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Volumn 29, Issue 5, 2005, Pages 961-985

Prokaryotic K+ channels: From crystal structures to diversity

Author keywords

Membrane potential; Parasitism; Potassium channels; Potassium filter; RCK KTN

Indexed keywords

CYCLIC NUCLEOTIDE; GLUTAMATE RECEPTOR; POTASSIUM CHANNEL; POTASSIUM PUMP;

EID: 22244458104     PISSN: 01686445     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.femsre.2005.03.003     Document Type: Review
Times cited : (96)

References (150)
  • 3
    • 3242887060 scopus 로고    scopus 로고
    • Channels in microbes: So many holes to fill
    • C. Kung, and P. Blount Channels in microbes: So many holes to fill Molecular Microbiology 53 2004 373 380
    • (2004) Molecular Microbiology , vol.53 , pp. 373-380
    • Kung, C.1    Blount, P.2
  • 8
    • 0037126294 scopus 로고    scopus 로고
    • A biological role for prokaryotic ClC chloride channels
    • R. Iyer, T. Iverson, A. Accardi, and C. Miller A biological role for prokaryotic ClC chloride channels Nature 419 2002 715 718
    • (2002) Nature , vol.419 , pp. 715-718
    • Iyer, R.1    Iverson, T.2    Accardi, A.3    Miller, C.4
  • 9
    • 0037122805 scopus 로고    scopus 로고
    • X-ray structure of a CIC chloride channel at 3.0 angstrom reveals the molecular basis of anion selectivity
    • R. Dutzler, E.B. Campbell, M. Cadene, B.T. Chait, and R. MacKinnon X-ray structure of a CIC chloride channel at 3.0 angstrom reveals the molecular basis of anion selectivity Nature 415 2002 287 294
    • (2002) Nature , vol.415 , pp. 287-294
    • Dutzler, R.1    Campbell, E.B.2    Cadene, M.3    Chait, B.T.4    MacKinnon, R.5
  • 10
    • 0028224356 scopus 로고
    • A large-conductance mechanosensitive channel in E. coli encoded by mscL alone
    • S.I. Sukharev, P. Blount, B. Martinac, F.R. Blattner, and C. Kung A large-conductance mechanosensitive channel in E. coli encoded by mscL alone Nature 368 1994 265 268
    • (1994) Nature , vol.368 , pp. 265-268
    • Sukharev, S.I.1    Blount, P.2    Martinac, B.3    Blattner, F.R.4    Kung, C.5
  • 11
    • 0032545321 scopus 로고    scopus 로고
    • Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel
    • G. Chang, R.H. Spencer, A.T. Lee, M.T. Barclay, and D.C. Rees Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel Science 282 1998 2220 2226
    • (1998) Science , vol.282 , pp. 2220-2226
    • Chang, G.1    Spencer, R.H.2    Lee, A.T.3    Barclay, M.T.4    Rees, D.C.5
  • 12
    • 0345196593 scopus 로고    scopus 로고
    • Protection of Escherichia coli cells against extreme turgor by activation of MscS and MscL methanosensitive channels: Identification of genes required for MscS activity
    • N. Levina, S. Totemeyer, N.R. Stokes, P. Louis, M.A. Jones, and I.R. Booth Protection of Escherichia coli cells against extreme turgor by activation of MscS and MscL methanosensitive channels: Identification of genes required for MscS activity EMBO Journal 18 1999 1730 1737
    • (1999) EMBO Journal , vol.18 , pp. 1730-1737
    • Levina, N.1    Totemeyer, S.2    Stokes, N.R.3    Louis, P.4    Jones, M.A.5    Booth, I.R.6
  • 13
    • 2242431668 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel
    • R.B. Bass, P. Strop, M. Barclay, and D.C. Rees Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel Science 298 2002 1582 1587
    • (2002) Science , vol.298 , pp. 1582-1587
    • Bass, R.B.1    Strop, P.2    Barclay, M.3    Rees, D.C.4
  • 15
    • 0007388049 scopus 로고
    • Cation transport in Escherichia coli I: Intracellular Na and K concentrations and net cation movement
    • S.G. Schultz, and A.K. Solomon Cation transport in Escherichia coli I: Intracellular Na and K concentrations and net cation movement Journal of General Physiology 45 1961 355 369
    • (1961) Journal of General Physiology , vol.45 , pp. 355-369
    • Schultz, S.G.1    Solomon, A.K.2
  • 16
    • 0033823402 scopus 로고    scopus 로고
    • The bacterium's way for safe enlargement and division
    • A.L. Koch The bacterium's way for safe enlargement and division Applied and Environmental Microbiology 66 2000 3657 3663
    • (2000) Applied and Environmental Microbiology , vol.66 , pp. 3657-3663
    • Koch, A.L.1
  • 19
    • 0000898514 scopus 로고    scopus 로고
    • F.C. Neidhardt ASM Press Washington, D.C. USA
    • F.M.a.M.P.C. Harold F.C. Neidhardt Escherichia coli and Salmonella Vol. 1 1996 ASM Press Washington, D.C. USA 283 306
    • (1996) Escherichia Coli and Salmonella , vol.1 , pp. 283-306
    • Harold, F.C.1
  • 20
    • 0020361477 scopus 로고
    • +-ATPase of growing and resting, aerobic Escherichia coli
    • +-ATPase of growing and resting, aerobic Escherichia coli Biochemistry 21 1982 5534 5538
    • (1982) Biochemistry , vol.21 , pp. 5534-5538
    • Kashket, E.R.1
  • 23
    • 3843119810 scopus 로고    scopus 로고
    • Amino acid substitutions in putative selectivity filter regions III and IV in KdpA alter ion selectivity of the KdpFABC complex from Escherichia coli
    • J. Bertrand, K. Altendorf, and M. Bramkamp Amino acid substitutions in putative selectivity filter regions III and IV in KdpA alter ion selectivity of the KdpFABC complex from Escherichia coli Journal of Bacteriology 186 2004 5519 5522
    • (2004) Journal of Bacteriology , vol.186 , pp. 5519-5522
    • Bertrand, J.1    Altendorf, K.2    Bramkamp, M.3
  • 24
    • 0036778469 scopus 로고    scopus 로고
    • Characterization of amino acid substitutions in KdpA, the K+-binding and -translocating subunit of the KdpFABC complex of Escherichia coli
    • M. van der Laan, M. Gassel, and K. Altendorf Characterization of amino acid substitutions in KdpA, the K+-binding and -translocating subunit of the KdpFABC complex of Escherichia coli Journal of Bacteriology 184 2002 5491 5494
    • (2002) Journal of Bacteriology , vol.184 , pp. 5491-5494
    • Van Der Laan, M.1    Gassel, M.2    Altendorf, K.3
  • 26
    • 0033010261 scopus 로고    scopus 로고
    • + uptake system in Escherichia coli upon hyper-osmotic stress at a low pH
    • + uptake system in Escherichia coli upon hyper-osmotic stress at a low pH FEBS Letters 447 1999 144 148
    • (1999) FEBS Letters , vol.447 , pp. 144-148
    • Trchounian, A.1    Kobayashi, H.2
  • 28
    • 0032496329 scopus 로고    scopus 로고
    • A role for the AKT1 potassium channel in plant nutrition
    • R.E. Hirsch, B.D. Lewis, E.P. Spalding, and M.R. Sussman A role for the AKT1 potassium channel in plant nutrition Science 280 1998 918 921
    • (1998) Science , vol.280 , pp. 918-921
    • Hirsch, R.E.1    Lewis, B.D.2    Spalding, E.P.3    Sussman, M.R.4
  • 29
    • 0028609781 scopus 로고
    • + channel beta-subunits belong to an NAD(P)H-dependent oxidoreductase superfamily
    • + channel beta-subunits belong to an NAD(P)H-dependent oxidoreductase superfamily Cell 79 1994 1133 1135
    • (1994) Cell , vol.79 , pp. 1133-1135
    • McCormack, T.1    McCormack, K.2
  • 33
    • 0023225798 scopus 로고
    • Cloning of genomic and complementary DNA from Shaker, a putative potassium channel gene from Drosophila
    • D.M. Papazian, T.L. Schwarz, B.L. Tempel, Y.N. Jan, and L.Y. Jan Cloning of genomic and complementary DNA from Shaker, a putative potassium channel gene from Drosophila Science 237 1987 749 753
    • (1987) Science , vol.237 , pp. 749-753
    • Papazian, D.M.1    Schwarz, T.L.2    Tempel, B.L.3    Jan, Y.N.4    Jan, L.Y.5
  • 34
    • 0023270432 scopus 로고
    • Sequence of a probable potassium channel component encoded at Shaker locus of Drosophila
    • B.L. Tempel, D.M. Papazian, T.L. Schwarz, Y.N. Jan, and L.Y. Jan Sequence of a probable potassium channel component encoded at Shaker locus of Drosophila Science 237 1987 770 775
    • (1987) Science , vol.237 , pp. 770-775
    • Tempel, B.L.1    Papazian, D.M.2    Schwarz, T.L.3    Jan, Y.N.4    Jan, L.Y.5
  • 35
    • 0029099458 scopus 로고
    • A new family of outwardly rectifying potassium channel proteins with two pore domains in tandem
    • K.A. Ketchum, W.J. Joiner, A.J. Sellers, L.K. Kaczmarek, and S.A. Goldstein A new family of outwardly rectifying potassium channel proteins with two pore domains in tandem Nature 376 1995 690 695
    • (1995) Nature , vol.376 , pp. 690-695
    • Ketchum, K.A.1    Joiner, W.J.2    Sellers, A.J.3    Kaczmarek, L.K.4    Goldstein, S.A.5
  • 37
    • 0015881172 scopus 로고
    • Potassium channels in myelinated nerve - Selective permeability to small cations
    • B. Hille Potassium channels in myelinated nerve - selective permeability to small cations Journal of General Physiology 61 1973 669 686
    • (1973) Journal of General Physiology , vol.61 , pp. 669-686
    • Hille, B.1
  • 38
    • 1542288949 scopus 로고    scopus 로고
    • Secondary active transport mediated by a prokaryotic homologue of ClC Cl-channels
    • A. Accardi, and C. Miller Secondary active transport mediated by a prokaryotic homologue of ClC Cl-channels Nature 427 2004 803 807
    • (2004) Nature , vol.427 , pp. 803-807
    • Accardi, A.1    Miller, C.2
  • 39
    • 0037421991 scopus 로고    scopus 로고
    • Molecular mechanisms of mechanosensation: Big lessons from small cells
    • P. Blount Molecular mechanisms of mechanosensation: Big lessons from small cells Neuron 37 2003 731 734
    • (2003) Neuron , vol.37 , pp. 731-734
    • Blount, P.1
  • 43
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • J.D. Thompson, T.J. Gibson, F. Plewniak, F. Jeanmougin, and D.G. Higgins The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools Nucleic Acids Research 25 1997 4876 4882
    • (1997) Nucleic Acids Research , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 44
    • 0036793591 scopus 로고    scopus 로고
    • Family ties of gated pores: Evolution of the sensor module
    • A. Kumanovics, G. Levin, and P. Blount Family ties of gated pores: Evolution of the sensor module FASEB Journal 16 2002 1623 1629
    • (2002) FASEB Journal , vol.16 , pp. 1623-1629
    • Kumanovics, A.1    Levin, G.2    Blount, P.3
  • 51
    • 0035827328 scopus 로고    scopus 로고
    • Microbial genes in the human genome: Lateral transfer or gene loss?
    • S.L. Salzberg, O. White, J. Peterson, and J.A. Eisen Microbial genes in the human genome: Lateral transfer or gene loss? Science 292 2001 1903 1906
    • (2001) Science , vol.292 , pp. 1903-1906
    • Salzberg, S.L.1    White, O.2    Peterson, J.3    Eisen, J.A.4
  • 52
    • 0035106010 scopus 로고    scopus 로고
    • Phylogenetic analyses of two "archaeal" genes in Thermotoga maritima reveal multiple transfers between Archaea and Bacteria
    • C.L. Nesbo, S. L'Haridon, K.O. Stetter, and W.F. Doolittle Phylogenetic analyses of two "Archaeal" genes in Thermotoga maritima reveal multiple transfers between Archaea and Bacteria Molecular Biology and Evolution 18 2001 362 375
    • (2001) Molecular Biology and Evolution , vol.18 , pp. 362-375
    • Nesbo, C.L.1    L'Haridon, S.2    Stetter, K.O.3    Doolittle, W.F.4
  • 54
    • 0034696954 scopus 로고    scopus 로고
    • Pore mutations affecting tetrameric assembly and functioning of the potassium channel KcsA from Streptomyces lividans
    • H. Splitt, D. Meuser, I. Borovok, M. Betzler, and H. Schrempf Pore mutations affecting tetrameric assembly and functioning of the potassium channel KcsA from Streptomyces lividans FEBS Letters 472 2000 83 87
    • (2000) FEBS Letters , vol.472 , pp. 83-87
    • Splitt, H.1    Meuser, D.2    Borovok, I.3    Betzler, M.4    Schrempf, H.5
  • 58
    • 35649001607 scopus 로고
    • A quantitative description of membrane current and its application to conduction and excitation in nerve
    • A.L. Hodgkin, and A.F. Huxley A quantitative description of membrane current and its application to conduction and excitation in nerve Journal of Physiology 117 1952 500 544
    • (1952) Journal of Physiology , vol.117 , pp. 500-544
    • Hodgkin, A.L.1    Huxley, A.F.2
  • 59
    • 0015868742 scopus 로고
    • Currents related to movement of gating particles of sodium channels
    • C.D. Armstrong, and F. Bezanilla Currents related to movement of gating particles of sodium channels Nature 242 1973 459 461
    • (1973) Nature , vol.242 , pp. 459-461
    • Armstrong, C.D.1    Bezanilla, F.2
  • 63
    • 0037381334 scopus 로고    scopus 로고
    • Hyperpolarization moves S4 sensors inward to open MVP, a methanococcal voltage-gated potassium channel
    • F. Sesti, S. Rajan, R. Gonzalez-Colaso, N. Nikolaeva, and S.A. Goldstein Hyperpolarization moves S4 sensors inward to open MVP, a methanococcal voltage-gated potassium channel Nature Neuroscience 6 2003 353 361
    • (2003) Nature Neuroscience , vol.6 , pp. 353-361
    • Sesti, F.1    Rajan, S.2    Gonzalez-Colaso, R.3    Nikolaeva, N.4    Goldstein, S.A.5
  • 65
    • 0035950089 scopus 로고    scopus 로고
    • Ion conduction pore is conserved among potassium channels
    • Z. Lu, A.M. Klem, and Y. Ramu Ion conduction pore is conserved among potassium channels Nature 413 2001 809 813
    • (2001) Nature , vol.413 , pp. 809-813
    • Lu, Z.1    Klem, A.M.2    Ramu, Y.3
  • 66
    • 0029913403 scopus 로고    scopus 로고
    • A structural vignette common to voltage sensors and conduction pores: Canaliculi
    • S.A. Goldstein A structural vignette common to voltage sensors and conduction pores: Canaliculi Neuron 16 1996 717 722
    • (1996) Neuron , vol.16 , pp. 717-722
    • Goldstein, S.A.1
  • 67
    • 1942532333 scopus 로고    scopus 로고
    • Critical assessment of a proposed model of Shaker
    • M. Laine, D.M. Papazian, and B. Roux Critical assessment of a proposed model of Shaker FEBS Letters 564 2004 257 263
    • (2004) FEBS Letters , vol.564 , pp. 257-263
    • Laine, M.1    Papazian, D.M.2    Roux, B.3
  • 68
    • 0041695463 scopus 로고    scopus 로고
    • Answers and questions from the KvAP structures
    • B.E. Cohen, M. Grabe, and L.Y. Jan Answers and questions from the KvAP structures Neuron 39 2004 395 400
    • (2004) Neuron , vol.39 , pp. 395-400
    • Cohen, B.E.1    Grabe, M.2    Jan, L.Y.3
  • 69
    • 0033576580 scopus 로고    scopus 로고
    • Atomic scale movement of the voltage-sensing region in a potassium channel measured via spectroscopy
    • A. Cha, G.E. Snyder, P.R. Selvin, and F. Bezanilla Atomic scale movement of the voltage-sensing region in a potassium channel measured via spectroscopy Nature 402 1999 809 813
    • (1999) Nature , vol.402 , pp. 809-813
    • Cha, A.1    Snyder, G.E.2    Selvin, P.R.3    Bezanilla, F.4
  • 70
    • 1142274549 scopus 로고    scopus 로고
    • A proton pore in a potassium channel voltage sensor reveals a focused electric field
    • D.M. Starace, and F. Bezanilla A proton pore in a potassium channel voltage sensor reveals a focused electric field Nature 427 2004 548 553
    • (2004) Nature , vol.427 , pp. 548-553
    • Starace, D.M.1    Bezanilla, F.2
  • 71
    • 3142580385 scopus 로고    scopus 로고
    • A membrane-access mechanism of ion channel inhibition by voltage sensor toxins from spider venom
    • S.Y. Lee, and R. MacKinnon A membrane-access mechanism of ion channel inhibition by voltage sensor toxins from spider venom Nature 430 2004 232 235
    • (2004) Nature , vol.430 , pp. 232-235
    • Lee, S.Y.1    MacKinnon, R.2
  • 76
    • 0016345760 scopus 로고
    • Chemical and biological evolution of a nucleotide-binding protein
    • M.G. Rossmann, D. Moras, and K.W. Olsen Chemical and biological evolution of a nucleotide-binding protein Nature 250 1974 194 199
    • (1974) Nature , vol.250 , pp. 194-199
    • Rossmann, M.G.1    Moras, D.2    Olsen, K.W.3
  • 81
    • 0037077136 scopus 로고    scopus 로고
    • A mechanism of regulating transmembrane potassium flux through a ligand-mediated conformational switch
    • T.P. Roosild, S. Miller, I.R. Booth, and S. Choe A mechanism of regulating transmembrane potassium flux through a ligand-mediated conformational switch Cell 109 2002 781 791
    • (2002) Cell , vol.109 , pp. 781-791
    • Roosild, T.P.1    Miller, S.2    Booth, I.R.3    Choe, S.4
  • 83
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • Y.X. Jiang, A. Lee, J.Y. Chen, M. Cadene, B.T. Chait, and R. MacKinnon Crystal structure and mechanism of a calcium-gated potassium channel Nature 417 2002 515 522
    • (2002) Nature , vol.417 , pp. 515-522
    • Jiang, Y.X.1    Lee, A.2    Chen, J.Y.3    Cadene, M.4    Chait, B.T.5    MacKinnon, R.6
  • 85
    • 0141831003 scopus 로고    scopus 로고
    • Structural basis for modulation and agonist specificity of HCN pacemaker channels
    • W.N. Zagotta, N.B. Olivier, K.D. Black, E.C. Young, R. Olson, and E. Gouaux Structural basis for modulation and agonist specificity of HCN pacemaker channels Nature 425 2003 200 205
    • (2003) Nature , vol.425 , pp. 200-205
    • Zagotta, W.N.1    Olivier, N.B.2    Black, K.D.3    Young, E.C.4    Olson, R.5    Gouaux, E.6
  • 87
    • 8844263765 scopus 로고    scopus 로고
    • Structural basis of ligand activation in a cyclic nucleotide regulated potassium channel
    • G.M. Clayton, W.R. Silverman, L. Heginbotham, and J.H. Morais-Cabral Structural basis of ligand activation in a cyclic nucleotide regulated potassium channel Cell 119 2004 615 627
    • (2004) Cell , vol.119 , pp. 615-627
    • Clayton, G.M.1    Silverman, W.R.2    Heginbotham, L.3    Morais-Cabral, J.H.4
  • 88
    • 0033576612 scopus 로고    scopus 로고
    • Functional characterization of a potassium-selective prokaryotic glutamate receptor
    • G.Q. Chen, C. Cui, M.L. Mayer, and E. Gouaux Functional characterization of a potassium-selective prokaryotic glutamate receptor Nature 402 1999 817 821
    • (1999) Nature , vol.402 , pp. 817-821
    • Chen, G.Q.1    Cui, C.2    Mayer, M.L.3    Gouaux, E.4
  • 89
    • 0032578635 scopus 로고    scopus 로고
    • Structure of a glutamate-receptor ligand-binding core in complex with kainate
    • N. Armstrong, Y. Sun, G.Q. Chen, and E. Gouaux Structure of a glutamate-receptor ligand-binding core in complex with kainate Nature 395 1998 913 917
    • (1998) Nature , vol.395 , pp. 913-917
    • Armstrong, N.1    Sun, Y.2    Chen, G.Q.3    Gouaux, E.4
  • 90
    • 0032562651 scopus 로고    scopus 로고
    • The structure of glutamine-binding protein complexed with glutamine at 1.94 angstrom resolution: Comparisons with other amino acid binding proteins
    • Y.J. Sun, J. Rose, B.C. Wang, and C.D. Hsiao The structure of glutamine-binding protein complexed with glutamine at 1.94 angstrom resolution: Comparisons with other amino acid binding proteins Journal of Molecular Biology 278 1998 219 229
    • (1998) Journal of Molecular Biology , vol.278 , pp. 219-229
    • Sun, Y.J.1    Rose, J.2    Wang, B.C.3    Hsiao, C.D.4
  • 91
    • 0035943408 scopus 로고    scopus 로고
    • Mechanisms for ligand binding to GluR0 ion channels: Crystal structures of the glutamate and serine complexes and a closed apo state
    • M.L. Mayer, R. Olson, and E. Gouaux Mechanisms for ligand binding to GluR0 ion channels: Crystal structures of the glutamate and serine complexes and a closed apo state Journal of Molecular Biology 311 2001 815 836
    • (2001) Journal of Molecular Biology , vol.311 , pp. 815-836
    • Mayer, M.L.1    Olson, R.2    Gouaux, E.3
  • 95
    • 0036842986 scopus 로고    scopus 로고
    • Genome sequence of the endocellular obligate symbiont of tsetse flies, Wigglesworthia glossinidia
    • L. Akman, A. Yamashita, H. Watanabe, K. Oshima, T. Shiba, M. Hattori, and S. Aksoy Genome sequence of the endocellular obligate symbiont of tsetse flies, Wigglesworthia glossinidia Nature Genetics 32 2002 402 407
    • (2002) Nature Genetics , vol.32 , pp. 402-407
    • Akman, L.1    Yamashita, A.2    Watanabe, H.3    Oshima, K.4    Shiba, T.5    Hattori, M.6    Aksoy, S.7
  • 97
    • 0034618559 scopus 로고    scopus 로고
    • Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS
    • S. Shigenobu, H. Watanabe, M. Hattori, Y. Sakaki, and H. Ishikawa Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS Nature 407 2000 81 86
    • (2000) Nature , vol.407 , pp. 81-86
    • Shigenobu, S.1    Watanabe, H.2    Hattori, M.3    Sakaki, Y.4    Ishikawa, H.5
  • 109
    • 10944235924 scopus 로고    scopus 로고
    • Comparative genomic structure of prokaryotes
    • S.D. Bentley, and J. Parkhill Comparative genomic structure of prokaryotes Annual Review of Genetics 38 2004 771 791
    • (2004) Annual Review of Genetics , vol.38 , pp. 771-791
    • Bentley, S.D.1    Parkhill, J.2
  • 144
    • 0014748661 scopus 로고
    • Potassium-dependent mutatnts of Escherichia coli K-12
    • W. Epstein, and M. Davies Potassium-dependent mutatnts of Escherichia coli K-12 Journal of Bacteriology 101 1970 836 843
    • (1970) Journal of Bacteriology , vol.101 , pp. 836-843
    • Epstein, W.1    Davies, M.2
  • 145
    • 0015155178 scopus 로고
    • Potassium transport loci in Escherichia coli K-12
    • W. Epstein, and B.S. Kim Potassium transport loci in Escherichia coli K-12 Journal of Bacteriology 108 1971 639 644
    • (1971) Journal of Bacteriology , vol.108 , pp. 639-644
    • Epstein, W.1    Kim, B.S.2
  • 146
    • 0017276787 scopus 로고
    • Cation transport in Escherichia coli VIII: Potassium transport mutants
    • D. Rhoads, F. Waters, and W. Epstein Cation transport in Escherichia coli VIII: Potassium transport mutants Jorunal of General Physiology 67 1976 325 341
    • (1976) Jorunal of General Physiology , vol.67 , pp. 325-341
    • Rhoads, D.1    Waters, F.2    Epstein, W.3


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