메뉴 건너뛰기




Volumn 54, Issue 37, 2015, Pages 5673-5683

Structure and Function of Cu(I)- and Zn(II)-ATPases

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANES; CRYSTAL STRUCTURE; TRANSITION METAL COMPOUNDS; TRANSITION METALS; ZINC; ZINC COMPOUNDS;

EID: 84942083510     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/acs.biochem.5b00512     Document Type: Article
Times cited : (45)

References (114)
  • 1
    • 0001409028 scopus 로고
    • The influence of some cations on an adenosine triphosphatase from peripheral nerves
    • Skou, J. C. (1957) The influence of some cations on an adenosine triphosphatase from peripheral nerves Biochim. Biophys. Acta 23, 394-401 10.1016/0006-3002(57)90343-8
    • (1957) Biochim. Biophys. Acta , vol.23 , pp. 394-401
    • Skou, J.C.1
  • 2
    • 84946069451 scopus 로고    scopus 로고
    • UniProt: A hub for protein information
    • UniProt (2015) UniProt: a hub for protein information Nucleic Acids Res. 43, D204-D212 10.1093/nar/gku989
    • (2015) Nucleic Acids Res. , vol.43 , pp. D204-D212
    • UniProt1
  • 3
    • 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 10.1007/PL00006286
    • (1998) J. Mol. Evol. , vol.46 , pp. 84-101
    • Axelsen, K.B.1    Palmgren, M.G.2
  • 4
    • 13344294802 scopus 로고
    • An Enzymatic Mechanism of Active Sodium and Potassium Transport
    • Post, R. L. and Sen, A. K. (1965) An Enzymatic Mechanism of Active Sodium and Potassium Transport J. Histochem. Cytochem. 13, 105-112 10.1177/13.2.105
    • (1965) J. Histochem. Cytochem. , vol.13 , pp. 105-112
    • Post, R.L.1    Sen, A.K.2
  • 5
    • 0000395323 scopus 로고
    • The Role of Sodium Ions in the Activation of Electrophorus Electric Organ Adenosine Triphosphatase
    • Albers, R. W., Fahn, S., and Koval, G. J. (1963) The Role of Sodium Ions in the Activation of Electrophorus Electric Organ Adenosine Triphosphatase Proc. Natl. Acad. Sci. U. S. A. 50, 474-481 10.1073/pnas.50.3.474
    • (1963) Proc. Natl. Acad. Sci. U. S. A. , vol.50 , pp. 474-481
    • Albers, R.W.1    Fahn, S.2    Koval, G.J.3
  • 6
    • 0014029736 scopus 로고
    • Simple Allosteric Model for Membrane Pumps
    • Jardetsky, O. (1966) Simple Allosteric Model for Membrane Pumps Nature 211, 969-970 10.1038/211969a0
    • (1966) Nature , vol.211 , pp. 969-970
    • Jardetsky, O.1
  • 7
    • 77955983837 scopus 로고    scopus 로고
    • In and out of the cation pumps: P-type ATPase structure revisited
    • Bublitz, M., Poulsen, H., Morth, J. P., and Nissen, P. (2010) In and out of the cation pumps: P-type ATPase structure revisited Curr. Opin. Struct. Biol. 20, 431-439 10.1016/j.sbi.2010.06.007
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 431-439
    • Bublitz, M.1    Poulsen, H.2    Morth, J.P.3    Nissen, P.4
  • 8
    • 0024399371 scopus 로고
    • Location of high affinity Ca2+-binding sites within the predicted transmembrane domain of the sarcoplasmic reticulum Ca2+-ATPase
    • Clarke, D. M., Loo, T. W., Inesi, G., and MacLennan, D. H. (1989) Location of high affinity Ca2+-binding sites within the predicted transmembrane domain of the sarcoplasmic reticulum Ca2+-ATPase Nature 339, 476-478 10.1038/339476a0
    • (1989) Nature , vol.339 , pp. 476-478
    • Clarke, D.M.1    Loo, T.W.2    Inesi, G.3    MacLennan, D.H.4
  • 9
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution
    • Toyoshima, C., Nakasako, M., Nomura, H., and Ogawa, H. (2000) Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution Nature 405, 647-655 10.1038/35015017
    • (2000) Nature , vol.405 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 10
    • 0037043709 scopus 로고    scopus 로고
    • Structural changes in the calcium pump accompanying the dissociation of calcium
    • Toyoshima, C. and Nomura, H. (2002) Structural changes in the calcium pump accompanying the dissociation of calcium Nature 418, 605-611 10.1038/nature00944
    • (2002) Nature , vol.418 , pp. 605-611
    • Toyoshima, C.1    Nomura, H.2
  • 11
    • 11144330054 scopus 로고    scopus 로고
    • Dephosphorylation of the calcium pump coupled to counterion occlusion
    • Olesen, C., Sorensen, T. L., Nielsen, R. C., Møller, J. V., and Nissen, P. (2004) Dephosphorylation of the calcium pump coupled to counterion occlusion Science 306, 2251-2255 10.1126/science.1106289
    • (2004) Science , vol.306 , pp. 2251-2255
    • Olesen, C.1    Sorensen, T.L.2    Nielsen, R.C.3    Møller, J.V.4    Nissen, P.5
  • 12
    • 2942668632 scopus 로고    scopus 로고
    • Phosphoryl transfer and calcium ion occlusion in the calcium pump
    • Sorensen, T. L., Møller, J. V., and Nissen, P. (2004) Phosphoryl transfer and calcium ion occlusion in the calcium pump Science 304, 1672-1675 10.1126/science.1099366
    • (2004) Science , vol.304 , pp. 1672-1675
    • Sorensen, T.L.1    Møller, J.V.2    Nissen, P.3
  • 13
    • 3242888769 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump with a bound ATP analogue
    • Toyoshima, C. and Mizutani, T. (2004) Crystal structure of the calcium pump with a bound ATP analogue Nature 430, 529-535 10.1038/nature02680
    • (2004) Nature , vol.430 , pp. 529-535
    • Toyoshima, C.1    Mizutani, T.2
  • 14
    • 9244232176 scopus 로고    scopus 로고
    • Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues
    • Toyoshima, C., Nomura, H., and Tsuda, T. (2004) Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues Nature 432, 361-368 10.1038/nature02981
    • (2004) Nature , vol.432 , pp. 361-368
    • Toyoshima, C.1    Nomura, H.2    Tsuda, T.3
  • 15
    • 26844439857 scopus 로고    scopus 로고
    • Structural role of countertransport revealed in Ca(2+) pump crystal structure in the absence of Ca(2+)
    • Obara, K., Miyashita, N., Xu, C., Toyoshima, I., Sugita, Y., Inesi, G., and Toyoshima, C. (2005)) Structural role of countertransport revealed in Ca(2+) pump crystal structure in the absence of Ca(2+) Proc. Natl. Acad. Sci. U. S. A. 102, 14489-14496 10.1073/pnas.0506222102
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 14489-14496
    • Obara, K.1    Miyashita, N.2    Xu, C.3    Toyoshima, I.4    Sugita, Y.5    Inesi, G.6    Toyoshima, C.7
  • 19
    • 34347247711 scopus 로고    scopus 로고
    • Interdomain communication in calcium pump as revealed in the crystal structures with transmembrane inhibitors
    • Takahashi, M., Kondou, Y., and Toyoshima, C. (2007) Interdomain communication in calcium pump as revealed in the crystal structures with transmembrane inhibitors Proc. Natl. Acad. Sci. U. S. A. 104, 5800-5805 10.1073/pnas.0700979104
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 5800-5805
    • Takahashi, M.1    Kondou, Y.2    Toyoshima, C.3
  • 20
    • 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 10.1073/pnas.0709978104
    • (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
  • 21
    • 69549106325 scopus 로고    scopus 로고
    • Crystal structure of the sodium-potassium pump (Na+,K+-ATPase) with bound potassium and ouabain
    • Ogawa, H., Shinoda, T., Cornelius, F., and Toyoshima, C. (2009) Crystal structure of the sodium-potassium pump (Na+,K+-ATPase) with bound potassium and ouabain Proc. Natl. Acad. Sci. U. S. A. 106, 13742-13747 10.1073/pnas.0907054106
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 13742-13747
    • Ogawa, H.1    Shinoda, T.2    Cornelius, F.3    Toyoshima, C.4
  • 22
    • 66249147196 scopus 로고    scopus 로고
    • Crystal structure of the sodium-potassium pump at 2.4 A resolution
    • Shinoda, T., Ogawa, H., Cornelius, F., and Toyoshima, C. (2009) Crystal structure of the sodium-potassium pump at 2.4 A resolution Nature 459, 446-450 10.1038/nature07939
    • (2009) Nature , vol.459 , pp. 446-450
    • Shinoda, T.1    Ogawa, H.2    Cornelius, F.3    Toyoshima, C.4
  • 24
    • 79955879215 scopus 로고    scopus 로고
    • Mutual adaptation of a membrane protein and its lipid bilayer during conformational changes
    • Sonntag, Y., Musgaard, M., Olesen, C., Schiott, B., Møller, J. V., Nissen, P., and Thogersen, L. (2011) Mutual adaptation of a membrane protein and its lipid bilayer during conformational changes Nat. Commun. 2, 304 10.1038/ncomms1307
    • (2011) Nat. Commun. , vol.2 , pp. 304
    • Sonntag, Y.1    Musgaard, M.2    Olesen, C.3    Schiott, B.4    Møller, J.V.5    Nissen, P.6    Thogersen, L.7
  • 25
    • 79952162827 scopus 로고    scopus 로고
    • Trinitrophenyl derivatives bind differently from parent adenine nucleotides to Ca2+-ATPase in the absence of Ca2+
    • Toyoshima, C., Yonekura, S., Tsueda, J., and Iwasawa, S. (2011) Trinitrophenyl derivatives bind differently from parent adenine nucleotides to Ca2+-ATPase in the absence of Ca2+ Proc. Natl. Acad. Sci. U. S. A. 108, 1833-1838 10.1073/pnas.1017659108
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 1833-1838
    • Toyoshima, C.1    Yonekura, S.2    Tsueda, J.3    Iwasawa, S.4
  • 26
    • 84885654984 scopus 로고    scopus 로고
    • Crystal structure of a Na+-bound Na+,K+-ATPase preceding the E1P state
    • Kanai, R., Ogawa, H., Vilsen, B., Cornelius, F., and Toyoshima, C. (2013) Crystal structure of a Na+-bound Na+,K+-ATPase preceding the E1P state Nature 502, 201-206 10.1038/nature12578
    • (2013) Nature , vol.502 , pp. 201-206
    • Kanai, R.1    Ogawa, H.2    Vilsen, B.3    Cornelius, F.4    Toyoshima, C.5
  • 27
    • 84879701596 scopus 로고    scopus 로고
    • Crystal structure of the high-affinity Na+K+-ATPase-ouabain complex with Mg2+ bound in the cation binding site
    • Laursen, M., Yatime, L., Nissen, P., and Fedosova, N. U. (2013) Crystal structure of the high-affinity Na+K+-ATPase-ouabain complex with Mg2+ bound in the cation binding site Proc. Natl. Acad. Sci. U. S. A. 110, 10958-10963 10.1073/pnas.1222308110
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 10958-10963
    • Laursen, M.1    Yatime, L.2    Nissen, P.3    Fedosova, N.U.4
  • 29
    • 84874957001 scopus 로고    scopus 로고
    • Crystal structures of the calcium pump and sarcolipin in the Mg2+-bound E1 state
    • Toyoshima, C., Iwasawa, S., Ogawa, H., Hirata, A., Tsueda, J., and Inesi, G. (2013) Crystal structures of the calcium pump and sarcolipin in the Mg2+-bound E1 state Nature 495, 260-264 10.1038/nature11899
    • (2013) Nature , vol.495 , pp. 260-264
    • Toyoshima, C.1    Iwasawa, S.2    Ogawa, H.3    Hirata, A.4    Tsueda, J.5    Inesi, G.6
  • 32
    • 84922633960 scopus 로고    scopus 로고
    • Structures and characterization of digoxin- and bufalin-bound Na+,K+-ATPase compared with the ouabain-bound complex
    • Laursen, M., Gregersen, J. L., Yatime, L., Nissen, P., and Fedosova, N. U. (2015) Structures and characterization of digoxin- and bufalin-bound Na+,K+-ATPase compared with the ouabain-bound complex Proc. Natl. Acad. Sci. U. S. A. 112, 1755-1760 10.1073/pnas.1422997112
    • (2015) Proc. Natl. Acad. Sci. U. S. A. , vol.112 , pp. 1755-1760
    • Laursen, M.1    Gregersen, J.L.2    Yatime, L.3    Nissen, P.4    Fedosova, N.U.5
  • 33
    • 0025775022 scopus 로고
    • Electrogenic pump current of sarcoplasmic reticulum Ca(2+)-ATPase reconstituted at high lipid/protein ratio
    • Cornelius, F. and Møller, J. V. (1991) Electrogenic pump current of sarcoplasmic reticulum Ca(2+)-ATPase reconstituted at high lipid/protein ratio FEBS Lett. 284, 46-50 10.1016/0014-5793(91)80758-U
    • (1991) FEBS Lett. , vol.284 , pp. 46-50
    • Cornelius, F.1    Møller, J.V.2
  • 34
    • 0027266757 scopus 로고
    • H+ countertransport and electrogenicity of the sarcoplasmic reticulum Ca2+ pump in reconstituted proteoliposomes
    • Yu, X., Carroll, S., Rigaud, J. L., and Inesi, G. (1993) H+ countertransport and electrogenicity of the sarcoplasmic reticulum Ca2+ pump in reconstituted proteoliposomes Biophys. J. 64, 1232-1242 10.1016/S0006-3495(93)81489-9
    • (1993) Biophys. J. , vol.64 , pp. 1232-1242
    • Yu, X.1    Carroll, S.2    Rigaud, J.L.3    Inesi, G.4
  • 35
    • 79954415607 scopus 로고    scopus 로고
    • Structural insights into the high affinity binding of cardiotonic steroids to the Na+,K+-ATPase
    • Yatime, L., Laursen, M., Morth, J. P., Esmann, M., Nissen, P., and Fedosova, N. U. (2011) Structural insights into the high affinity binding of cardiotonic steroids to the Na+,K+-ATPase J. Struct. Biol. 174, 296-306 10.1016/j.jsb.2010.12.004
    • (2011) J. Struct. Biol. , vol.174 , pp. 296-306
    • Yatime, L.1    Laursen, M.2    Morth, J.P.3    Esmann, M.4    Nissen, P.5    Fedosova, N.U.6
  • 36
    • 0000760057 scopus 로고
    • The linkage of sodium, potassium, and ammonium active transport across the human erythrocyte membrane
    • Post, R. L. and Jolly, P. C. (1957) The linkage of sodium, potassium, and ammonium active transport across the human erythrocyte membrane Biochim. Biophys. Acta 25, 118-128 10.1016/0006-3002(57)90426-2
    • (1957) Biochim. Biophys. Acta , vol.25 , pp. 118-128
    • Post, R.L.1    Jolly, P.C.2
  • 37
    • 0000193823 scopus 로고
    • Determination of H/ATP Stoichiometry for the Plasma Membrane H-ATPase from Red Beet (Beta vulgaris L.) Storage Tissue
    • Briskin, D. P. and Reynolds-Niesman, I. (1991) Determination of H/ATP Stoichiometry for the Plasma Membrane H-ATPase from Red Beet (Beta vulgaris L.) Storage Tissue Plant Physiol. 95, 242-250 10.1104/pp.95.1.242
    • (1991) Plant Physiol. , vol.95 , pp. 242-250
    • Briskin, D.P.1    Reynolds-Niesman, I.2
  • 38
    • 0017883657 scopus 로고
    • Current-voltage relationships for the plasma membrane and its principal electrogenic pump in Neurospora crassa: I. Steady-state conditions
    • Gradmann, D., Hansen, U. P., Long, W. S., Slayman, C. L., and Warncke, J. (1978) Current-voltage relationships for the plasma membrane and its principal electrogenic pump in Neurospora crassa: I. Steady-state conditions J. Membr. Biol. 39, 333-367 10.1007/BF01869898
    • (1978) J. Membr. Biol. , vol.39 , pp. 333-367
    • Gradmann, D.1    Hansen, U.P.2    Long, W.S.3    Slayman, C.L.4    Warncke, J.5
  • 40
    • 79955814329 scopus 로고    scopus 로고
    • P-type ATPases
    • Palmgren, M. G. and Nissen, P. (2011) P-type ATPases Annu. Rev. Biophys. 40, 243-266 10.1146/annurev.biophys.093008.131331
    • (2011) Annu. Rev. Biophys. , vol.40 , pp. 243-266
    • Palmgren, M.G.1    Nissen, P.2
  • 41
    • 79951681214 scopus 로고    scopus 로고
    • The sarcoplasmic Ca2+-ATPase: Design of a perfect chemi-osmotic pump
    • Møller, J. V., Olesen, C., Winther, A. M., and Nissen, P. (2010) The sarcoplasmic Ca2+-ATPase: design of a perfect chemi-osmotic pump Q. Rev. Biophys. 43, 501-566 10.1017/S003358351000017X
    • (2010) Q. Rev. Biophys. , vol.43 , pp. 501-566
    • Møller, J.V.1    Olesen, C.2    Winther, A.M.3    Nissen, P.4
  • 42
    • 67349157973 scopus 로고    scopus 로고
    • How Ca2+-ATPase pumps ions across the sarcoplasmic reticulum membrane
    • Toyoshima, C. (2009) How Ca2+-ATPase pumps ions across the sarcoplasmic reticulum membrane Biochim. Biophys. Acta, Mol. Cell Res. 1793, 941-946 10.1016/j.bbamcr.2008.10.008
    • (2009) Biochim. Biophys. Acta, Mol. Cell Res. , vol.1793 , pp. 941-946
    • Toyoshima, C.1
  • 43
    • 77956312761 scopus 로고    scopus 로고
    • Neurological disease mutations compromise a C-terminal ion pathway in the Na(+)/K(+)-ATPase
    • Poulsen, H., Khandelia, H., Morth, J. P., Bublitz, M., Mouritsen, O. G., Egebjerg, J., and Nissen, P. (2010) Neurological disease mutations compromise a C-terminal ion pathway in the Na(+)/K(+)-ATPase Nature 467, 99-102 10.1038/nature09309
    • (2010) Nature , vol.467 , pp. 99-102
    • Poulsen, H.1    Khandelia, H.2    Morth, J.P.3    Bublitz, M.4    Mouritsen, O.G.5    Egebjerg, J.6    Nissen, P.7
  • 45
    • 84905819099 scopus 로고    scopus 로고
    • Diversity of the metal-transporting P1B-type ATPases
    • Smith, A. T., Smith, K. P., and Rosenzweig, A. C. (2014) Diversity of the metal-transporting P1B-type ATPases JBIC, J. Biol. Inorg. Chem. 19, 947-960 10.1007/s00775-014-1129-2
    • (2014) JBIC, J. Biol. Inorg. Chem. , vol.19 , pp. 947-960
    • Smith, A.T.1    Smith, K.P.2    Rosenzweig, A.C.3
  • 46
    • 0141987910 scopus 로고    scopus 로고
    • Identification of ion-selectivity determinants in heavy-metal transport P1B-type ATPases
    • Arguello, J. M. (2003) Identification of ion-selectivity determinants in heavy-metal transport P1B-type ATPases J. Membr. Biol. 195, 93-108 10.1007/s00232-003-2048-2
    • (2003) J. Membr. Biol. , vol.195 , pp. 93-108
    • Arguello, J.M.1
  • 47
    • 84876571224 scopus 로고    scopus 로고
    • A novel P(1B)-type Mn2+-transporting ATPase is required for secreted protein metallation in mycobacteria
    • Padilla-Benavides, T., Long, J. E., Raimunda, D., Sassetti, C. M., and Arguello, J. M. (2013) A novel P(1B)-type Mn2+-transporting ATPase is required for secreted protein metallation in mycobacteria J. Biol. Chem. 288, 11334-11347 10.1074/jbc.M112.448175
    • (2013) J. Biol. Chem. , vol.288 , pp. 11334-11347
    • Padilla-Benavides, T.1    Long, J.E.2    Raimunda, D.3    Sassetti, C.M.4    Arguello, J.M.5
  • 49
    • 0029967233 scopus 로고    scopus 로고
    • The Bradyrhizobium japonicum fixGHIS genes are required for the formation of the high-affinity cbb3-type cytochrome oxidase
    • Preisig, O., Zufferey, R., and Hennecke, H. (1996) The Bradyrhizobium japonicum fixGHIS genes are required for the formation of the high-affinity cbb3-type cytochrome oxidase Arch. Microbiol. 165, 297-305 10.1007/s002030050330
    • (1996) Arch. Microbiol. , vol.165 , pp. 297-305
    • Preisig, O.1    Zufferey, R.2    Hennecke, H.3
  • 50
    • 77953503319 scopus 로고    scopus 로고
    • CtpA, a copper-translocating P-type ATPase involved in the biogenesis of multiple copper-requiring enzymes
    • Hassani, B. K., Astier, C., Nitschke, W., and Ouchane, S. (2010) CtpA, a copper-translocating P-type ATPase involved in the biogenesis of multiple copper-requiring enzymes J. Biol. Chem. 285, 19330-19337 10.1074/jbc.M110.116020
    • (2010) J. Biol. Chem. , vol.285 , pp. 19330-19337
    • Hassani, B.K.1    Astier, C.2    Nitschke, W.3    Ouchane, S.4
  • 51
    • 0034677662 scopus 로고    scopus 로고
    • Roles of the ccoGHIS gene products in the biogenesis of the cbb(3)-type cytochrome c oxidase
    • Koch, H. G., Winterstein, C., Saribas, A. S., Alben, J. O., and Daldal, F. (2000) Roles of the ccoGHIS gene products in the biogenesis of the cbb(3)-type cytochrome c oxidase J. Mol. Biol. 297, 49-65 10.1006/jmbi.2000.3555
    • (2000) J. Mol. Biol. , vol.297 , pp. 49-65
    • Koch, H.G.1    Winterstein, C.2    Saribas, A.S.3    Alben, J.O.4    Daldal, F.5
  • 52
    • 0035827547 scopus 로고    scopus 로고
    • Two Menkes-type atpases supply copper for photosynthesis in Synechocystis PCC 6803
    • Tottey, S., Rich, P. R., Rondet, S. A., and Robinson, N. J. (2001) Two Menkes-type atpases supply copper for photosynthesis in Synechocystis PCC 6803 J. Biol. Chem. 276, 19999-20004 10.1074/jbc.M011243200
    • (2001) J. Biol. Chem. , vol.276 , pp. 19999-20004
    • Tottey, S.1    Rich, P.R.2    Rondet, S.A.3    Robinson, N.J.4
  • 53
    • 25844489990 scopus 로고    scopus 로고
    • P(1B)-ATPases - An ancient family of transition metal pumps with diverse functions in plants
    • Williams, L. E. and Mills, R. F. (2005) P(1B)-ATPases - an ancient family of transition metal pumps with diverse functions in plants Trends Plant Sci. 10, 491-502 10.1016/j.tplants.2005.08.008
    • (2005) Trends Plant Sci. , vol.10 , pp. 491-502
    • Williams, L.E.1    Mills, R.F.2
  • 54
    • 81255142801 scopus 로고    scopus 로고
    • Bacterial transition metal P(1B)-ATPases: Transport mechanism and roles in virulence
    • Arguello, J. M., Gonzalez-Guerrero, M., and Raimunda, D. (2011) Bacterial transition metal P(1B)-ATPases: transport mechanism and roles in virulence Biochemistry 50, 9940-9949 10.1021/bi201418k
    • (2011) Biochemistry , vol.50 , pp. 9940-9949
    • Arguello, J.M.1    Gonzalez-Guerrero, M.2    Raimunda, D.3
  • 56
    • 0141431021 scopus 로고    scopus 로고
    • Functional roles of metal binding domains of the Archaeoglobus fulgidus Cu(+)-ATPase CopA
    • Mandal, A. K. and Arguello, J. M. (2003) Functional roles of metal binding domains of the Archaeoglobus fulgidus Cu(+)-ATPase CopA Biochemistry 42, 11040-11047 10.1021/bi034806y
    • (2003) Biochemistry , vol.42 , pp. 11040-11047
    • Mandal, A.K.1    Arguello, J.M.2
  • 58
    • 43149096496 scopus 로고    scopus 로고
    • Mechanism of Cu+-transporting ATPases: Soluble Cu+ chaperones directly transfer Cu+ to transmembrane transport sites
    • Gonzalez-Guerrero, M. and Arguello, J. M. (2008) Mechanism of Cu+-transporting ATPases: soluble Cu+ chaperones directly transfer Cu+ to transmembrane transport sites Proc. Natl. Acad. Sci. U. S. A. 105, 5992-5997 10.1073/pnas.0711446105
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 5992-5997
    • Gonzalez-Guerrero, M.1    Arguello, J.M.2
  • 59
    • 0023872238 scopus 로고
    • Identification and primary structure of a calmodulin binding domain of the Ca2+ pump of human erythrocytes
    • James, P., Maeda, M., Fischer, R., Verma, A. K., Krebs, J., Penniston, J. T., and Carafoli, E. (1988) Identification and primary structure of a calmodulin binding domain of the Ca2+ pump of human erythrocytes J. Biol. Chem. 263, 2905-2910
    • (1988) J. Biol. Chem. , vol.263 , pp. 2905-2910
    • James, P.1    Maeda, M.2    Fischer, R.3    Verma, A.K.4    Krebs, J.5    Penniston, J.T.6    Carafoli, E.7
  • 60
    • 77951210563 scopus 로고    scopus 로고
    • A Novel Mechanism of P-type ATPase Autoinhibition Involving Both Termini of the Protein
    • Ekberg, K., Palmgren, M. G., Veierskov, B., and Buch-Pedersen, M. J. (2010) A Novel Mechanism of P-type ATPase Autoinhibition Involving Both Termini of the Protein J. Biol. Chem. 285, 7344-7350 10.1074/jbc.M109.096123
    • (2010) J. Biol. Chem. , vol.285 , pp. 7344-7350
    • Ekberg, K.1    Palmgren, M.G.2    Veierskov, B.3    Buch-Pedersen, M.J.4
  • 63
    • 0033617292 scopus 로고    scopus 로고
    • RESPONSIVE-TO-ANTAGONIST1, a Menkes/Wilson disease-related copper transporter, is required for ethylene signaling in Arabidopsis
    • Hirayama, T., Kieber, J. J., Hirayama, N., Kogan, M., Guzman, P., Nourizadeh, S., Alonso, J. M., Dailey, W. P., Dancis, A., and Ecker, J. R. (1999) RESPONSIVE-TO-ANTAGONIST1, a Menkes/Wilson disease-related copper transporter, is required for ethylene signaling in Arabidopsis Cell 97, 383-393 10.1016/S0092-8674(00)80747-3
    • (1999) Cell , vol.97 , pp. 383-393
    • Hirayama, T.1    Kieber, J.J.2    Hirayama, N.3    Kogan, M.4    Guzman, P.5    Nourizadeh, S.6    Alonso, J.M.7    Dailey, W.P.8    Dancis, A.9    Ecker, J.R.10
  • 65
    • 84872072402 scopus 로고    scopus 로고
    • The mechanism of Cu+ transport ATPases: Interaction with Cu+ chaperones and the role of transient metal-binding sites
    • Padilla-Benavides, T., McCann, C. J., and Arguello, J. M. (2013) The mechanism of Cu+ transport ATPases: interaction with Cu+ chaperones and the role of transient metal-binding sites J. Biol. Chem. 288, 69-78 10.1074/jbc.M112.420810
    • (2013) J. Biol. Chem. , vol.288 , pp. 69-78
    • Padilla-Benavides, T.1    McCann, C.J.2    Arguello, J.M.3
  • 66
    • 70349211883 scopus 로고    scopus 로고
    • Copper, iron, and zinc ions homeostasis and their role in neurodegenerative disorders (metal uptake, transport, distribution and regulation)
    • Kozlowski, H., Janicka-Klos, A., Brasun, J., Gaggelli, E., Valensin, D., and Valensin, G. (2009) Copper, iron, and zinc ions homeostasis and their role in neurodegenerative disorders (metal uptake, transport, distribution and regulation) Coord. Chem. Rev. 253, 2665-2685 10.1016/j.ccr.2009.05.011
    • (2009) Coord. Chem. Rev. , vol.253 , pp. 2665-2685
    • Kozlowski, H.1    Janicka-Klos, A.2    Brasun, J.3    Gaggelli, E.4    Valensin, D.5    Valensin, G.6
  • 67
    • 66249112833 scopus 로고    scopus 로고
    • The iron-sulfur clusters of dehydratases are primary intracellular targets of copper toxicity
    • Macomber, L. and Imlay, J. A. (2009) The iron-sulfur clusters of dehydratases are primary intracellular targets of copper toxicity Proc. Natl. Acad. Sci. U. S. A. 106, 8344-8349 10.1073/pnas.0812808106
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 8344-8349
    • Macomber, L.1    Imlay, J.A.2
  • 68
    • 0033617578 scopus 로고    scopus 로고
    • Undetectable intracellular free copper: The requirement of a copper chaperone for superoxide dismutase
    • Rae, T. D., Schmidt, P. J., Pufahl, R. A., Culotta, V. C., and O'Halloran, T. V. (1999) Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase Science 284, 805-808 10.1126/science.284.5415.805
    • (1999) Science , vol.284 , pp. 805-808
    • Rae, T.D.1    Schmidt, P.J.2    Pufahl, R.A.3    Culotta, V.C.4    O'Halloran, T.V.5
  • 69
    • 84903594596 scopus 로고    scopus 로고
    • Analyzing free zinc(II) ion concentrations in cell biology with fluorescent chelating molecules
    • Maret, W. (2014) Analyzing free zinc(ii) ion concentrations in cell biology with fluorescent chelating molecules Metallomics 6, 1174 10.1039/C4MT90021A
    • (2014) Metallomics , vol.6 , pp. 1174
    • Maret, W.1
  • 70
    • 80052768714 scopus 로고    scopus 로고
    • The toxicity redox mechanisms of cadmium alone or together with copper and zinc homeostasis alteration: Its redox biomarkers
    • Nzengue, Y., Candeias, S. M., Sauvaigo, S., Douki, T., Favier, A., Rachidi, W., and Guiraud, P. (2011) The toxicity redox mechanisms of cadmium alone or together with copper and zinc homeostasis alteration: Its redox biomarkers J. Trace Elem. Med. Biol. 25, 171-180 10.1016/j.jtemb.2011.06.002
    • (2011) J. Trace Elem. Med. Biol. , vol.25 , pp. 171-180
    • Nzengue, Y.1    Candeias, S.M.2    Sauvaigo, S.3    Douki, T.4    Favier, A.5    Rachidi, W.6    Guiraud, P.7
  • 71
    • 0028798434 scopus 로고
    • Oxidative mechanisms in the toxicity of metal ions
    • Stohs, S. J. and Bagchi, D. (1995) Oxidative mechanisms in the toxicity of metal ions Free Radical Biol. Med. 18, 321-336 10.1016/0891-5849(94)00159-H
    • (1995) Free Radical Biol. Med. , vol.18 , pp. 321-336
    • Stohs, S.J.1    Bagchi, D.2
  • 72
    • 67649509594 scopus 로고    scopus 로고
    • Nucleotide recognition by CopA, a Cu+-transporting P-type ATPase
    • Tsuda, T. and Toyoshima, C. (2009) Nucleotide recognition by CopA, a Cu+-transporting P-type ATPase EMBO J. 28, 1782-1791 10.1038/emboj.2009.143
    • (2009) EMBO J. , vol.28 , pp. 1782-1791
    • Tsuda, T.1    Toyoshima, C.2
  • 73
    • 0037565100 scopus 로고    scopus 로고
    • Copper homeostasis in Enterococcus hirae
    • Solioz, M. and Stoyanov, J. V. (2003) Copper homeostasis in Enterococcus hirae FEMS microbiology reviews 27, 183-195 10.1016/S0168-6445(03)00053-6
    • (2003) FEMS Microbiology Reviews , vol.27 , pp. 183-195
    • Solioz, M.1    Stoyanov, J.V.2
  • 74
    • 0032926864 scopus 로고    scopus 로고
    • ZntR is a Zn(II)-responsive MerR-like transcriptional regulator of zntA in Escherichia coli
    • Brocklehurst, K. R., Hobman, J. L., Lawley, B., Blank, L., Marshall, S. J., Brown, N. L., and Morby, A. P. (1999) ZntR is a Zn(II)-responsive MerR-like transcriptional regulator of zntA in Escherichia coli Mol. Microbiol. 31, 893-902 10.1046/j.1365-2958.1999.01229.x
    • (1999) Mol. Microbiol. , vol.31 , pp. 893-902
    • Brocklehurst, K.R.1    Hobman, J.L.2    Lawley, B.3    Blank, L.4    Marshall, S.J.5    Brown, N.L.6    Morby, A.P.7
  • 75
    • 24944583149 scopus 로고    scopus 로고
    • Transcriptional response of Escherichia coli to external zinc
    • Yamamoto, K. and Ishihama, A. (2005) Transcriptional response of Escherichia coli to external zinc Journal of bacteriology 187, 6333-6340 10.1128/JB.187.18.6333-6340.2005
    • (2005) Journal of Bacteriology , vol.187 , pp. 6333-6340
    • Yamamoto, K.1    Ishihama, A.2
  • 76
    • 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 10.1101/gr.196802
    • (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
  • 78
    • 84875998903 scopus 로고    scopus 로고
    • A conserved asparagine in a P-type proton pump is required for efficient gating of protons
    • Ekberg, K., Wielandt, A. G., Buch-Pedersen, M. J., and Palmgren, M. G. (2013) A conserved asparagine in a P-type proton pump is required for efficient gating of protons J. Biol. Chem. 288, 9610-9618 10.1074/jbc.M112.417345
    • (2013) J. Biol. Chem. , vol.288 , pp. 9610-9618
    • Ekberg, K.1    Wielandt, A.G.2    Buch-Pedersen, M.J.3    Palmgren, M.G.4
  • 79
    • 84859972108 scopus 로고    scopus 로고
    • Metal transport across biomembranes: Emerging models for a distinct chemistry
    • Arguello, J. M., Raimunda, D., and Gonzalez-Guerrero, M. (2012) Metal transport across biomembranes: emerging models for a distinct chemistry J. Biol. Chem. 287, 13510-13517 10.1074/jbc.R111.319343
    • (2012) J. Biol. Chem. , vol.287 , pp. 13510-13517
    • Arguello, J.M.1    Raimunda, D.2    Gonzalez-Guerrero, M.3
  • 80
    • 0035954407 scopus 로고    scopus 로고
    • The cysteine-rich amino-terminal domain of ZntA, a Pb(II)/Zn(II)/Cd(II)-translocating ATPase from Escherichia coli, is not essential for its function
    • Mitra, B. and Sharma, R. (2001) The cysteine-rich amino-terminal domain of ZntA, a Pb(II)/Zn(II)/Cd(II)-translocating ATPase from Escherichia coli, is not essential for its function Biochemistry 40, 7694-7699 10.1021/bi010576g
    • (2001) Biochemistry , vol.40 , pp. 7694-7699
    • Mitra, B.1    Sharma, R.2
  • 81
    • 63149174239 scopus 로고    scopus 로고
    • Structural model of the CopA copper ATPase of Enterococcus hirae based on chemical cross-linking
    • Lubben, M., Portmann, R., Kock, G., Stoll, R., Young, M. M., and Solioz, M. (2009) Structural model of the CopA copper ATPase of Enterococcus hirae based on chemical cross-linking BioMetals 22, 363-375 10.1007/s10534-008-9173-4
    • (2009) BioMetals , vol.22 , pp. 363-375
    • Lubben, M.1    Portmann, R.2    Kock, G.3    Stoll, R.4    Young, M.M.5    Solioz, M.6
  • 82
    • 33750601861 scopus 로고    scopus 로고
    • The metal-binding sites of the zinc-transporting P-type ATPase of Escherichia coli. Lys693 and Asp714 in the seventh and eighth transmembrane segments of ZntA contribute to the coupling of metal binding and ATPase activity
    • Okkeri, J. and Haltia, T. (2006) The metal-binding sites of the zinc-transporting P-type ATPase of Escherichia coli. Lys693 and Asp714 in the seventh and eighth transmembrane segments of ZntA contribute to the coupling of metal binding and ATPase activity Biochim. Biophys. Acta, Bioenerg. 1757, 1485-1495 10.1016/j.bbabio.2006.06.008
    • (2006) Biochim. Biophys. Acta, Bioenerg. , vol.1757 , pp. 1485-1495
    • Okkeri, J.1    Haltia, T.2
  • 83
    • 84859832471 scopus 로고    scopus 로고
    • Structural models of the human copper P-type ATPases ATP7A and ATP7B
    • Gourdon, P., Sitsel, O., Lykkegaard Karlsen, J., Birk Møller, L., and Nissen, P. (2012) Structural models of the human copper P-type ATPases ATP7A and ATP7B Biol. Chem. 393, 205-216 10.1515/hsz-2011-0249
    • (2012) Biol. Chem. , vol.393 , pp. 205-216
    • Gourdon, P.1    Sitsel, O.2    Lykkegaard Karlsen, J.3    Birk Møller, L.4    Nissen, P.5
  • 85
    • 79751527206 scopus 로고    scopus 로고
    • Golgi membranes from liver express an ATPase with femtomolar copper affinity, inhibited by cAMP-dependent protein kinase
    • Hilario-Souza, E., Valverde, R. H., Britto-Borges, T., Vieyra, A., and Lowe, J. (2011) Golgi membranes from liver express an ATPase with femtomolar copper affinity, inhibited by cAMP-dependent protein kinase Int. J. Biochem. Cell Biol. 43, 358-362 10.1016/j.biocel.2010.11.004
    • (2011) Int. J. Biochem. Cell Biol. , vol.43 , pp. 358-362
    • Hilario-Souza, E.1    Valverde, R.H.2    Britto-Borges, T.3    Vieyra, A.4    Lowe, J.5
  • 86
    • 31044446123 scopus 로고    scopus 로고
    • Metal-binding affinity of the transmembrane site in ZntA: Implications for metal selectivity
    • 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 10.1021/bi051836n
    • (2006) Biochemistry , vol.45 , pp. 763-772
    • Liu, J.1    Dutta, S.J.2    Stemmler, A.J.3    Mitra, B.4
  • 87
    • 84255178757 scopus 로고    scopus 로고
    • Coordination chemistry of copper proteins: How nature handles a toxic cargo for essential function
    • Rubino, J. T. and Franz, K. J. (2012) Coordination chemistry of copper proteins: how nature handles a toxic cargo for essential function J. Inorg. Biochem. 107, 129-143 10.1016/j.jinorgbio.2011.11.024
    • (2012) J. Inorg. Biochem. , vol.107 , pp. 129-143
    • Rubino, J.T.1    Franz, K.J.2
  • 88
    • 0035690880 scopus 로고    scopus 로고
    • Zinc coordination sphere in biochemical zinc sites
    • Auld, D. S. (2001) Zinc coordination sphere in biochemical zinc sites BioMetals 14, 271-313 10.1023/A:1012976615056
    • (2001) BioMetals , vol.14 , pp. 271-313
    • Auld, D.S.1
  • 90
    • 57649148770 scopus 로고    scopus 로고
    • Structure of the two transmembrane Cu+ transport sites of the Cu+ -ATPases
    • Gonzalez-Guerrero, M., Eren, E., Rawat, S., Stemmler, T. L., and Arguello, J. M. (2008) Structure of the two transmembrane Cu+ transport sites of the Cu+ -ATPases J. Biol. Chem. 283, 29753-29759 10.1074/jbc.M803248200
    • (2008) J. Biol. Chem. , vol.283 , pp. 29753-29759
    • Gonzalez-Guerrero, M.1    Eren, E.2    Rawat, S.3    Stemmler, T.L.4    Arguello, J.M.5
  • 91
    • 84858737783 scopus 로고    scopus 로고
    • A tetrahedral coordination of Zinc during transmembrane transport by P-type Zn(2+)-ATPases
    • Raimunda, D., Subramanian, P., Stemmler, T., and Arguello, J. M. (2012) A tetrahedral coordination of Zinc during transmembrane transport by P-type Zn(2+)-ATPases Biochim. Biophys. Acta, Biomembr. 1818, 1374-1377 10.1016/j.bbamem.2012.02.020
    • (2012) Biochim. Biophys. Acta, Biomembr. , vol.1818 , pp. 1374-1377
    • Raimunda, D.1    Subramanian, P.2    Stemmler, T.3    Arguello, J.M.4
  • 92
    • 34748870747 scopus 로고    scopus 로고
    • Analysis of the structural consensus of the zinc coordination centers of metalloprotein structures
    • Patel, K., Kumar, A., and Durani, S. (2007) Analysis of the structural consensus of the zinc coordination centers of metalloprotein structures Biochim. Biophys. Acta, Proteins Proteomics 1774, 1247-1253 10.1016/j.bbapap.2007.07.010
    • (2007) Biochim. Biophys. Acta, Proteins Proteomics , vol.1774 , pp. 1247-1253
    • Patel, K.1    Kumar, A.2    Durani, S.3
  • 93
    • 80054737086 scopus 로고    scopus 로고
    • Minimal functional sites allow a classification of zinc sites in proteins
    • Andreini, C., Bertini, I., and Cavallaro, G. (2011) Minimal functional sites allow a classification of zinc sites in proteins PLoS One 6, e26325 10.1371/journal.pone.0026325
    • (2011) PLoS One , vol.6 , pp. e26325
    • Andreini, C.1    Bertini, I.2    Cavallaro, G.3
  • 94
    • 77951991586 scopus 로고    scopus 로고
    • Chaperone-mediated copper handling in the periplasm
    • Kim, E. H., Rensing, C., and McEvoy, M. M. (2010) Chaperone-mediated copper handling in the periplasm Nat. Prod. Rep. 27, 711-719 10.1039/b906681k
    • (2010) Nat. Prod. Rep. , vol.27 , pp. 711-719
    • Kim, E.H.1    Rensing, C.2    McEvoy, M.M.3
  • 95
    • 84905402461 scopus 로고    scopus 로고
    • Mechanism of ATPase-mediated Cu+ export and delivery to periplasmic chaperones: The interaction of Escherichia coli CopA and CusF
    • Padilla-Benavides, T., Thompson, A. M. G., McEvoy, M. M., and Arguello, J. M. (2014) Mechanism of ATPase-mediated Cu+ export and delivery to periplasmic chaperones: the interaction of Escherichia coli CopA and CusF J. Biol. Chem. 289, 20492-20501 10.1074/jbc.M114.577668
    • (2014) J. Biol. Chem. , vol.289 , pp. 20492-20501
    • Padilla-Benavides, T.1    Thompson, A.M.G.2    McEvoy, M.M.3    Arguello, J.M.4
  • 96
    • 78249289106 scopus 로고    scopus 로고
    • ATP dependent charge movement in ATP7B Cu+-ATPase is demonstrated by pre-steady state electrical measurements
    • Tadini-Buoninsegni, F., Bartolommei, G., Moncelli, M. R., Pilankatta, R., Lewis, D., and Inesi, G. (2010) ATP dependent charge movement in ATP7B Cu+-ATPase is demonstrated by pre-steady state electrical measurements FEBS Lett. 584, 4619-4622 10.1016/j.febslet.2010.10.029
    • (2010) FEBS Lett. , vol.584 , pp. 4619-4622
    • Tadini-Buoninsegni, F.1    Bartolommei, G.2    Moncelli, M.R.3    Pilankatta, R.4    Lewis, D.5    Inesi, G.6
  • 97
    • 84901007672 scopus 로고    scopus 로고
    • Role of protons in the pump cycle of KdpFABC investigated by time-resolved kinetic experiments
    • Damnjanovic, B. and Apell, H. J. (2014) Role of protons in the pump cycle of KdpFABC investigated by time-resolved kinetic experiments Biochemistry 53, 3218-3228 10.1021/bi500336w
    • (2014) Biochemistry , vol.53 , pp. 3218-3228
    • Damnjanovic, B.1    Apell, H.J.2
  • 98
    • 34548078365 scopus 로고    scopus 로고
    • Common patterns and unique features of P-type ATPases: A comparative view on the KdpFABC complex from Escherichia coli (Review)
    • Bramkamp, M., Altendorf, K., and Greie, J. C. (2007) Common patterns and unique features of P-type ATPases: a comparative view on the KdpFABC complex from Escherichia coli (Review) Mol. Membr. Biol. 24, 375-386 10.1080/09687680701418931
    • (2007) Mol. Membr. Biol. , vol.24 , pp. 375-386
    • Bramkamp, M.1    Altendorf, K.2    Greie, J.C.3
  • 99
    • 0031664331 scopus 로고    scopus 로고
    • The medial-Golgi ion pump Pmr1 supplies the yeast secretory pathway with Ca2+ and Mn2+ required for glycosylation, sorting, and endoplasmic reticulum-associated protein degradation
    • Durr, G., Strayle, J., Plemper, R., Elbs, S., Klee, S. K., Catty, P., Wolf, D. H., and Rudolph, H. K. (1998) The medial-Golgi ion pump Pmr1 supplies the yeast secretory pathway with Ca2+ and Mn2+ required for glycosylation, sorting, and endoplasmic reticulum-associated protein degradation Molecular biology of the cell 9, 1149-1162 10.1091/mbc.9.5.1149
    • (1998) Molecular Biology of the Cell , vol.9 , pp. 1149-1162
    • Durr, G.1    Strayle, J.2    Plemper, R.3    Elbs, S.4    Klee, S.K.5    Catty, P.6    Wolf, D.H.7    Rudolph, H.K.8
  • 100
    • 0032540752 scopus 로고    scopus 로고
    • Ca2+ transport by reconstituted synaptosomal ATPase is associated with H+ countertransport and net charge displacement
    • Salvador, J. M., Inesi, G., Rigaud, J. L., and Mata, A. M. (1998) Ca2+ transport by reconstituted synaptosomal ATPase is associated with H+ countertransport and net charge displacement J. Biol. Chem. 273, 18230-18234 10.1074/jbc.273.29.18230
    • (1998) J. Biol. Chem. , vol.273 , pp. 18230-18234
    • Salvador, J.M.1    Inesi, G.2    Rigaud, J.L.3    Mata, A.M.4
  • 101
    • 0028174326 scopus 로고
    • Ca2+/H+ countertransport and electrogenicity in proteoliposomes containing erythrocyte plasma membrane Ca-ATPase and exogenous lipids
    • Hao, L., Rigaud, J. L., and Inesi, G. (1994) Ca2+/H+ countertransport and electrogenicity in proteoliposomes containing erythrocyte plasma membrane Ca-ATPase and exogenous lipids J. Biol. Chem. 269, 14268-14275
    • (1994) J. Biol. Chem. , vol.269 , pp. 14268-14275
    • Hao, L.1    Rigaud, J.L.2    Inesi, G.3
  • 102
    • 0019831037 scopus 로고
    • H+/ATP stoichiometry for the gastric (K+ + H+)-ATPase
    • Reenstra, W. W. and Forte, J. G. (1981) H+/ATP stoichiometry for the gastric (K+ + H+)-ATPase J. Membr. Biol. 61, 55-60 10.1007/BF01870752
    • (1981) J. Membr. Biol. , vol.61 , pp. 55-60
    • Reenstra, W.W.1    Forte, J.G.2
  • 103
    • 0025947113 scopus 로고
    • Identification of an extracytoplasmic region of H+,K(+)-ATPase labeled by a K(+)-competitive photoaffinity inhibitor
    • Munson, K. B., Gutierrez, C., Balaji, V. N., Ramnarayan, K., and Sachs, G. (1991) Identification of an extracytoplasmic region of H+,K(+)-ATPase labeled by a K(+)-competitive photoaffinity inhibitor J. Biol. Chem. 266, 18976-18988
    • (1991) J. Biol. Chem. , vol.266 , pp. 18976-18988
    • Munson, K.B.1    Gutierrez, C.2    Balaji, V.N.3    Ramnarayan, K.4    Sachs, G.5
  • 104
    • 0020479096 scopus 로고
    • The gastric [H,K]ATPase:H+/ATP stoichiometry
    • Rabon, E. C., McFall, T. L., and Sachs, G. (1982) The gastric [H,K]ATPase:H+/ATP stoichiometry J. Biol. Chem. 257, 6296-6299
    • (1982) J. Biol. Chem. , vol.257 , pp. 6296-6299
    • Rabon, E.C.1    McFall, T.L.2    Sachs, G.3
  • 105
    • 84873901917 scopus 로고    scopus 로고
    • Na(+) regulation in the malaria parasite Plasmodium falciparum involves the cation ATPase PfATP4 and is a target of the spiroindolone antimalarials
    • Spillman, N. J., Allen, R. J., McNamara, C. W., Yeung, B. K., Winzeler, E. A., Diagana, T. T., and Kirk, K. (2013) Na(+) regulation in the malaria parasite Plasmodium falciparum involves the cation ATPase PfATP4 and is a target of the spiroindolone antimalarials Cell Host Microbe 13, 227-237 10.1016/j.chom.2012.12.006
    • (2013) Cell Host Microbe , vol.13 , pp. 227-237
    • Spillman, N.J.1    Allen, R.J.2    McNamara, C.W.3    Yeung, B.K.4    Winzeler, E.A.5    Diagana, T.T.6    Kirk, K.7
  • 107
    • 77955660389 scopus 로고    scopus 로고
    • Sodium or potassium efflux ATPase a fungal, bryophyte, and protozoal ATPase
    • Rodriguez-Navarro, A. and Benito, B. (2010) Sodium or potassium efflux ATPase a fungal, bryophyte, and protozoal ATPase Biochim. Biophys. Acta, Biomembr. 1798, 1841-1853 10.1016/j.bbamem.2010.07.009
    • (2010) Biochim. Biophys. Acta, Biomembr. , vol.1798 , pp. 1841-1853
    • Rodriguez-Navarro, A.1    Benito, B.2
  • 108
    • 0022531811 scopus 로고
    • H+/ATP stoichiometry of proton pumps from Neurospora crassa and Escherichia coli
    • Perlin, D. S., San Francisco, M. J., Slayman, C. W., and Rosen, B. P. (1986) H+/ATP stoichiometry of proton pumps from Neurospora crassa and Escherichia coli Arch. Biochem. Biophys. 248, 53-61 10.1016/0003-9861(86)90400-5
    • (1986) Arch. Biochem. Biophys. , vol.248 , pp. 53-61
    • Perlin, D.S.1    San Francisco, M.J.2    Slayman, C.W.3    Rosen, B.P.4
  • 109
    • 0002398729 scopus 로고
    • Structure and Function of Plasma-Membrane Atpase
    • Serrano, R. (1989) Structure and Function of Plasma-Membrane Atpase Annu. Rev. Plant Physiol. Plant Mol. Biol. 40, 61-94 10.1146/annurev.pp.40.060189.000425
    • (1989) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.40 , pp. 61-94
    • Serrano, R.1
  • 110
    • 0029992825 scopus 로고    scopus 로고
    • A subfamily of P-type ATPases with aminophospholipid transporting activity
    • Tang, X., Halleck, M. S., Schlegel, R. A., and Williamson, P. (1996) A subfamily of P-type ATPases with aminophospholipid transporting activity Science 272, 1495-1497 10.1126/science.272.5267.1495
    • (1996) Science , vol.272 , pp. 1495-1497
    • Tang, X.1    Halleck, M.S.2    Schlegel, R.A.3    Williamson, P.4
  • 112
    • 84893714128 scopus 로고    scopus 로고
    • Identification of functionally important conserved trans-membrane residues of bacterial PIB -type ATPases
    • Zhitnitsky, D. and Lewinson, O. (2014) Identification of functionally important conserved trans-membrane residues of bacterial PIB -type ATPases Mol. Microbiol. 91, 777-789 10.1111/mmi.12495
    • (2014) Mol. Microbiol. , vol.91 , pp. 777-789
    • Zhitnitsky, D.1    Lewinson, O.2
  • 113
    • 84900461694 scopus 로고    scopus 로고
    • Transmembrane type-2-like Cu2+ site in the P1B-3-type ATPase CopB: Implications for metal selectivity
    • Meloni, G., Zhang, L., and Rees, D. C. (2014) Transmembrane type-2-like Cu2+ site in the P1B-3-type ATPase CopB: implications for metal selectivity ACS Chem. Biol. 9, 116-121 10.1021/cb400603t
    • (2014) ACS Chem. Biol. , vol.9 , pp. 116-121
    • Meloni, G.1    Zhang, L.2    Rees, D.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.