopus 로고    scopus 로고
    • Comparative features of copper ATPases ATP7A and ATP7B heterologously expressed in COS-1 cells
    • Liu, Y., Pilankatta, R., Hatori, Y., Lewis, D. and Inesi, G. (2010) Comparative features of copper ATPases ATP7A and ATP7B heterologously expressed in COS-1 cells. Biochemistry 49, 10006-10012 CrossRef PubMed.
    • (2010) Biochemistry , vol.49 , pp. 10006-10012
    • Liu, Y.1    Pilankatta, R.2    Hatori, Y.3    Lewis, D.4    Inesi, G.5
  • 62
    • 0027233829 scopus 로고
    • Cellular accumulation of the anticancer agent cisplatin: A review
    • Gately, D. P. and Howell, S. B. (1993) Cellular accumulation of the anticancer agent cisplatin: a review. Br. J. Cancer 67, 1171-1176 CrossRef PubMed.
    • (1993) Br. J. Cancer , vol.67 , pp. 1171-1176
    • Gately, D.P.1    Howell, S.B.2
  • 64
    • 0041341920 scopus 로고    scopus 로고
    • The copper export pump ATP7B modulates the cellular pharmacology of carboplatin in ovarian carcinoma cells
    • Katano, K., Safaei, R., Samimi, G., Holzer, A., Rochdi, M. and Howell, S. B. (2003) The copper export pump ATP7B modulates the cellular pharmacology of carboplatin in ovarian carcinoma cells. Mol. Pharmacol. 64, 466-473 CrossRef PubMed.
    • (2003) Mol. Pharmacol. , vol.64 , pp. 466-473
    • Katano, K.1    Safaei, R.2    Samimi, G.3    Holzer, A.4    Rochdi, M.5    Howell, S.B.6
  • 65
    • 5444256896 scopus 로고    scopus 로고
    • The role of copper transporters in the development of resistance to Pt drugs
    • Safaei, R., Holzer, A. K., Katano, K., Samimi, G. and Howell, S. B. (2004) The role of copper transporters in the development of resistance to Pt drugs. J. Inorg. Biochem. 98, 1607-1613 CrossRef PubMed.
    • (2004) J. Inorg. Biochem. , vol.98 , pp. 1607-1613
    • Safaei, R.1    Holzer, A.K.2    Katano, K.3    Samimi, G.4    Howell, S.B.5
  • 66
    • 3042663282 scopus 로고    scopus 로고
    • Modulation of the cellular pharmacology of cisplatin and its analogs by the copper exporters ATP7A and ATP7B
    • Samimi, G., Katano, K., Holzer, A. K., Safaei, R. and Howell, S. B. (2004) Modulation of the cellular pharmacology of cisplatin and its analogs by the copper exporters ATP7A and ATP7B. Mol. Pharmacol. 66, 25-32 CrossRef PubMed.
    • (2004) Mol. Pharmacol. , vol.66 , pp. 25-32
    • Samimi, G.1    Katano, K.2    Holzer, A.K.3    Safaei, R.4    Howell, S.B.5
  • 67
    • 10644269449 scopus 로고    scopus 로고
    • Copper transporters regulate the cellular pharmacology and sensitivity to Pt drugs
    • Safaei, R. and Howell, S. B. (2005) Copper transporters regulate the cellular pharmacology and sensitivity to Pt drugs. Crit. Rev. Oncol. Hematol. 53, 13-23 CrossRef PubMed.
    • (2005) Crit. Rev. Oncol. Hematol. , vol.53 , pp. 13-23
    • Safaei, R.1    Howell, S.B.2
  • 68
    • 38549147706 scopus 로고    scopus 로고
    • Transport of cisplatin by the copper efflux transporter ATP7B
    • Safaei, R., Otani, S., Larson, B. J., Rasmussen, M. L. and Howell, S. B. (2008) Transport of cisplatin by the copper efflux transporter ATP7B. Mol. Pharmacol. 73, 461-468 CrossRef PubMed.
    • (2008) Mol. Pharmacol. , vol.73 , pp. 461-468
    • Safaei, R.1    Otani, S.2    Larson, B.J.3    Rasmussen, M.L.4    Howell, S.B.5
  • 69
    • 62749183648 scopus 로고    scopus 로고
    • The soluble metal-binding domain of the copper transporter ATP7B binds and detoxifies cisplatin
    • Dolgova, N. W., Olson, D., Lutsenko, S. and Dmitriev, O. Y. (2009) The soluble metal-binding domain of the copper transporter ATP7B binds and detoxifies cisplatin. Biochem. J. 419, 51-56 CrossRef PubMed.
    • (2009) Biochem. J. , vol.419 , pp. 51-56
    • Dolgova, N.W.1    Olson, D.2    Lutsenko, S.3    Dmitriev, O.Y.4
  • 70
    • 65549155349 scopus 로고    scopus 로고
    • Functional interactions of Cu-ATPase ATP7B with cisplatin and the role of ATP7B in the resistance of cells to the drug
    • Leonhardt, K., Gebhardt, R., Mössner, J., Lutsenko, S. and Huster, D. (2009) Functional interactions of Cu-ATPase ATP7B with cisplatin and the role of ATP7B in the resistance of cells to the drug. J. Biol. Chem. 284, 7793-7802 CrossRef PubMed.
    • (2009) J. Biol. Chem. , vol.284 , pp. 7793-7802
    • Leonhardt, K.1    Gebhardt, R.2    Mössner, J.3    Lutsenko, S.4    Huster, D.5
  • 72
    • 84858981234 scopus 로고    scopus 로고
    • The CXXC motifs in the metal binding domains are required for ATP7B to mediate resistance to cisplatin
    • Safaei, R., Adams, P. L., Maktabi, M. H., Mathews, R. A. and Howell, S. B. (2012) The CXXC motifs in the metal binding domains are required for ATP7B to mediate resistance to cisplatin. J. Inorg. Biochem. 110, 8-17 CrossRef PubMed.
    • (2012) J. Inorg. Biochem. , vol.110 , pp. 8-17
    • Safaei, R.1    Adams, P.L.2    Maktabi, M.H.3    Mathews, R.A.4    Howell, S.B.5
  • 74
    • 53049099060 scopus 로고    scopus 로고
    • Intermediate phosphorylation reactions in the mechanism of ATP utilization by the copper ATPase (CopA) of Thermotoga maritima
    • Hatori, Y., Hirata, A., Toyoshima, C., Lewis, D., Pilankatta, R. and Inesi, G. (2008) Intermediate phosphorylation reactions in the mechanism of ATP utilization by the copper ATPase (CopA) of Thermotoga maritima . J. Biol. Chem. 283, 22541-22549 CrossRef PubMed.
    • (2008) J. Biol. Chem. , vol.283 , pp. 22541-22549
    • Hatori, Y.1    Hirata, A.2    Toyoshima, C.3    Lewis, D.4    Pilankatta, R.5    Inesi, G.6
  • 75
    • 69249092561 scopus 로고    scopus 로고
    • +-ATPase (ATP7B, Wilson disease protein) for functional characterization of catalytic activity and serine residues undergoing copper-dependent phosphorylation
    • +-ATPase (ATP7B, Wilson disease protein) for functional characterization of catalytic activity and serine residues undergoing copper-dependent phosphorylation. J. Biol. Chem. 284, 21307-21316 CrossRef PubMed.
    • (2009) J. Biol. Chem. , vol.284 , pp. 21307-21316
    • Pilankatta, R.1    Lewis, D.2    Adams, C.M.3    Inesi, G.4
  • 76
    • 79953186625 scopus 로고    scopus 로고
    • Involvement of protein kinase D in expression and trafficking of ATP7B (copper ATPase)
    • Pilankatta,, R., Lewis, D. and Inesi, G. (2011) Involvement of protein kinase D in expression and trafficking of ATP7B (copper ATPase). J. Biol. Chem. 286, 7389-7396 CrossRef PubMed.
    • (2011) J. Biol. Chem. , vol.286 , pp. 7389-7396
    • Pilankatta, R.1    Lewis, D.2    Inesi, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.