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Volumn 80, Issue 5, 2015, Pages 495-516

Ancient systems of sodium/potassium homeostasis as predecessors of membrane bioenergetics

Author keywords

abiogenesis; anoxic geothermal fields; ATP synthase; membrane efflux pumps; proton motive force; sodium symporter; sodium motive force

Indexed keywords

EUKARYOTA;

EID: 84928992317     PISSN: 00062979     EISSN: 16083040     Source Type: Journal    
DOI: 10.1134/S0006297915050016     Document Type: Article
Times cited : (54)

References (165)
  • 2
    • 36949083936 scopus 로고
    • Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism
    • 13771349
    • Mitchell, P. (1961) Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism, Nature, 191, 144-148.
    • (1961) Nature , vol.191 , pp. 144-148
    • Mitchell, P.1
  • 3
    • 0017599059 scopus 로고
    • +-potential as a convertible energy source for the living cell
    • 14031
    • +-potential as a convertible energy source for the living cell, FEBS Lett., 74, 1-9.
    • (1977) FEBS Lett. , vol.74 , pp. 1-9
    • Skulachev, V.P.1
  • 6
    • 0024804206 scopus 로고
    • The sodium cycle: A novel type of bacterial energetics
    • 2687258
    • Skulachev, V. P. (1989) The sodium cycle: a novel type of bacterial energetics, J. Bioenerg. Biomembr., 21, 635-647.
    • (1989) J. Bioenerg. Biomembr. , vol.21 , pp. 635-647
    • Skulachev, V.P.1
  • 8
    • 0027956427 scopus 로고
    • Bacterial sodium ion-coupled energetics
    • 7832594
    • Dimroth, P. (1994) Bacterial sodium ion-coupled energetics, Antonie Van Leeuwenhoek, 65, 381-395.
    • (1994) Antonie Van Leeuwenhoek , vol.65 , pp. 381-395
    • Dimroth, P.1
  • 9
    • 0034835047 scopus 로고    scopus 로고
    • Sodium ion cycle in bacterial pathogens: Evidence from cross-genome comparisons
    • 1:CAS:528:DC%2BD3MXnt12nuro%3D 11528000
    • Hase, C. C., Fedorova, N. D., Galperin, M. Y., and Dibrov, P. A. (2001) Sodium ion cycle in bacterial pathogens: evidence from cross-genome comparisons, Microbiol. Mol. Biol. Rev., 65, 353-370.
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 353-370
    • Hase, C.C.1    Fedorova, N.D.2    Galperin, M.Y.3    Dibrov, P.A.4
  • 11
    • 46349090280 scopus 로고    scopus 로고
    • The past and present of sodium energetics: May the sodium-motive force be with you
    • 1:CAS:528:DC%2BD1cXnsFCls7o%3D 18485887
    • Mulkidjanian, A. Y., Dibrov, P., and Galperin, M. Y. (2008) The past and present of sodium energetics: may the sodium-motive force be with you, Biochim. Biophys. Acta, 1777, 985-992.
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 985-992
    • Mulkidjanian, A.Y.1    Dibrov, P.2    Galperin, M.Y.3
  • 12
    • 63549086214 scopus 로고    scopus 로고
    • Co-evolution of primordial membranes and membrane proteins
    • 1:CAS:528:DC%2BD1MXksVSktL4%3D 19303305
    • Mulkidjanian, A. Y., Galperin, M. Y., and Koonin, E. V. (2009) Co-evolution of primordial membranes and membrane proteins, Trends Biochem. Sci., 34, 206-215.
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 206-215
    • Mulkidjanian, A.Y.1    Galperin, M.Y.2    Koonin, E.V.3
  • 13
    • 0023429474 scopus 로고
    • Proton permeation of lipid bilayers
    • 2447068
    • Deamer, D. W. (1987) Proton permeation of lipid bilayers, J. Bioenerg. Biomembr., 19, 457-479.
    • (1987) J. Bioenerg. Biomembr. , vol.19 , pp. 457-479
    • Deamer, D.W.1
  • 14
    • 0029591357 scopus 로고
    • Ion permeability of the cytoplasmic membrane limits the maximum growth temperature of bacteria and archaea
    • Van de Vossenberg, J. L., Ubbink-Kok, T., Elferink, M. G., Driessen, A. J., and Konings, W. N. (1995) Ion permeability of the cytoplasmic membrane limits the maximum growth temperature of bacteria and archaea, Mol. Microbiol., 18, 925-932.
    • (1995) Mol. Microbiol. , vol.18 , pp. 925-932
    • Van De Vossenberg, J.L.1    Ubbink-Kok, T.2    Elferink, M.G.3    Driessen, A.J.4    Konings, W.N.5
  • 16
    • 33750607429 scopus 로고    scopus 로고
    • Microbial transport: Adaptations to natural environments
    • 17043914
    • Konings, W. N. (2006) Microbial transport: adaptations to natural environments, Antonie Van Leeuwenhoek, 90, 325-342.
    • (2006) Antonie Van Leeuwenhoek , vol.90 , pp. 325-342
    • Konings, W.N.1
  • 17
    • 0011122028 scopus 로고
    • The paleochemistry of the body fluids and tissues
    • Macallum, A. B. (1926) The paleochemistry of the body fluids and tissues, Physiol. Rev., 6, 316-357.
    • (1926) Physiol. Rev. , vol.6 , pp. 316-357
    • Macallum, A.B.1
  • 20
    • 0141844665 scopus 로고    scopus 로고
    • Elemental composition of single cells of various strains of marine prochlorococcus and synechococcus using X-ray microanalysis
    • Heldal, M., Scanlan, D. J., Norland, S., Thingstad, F., and Mann, N. H. (2010) Elemental composition of single cells of various strains of marine prochlorococcus and synechococcus using X-ray microanalysis, Limnol. Oceanogr., 48, 1732-1743.
    • (2010) Limnol. Oceanogr. , vol.48 , pp. 1732-1743
    • Heldal, M.1    Scanlan, D.J.2    Norland, S.3    Thingstad, F.4    Mann, N.H.5
  • 21
    • 0031810562 scopus 로고    scopus 로고
    • Biology of moderately halophilic aerobic bacteria
    • 1:CAS:528:DyaK1cXkt1Oitb0%3D 9618450
    • Ventosa, A., Nieto, J. J., and Oren, A. (1998) Biology of moderately halophilic aerobic bacteria, Microbiol. Mol. Biol. Rev., 62, 504-544.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 504-544
    • Ventosa, A.1    Nieto, J.J.2    Oren, A.3
  • 22
    • 0032819747 scopus 로고    scopus 로고
    • The inorganic ion content of native aquatic bacteria
    • 10420582
    • Fagerbakke, K. M., Norland, S., and Heldal, M. (1999) The inorganic ion content of native aquatic bacteria, Can. J. Microbiol., 45, 304-311.
    • (1999) Can. J. Microbiol. , vol.45 , pp. 304-311
    • Fagerbakke, K.M.1    Norland, S.2    Heldal, M.3
  • 23
    • 10644230266 scopus 로고    scopus 로고
    • A genomic timescale of prokaryote evolution: Insights into the origin of methanogenesis, phototrophy, and the colonization of land
    • 15535883
    • Battistuzzi, F. U., Feijao, A., and Hedges, S. B. (2004) A genomic timescale of prokaryote evolution: insights into the origin of methanogenesis, phototrophy, and the colonization of land, BMC Evol. Biol., 4, 44.
    • (2004) BMC Evol. Biol. , vol.4 , pp. 44
    • Battistuzzi, F.U.1    Feijao, A.2    Hedges, S.B.3
  • 24
    • 0020490391 scopus 로고
    • Hydrolysis of GTP by elongation factor Tu can be induced by monovalent cations in the absence of other effectors
    • 7037779
    • Fasano, O., De Vendittis, E., and Parmeggiani, A. (1982) Hydrolysis of GTP by elongation factor Tu can be induced by monovalent cations in the absence of other effectors, J. Biol. Chem., 257, 3145-3150.
    • (1982) J. Biol. Chem. , vol.257 , pp. 3145-3150
    • Fasano, O.1    De Vendittis, E.2    Parmeggiani, A.3
  • 25
    • 12844272179 scopus 로고    scopus 로고
    • Crystal structure of an ATPase-active form of Rad51 homolog from Methanococcus voltae. Insights into potassium dependence
    • 15537659
    • Wu, Y., Qian, X., He, Y., Moya, I. A., and Luo, Y. (2005) Crystal structure of an ATPase-active form of Rad51 homolog from Methanococcus voltae. Insights into potassium dependence, J. Biol. Chem., 280, 722-728.
    • (2005) J. Biol. Chem. , vol.280 , pp. 722-728
    • Wu, Y.1    Qian, X.2    He, Y.3    Moya, I.A.4    Luo, Y.5
  • 27
    • 0017654538 scopus 로고
    • Immunochemical evidence for the difference between coenzyme-B12-dependent diol dehydratase and glycerol dehydratase
    • 407082
    • Toraya, T., and Fukui, S. (1977) Immunochemical evidence for the difference between coenzyme-B12-dependent diol dehydratase and glycerol dehydratase, Eur. J. Biochem., 76, 285-289.
    • (1977) Eur. J. Biochem. , vol.76 , pp. 285-289
    • Toraya, T.1    Fukui, S.2
  • 28
    • 0031574153 scopus 로고    scopus 로고
    • The monovalent cation requirement of rabbit muscle pyruvate kinase is eliminated by substitution of lysine for glutamate 117
    • 9434737
    • Laughlin, L. T., and Reed, G. H. (1997) The monovalent cation requirement of rabbit muscle pyruvate kinase is eliminated by substitution of lysine for glutamate 117, Arch. Biochem. Biophys., 348, 262-267.
    • (1997) Arch. Biochem. Biophys. , vol.348 , pp. 262-267
    • Laughlin, L.T.1    Reed, G.H.2
  • 29
    • 0029097637 scopus 로고
    • Investigation of monovalent cation activation of S-adenosylmethionine synthetase using mutagenesis and uranyl inhibition
    • 7629147
    • McQueney, M. S., and Markham, G. D. (1995) Investigation of monovalent cation activation of S-adenosylmethionine synthetase using mutagenesis and uranyl inhibition, J. Biol. Chem., 270, 18277-18284.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18277-18284
    • McQueney, M.S.1    Markham, G.D.2
  • 30
    • 0028885266 scopus 로고
    • Structural and mechanistic analysis of two refined crystal structures of the pyridoxal phosphate-dependent enzyme dialkylglycine decarboxylase
    • 7799433
    • Toney, M. D., Hohenester, E., Keller, J. W., and Jansonius, J. N. (1995) Structural and mechanistic analysis of two refined crystal structures of the pyridoxal phosphate-dependent enzyme dialkylglycine decarboxylase, J. Mol. Biol., 245, 151-179.
    • (1995) J. Mol. Biol. , vol.245 , pp. 151-179
    • Toney, M.D.1    Hohenester, E.2    Keller, J.W.3    Jansonius, J.N.4
  • 31
    • 0037147233 scopus 로고    scopus 로고
    • +-pyrophosphatase of Carboxydothermus hydrogenoformans
    • 12401795
    • +-pyrophosphatase of Carboxydothermus hydrogenoformans, J. Biol. Chem., 277, 49651-49654.
    • (2002) J. Biol. Chem. , vol.277 , pp. 49651-49654
    • Belogurov, G.A.1    Lahti, R.2
  • 32
    • 0014409989 scopus 로고
    • Biosynthesis of cytidine diphosphate-diglyceride by a particulate fraction from Micrococcus cerificans
    • 5679981
    • McCaman, R. E., and Finnerty, W. R. (1968) Biosynthesis of cytidine diphosphate-diglyceride by a particulate fraction from Micrococcus cerificans, J. Biol. Chem., 243, 5074-5080.
    • (1968) J. Biol. Chem. , vol.243 , pp. 5074-5080
    • McCaman, R.E.1    Finnerty, W.R.2
  • 34
    • 0014945730 scopus 로고
    • Inactivation and reactivation of ribosomal subunits: The peptidyl transferase activity of the 50 S subunit of Escherihia coli
    • 4924204
    • Miskin, R., Zamir, A., and Elson, D. (1970) Inactivation and reactivation of ribosomal subunits: the peptidyl transferase activity of the 50 S subunit of Escherihia coli, J. Mol. Biol., 54, 355-378.
    • (1970) J. Mol. Biol. , vol.54 , pp. 355-378
    • Miskin, R.1    Zamir, A.2    Elson, D.3
  • 35
    • 33846887629 scopus 로고    scopus 로고
    • Alternative roles for metal ions in enzyme catalysis and the implications for ribozyme chemistry
    • 17212472
    • Sigel, R. K. O., and Pyle, A. M. (2007) Alternative roles for metal ions in enzyme catalysis and the implications for ribozyme chemistry, Chem. Rev., 107, 97-113.
    • (2007) Chem. Rev. , vol.107 , pp. 97-113
    • Sigel, R.K.O.1    Pyle, A.M.2
  • 36
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 - Resolution
    • 10937989
    • Ban, N., Nissen, P., Hansen, J., Moore, P. B., and Steitz, T. A. (2000) The complete atomic structure of the large ribosomal subunit at 2.4 - resolution, Science, 289, 905-920.
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 37
    • 4344569647 scopus 로고    scopus 로고
    • The contribution of metal ions to the structural stability of the large ribosomal subunit
    • 1:CAS:528:DC%2BD2cXnsVejsb0%3D 15317974
    • Klein, D. J., Moore, P. B., and Steitz, T. A. (2004) The contribution of metal ions to the structural stability of the large ribosomal subunit, RNA, 10, 1366-1379.
    • (2004) RNA , vol.10 , pp. 1366-1379
    • Klein, D.J.1    Moore, P.B.2    Steitz, T.A.3
  • 38
    • 60549112849 scopus 로고    scopus 로고
    • A hierarchical model for evolution of 23S ribosomal RNA
    • 19225518
    • Bokov, K., and Steinberg, S. V. (2009) A hierarchical model for evolution of 23S ribosomal RNA, Nature, 457, 977-980.
    • (2009) Nature , vol.457 , pp. 977-980
    • Bokov, K.1    Steinberg, S.V.2
  • 39
    • 70349988824 scopus 로고    scopus 로고
    • The evolving ribosome: From non-coded peptide bond formation to sophisticated translation machinery
    • 19619641
    • Davidovich, C., Belousoff, M., Bashan, A., and Yonath, A. (2009) The evolving ribosome: from non-coded peptide bond formation to sophisticated translation machinery, Res. Microbiol., 160, 487-492.
    • (2009) Res. Microbiol. , vol.160 , pp. 487-492
    • Davidovich, C.1    Belousoff, M.2    Bashan, A.3    Yonath, A.4
  • 40
    • 84856392922 scopus 로고    scopus 로고
    • An exit cavity was crucial to the polymerase activity of the early ribosome
    • 1:CAS:528:DC%2BC38XhtV2ksbo%3D 22191510
    • Fox, G. E., Tran, Q., and Yonath, A. (2012) An exit cavity was crucial to the polymerase activity of the early ribosome, Astrobiology, 12, 57-60.
    • (2012) Astrobiology , vol.12 , pp. 57-60
    • Fox, G.E.1    Tran, Q.2    Yonath, A.3
  • 41
    • 1542272747 scopus 로고    scopus 로고
    • Comparative genomics, minimal gene-sets and the last universal common ancestor
    • 15035042
    • Koonin, E. V. (2003) Comparative genomics, minimal gene-sets and the last universal common ancestor, Nat. Rev. Microbiol., 1, 127-136.
    • (2003) Nat. Rev. Microbiol. , vol.1 , pp. 127-136
    • Koonin, E.V.1
  • 42
    • 0034571148 scopus 로고    scopus 로고
    • How many genes can make a cell: The minimal-gene-set concept
    • Koonin, E. V. (2000) How many genes can make a cell: the minimal-gene-set concept, Annu. Rev. Genom. Hum. Genet., 1, 99-116.
    • (2000) Annu. Rev. Genom. Hum. Genet. , vol.1 , pp. 99-116
    • Koonin, E.V.1
  • 43
    • 10944248427 scopus 로고    scopus 로고
    • Computing prokaryotic gene ubiquity: Rescuing the core from extinction
    • 1:CAS:528:DC%2BD2cXhtVyiurzM 15574825
    • Charlebois, R. L., and Doolittle, W. F. (2004) Computing prokaryotic gene ubiquity: rescuing the core from extinction, Genome Res., 14, 2469-2477.
    • (2004) Genome Res. , vol.14 , pp. 2469-2477
    • Charlebois, R.L.1    Doolittle, W.F.2
  • 44
    • 24044503087 scopus 로고    scopus 로고
    • Protein content of minimal and ancestral ribosome
    • 1:CAS:528:DC%2BD2MXpvVKgs7w%3D 16043494
    • Mushegian, A. (2005) Protein content of minimal and ancestral ribosome, RNA, 11, 1400-1406.
    • (2005) RNA , vol.11 , pp. 1400-1406
    • Mushegian, A.1
  • 45
    • 71049128162 scopus 로고    scopus 로고
    • On the origin of life in the zinc world. 2. Validation of the hypothesis on the photosynthesizing zinc sulfide edifices as cradles of life on Earth
    • 19703275
    • Mulkidjanian, A. Y., and Galperin, M. Y. (2009) On the origin of life in the zinc world. 2. Validation of the hypothesis on the photosynthesizing zinc sulfide edifices as cradles of life on Earth, Biol. Direct., 4, 27.
    • (2009) Biol. Direct. , vol.4 , pp. 27
    • Mulkidjanian, A.Y.1    Galperin, M.Y.2
  • 46
    • 77957661775 scopus 로고    scopus 로고
    • On the abundance of zinc in the evolutionarily old protein domains
    • 1:CAS:528:DC%2BC3cXhtFOrurnP 20693418
    • Mulkidjanian, A. Y., and Galperin, M. Y. (2010) On the abundance of zinc in the evolutionarily old protein domains, Proc. Natl. Acad. Sci. USA, 107, E137.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 137
    • Mulkidjanian, A.Y.1    Galperin, M.Y.2
  • 47
    • 77956326447 scopus 로고    scopus 로고
    • Deciphering the catalytic machinery in 30S ribosome assembly GTPase YqeH
    • 20376346
    • Anand, B., Surana, P., and Prakash, B. (2010) Deciphering the catalytic machinery in 30S ribosome assembly GTPase YqeH, PLoS One, 5, e9944.
    • (2010) PLoS One , vol.5 , pp. 9944
    • Anand, B.1    Surana, P.2    Prakash, B.3
  • 48
    • 33745520400 scopus 로고    scopus 로고
    • Dimerisation-dependent GTPase reaction of MnmE: How potassium acts as GTPase-activating element
    • 1:CAS:528:DC%2BD28XlvFKhsLY%3D 16763562
    • Scrima, A., and Wittinghofer, A. (2006) Dimerisation-dependent GTPase reaction of MnmE: how potassium acts as GTPase-activating element, EMBO J., 25, 2940-2951.
    • (2006) EMBO J. , vol.25 , pp. 2940-2951
    • Scrima, A.1    Wittinghofer, A.2
  • 49
    • 0034461401 scopus 로고    scopus 로고
    • Characterization of GTPase activity of TrmE, a member of a novel GTPase superfamily, from Thermotoga maritima
    • 1:CAS:528:DC%2BD3MXitVClsrs%3D 11092873
    • Yamanaka, K., Hwang, J., and Inouye, M. (2000) Characterization of GTPase activity of TrmE, a member of a novel GTPase superfamily, from Thermotoga maritima, J. Bacteriol., 182, 7078-7082.
    • (2000) J. Bacteriol. , vol.182 , pp. 7078-7082
    • Yamanaka, K.1    Hwang, J.2    Inouye, M.3
  • 50
    • 77951980333 scopus 로고    scopus 로고
    • Potassium-activated GTPase reaction in the G protein-coupled ferrous iron transporter B
    • 1:CAS:528:DC%2BC3cXlsVOhsL8%3D 20220129
    • Ash, M. R., Guilfoyle, A., Clarke, R. J., Guss, J. M., Maher, M. J., and Jormakka, M. (2010) Potassium-activated GTPase reaction in the G protein-coupled ferrous iron transporter B, J. Biol. Chem., 285, 14594-14602.
    • (2010) J. Biol. Chem. , vol.285 , pp. 14594-14602
    • Ash, M.R.1    Guilfoyle, A.2    Clarke, R.J.3    Guss, J.M.4    Maher, M.J.5    Jormakka, M.6
  • 51
    • 84867285085 scopus 로고    scopus 로고
    • Potassium acts as a GTPase-activating element on each nucleotide-binding domain of the essential Bacillus subtilis EngA
    • 1:CAS:528:DC%2BC38XhsFCktb%2FP 23056455
    • Foucher, A. E., Reiser, J. B., Ebel, C., Housset, D., and Jault, J. M. (2012) Potassium acts as a GTPase-activating element on each nucleotide-binding domain of the essential Bacillus subtilis EngA, PLoS One, 7, e46795.
    • (2012) PLoS One , vol.7 , pp. 46795
    • Foucher, A.E.1    Reiser, J.B.2    Ebel, C.3    Housset, D.4    Jault, J.M.5
  • 52
    • 0036295212 scopus 로고    scopus 로고
    • Classification and evolution of P-loop GTPases and related ATPases
    • 11916378
    • Leipe, D. D., Wolf, Y. I., Koonin, E. V., and Aravind, L. (2002) Classification and evolution of P-loop GTPases and related ATPases, J. Mol. Biol., 317, 41-72.
    • (2002) J. Mol. Biol. , vol.317 , pp. 41-72
    • Leipe, D.D.1    Wolf, Y.I.2    Koonin, E.V.3    Aravind, L.4
  • 53
    • 84891136247 scopus 로고    scopus 로고
    • Bacterial Obg proteins: GTPases at the nexus of protein and DNA synthesis
    • 23537324
    • Kint, C., Verstraeten, N., Hofkens, J., Fauvart, M., and Michiels, J. (2014) Bacterial Obg proteins: GTPases at the nexus of protein and DNA synthesis, Crit. Rev. Microbiol., 40, 207-224.
    • (2014) Crit. Rev. Microbiol. , vol.40 , pp. 207-224
    • Kint, C.1    Verstraeten, N.2    Hofkens, J.3    Fauvart, M.4    Michiels, J.5
  • 54
    • 0142011067 scopus 로고    scopus 로고
    • Evolution and classification of P-loop kinases and related proteins
    • 14568537
    • Leipe, D. D., Koonin, E. V., and Aravind, L. (2003) Evolution and classification of P-loop kinases and related proteins, J. Mol. Biol., 333, 781-815.
    • (2003) J. Mol. Biol. , vol.333 , pp. 781-815
    • Leipe, D.D.1    Koonin, E.V.2    Aravind, L.3
  • 55
    • 66249114010 scopus 로고    scopus 로고
    • Conservation of a conformational switch in RadA recombinase from Methanococcus maripaludis
    • 1:CAS:528:DC%2BD1MXmsVGjsbs%3D 19465774
    • Li, Y., He, Y., and Luo, Y. (2009) Conservation of a conformational switch in RadA recombinase from Methanococcus maripaludis, Acta Crystallogr. D Biol. Crystallogr., 65, 602-610.
    • (2009) Acta Crystallogr. D Biol. Crystallogr. , vol.65 , pp. 602-610
    • Li, Y.1    He, Y.2    Luo, Y.3
  • 56
    • 44349162159 scopus 로고    scopus 로고
    • Mechanism of homologous recombination from the RecA-ssDNA/dsDNA structures
    • 18497818
    • Chen, Z., Yang, H., and Pavletich, N. P. (2008) Mechanism of homologous recombination from the RecA-ssDNA/dsDNA structures, Nature, 453, 489-484.
    • (2008) Nature , vol.453 , pp. 489-484
    • Chen, Z.1    Yang, H.2    Pavletich, N.P.3
  • 57
    • 59749105974 scopus 로고    scopus 로고
    • RecA family proteins in archaea: RadA and its cousins
    • 19143611
    • Haldenby, S., White, M. F., and Allers, T. (2009) RecA family proteins in archaea: RadA and its cousins, Biochem. Soc. Trans., 37, 102-107.
    • (2009) Biochem. Soc. Trans. , vol.37 , pp. 102-107
    • Haldenby, S.1    White, M.F.2    Allers, T.3
  • 58
    • 0032942273 scopus 로고    scopus 로고
    • Diversity of radA genes from cultured and uncultured archaea: Comparative analysis of putative RadA proteins and their use as a phylogenetic marker
    • 1:CAS:528:DyaK1MXhtVGju7c%3D 9922255
    • Sandler, S. J., Hugenholtz, P., Schleper, C., DeLong, E. F., Pace, N. R., and Clark, A. J. (1999) Diversity of radA genes from cultured and uncultured archaea: comparative analysis of putative RadA proteins and their use as a phylogenetic marker, J. Bacteriol., 181, 907-915.
    • (1999) J. Bacteriol. , vol.181 , pp. 907-915
    • Sandler, S.J.1    Hugenholtz, P.2    Schleper, C.3    Delong, E.F.4    Pace, N.R.5    Clark, A.J.6
  • 59
    • 33745874687 scopus 로고    scopus 로고
    • Origins and evolution of the recA/RAD51 gene family: Evidence for ancient gene duplication and endosymbiotic gene transfer
    • 1:CAS:528:DC%2BD28XntlOisb0%3D 16798872
    • Lin, Z., Kong, H., Nei, M., and Ma, H. (2006) Origins and evolution of the recA/RAD51 gene family: evidence for ancient gene duplication and endosymbiotic gene transfer, Proc. Natl. Acad. Sci. USA, 103, 10328-10333.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 10328-10333
    • Lin, Z.1    Kong, H.2    Nei, M.3    Ma, H.4
  • 61
    • 72849154716 scopus 로고
    • The stimulation of transphosphorylation by alkali-metal ions
    • 1:CAS:528:DyaF3cXht12ns78%3D 14418551
    • Lowenstein, J. M. (1960) The stimulation of transphosphorylation by alkali-metal ions, Biochem. J., 75, 269-274.
    • (1960) Biochem. J. , vol.75 , pp. 269-274
    • Lowenstein, J.M.1
  • 62
    • 0038642763 scopus 로고    scopus 로고
    • Nested cooperativity and salt dependence of the ATPase activity of the archaeal chaperonin Mm-cpn
    • 12860414
    • Kusmierczyk, A. R., and Martin, J. (2003) Nested cooperativity and salt dependence of the ATPase activity of the archaeal chaperonin Mm-cpn, FEBS Lett., 547, 201-204.
    • (2003) FEBS Lett. , vol.547 , pp. 201-204
    • Kusmierczyk, A.R.1    Martin, J.2
  • 63
    • 84864280580 scopus 로고    scopus 로고
    • The cation-dependent G-proteins: In a class of their own
    • 22750478
    • Ash, M. R., Maher, M. J., Mitchell Guss, J., and Jormakka, M. (2012) The cation-dependent G-proteins: in a class of their own, FEBS Lett., 586, 2218-2224.
    • (2012) FEBS Lett. , vol.586 , pp. 2218-2224
    • Ash, M.R.1    Maher, M.J.2    Mitchell Guss, J.3    Jormakka, M.4
  • 66
  • 67
    • 0030741176 scopus 로고    scopus 로고
    • The first living systems: A bioenergetic perspective
    • 1:CAS:528:DyaK2sXktFGqtb4%3D 9184012
    • Deamer, D. W. (1997) The first living systems: a bioenergetic perspective, Microbiol. Mol. Biol. Rev., 61, 239-261.
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 239-261
    • Deamer, D.W.1
  • 68
    • 46449087871 scopus 로고    scopus 로고
    • Origins of life: How leaky were primitive cells?
    • 18596792
    • Deamer, D. W. (2008) Origins of life: how leaky were primitive cells? Nature, 454, 37-38.
    • (2008) Nature , vol.454 , pp. 37-38
    • Deamer, D.W.1
  • 69
    • 0030045955 scopus 로고    scopus 로고
    • Permeation of protons, potassium ions, and small polar molecules through phospholipid bilayers as a function of membrane thickness
    • 1:CAS:528:DyaK28XjslGksQ%3D%3D 8770210
    • Paula, S., Volkov, A. G., Van Hoek, A. N., Haines, T. H., and Deamer, D. W. (1996) Permeation of protons, potassium ions, and small polar molecules through phospholipid bilayers as a function of membrane thickness, Biophys. J., 70, 339-348.
    • (1996) Biophys. J. , vol.70 , pp. 339-348
    • Paula, S.1    Volkov, A.G.2    Van Hoek, A.N.3    Haines, T.H.4    Deamer, D.W.5
  • 70
    • 1942532925 scopus 로고    scopus 로고
    • Origins and evolution of isoprenoid lipid biosynthesis in archaea
    • 15066037
    • Boucher, Y., Kamekura, M., and Doolittle, W. F. (2004) Origins and evolution of isoprenoid lipid biosynthesis in archaea, Mol. Microbiol., 52, 515-527.
    • (2004) Mol. Microbiol. , vol.52 , pp. 515-527
    • Boucher, Y.1    Kamekura, M.2    Doolittle, W.F.3
  • 71
    • 4344618574 scopus 로고    scopus 로고
    • Ancestral lipid biosynthesis and early membrane evolution
    • 15337120
    • Pereto, J., Lopez-Garcia, P., and Moreira, D. (2004) Ancestral lipid biosynthesis and early membrane evolution, Trends Biochem. Sci., 29, 469-477.
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 469-477
    • Pereto, J.1    Lopez-Garcia, P.2    Moreira, D.3
  • 72
    • 27744591844 scopus 로고    scopus 로고
    • On the origin of genomes and cells within inorganic compartments
    • 16223546
    • Koonin, E. V., and Martin, W. (2005) On the origin of genomes and cells within inorganic compartments, Trends Genet., 21, 647-654.
    • (2005) Trends Genet. , vol.21 , pp. 647-654
    • Koonin, E.V.1    Martin, W.2
  • 73
    • 33947425547 scopus 로고    scopus 로고
    • Biosynthesis of ether-type polar lipids in archaea and evolutionary considerations
    • 1:CAS:528:DC%2BD2sXksleqsb8%3D 17347520
    • Koga, Y., and Morii, H. (2007) Biosynthesis of ether-type polar lipids in archaea and evolutionary considerations, Microbiol. Mol. Biol. Rev., 71, 97-120.
    • (2007) Microbiol. Mol. Biol. Rev. , vol.71 , pp. 97-120
    • Koga, Y.1    Morii, H.2
  • 74
    • 84898058598 scopus 로고    scopus 로고
    • Phylogenomic reconstruction of archaeal fatty acid metabolism
    • 1:CAS:528:DC%2BC2cXlsF2jsbs%3D 24818264
    • Dibrova, D. V., Galperin, M. Y., and Mulkidjanian, A. Y. (2014) Phylogenomic reconstruction of archaeal fatty acid metabolism, Environ. Microbiol., 16, 907-918.
    • (2014) Environ. Microbiol. , vol.16 , pp. 907-918
    • Dibrova, D.V.1    Galperin, M.Y.2    Mulkidjanian, A.Y.3
  • 75
    • 0033793828 scopus 로고    scopus 로고
    • Biosynthesis of isoprenoids via mevalonate in Archaea: The lost pathway
    • 11042147
    • Smit, A., and Mushegian, A. (2000) Biosynthesis of isoprenoids via mevalonate in Archaea: the lost pathway, Genome Res., 10, 1468-1484.
    • (2000) Genome Res. , vol.10 , pp. 1468-1484
    • Smit, A.1    Mushegian, A.2
  • 76
    • 0028505013 scopus 로고
    • The terpenoid theory of the origin of cellular life: The evolution of terpenoids to cholesterol
    • 9383366
    • Ourisson, G., and Nakatani, Y. (1994) The terpenoid theory of the origin of cellular life: the evolution of terpenoids to cholesterol, Chem. Biol., 1, 11-23.
    • (1994) Chem. Biol. , vol.1 , pp. 11-23
    • Ourisson, G.1    Nakatani, Y.2
  • 77
    • 34250626837 scopus 로고    scopus 로고
    • Possible molecular evolution of biomembranes: From single-chain to doublechain lipids
    • 17510999
    • Gotoh, M., Sugawara, A., Akiyoshi, K., Matsumoto, I., Ourisson, G., and Nakatani, Y. (2007) Possible molecular evolution of biomembranes: from single-chain to doublechain lipids, Chem. Biodivers., 4, 837-848.
    • (2007) Chem. Biodivers. , vol.4 , pp. 837-848
    • Gotoh, M.1    Sugawara, A.2    Akiyoshi, K.3    Matsumoto, I.4    Ourisson, G.5    Nakatani, Y.6
  • 81
    • 2542533863 scopus 로고    scopus 로고
    • Membrane growth can generate a transmembrane pH gradient in fatty acid vesicles
    • 1:CAS:528:DC%2BD2cXkslCisL0%3D 15148394
    • Chen, I. A., and Szostak, J. W. (2004) Membrane growth can generate a transmembrane pH gradient in fatty acid vesicles, Proc. Natl. Acad. Sci. USA, 101, 7965-7970.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 7965-7970
    • Chen, I.A.1    Szostak, J.W.2
  • 82
    • 78349257478 scopus 로고    scopus 로고
    • Membrane transport in primitive cells
    • 20679338
    • Mansy, S. S. (2010) Membrane transport in primitive cells, Cold Spring Harb. Perspect. Biol., 2, a002188.
    • (2010) Cold Spring Harb. Perspect. Biol. , vol.2 , pp. 002188
    • Mansy, S.S.1
  • 84
    • 46449105488 scopus 로고    scopus 로고
    • Template-directed synthesis of a genetic polymer in a model protocell
    • 1:CAS:528:DC%2BD1cXotVertLw%3D 18528332
    • Mansy, S. S., Schrum, J. P., Krishnamurthy, M., Tobe, S., Treco, D. A., and Szostak, J. W. (2008) Template-directed synthesis of a genetic polymer in a model protocell, Nature, 454, 122-125.
    • (2008) Nature , vol.454 , pp. 122-125
    • Mansy, S.S.1    Schrum, J.P.2    Krishnamurthy, M.3    Tobe, S.4    Treco, D.A.5    Szostak, J.W.6
  • 86
    • 43049130286 scopus 로고    scopus 로고
    • (Gargaud, M., Barbier, B., Martin, H., and Reisse, J., eds.) Springer-Verlag, Berlin
    • Pinti, D. L. (2005) in Lectures in Astrobiology (Gargaud, M., Barbier, B., Martin, H., and Reisse, J., eds.) Springer-Verlag, Berlin, pp. 83-111.
    • (2005) Lectures in Astrobiology , pp. 83-111
    • Pinti, D.L.1
  • 87
    • 10844271350 scopus 로고    scopus 로고
    • Biological control of Cl/Br and low sulfate concentration in a 3.5-Gyr-old seawater from North Pole, Western Australia
    • Foriel, J., Philippot, P., Rey, P., Somogyi, A., Banks, D., and Menez, B. (2004) Biological control of Cl/Br and low sulfate concentration in a 3.5-Gyr-old seawater from North Pole, Western Australia, Earth Planet. Sci. Lett., 228, 451-463.
    • (2004) Earth Planet. Sci. Lett. , vol.228 , pp. 451-463
    • Foriel, J.1    Philippot, P.2    Rey, P.3    Somogyi, A.4    Banks, D.5    Menez, B.6
  • 89
    • 0002552344 scopus 로고
    • Vapor-dominated hydrothermal systems compared with hot-water systems
    • White, D. E., Muffler, L. J. P., and Truesdell, A. N. (1971) Vapor-dominated hydrothermal systems compared with hot-water systems, Econ. Geol., 66, 75-97.
    • (1971) Econ. Geol. , vol.66 , pp. 75-97
    • White, D.E.1    Muffler, L.J.P.2    Truesdell, A.N.3
  • 91
  • 93
    • 84874108017 scopus 로고    scopus 로고
    • The naked planet Earth: Most essential pre-requisite for the origin and evolution of life
    • Maruyama, S., Ikoma, M., Genda, H., Hirose, K., Yokoyama, T., and Santosh, M. (2013) The naked planet Earth: most essential pre-requisite for the origin and evolution of life, Geosci. Front., 4, 141-165.
    • (2013) Geosci. Front. , vol.4 , pp. 141-165
    • Maruyama, S.1    Ikoma, M.2    Genda, H.3    Hirose, K.4    Yokoyama, T.5    Santosh, M.6
  • 94
    • 84870758075 scopus 로고    scopus 로고
    • Chemical composition of the primary aqueous phase of the Earth and origin of life
    • Galimov, E. M., Natochin, Yu. V., Ryzhenko, B. N., and Cherkasova, E. V. (2012) Chemical composition of the primary aqueous phase of the Earth and origin of life, Geochem. Int., 50, 1048-1068.
    • (2012) Geochem. Int. , vol.50 , pp. 1048-1068
    • Galimov, E.M.1    Natochin, Y.V.2    Ryzhenko, B.N.3    Cherkasova, E.V.4
  • 95
    • 84862698762 scopus 로고    scopus 로고
    • Hf isotope evidence from Archean granitic rocks for deep-mantle origin of continental crust
    • Guitreau, M., Blichert-Toft, J., Martin, H., Mojzsis, S. J., and Albarede, F. (2012) Hf isotope evidence from Archean granitic rocks for deep-mantle origin of continental crust, Earth Planet. Sci. Lett., 337/338, 211-223.
    • (2012) Earth Planet. Sci. Lett. , vol.337-338 , pp. 211-223
    • Guitreau, M.1    Blichert-Toft, J.2    Martin, H.3    Mojzsis, S.J.4    Albarede, F.5
  • 97
    • 84868677049 scopus 로고    scopus 로고
    • Asphalt, water, and the prebiotic synthesis of ribose, ribonucleosides, and RNA
    • 22455515
    • Benner, S. A., Kim, H. J., and Carrigan, M. A. (2012) Asphalt, water, and the prebiotic synthesis of ribose, ribonucleosides, and RNA, Acc. Chem. Res., 45, 2025-2034.
    • (2012) Acc. Chem. Res. , vol.45 , pp. 2025-2034
    • Benner, S.A.1    Kim, H.J.2    Carrigan, M.A.3
  • 98
    • 38149118222 scopus 로고    scopus 로고
    • The physiological evolution of animals: Sodium is the clue to resolving contradictions
    • Natochin, Y. V. (2007) The physiological evolution of animals: sodium is the clue to resolving contradictions, Herald Russ. Acad Sci., 77, 581-591.
    • (2007) Herald Russ. Acad Sci. , vol.77 , pp. 581-591
    • Natochin, Y.V.1
  • 99
    • 0019335466 scopus 로고
    • A new sodium-transport system energized by the decarboxylation of oxaloacetate
    • 7009209
    • Dimroth, P. (1980) A new sodium-transport system energized by the decarboxylation of oxaloacetate, FEBS Lett., 122, 234-236.
    • (1980) FEBS Lett. , vol.122 , pp. 234-236
    • Dimroth, P.1
  • 100
    • 0020427791 scopus 로고
    • + pump in the marine bacterium Vibrio alginolyticus
    • 7107593
    • + pump in the marine bacterium Vibrio alginolyticus, J. Biol. Chem., 257, 10007-10014.
    • (1982) J. Biol. Chem. , vol.257 , pp. 10007-10014
    • Tokuda, H.1    Unemoto, T.2
  • 102
  • 103
    • 84899913081 scopus 로고    scopus 로고
    • Adaptations of anaerobic archaea to life under extreme energy limitation
    • 24118021
    • Mayer, F., and Muller, V. (2014) Adaptations of anaerobic archaea to life under extreme energy limitation, FEMS Microbiol. Rev., 38, 449-472.
    • (2014) FEMS Microbiol. Rev. , vol.38 , pp. 449-472
    • Mayer, F.1    Muller, V.2
  • 104
    • 84888116310 scopus 로고    scopus 로고
    • + transport in gram-positive bacteria defect in the Mrp antiporter complex measured with 23Na nuclear magnetic resonance
    • 24139955
    • + transport in gram-positive bacteria defect in the Mrp antiporter complex measured with 23Na nuclear magnetic resonance, Anal. Biochem., 445, 80-86.
    • (2014) Anal. Biochem. , vol.445 , pp. 80-86
    • Gorecki, K.1    Hagerhall, C.2    Drakenberg, T.3
  • 105
    • 84885365932 scopus 로고    scopus 로고
    • Functional role of the MrpA- and MrpD-homologous protein subunits in enzyme complexes evolutionary related to respiratory chain complex i
    • 24095649
    • Moparthi, V. K., Kumar, B., Al-Eryani, Y., Sperling, E., Gorecki, K., Drakenberg, T., and Hagerhall, C. (2014) Functional role of the MrpA- and MrpD-homologous protein subunits in enzyme complexes evolutionary related to respiratory chain complex I, Biochim. Biophys. Acta, 1837, 178-185.
    • (2014) Biochim. Biophys. Acta , vol.1837 , pp. 178-185
    • Moparthi, V.K.1    Kumar, B.2    Al-Eryani, Y.3    Sperling, E.4    Gorecki, K.5    Drakenberg, T.6    Hagerhall, C.7
  • 106
    • 84905659301 scopus 로고    scopus 로고
    • Energy conservation by oxidation of formate to carbon dioxide and hydrogen via a sodium ion current in a hyperthermophilic archaeon
    • 1:CAS:528:DC%2BC2cXhtFyqtLvO 25049407
    • Lim, J. K., Mayer, F., Kang, S. G., and Muller, V. (2014) Energy conservation by oxidation of formate to carbon dioxide and hydrogen via a sodium ion current in a hyperthermophilic archaeon, Proc. Natl. Acad. Sci. USA, 111, 11497-11502.
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 11497-11502
    • Lim, J.K.1    Mayer, F.2    Kang, S.G.3    Muller, V.4
  • 109
    • 0038053885 scopus 로고    scopus 로고
    • ATP synthesis driven by proton transport in F1F0-ATP synthase
    • 12788493
    • Weber, J., and Senior, A. E. (2003) ATP synthesis driven by proton transport in F1F0-ATP synthase, FEBS Lett., 545, 61-70.
    • (2003) FEBS Lett. , vol.545 , pp. 61-70
    • Weber, J.1    Senior, A.E.2
  • 110
    • 35348829149 scopus 로고    scopus 로고
    • Inventing the dynamo machine: The evolution of the F-type and V-type ATPases
    • 17938630
    • Mulkidjanian, A. Y., Makarova, K. S., Galperin, M. Y., and Koonin, E. V. (2007) Inventing the dynamo machine: the evolution of the F-type and V-type ATPases, Nat. Rev. Microbiol., 5, 892-899.
    • (2007) Nat. Rev. Microbiol. , vol.5 , pp. 892-899
    • Mulkidjanian, A.Y.1    Makarova, K.S.2    Galperin, M.Y.3    Koonin, E.V.4
  • 111
    • 0031008228 scopus 로고    scopus 로고
    • The ATP synthase - A splendid molecular machine
    • 9242922
    • Boyer, P. D. (1997) The ATP synthase - a splendid molecular machine, Annu. Rev. Biochem., 66, 717-749.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 717-749
    • Boyer, P.D.1
  • 112
    • 78649327875 scopus 로고    scopus 로고
    • Microscopic rotary mechanism of ion translocation in the Fo complex of ATP synthases
    • 20972431
    • Pogoryelov, D., Krah, A., Langer, J. D., Yildiz, O., Faraldo-Gomez, J. D., and Meier, T. (2010) Microscopic rotary mechanism of ion translocation in the Fo complex of ATP synthases, Nat. Chem. Biol., 6, 891-899.
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 891-899
    • Pogoryelov, D.1    Krah, A.2    Langer, J.D.3    Yildiz, O.4    Faraldo-Gomez, J.D.5    Meier, T.6
  • 113
    • 84874456850 scopus 로고    scopus 로고
    • Rotating proton pumping ATPases: Subunit/subunit interactions and thermodynamics
    • 23441040
    • Nakanishi-Matsui, M., Sekiya, M., and Futai, M. (2013) Rotating proton pumping ATPases: subunit/subunit interactions and thermodynamics, IUBMB Life, 65, 247-254.
    • (2013) IUBMB Life , vol.65 , pp. 247-254
    • Nakanishi-Matsui, M.1    Sekiya, M.2    Futai, M.3
  • 114
    • 84873120174 scopus 로고    scopus 로고
    • The ATP synthase: The understood, the uncertain and the unknown
    • 23356252
    • Walker, J. E. (2013) The ATP synthase: the understood, the uncertain and the unknown, Biochem. Soc. Trans., 41, 1-16.
    • (2013) Biochem. Soc. Trans. , vol.41 , pp. 1-16
    • Walker, J.E.1
  • 115
    • 77954202864 scopus 로고    scopus 로고
    • +-translocating form of the bacterial F-type membrane ATPase
    • 1:CAS:528:DC%2BC3cXnsVOltL4%3D 20472544
    • +-translocating form of the bacterial F-type membrane ATPase, Bioinformatics, 26, 1473-1476.
    • (2010) Bioinformatics , vol.26 , pp. 1473-1476
    • Dibrova, D.V.1    Galperin, M.Y.2    Mulkidjanian, A.Y.3
  • 116
    • 0037955289 scopus 로고    scopus 로고
    • ATP synthases: Structure, function and evolution of unique energy converters
    • 12737308
    • Muller, V., and Gruber, G. (2003) ATP synthases: structure, function and evolution of unique energy converters, Cell Mol. Life Sci., 60, 474-494.
    • (2003) Cell Mol. Life Sci. , vol.60 , pp. 474-494
    • Muller, V.1    Gruber, G.2
  • 118
    • 35148861695 scopus 로고    scopus 로고
    • On the origin of biochemistry at an alkaline hydrothermal vent
    • 1:CAS:528:DC%2BD2sXht1eiu7fO 17255002
    • Martin, W., and Russell, M. J. (2007) On the origin of biochemistry at an alkaline hydrothermal vent, Philos. Trans. R. Soc. Lond. B Biol. Sci., 362, 1887-1925.
    • (2007) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.362 , pp. 1887-1925
    • Martin, W.1    Russell, M.J.2
  • 119
    • 84914680694 scopus 로고    scopus 로고
    • A bioenergetic basis for membrane divergence in archaea and bacteria
    • 25116890
    • Sojo, V., Pomiankowski, A., and Lane, N. (2014) A bioenergetic basis for membrane divergence in archaea and bacteria, PLoS Biol., 12, e1001926.
    • (2014) PLoS Biol. , vol.12 , pp. 1001926
    • Sojo, V.1    Pomiankowski, A.2    Lane, N.3
  • 120
    • 0021759406 scopus 로고
    • Non-ohmic proton conductance of mitochondria and liposomes
    • 6722116
    • Krishnamoorthy, G., and Hinkle, P. C. (1984) Non-ohmic proton conductance of mitochondria and liposomes, Biochemistry, 23, 1640-1645.
    • (1984) Biochemistry , vol.23 , pp. 1640-1645
    • Krishnamoorthy, G.1    Hinkle, P.C.2
  • 121
    • 68949149185 scopus 로고    scopus 로고
    • The temperature dependence of lipid membrane permeability, its quantized nature, and the influence of anesthetics
    • 1:CAS:528:DC%2BD1MXpsFOrt7k%3D 19486680
    • Blicher, A., Wodzinska, K., Fidorra, M., Winterhalter, M., and Heimburg, T. (2009) The temperature dependence of lipid membrane permeability, its quantized nature, and the influence of anesthetics, Biophys. J., 96, 4581-4591.
    • (2009) Biophys. J. , vol.96 , pp. 4581-4591
    • Blicher, A.1    Wodzinska, K.2    Fidorra, M.3    Winterhalter, M.4    Heimburg, T.5
  • 122
    • 0014674557 scopus 로고
    • Mechanism of coupling of oxidative phosphorylation and the membrane potential of mitochondria
    • 5787094
    • Liberman, E. A., Topaly, V. P., Tsofina, L. M., Jasaitis, A. A., and Skulachev, V. P. (1969) Mechanism of coupling of oxidative phosphorylation and the membrane potential of mitochondria, Nature, 222, 1076-1078.
    • (1969) Nature , vol.222 , pp. 1076-1078
    • Liberman, E.A.1    Topaly, V.P.2    Tsofina, L.M.3    Jasaitis, A.A.4    Skulachev, V.P.5
  • 123
    • 0014210510 scopus 로고
    • Proton conductors in the respiratory chain and artificial membranes
    • 6082493
    • Skulachev, V. P., Sharaf, A. A., and Liberman, E. A. (1967) Proton conductors in the respiratory chain and artificial membranes, Nature, 216, 718-719.
    • (1967) Nature , vol.216 , pp. 718-719
    • Skulachev, V.P.1    Sharaf, A.A.2    Liberman, E.A.3
  • 124
    • 0000848071 scopus 로고
    • Effect of surface active agents on the latent ATPase of mitochondria
    • 13363952
    • Lardy, H. A., and Pressman, B. C. (1956) Effect of surface active agents on the latent ATPase of mitochondria, Biochim. Biophys. Acta, 21, 458-466.
    • (1956) Biochim. Biophys. Acta , vol.21 , pp. 458-466
    • Lardy, H.A.1    Pressman, B.C.2
  • 126
    • 0025930608 scopus 로고
    • Fatty acid circuit as a physiological mechanism of uncoupling of oxidative phosphorylation
    • 1756853
    • Skulachev, V. P. (1991) Fatty acid circuit as a physiological mechanism of uncoupling of oxidative phosphorylation, FEBS Lett., 294, 158-162.
    • (1991) FEBS Lett. , vol.294 , pp. 158-162
    • Skulachev, V.P.1
  • 127
    • 27444434694 scopus 로고    scopus 로고
    • Lysolipid incorporation in dipalmitoylphosphatidylcholine bilayer membranes enhances the ion permeability and drug release rates at the membrane phase transition
    • 16216216
    • Mills, J. K., and Needham, D. (2005) Lysolipid incorporation in dipalmitoylphosphatidylcholine bilayer membranes enhances the ion permeability and drug release rates at the membrane phase transition, Biochim. Biophys. Acta, 1716, 77-96.
    • (2005) Biochim. Biophys. Acta , vol.1716 , pp. 77-96
    • Mills, J.K.1    Needham, D.2
  • 130
    • 78651464863 scopus 로고    scopus 로고
    • Energy sources, self-organization, and the origin of life
    • 20333546
    • Boiteau, L., and Pascal, R. (2011) Energy sources, self-organization, and the origin of life, Orig. Life Evol. Biosph., 41, 23-33.
    • (2011) Orig. Life Evol. Biosph. , vol.41 , pp. 23-33
    • Boiteau, L.1    Pascal, R.2
  • 131
    • 0017835741 scopus 로고
    • The proton pump is a molecular engine of motile bacteria
    • 24186
    • Glagolev, A. N., and Skulachev, V. P. (1978) The proton pump is a molecular engine of motile bacteria, Nature, 272, 280-282.
    • (1978) Nature , vol.272 , pp. 280-282
    • Glagolev, A.N.1    Skulachev, V.P.2
  • 132
    • 0027970177 scopus 로고
    • A mechanism of proton translocation by F1F0 ATP synthases suggested by double mutants of the a subunit
    • 7982950
    • Vik, S. B., and Antonio, B. J. (1994) A mechanism of proton translocation by F1F0 ATP synthases suggested by double mutants of the a subunit, J. Biol. Chem., 269, 30364-30369.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30364-30369
    • Vik, S.B.1    Antonio, B.J.2
  • 133
    • 0030863908 scopus 로고    scopus 로고
    • ATP synthase: A tentative structural model
    • 9323021
    • Engelbrecht, S., and Junge, W. (1997) ATP synthase: a tentative structural model, FEBS Lett., 414, 485-491.
    • (1997) FEBS Lett. , vol.414 , pp. 485-491
    • Engelbrecht, S.1    Junge, W.2
  • 134
    • 0032947857 scopus 로고    scopus 로고
    • Transient accumulation of elastic energy in proton translocating ATP synthase
    • 10225416
    • Cherepanov, D. A., Mulkidjanian, A. Y., and Junge, W. (1999) Transient accumulation of elastic energy in proton translocating ATP synthase, FEBS Lett., 449, 1-6.
    • (1999) FEBS Lett. , vol.449 , pp. 1-6
    • Cherepanov, D.A.1    Mulkidjanian, A.Y.2    Junge, W.3
  • 135
    • 0344279652 scopus 로고
    • Generation of an electrochemical proton gradient in Streptococcus cremoris by lactate efflux
    • 1:CAS:528:DyaL3cXmtlCkt7Y%3D 6254084
    • Otto, R., Sonnenberg, A. S., Veldkamp, H., and Konings, W. N. (1980) Generation of an electrochemical proton gradient in Streptococcus cremoris by lactate efflux, Proc. Natl. Acad. Sci. USA, 77, 5502-5506.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 5502-5506
    • Otto, R.1    Sonnenberg, A.S.2    Veldkamp, H.3    Konings, W.N.4
  • 136
    • 0025219626 scopus 로고
    • Generation of a membrane potential by sodium-dependent succinate efflux in Selenomonas ruminantium
    • 1:CAS:528:DyaK3cXhsFGjsro%3D 2307654
    • Michel, T. A., and Macy, J. M. (1990) Generation of a membrane potential by sodium-dependent succinate efflux in Selenomonas ruminantium, J. Bacteriol., 172, 1430-1435.
    • (1990) J. Bacteriol. , vol.172 , pp. 1430-1435
    • Michel, T.A.1    Macy, J.M.2
  • 137
    • 77950456083 scopus 로고    scopus 로고
    • How did LUCA make a living? Chemiosmosis in the origin of life
    • 20108228
    • Lane, N., Allen, J. F., and Martin, W. (2010) How did LUCA make a living? Chemiosmosis in the origin of life, Bioessays, 32, 271-280.
    • (2010) Bioessays , vol.32 , pp. 271-280
    • Lane, N.1    Allen, J.F.2    Martin, W.3
  • 138
    • 0017642503 scopus 로고
    • + across the plasma membrane is not obligatory for bacterial growth
    • 69317
    • + across the plasma membrane is not obligatory for bacterial growth, Science, 197, 372-373.
    • (1977) Science , vol.197 , pp. 372-373
    • Harold, F.M.1    Van Brunt, J.2
  • 139
    • 0031239472 scopus 로고    scopus 로고
    • + ATPase in mammalian astrocytes
    • 9298845
    • + ATPase in mammalian astrocytes, Glia, 21, 35-45.
    • (1997) Glia , vol.21 , pp. 35-45
    • Silver, I.A.1    Erecinska, M.2
  • 140
    • 0025278430 scopus 로고
    • Energy transduction in the bacterial flagellar motor. Effects of load and pH
    • 1:STN:280:DyaK3c3mt1ygsg%3D%3D 2160845
    • Khan, S., Dapice, M., and Humayun, I. (1990) Energy transduction in the bacterial flagellar motor. Effects of load and pH, Biophys. J., 57, 779-796.
    • (1990) Biophys. J. , vol.57 , pp. 779-796
    • Khan, S.1    Dapice, M.2    Humayun, I.3
  • 142
    • 34249879293 scopus 로고    scopus 로고
    • Cell shrinkage and monovalent cation fluxes: Role in apoptosis
    • 1:CAS:528:DC%2BD2sXmt1ygsr0%3D 17321483
    • Bortner, C. D., and Cidlowski, J. A. (2007) Cell shrinkage and monovalent cation fluxes: role in apoptosis, Arch. Biochem. Biophys., 462, 176-188.
    • (2007) Arch. Biochem. Biophys. , vol.462 , pp. 176-188
    • Bortner, C.D.1    Cidlowski, J.A.2
  • 143
    • 0030580287 scopus 로고    scopus 로고
    • Why are mitochondria involved in apoptosis? Permeability transition pores and apoptosis as selective mechanisms to eliminate superoxide-producing mitochondria and cell
    • 8941703
    • Skulachev, V. P. (1996) Why are mitochondria involved in apoptosis? Permeability transition pores and apoptosis as selective mechanisms to eliminate superoxide-producing mitochondria and cell, FEBS Lett., 397, 7-10.
    • (1996) FEBS Lett. , vol.397 , pp. 7-10
    • Skulachev, V.P.1
  • 145
    • 0031970010 scopus 로고    scopus 로고
    • The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold
    • 9584613
    • Aravind, L., Galperin, M. Y., and Koonin, E. V. (1998) The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold, Trends Biochem. Sci., 23, 127-129.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 127-129
    • Aravind, L.1    Galperin, M.Y.2    Koonin, E.V.3
  • 147
    • 13244255415 scopus 로고    scopus 로고
    • MUSCLE: A multiple sequence alignment method with reduced time and space complexity
    • 15318951
    • Edgar, R. C. (2004) MUSCLE: a multiple sequence alignment method with reduced time and space complexity, BMC Bioinformatics, 5, 113.
    • (2004) BMC Bioinformatics , vol.5 , pp. 113
    • Edgar, R.C.1
  • 148
    • 84941067064 scopus 로고    scopus 로고
    • Expanded microbial genome coverage and improved protein family annotation in the COG database
    • 25428365
    • Galperin, M. Y., Makarova, K. S., Wolf, Y. I., and Koonin, E. V. (2015) Expanded microbial genome coverage and improved protein family annotation in the COG database, Nucleic Acids Res., 43, D261-D269.
    • (2015) Nucleic Acids Res. , vol.43 , pp. 261-D269
    • Galperin, M.Y.1    Makarova, K.S.2    Wolf, Y.I.3    Koonin, E.V.4
  • 149
    • 2142738304 scopus 로고    scopus 로고
    • WebLogo: A sequence logo generator
    • 1:CAS:528:DC%2BD2cXkvFGht7Y%3D 15173120
    • Crooks, G. E., Hon, G., Chandonia, J. M., and Brenner, S. E. (2004) WebLogo: a sequence logo generator, Genome Res., 14, 1188-1190.
    • (2004) Genome Res. , vol.14 , pp. 1188-1190
    • Crooks, G.E.1    Hon, G.2    Chandonia, J.M.3    Brenner, S.E.4
  • 150
    • 78149302861 scopus 로고    scopus 로고
    • The mechanism for activation of GTP hydrolysis on the ribosome
    • 1:CAS:528:DC%2BC3cXhtlKht7vN 21051640
    • Voorhees, R. M., Schmeing, T. M., Kelley, A. C., and Ramakrishnan, V. (2010) The mechanism for activation of GTP hydrolysis on the ribosome, Science, 330, 835-838.
    • (2010) Science , vol.330 , pp. 835-838
    • Voorhees, R.M.1    Schmeing, T.M.2    Kelley, A.C.3    Ramakrishnan, V.4
  • 151
    • 77950806408 scopus 로고    scopus 로고
    • New algorithms and methods to estimate maximum-likelihood phylogenies: Assessing the performance of PhyML 3.0
    • 20525638
    • Guindon, S., Dufayard, J. F., Lefort, V., Anisimova, M., Hordijk, W., and Gascuel, O. (2010) New algorithms and methods to estimate maximum-likelihood phylogenies: assessing the performance of PhyML 3.0, Syst. Biol., 59, 307-321.
    • (2010) Syst. Biol. , vol.59 , pp. 307-321
    • Guindon, S.1    Dufayard, J.F.2    Lefort, V.3    Anisimova, M.4    Hordijk, W.5    Gascuel, O.6
  • 152
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: Molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • 1:CAS:528:DC%2BC3MXht1eiu73K 21546353
    • Tamura, K., Peterson, D., Peterson, N., Stecher, G., Nei, M., and Kumar, S. (2011) MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods, Mol. Biol. Evol., 28, 2731-2739.
    • (2011) Mol. Biol. Evol. , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6
  • 153
    • 0029666434 scopus 로고    scopus 로고
    • The structure of bovine F1-ATPase complexed with the antibiotic inhibitor aurovertin B
    • 8692918
    • Van Raaij, M. J., Abrahams, J. P., Leslie, A. G., and Walker, J. E. (1996) The structure of bovine F1-ATPase complexed with the antibiotic inhibitor aurovertin B, Proc. Natl. Acad. Sci. USA, 93, 6913-6917.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6913-6917
    • Van Raaij, M.J.1    Abrahams, J.P.2    Leslie, A.G.3    Walker, J.E.4
  • 154
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel, E., and Henrick, K. (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions, Acta Cryst., D60, 2256-2268.
    • (2004) Acta Cryst. , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 155
    • 84876522835 scopus 로고    scopus 로고
    • BRENDA in 2013: Integrated reactions, kinetic data, enzyme function data, improved disease classification: New options and contents in BRENDA
    • 1:CAS:528:DC%2BC38XhvV2ksb3O 23203881
    • Schomburg, I., Chang, A., Placzek, S., Sohngen, C., Rother, M., Lang, M., Munaretto, C., Ulas, S., Stelzer, M., Grote, A., et al. (2013) BRENDA in 2013: integrated reactions, kinetic data, enzyme function data, improved disease classification: new options and contents in BRENDA, Nucleic Acids Res., 41, D764-772.
    • (2013) Nucleic Acids Res. , vol.41 , pp. 764-772
    • Schomburg, I.1    Chang, A.2    Placzek, S.3    Sohngen, C.4    Rother, M.5    Lang, M.6    Munaretto, C.7    Ulas, S.8    Stelzer, M.9    Grote, A.10
  • 156
    • 0031016071 scopus 로고    scopus 로고
    • Primary sodium ion translocating enzymes
    • 9030254
    • Dimroth, P. (1997) Primary sodium ion translocating enzymes, Biochim. Biophys. Acta, 1318, 11-51.
    • (1997) Biochim. Biophys. Acta , vol.1318 , pp. 11-51
    • Dimroth, P.1
  • 157
    • 44449151647 scopus 로고    scopus 로고
    • ATP synthesis by decarboxylation phosphorylation
    • 18049805
    • Dimroth, P., and von Ballmoos, C. (2008) ATP synthesis by decarboxylation phosphorylation, Results Probl. Cell Differ., 45, 153-184.
    • (2008) Results Probl. Cell Differ. , vol.45 , pp. 153-184
    • Dimroth, P.1    Von Ballmoos, C.2
  • 159
    • 78149247216 scopus 로고    scopus 로고
    • +-translocating ferredoxin:NAD+ oxidoreductase
    • 1:CAS:528:DC%2BC3cXhtlCrs7nM 20921383
    • +-translocating ferredoxin:NAD+ oxidoreductase, Proc. Natl. Acad. Sci. USA, 107, 18138-18142.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 18138-18142
    • Biegel, E.1    Muller, V.2
  • 160
    • 0024293219 scopus 로고
    • Characterization of the ATP synthase of Propionigenium modestum as a primary sodium pump
    • 2905167
    • Laubinger, W., and Dimroth, P. (1988) Characterization of the ATP synthase of Propionigenium modestum as a primary sodium pump, Biochemistry, 27, 7531-7537.
    • (1988) Biochemistry , vol.27 , pp. 7531-7537
    • Laubinger, W.1    Dimroth, P.2
  • 161
    • 0027245710 scopus 로고
    • +-ATPase from Enterococcus hirae. Coexistence of vacuolar- and F0F1-type ATPases in one bacterial cell
    • 8505293
    • +-ATPase from Enterococcus hirae. Coexistence of vacuolar- and F0F1-type ATPases in one bacterial cell, J. Biol. Chem., 268, 11610-11616.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11610-11616
    • Takase, K.1    Yamato, I.2    Kakinuma, Y.3
  • 162
    • 0028361952 scopus 로고
    • +-ATPase of Enterococcus hirae
    • 8144530
    • +-ATPase of Enterococcus hirae, J. Biol. Chem., 269, 9453-9459.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9453-9459
    • Solioz, M.1    Davies, K.2
  • 163


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