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Volumn 35, Issue 6, 2000, Pages 1360-1374

Escherichia coli DipZ: Anatomy of a transmembrane protein disulphide reductase in which three pairs of cysteine residues, one in each of three domains, contribute differentially to function

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; CYTOCHROME C; MEMBRANE PROTEIN; OXIDOREDUCTASE;

EID: 0034099457     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2000.01796.x     Document Type: Article
Times cited : (50)

References (60)
  • 2
    • 0033597878 scopus 로고    scopus 로고
    • Oxidative protein folding is driven by the electron transport system
    • Bader, M., Muse, W., Ballou, D.P., Gassner, C., and Bardwell, J.C.A. (1999) Oxidative protein folding is driven by the electron transport system. Cell 98: 217-227.
    • (1999) Cell , vol.98 , pp. 217-227
    • Bader, M.1    Muse, W.2    Ballou, D.P.3    Gassner, C.4    Bardwell, J.C.A.5
  • 3
    • 0027412196 scopus 로고
    • ALSCRIPT, a tool to format multiple sequence alignments
    • Barton, G.J. (1993) ALSCRIPT, a tool to format multiple sequence alignments. Protein Eng 6: 37-40.
    • (1993) Protein Eng , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 4
    • 0028407376 scopus 로고
    • Expression of human placental alkaline phosphatase in Escherichia coli
    • Beck, R., and Burtscher, H. (1994) Expression of human placental alkaline phosphatase in Escherichia coli. Protein Exp Purif 5: 192-197.
    • (1994) Protein Exp Purif , vol.5 , pp. 192-197
    • Beck, R.1    Burtscher, H.2
  • 5
    • 0028139367 scopus 로고
    • Mutation in dipZ leds to reduced production of active human placental alkaline phosphatase in Escherichia coli
    • Beck, R., Crooke, H., Jarsch, M., Cole, J., and Burtscher, H. (1994) Mutation in dipZ leds to reduced production of active human placental alkaline phosphatase in Escherichia coli. FEMS Microbiol Lett 124: 209-214.
    • (1994) FEMS Microbiol Lett , vol.124 , pp. 209-214
    • Beck, R.1    Crooke, H.2    Jarsch, M.3    Cole, J.4    Burtscher, H.5
  • 6
    • 0021914983 scopus 로고
    • Cloning, nucleotide sequencing and expression of cDNAs encoding mouse urokinase-type plasminogen activator
    • Belin, D., Vassalli, J.D., Combepine, C., Godeau, F., Nagamine, Y., Kocher, E., et al. (1985) Cloning, nucleotide sequencing and expression of cDNAs encoding mouse urokinase-type plasminogen activator. Eur J Biochem 148: 225-232.
    • (1985) Eur J Biochem , vol.148 , pp. 225-232
    • Belin, D.1    Vassalli, J.D.2    Combepine, C.3    Godeau, F.4    Nagamine, Y.5    Kocher, E.6
  • 9
    • 0023479265 scopus 로고
    • Determinants of membrane protein topology
    • Boyd, D., Manoil, C., and Beckwith, J. (1987) Determinants of membrane protein topology. Proc Natl Acad Sci USA 84: 8525-8529.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 8525-8529
    • Boyd, D.1    Manoil, C.2    Beckwith, J.3
  • 10
    • 0027509460 scopus 로고
    • Analysis of the topology of a membrane protein by using a minimum number of alkaline phosphatase fusions
    • Boyd, D., Traxler, B., and Beckwith, J. (1993) Analysis of the topology of a membrane protein by using a minimum number of alkaline phosphatase fusions. J Bacteriol 175: 553-556.
    • (1993) J Bacteriol , vol.175 , pp. 553-556
    • Boyd, D.1    Traxler, B.2    Beckwith, J.3
  • 11
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 12
    • 0016700103 scopus 로고
    • Analysis of the regulation of Escherichia coli alkaline phosphatase synthesis using deletions and Φ80 transducing phages
    • Brickman, E., and Beckwith, J. (1975) Analysis of the regulation of Escherichia coli alkaline phosphatase synthesis using deletions and Φ80 transducing phages. J Mol Biol 96: 307-316.
    • (1975) J Mol Biol , vol.96 , pp. 307-316
    • Brickman, E.1    Beckwith, J.2
  • 13
    • 0014314105 scopus 로고
    • On the localization of alkaline phosphatase and cyclic phosphodiesterase in Escherichia coli
    • Brockman, R.W., and Heppel, L.A. (1968) On the localization of alkaline phosphatase and cyclic phosphodiesterase in Escherichia coli. Biochemistry 7: 2554-2562.
    • (1968) Biochemistry , vol.7 , pp. 2554-2562
    • Brockman, R.W.1    Heppel, L.A.2
  • 14
    • 0017129243 scopus 로고
    • Transposition and fusion of the lac genes to selected promoters using bacteriophage lambda and mu
    • Casadaban, M.J. (1976) Transposition and fusion of the lac genes to selected promoters using bacteriophage lambda and mu. J Mol Biol 104: 541-555.
    • (1976) J Mol Biol , vol.104 , pp. 541-555
    • Casadaban, M.J.1
  • 15
    • 0028930524 scopus 로고
    • The biogenesis of c-type cytochromes in Escherichia coli requires a membrane-bound protein, DipZ, with a protein-disulphide isomerase-like domain
    • Crooke, H., and Cole, J. (1995). The biogenesis of c-type cytochromes in Escherichia coli requires a membrane-bound protein, DipZ, with a protein-disulphide isomerase-like domain. Mol Microbiol 15: 1139-1150.
    • (1995) Mol Microbiol , vol.15 , pp. 1139-1150
    • Crooke, H.1    Cole, J.2
  • 16
    • 0027321787 scopus 로고
    • Identification of the formate dehydrogenases and the genetic determinants of formate-dependent nitrite reduction by Escherichia coli K-12
    • Darwin, A., Tormay, P., Page, L., Griffiths, L., and Cole, J. (1993) Identification of the formate dehydrogenases and the genetic determinants of formate-dependent nitrite reduction by Escherichia coli K-12. J Gen Microbiol 139: 1829-1840.
    • (1993) J Gen Microbiol , vol.139 , pp. 1829-1840
    • Darwin, A.1    Tormay, P.2    Page, L.3    Griffiths, L.4    Cole, J.5
  • 17
    • 0023017879 scopus 로고
    • A plasmid vector that permits stabilisation of both mRNAs and proteins encoded by the cloned genes
    • Duvoisin, R.M., Belin, B., and Krish, H.M. (1986) A plasmid vector that permits stabilisation of both mRNAs and proteins encoded by the cloned genes. Gene 45: 193-201.
    • (1986) Gene , vol.45 , pp. 193-201
    • Duvoisin, R.M.1    Belin, B.2    Krish, H.M.3
  • 18
    • 0033032598 scopus 로고    scopus 로고
    • Characterisation of the Escherichia coli CcmH protein reveals new insights into the redox pathway required for cytochrome c maturation
    • Fabianek, R.A., Hofer, T., and Thöny-Meyer, L. (1999) Characterisation of the Escherichia coli CcmH protein reveals new insights into the redox pathway required for cytochrome c maturation. Arch Microbiol 171: 92-100.
    • (1999) Arch Microbiol , vol.171 , pp. 92-100
    • Fabianek, R.A.1    Hofer, T.2    Thöny-Meyer, L.3
  • 20
    • 0028965483 scopus 로고
    • Molecular genetics of a chromosomal locus involved in copper tolerance in Escherichia coli K-12
    • Fong, S.-T., Camakaris, J., and Lee, B.T.O. (1995) Molecular genetics of a chromosomal locus involved in copper tolerance in Escherichia coli K-12. Mol Microbiol 15: 1127-1137.
    • (1995) Mol Microbiol , vol.15 , pp. 1127-1137
    • Fong, S.-T.1    Camakaris, J.2    Lee, B.T.O.3
  • 21
    • 0029843116 scopus 로고    scopus 로고
    • Membrane topology of the sodium ion-dependent citrate carrier of Klebsiella pneumoniae
    • van Geest, M., and Lokelma, J.S. (1996) Membrane topology of the sodium ion-dependent citrate carrier of Klebsiella pneumoniae. J Biol Chem 271: 25582-25589.
    • (1996) J Biol Chem , vol.271 , pp. 25582-25589
    • Geest, M.1    Lokelma, J.S.2
  • 22
    • 0028176570 scopus 로고
    • Dorsal, a Drosophila Rel-like protein, is phosphorylated upon activation of the transmembrane protein Toll
    • Gillespie, S.K.H., and Wasserman, S.A. (1994) dorsal, a Drosophila Rel-like protein, is phosphorylated upon activation of the transmembrane protein Toll. Mol Cell Biol 14: 3559-3568.
    • (1994) Mol Cell Biol , vol.14 , pp. 3559-3568
    • Gillespie, S.K.H.1    Wasserman, S.A.2
  • 23
    • 0030857512 scopus 로고    scopus 로고
    • A Salmonella typhimurium genetic locus which confers copper tolerance on copper-sensitive mutants of Escherichia coli
    • Gupta, S.D., Wu, H.C., and Rick, P.D. (1997) A Salmonella typhimurium genetic locus which confers copper tolerance on copper-sensitive mutants of Escherichia coli. J Bacteriol 179: 4977-4984.
    • (1997) J Bacteriol , vol.179 , pp. 4977-4984
    • Gupta, S.D.1    Wu, H.C.2    Rick, P.D.3
  • 24
    • 0019447707 scopus 로고
    • Protein localization in E. coli: Is there a common step in the secretion of periplasmic and outer membrane proteins?
    • Ito, K., Bassford, P.J. Jr and Beckwith, J. (1981). Protein localization in E. coli: Is there a common step in the secretion of periplasmic and outer membrane proteins? Cell 24: 707-717.
    • (1981) Cell , vol.24 , pp. 707-717
    • Ito, K.1    Bassford P.J., Jr.2    Beckwith, J.3
  • 25
    • 0028154918 scopus 로고
    • Two cysteines in each periplasmic domain of the membrane protein DsbB are required for its function in protein disulfide bond formation
    • Jander, G., Martin, N.L., and Beckwith, J. (1994) Two cysteines in each periplasmic domain of the membrane protein DsbB are required for its function in protein disulfide bond formation. EMBO J 13: 5121-5127.
    • (1994) EMBO J , vol.13 , pp. 5121-5127
    • Jander, G.1    Martin, N.L.2    Beckwith, J.3
  • 26
    • 78651186104 scopus 로고
    • A direct spectrophotometric assay for penicillin β-lactamase (penicillinase)
    • Jansson, J.A.T. (1965) A direct spectrophotometric assay for penicillin β-lactamase (penicillinase). Biochim Biophys Acta 99: 171-172.
    • (1965) Biochim Biophys Acta , vol.99 , pp. 171-172
    • Jansson, J.A.T.1
  • 27
    • 0030787850 scopus 로고    scopus 로고
    • In vitro and in vivo redox states of the Escherichia coli periplasmic oxidoreductases DsbA and DsbC
    • Joly, J.C., and Schwarz, J.R. (1997) In vitro and in vivo redox states of the Escherichia coli periplasmic oxidoreductases DsbA and DsbC. Biochemistry 36: 10067-10072.
    • (1997) Biochemistry , vol.36 , pp. 10067-10072
    • Joly, J.C.1    Schwarz, J.R.2
  • 28
    • 0030072669 scopus 로고    scopus 로고
    • Roles of cysteine residues of DsbB in its activity to reoxidise DsbA, the protein disulfide bond catalyst of Escherichia coli
    • Kishigami, S., and Ito, K. (1996) Roles of cysteine residues of DsbB in its activity to reoxidise DsbA, the protein disulfide bond catalyst of Escherichia coli. Genes Cells 1: 201-208.
    • (1996) Genes Cells , vol.1 , pp. 201-208
    • Kishigami, S.1    Ito, K.2
  • 30
    • 0023613953 scopus 로고
    • Rapid and efficient site specific mutagenesis without phenotypic selection
    • Kunkel, T.A., and Roberts, J.D. (1987) Rapid and efficient site specific mutagenesis without phenotypic selection. Methods Enzymol 154: 367-382.
    • (1987) Methods Enzymol , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2
  • 31
    • 0029995754 scopus 로고    scopus 로고
    • Effects of mutations in genes for proteins involved in disulphide bond formation in the periplasm on the activities of anaerobically induced electron transfer chains in Escherichia coli K12
    • Metheringham, R., Tyson, K.L., Crooke, H., Missiakas, D., Raina, S., and Cole, J. (1996) Effects of mutations in genes for proteins involved in disulphide bond formation in the periplasm on the activities of anaerobically induced electron transfer chains in Escherichia coli K12. Mol Gen Genet 253: 95-102.
    • (1996) Mol Gen Genet , vol.253 , pp. 95-102
    • Metheringham, R.1    Tyson, K.L.2    Crooke, H.3    Missiakas, D.4    Raina, S.5    Cole, J.6
  • 32
    • 0028982630 scopus 로고
    • Specificity of the protein secretory apparatus: Secretion of the heat-labile enterotoxin B subunit pentamers by different species of Gram negative bacteria
    • Michel, L.O., Sandkvist, M., and Bagdasarian, M. (1995) Specificity of the protein secretory apparatus: secretion of the heat-labile enterotoxin B subunit pentamers by different species of Gram negative bacteria. Gene 152: 41-45.
    • (1995) Gene , vol.152 , pp. 41-45
    • Michel, L.O.1    Sandkvist, M.2    Bagdasarian, M.3
  • 33
    • 0024465189 scopus 로고
    • Use of phoA fusions to study the topology of the Escherichia coli inner membrane protein leader peptidase
    • Millan, J.L.S., Boyd, D., Dalbey, R., Wickner, W., and Beckwith, J. (1989) Use of phoA fusions to study the topology of the Escherichia coli inner membrane protein leader peptidase. J Bacteriol 171: 5536-5541.
    • (1989) J Bacteriol , vol.171 , pp. 5536-5541
    • Millan, J.L.S.1    Boyd, D.2    Dalbey, R.3    Wickner, W.4    Beckwith, J.5
  • 34
  • 35
    • 0021738991 scopus 로고
    • Improved plasmid vectors for the isolation of translational lac gene fusions
    • Minton, N.P. (1984) Improved plasmid vectors for the isolation of translational lac gene fusions. Gene 31: 269-273.
    • (1984) Gene , vol.31 , pp. 269-273
    • Minton, N.P.1
  • 36
    • 0028296940 scopus 로고
    • The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation
    • Missiakas, D., Georgopoulos, C., and Raina, S. (1994) The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation. EMBO J 13: 2013-2120.
    • (1994) EMBO J , vol.13 , pp. 2013-2120
    • Missiakas, D.1    Georgopoulos, C.2    Raina, S.3
  • 37
    • 0028979629 scopus 로고
    • Identification and characterisation of a new disulphide-isomerase-like protein (DsbD) in Escherichia coli
    • Missiakas, D., Schwager, F., and Raina, S. (1995) Identification and characterisation of a new disulphide-isomerase-like protein (DsbD) in Escherichia coli. EMBO J 14: 3415-3424.
    • (1995) EMBO J , vol.14 , pp. 3415-3424
    • Missiakas, D.1    Schwager, F.2    Raina, S.3
  • 38
    • 0019258558 scopus 로고
    • Excretion of glutathione by methyl-glyoxal-resistant Escherichia coli
    • Murata, K., Tani, K., Kato, J., and Chibata, I. (1980) Excretion of glutathione by methyl-glyoxal-resistant Escherichia coli. J Gen Microbiol 120: 545-547.
    • (1980) J Gen Microbiol , vol.120 , pp. 545-547
    • Murata, K.1    Tani, K.2    Kato, J.3    Chibata, I.4
  • 40
    • 0022513680 scopus 로고
    • Export of glutathione by some widely used Salmonella typhimurium and Escherichia coli strains
    • Owens, R.A., and Hartman, P.E. (1986) Export of glutathione by some widely used Salmonella typhimurium and Escherichia coli strains. J Bacteriol 168: 109-114.
    • (1986) J Bacteriol , vol.168 , pp. 109-114
    • Owens, R.A.1    Hartman, P.E.2
  • 41
    • 0013662535 scopus 로고    scopus 로고
    • Contrasting routes of c-type cytochrome assembly in mitochondria, chloroplasts and bacteria
    • Page, M.D., Sambongi, Y., and Ferguson, S.J. (1998) Contrasting routes of c-type cytochrome assembly in mitochondria, chloroplasts and bacteria. Trends Microbiol 23: 89-120.
    • (1998) Trends Microbiol , vol.23 , pp. 89-120
    • Page, M.D.1    Sambongi, Y.2    Ferguson, S.J.3
  • 42
    • 0030780084 scopus 로고    scopus 로고
    • Disruption of the Pseudomonas aeruginosa dipZ gene, encoding a putative protein-disulphide reductase, leads to partial pleiotropic deficiency in c-type cytochrome biogenesis
    • Page, M.D., Saunders, N.F.W., and Ferguson, S.J. (1997) Disruption of the Pseudomonas aeruginosa dipZ gene, encoding a putative protein-disulphide reductase, leads to partial pleiotropic deficiency in c-type cytochrome biogenesis. Microbiology 143: 3111-3122.
    • (1997) Microbiology , vol.143 , pp. 3111-3122
    • Page, M.D.1    Saunders, N.F.W.2    Ferguson, S.J.3
  • 43
    • 0013690451 scopus 로고    scopus 로고
    • Purification of IgG using affinity chromatography on antigen-ligand columns
    • Walker, J.M. (ed.). Totawa, NJ, USA: Humana
    • Page, M., andThorpe, R. (1996) Purification of IgG using affinity chromatography on antigen-ligand columns. In The Protein Protocols Handbook. Walker, J.M. (ed.). Totawa, NJ, USA: Humana, pp. 739-741.
    • (1996) The Protein Protocols Handbook , pp. 739-741
    • Page, M.1    Thorpe, R.2
  • 44
    • 0030765627 scopus 로고    scopus 로고
    • Making and breaking disulfide bonds
    • Raina, S., and Missiakas, D. (1997) Making and breaking disulfide bonds. Ann Rev Microbiol 51: 179-202.
    • (1997) Ann Rev Microbiol , vol.51 , pp. 179-202
    • Raina, S.1    Missiakas, D.2
  • 45
    • 0032529951 scopus 로고    scopus 로고
    • The CcmE protein from Escherichia coli is a haem-binding protein
    • Reid, E., Eaves, D.J., and Cole, J.A. (1998) The CcmE protein from Escherichia coli is a haem-binding protein. FEMS Microbiol Lett 166: 369-375.
    • (1998) FEMS Microbiol Lett , vol.166 , pp. 369-375
    • Reid, E.1    Eaves, D.J.2    Cole, J.A.3
  • 46
    • 0032411723 scopus 로고    scopus 로고
    • The genetics of disulfide bond metabolism
    • Reitsch, A., and Beckwith, J. (1998) The genetics of disulfide bond metabolism. Annu Rev Genet 32: 163-184.
    • (1998) Annu Rev Genet , vol.32 , pp. 163-184
    • Reitsch, A.1    Beckwith, J.2
  • 47
    • 0029822654 scopus 로고    scopus 로고
    • An in vivo pathway for disufide bond isomerisation in Escherichia coli
    • Reitsch, A., Belin, D., Martin, N., and Beckwith, J. (1996) An in vivo pathway for disufide bond isomerisation in Escherichia coli. Proc Natl Acad Sci USA 93: 13048-13053.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13048-13053
    • Reitsch, A.1    Belin, D.2    Martin, N.3    Beckwith, J.4
  • 48
    • 0030668672 scopus 로고    scopus 로고
    • Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin
    • Reitsch, A., Bessette, P., Georgiou, G., and Beckwith, J. (1997) Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin. J Bacteriol 179: 6602-6608.
    • (1997) J Bacteriol , vol.179 , pp. 6602-6608
    • Reitsch, A.1    Bessette, P.2    Georgiou, G.3    Beckwith, J.4
  • 50
    • 0028116313 scopus 로고
    • Specific thiol compounds complement deficiency in c-type cytochrome biogenesis in Escherichia coli carrying a mutation in a membrane-bound disulphide isomerase-like protein
    • Sambongi, Y., and Ferguson, S.J. (1994a) Specific thiol compounds complement deficiency in c-type cytochrome biogenesis in Escherichia coli carrying a mutation in a membrane-bound disulphide isomerase-like protein. FEBS Lett 353: 235-238.
    • (1994) FEBS Lett , vol.353 , pp. 235-238
    • Sambongi, Y.1    Ferguson, S.J.2
  • 51
    • 0028295739 scopus 로고
    • 552 does not. Implications for c-type cytochrome biogenesis
    • 552 does not. Implications for c-type cytochrome biogenesis FEBS Lett 340: 65-70.
    • (1994) FEBS Lett , vol.340 , pp. 65-70
    • Sambongi, Y.1    Ferguson, S.J.2
  • 52
    • 0030566826 scopus 로고    scopus 로고
    • Mutants of Escherichia coli lacking disulphide oxidoreductases DsbA and DsbB cannot synthesise an exogenous monohaem c-type cytochrome except in the presence of disulphide compounds
    • Sambongi, Y., and Ferguson, J. (1996) Mutants of Escherichia coli lacking disulphide oxidoreductases DsbA and DsbB cannot synthesise an exogenous monohaem c-type cytochrome except in the presence of disulphide compounds. FEBS Lett 398: 265-268.
    • (1996) FEBS Lett , vol.398 , pp. 265-268
    • Sambongi, Y.1    Ferguson, J.2
  • 54
    • 0030897419 scopus 로고    scopus 로고
    • Identification and characterisation of the ccdA gene, required for cytochrome c synthesis in Bacillus subtilis
    • Schiött, T., von Wachenfeldt, C., and Hederstedt, L. (1997) Identification and characterisation of the ccdA gene, required for cytochrome c synthesis in Bacillus subtilis. J Bacteriol 179: 1962-1973.
    • (1997) J Bacteriol , vol.179 , pp. 1962-1973
    • Schiött, T.1    Von Wachenfeldt, C.2    Hederstedt, L.3
  • 55
    • 0020480282 scopus 로고
    • Characteristics of translational initiation sites in E. coli
    • Stormo, G.D., Schneider, T.D., and Gold, L.M. (1982) Characteristics of translational initiation sites in E. coli. Nucleic Acids Res 10: 2971-2996.
    • (1982) Nucleic Acids Res , vol.10 , pp. 2971-2996
    • Stormo, G.D.1    Schneider, T.D.2    Gold, L.M.3
  • 56
    • 0027478779 scopus 로고
    • The topological analysis of integral cytoplasmic membrane proteins
    • Traxler, B., Boyd, D., and Beckwith, J. (1993) The topological analysis of integral cytoplasmic membrane proteins. J Membr Biol 132: 1-11.
    • (1993) J Membr Biol , vol.132 , pp. 1-11
    • Traxler, B.1    Boyd, D.2    Beckwith, J.3
  • 57
    • 0026688543 scopus 로고
    • The dynamics of assembly of a cytoplasmic membrane protein in Escherichia coli
    • Traxler, B., Lee, C., Boyd, D., and Beckwith, J. (1992) The dynamics of assembly of a cytoplasmic membrane protein in Escherichia coli. J Biol Chem 267: 5339-5345.
    • (1992) J Biol Chem , vol.267 , pp. 5339-5345
    • Traxler, B.1    Lee, C.2    Boyd, D.3    Beckwith, J.4
  • 58
    • 0001530324 scopus 로고
    • 2-terminal residue of the proteins from cell-free extract of E. coli
    • 2-terminal residue of the proteins from cell-free extract of E. coli. J Mol Biol 7: 483-496.
    • (1963) J Mol Biol , vol.7 , pp. 483-496
    • Waller, J.P.1
  • 59
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archean, and eukaryotic organisms
    • Wallin, E., and von Heijne, G. (1998) Genome-wide analysis of integral membrane proteins from eubacterial, archean, and eukaryotic organisms. Protein Sci 7: 1029-1038.
    • (1998) Protein Sci , vol.7 , pp. 1029-1038
    • Wallin, E.1    Von Heijne, G.2
  • 60
    • 0019181541 scopus 로고
    • Improved conversion of methanol to single-cell protein by Methylophilus methylotrophus
    • Windass, J.D., Worsey, M.J., Pioli, E.M., Pioli, D., Barth, P.T., Atherton, K.T., et al. (1980) Improved conversion of methanol to single-cell protein by Methylophilus methylotrophus. Nature 289: 396-401.
    • (1980) Nature , vol.289 , pp. 396-401
    • Windass, J.D.1    Worsey, M.J.2    Pioli, E.M.3    Pioli, D.4    Barth, P.T.5    Atherton, K.T.6


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