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Volumn 179, Issue 17, 1997, Pages 5333-5339

Leaderless polypeptides efficiently extracted from whole cells by osmotic shock

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOPHILIN;

EID: 0030964719     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.17.5333-5339.1997     Document Type: Article
Times cited : (50)

References (71)
  • 1
    • 0021711731 scopus 로고
    • Simple, rapid, and quantitative release of periplasmic proteins by chloroform
    • Ames, G. F.-L., C. Prody, and S. Kustu. 1984. Simple, rapid, and quantitative release of periplasmic proteins by chloroform. J. Bacteriol. 160:1181-1183.
    • (1984) J. Bacteriol. , vol.160 , pp. 1181-1183
    • Ames, G.F.-L.1    Prody, C.2    Kustu, S.3
  • 2
    • 0023783034 scopus 로고
    • A lacZ-pbpB gene fusion coding for an inducible hybrid protein that recognizes localized sites in the inner membrane of Escherichia coli
    • Ayala, J. A., J. Plá, L. R. Desviat, and M. A. de Pedro. 1988. A lacZ-pbpB gene fusion coding for an inducible hybrid protein that recognizes localized sites in the inner membrane of Escherichia coli. J. Bacteriol. 170:3333-3341.
    • (1988) J. Bacteriol. , vol.170 , pp. 3333-3341
    • Ayala, J.A.1    Plá, J.2    Desviat, L.R.3    De Pedro, M.A.4
  • 4
    • 0026091179 scopus 로고
    • Identification of a protein required for disulfide bond formation in vivo
    • Bardwell, J. C. A., K. McGovern, and J. Beckwith. 1991. Identification of a protein required for disulfide bond formation in vivo. Cell 67:581-589.
    • (1991) Cell , vol.67 , pp. 581-589
    • Bardwell, J.C.A.1    McGovern, K.2    Beckwith, J.3
  • 5
    • 0014346151 scopus 로고
    • Areas of adhesion between wall and membrane of Escherichia coli
    • Bayer, M. E. 1968. Areas of adhesion between wall and membrane of Escherichia coli. J. Gen. Microbiol. 53:395-404.
    • (1968) J. Gen. Microbiol. , vol.53 , pp. 395-404
    • Bayer, M.E.1
  • 6
    • 0020032425 scopus 로고
    • Isolation and partial characterization of membrane vesicles carrying markers of the membrane adhesion sites
    • Bayer, M. H., G. Costello, and M. E. Bayer. 1982. Isolation and partial characterization of membrane vesicles carrying markers of the membrane adhesion sites. J. Bacteriol. 149:758-767.
    • (1982) J. Bacteriol. , vol.149 , pp. 758-767
    • Bayer, M.H.1    Costello, G.2    Bayer, M.E.3
  • 7
    • 0023922661 scopus 로고
    • Escherichia coli secretion of an active chimeric antibody fragment
    • Better, M., C. P. Chang, R. R. Robinson, and A. H. Horowitz. 1988. Escherichia coli secretion of an active chimeric antibody fragment. Science 240: 2041-2043.
    • (1988) Science , vol.240 , pp. 2041-2043
    • Better, M.1    Chang, C.P.2    Robinson, R.R.3    Horowitz, A.H.4
  • 8
    • 0025357084 scopus 로고
    • FtsZ regulates frequency of cell division in Escherichia coli
    • Bi, E., and J. Lutkenhaus. 1990. FtsZ regulates frequency of cell division in Escherichia coli. J. Bacteriol. 172:2765-2768.
    • (1990) J. Bacteriol. , vol.172 , pp. 2765-2768
    • Bi, E.1    Lutkenhaus, J.2
  • 9
    • 0014044956 scopus 로고
    • Production and ultrastructure of lysozyme and ethylenediaminetetraacetate-lysozyme spheroplasts of Escherichia coli
    • Birdsell, D. C., and E. H. Cota-Robles. 1963. Production and ultrastructure of lysozyme and ethylenediaminetetraacetate-lysozyme spheroplasts of Escherichia coli. J. Bacteriol. 93:427-437.
    • (1963) J. Bacteriol. , vol.93 , pp. 427-437
    • Birdsell, D.C.1    Cota-Robles, E.H.2
  • 10
    • 0026721559 scopus 로고
    • Abnormal fractionation of β-lactamase in Escherichia coli: Evidence for an interaction with the inner membrane in the absence of a leader peptide
    • Bowden, G. A., F. Baneyx, and G. Georgiou. 1992. Abnormal fractionation of β-lactamase in Escherichia coli: evidence for an interaction with the inner membrane in the absence of a leader peptide. J. Bacteriol. 174:3407-3410.
    • (1992) J. Bacteriol. , vol.174 , pp. 3407-3410
    • Bowden, G.A.1    Baneyx, F.2    Georgiou, G.3
  • 11
    • 0027499213 scopus 로고
    • Immunogold localization of the DnaK heat shock protein in Escherichia coli cells
    • Bukau, B., P. Reilly, J. McCarty, and G. C. Walker. 1993. Immunogold localization of the DnaK heat shock protein in Escherichia coli cells. J Gen. Microbiol. 139:95-99.
    • (1993) J Gen. Microbiol. , vol.139 , pp. 95-99
    • Bukau, B.1    Reilly, P.2    McCarty, J.3    Walker, G.C.4
  • 12
    • 0017807890 scopus 로고
    • Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid
    • Chang, A., and S. N. Cohen. 1978. Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid. J. Bacteriol. 134:1141-1156.
    • (1978) J. Bacteriol. , vol.134 , pp. 1141-1156
    • Chang, A.1    Cohen, S.N.2
  • 13
    • 0028326431 scopus 로고
    • Three-dimensional solution structure of Escherichia coli periplasmic cyclophilin
    • Clubb, R. T., S. B. Ferguson, C. T. Walsh, and G. Wagner. 1994. Three-dimensional solution structure of Escherichia coli periplasmic cyclophilin. Biochemistry 33:2761-2772.
    • (1994) Biochemistry , vol.33 , pp. 2761-2772
    • Clubb, R.T.1    Ferguson, S.B.2    Walsh, C.T.3    Wagner, G.4
  • 14
    • 0025335432 scopus 로고
    • Evidence for export of a muscle lectin from cytosol to extracellular matrix and for a novel secretory mechanism
    • Cooper, D. N. W., and S. H. Barondes. 1990. Evidence for export of a muscle lectin from cytosol to extracellular matrix and for a novel secretory mechanism. J. Cell Biol. 110:1681-1691.
    • (1990) J. Cell Biol. , vol.110 , pp. 1681-1691
    • Cooper, D.N.W.1    Barondes, S.H.2
  • 15
    • 0028061311 scopus 로고
    • Heat shock proteins and molecular chaperones: Mediators of protein conformation and turnover in the cell
    • Craig, E. A., J. S. Weissman, and A. L. Horwich. 1994. Heat shock proteins and molecular chaperones: mediators of protein conformation and turnover in the cell. Cell 78:365-372.
    • (1994) Cell , vol.78 , pp. 365-372
    • Craig, E.A.1    Weissman, J.S.2    Horwich, A.L.3
  • 16
    • 0025293361 scopus 로고
    • Biotinylation of proteins in vivo
    • Cronan, J., and E. John. 1990. Biotinylation of proteins in vivo. J. Biol. Chem. 265:10327-10333.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10327-10333
    • Cronan, J.1    John, E.2
  • 17
    • 0025733254 scopus 로고
    • ftsZ is an essential cell division gene in Escherichia coli
    • Dai, K., and J. Lutkenhaus. 1991. ftsZ is an essential cell division gene in Escherichia coli. J. Bacteriol. 173:3500-3506.
    • (1991) J. Bacteriol. , vol.173 , pp. 3500-3506
    • Dai, K.1    Lutkenhaus, J.2
  • 18
    • 0028907619 scopus 로고
    • Gratuitous overexpression of genes in Escherichia coli leads to growth inhibition and ribosome destruction
    • Dong, H. 1995. Gratuitous overexpression of genes in Escherichia coli leads to growth inhibition and ribosome destruction. J. Bacteriol. 177:1497-1504.
    • (1995) J. Bacteriol. , vol.177 , pp. 1497-1504
    • Dong, H.1
  • 19
    • 0023274512 scopus 로고
    • Silent and functional changes in the periplasmic maltose-binding protein of Escherichia coli K12. I. Transport of maltose
    • Duplay, P., S. Szmelcman, H. Bedouelle, and M. Hofnung. 1987. Silent and functional changes in the periplasmic maltose-binding protein of Escherichia coli K12. I. Transport of maltose. J. Mol. Biol. 194:663-673.
    • (1987) J. Mol. Biol. , vol.194 , pp. 663-673
    • Duplay, P.1    Szmelcman, S.2    Bedouelle, H.3    Hofnung, M.4
  • 20
    • 0028064967 scopus 로고
    • SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion
    • Economou, A., and W. Wickner. 1994. SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion. Cell 78:835-843.
    • (1994) Cell , vol.78 , pp. 835-843
    • Economou, A.1    Wickner, W.2
  • 21
    • 0025954704 scopus 로고
    • Interleukin 1 receptor antagonist is a member of the interleukin 1 gene family: Evolution of a cytokine control mechanism
    • Eisenberg, S. P., M. T. Brewer, E. Verderber, P. Heimdal, B. J. Brandhuber, and R. C. Thompson. 1991. Interleukin 1 receptor antagonist is a member of the interleukin 1 gene family: evolution of a cytokine control mechanism. Proc. Natl. Acad. Sci. USA 88:5232-5236.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5232-5236
    • Eisenberg, S.P.1    Brewer, M.T.2    Verderber, E.3    Heimdal, P.4    Brandhuber, B.J.5    Thompson, R.C.6
  • 22
    • 0027132575 scopus 로고
    • ABC transporters: Bacterial exporters
    • Fath, M. J., and R. Kolter. 1993. ABC transporters: bacterial exporters. Microbiol. Rev. 57:995-1017.
    • (1993) Microbiol. Rev. , vol.57 , pp. 995-1017
    • Fath, M.J.1    Kolter, R.2
  • 23
    • 0028102530 scopus 로고
    • PrlA and PrlG suppressors reduce the requirement for signal sequence recognition
    • Flower, A. M., R. C. Doebele, and T. J. Silhavy. 1994. PrlA and PrlG suppressors reduce the requirement for signal sequence recognition. J. Bacteriol. 176:5607-5614.
    • (1994) J. Bacteriol. , vol.176 , pp. 5607-5614
    • Flower, A.M.1    Doebele, R.C.2    Silhavy, T.J.3
  • 24
    • 0028361309 scopus 로고
    • Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones
    • Frydman, J., E. Nimmesgern, K. Ohtsuka, and R. U. Hartl. 1994. Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones. Nature 370:111-117.
    • (1994) Nature , vol.370 , pp. 111-117
    • Frydman, J.1    Nimmesgern, E.2    Ohtsuka, K.3    Hartl, R.U.4
  • 25
    • 0017840096 scopus 로고
    • Role of murein lipoprotein in morphogenesis of the bacterial division septum: Phenotypic similarity of lkyD and lpo mutants
    • Fung, J., T. J. MacAlister, and L. I. Rothfield. 1978. Role of murein lipoprotein in morphogenesis of the bacterial division septum: phenotypic similarity of lkyD and lpo mutants. J. Bacteriol. 133:1467-1471.
    • (1978) J. Bacteriol. , vol.133 , pp. 1467-1471
    • Fung, J.1    MacAlister, T.J.2    Rothfield, L.I.3
  • 26
    • 0018956210 scopus 로고
    • Morphogenesis of the bacterial division septum: Identification of potential sites of division of lkyD mutants of Salmonella typhimurium
    • Fung, J. C., T. J. MacAlister, R. A. Weigand, and L. I. Rothfield. 1980. Morphogenesis of the bacterial division septum: identification of potential sites of division of lkyD mutants of Salmonella typhimurium. J. Bacteriol. 143:1019-1024.
    • (1980) J. Bacteriol. , vol.143 , pp. 1019-1024
    • Fung, J.C.1    MacAlister, T.J.2    Weigand, R.A.3    Rothfield, L.I.4
  • 27
    • 0025259865 scopus 로고
    • A point mutation uncouples human interleukin-1β biological activity and receptor binding
    • Gehrke, L., S. A. Jobling, L. S. K. Paik, B. McDonald, L. J. Rosenwasser, and P. E. Auron. 1990. A point mutation uncouples human interleukin-1β biological activity and receptor binding. J. Biol. Chem. 265:5922-5925.
    • (1990) J. Biol. Chem. , vol.265 , pp. 5922-5925
    • Gehrke, L.1    Jobling, S.A.2    Paik, L.S.K.3    McDonald, B.4    Rosenwasser, L.J.5    Auron, P.E.6
  • 28
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose p-BAD promoter
    • Guzman, L.-M., D. Belin, M. J. Carson, and J. Beckwith. 1995. Tight regulation, modulation, and high-level expression by vectors containing the arabinose p-BAD promoter. J. Bacteriol. 177:4121-4130.
    • (1995) J. Bacteriol. , vol.177 , pp. 4121-4130
    • Guzman, L.-M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 29
    • 0027940215 scopus 로고
    • Incomplete arrest in the outer membrane sorts NADH-cytochrome b5 reductase to two different submitochondrial compartments
    • Hahne, K., V. Haucke, L. Ramage, and G. Schatz. 1994. Incomplete arrest in the outer membrane sorts NADH-cytochrome b5 reductase to two different submitochondrial compartments. Cell 79:829-839.
    • (1994) Cell , vol.79 , pp. 829-839
    • Hahne, K.1    Haucke, V.2    Ramage, L.3    Schatz, G.4
  • 30
    • 0011889163 scopus 로고
    • Localization of thioredoxin, thioredoxin reductase and ribonucleotide reductase in cells: Immunohistochemical aspects
    • A. Holmgren, C.-I. Brändén, H. Jörnvall, and B.-M. Sjöberg (ed.) Raven Press, New York, N.Y.
    • Hansson, H., A. Holmgren, B. Rozell, and S. Stemme. 1986. Localization of thioredoxin, thioredoxin reductase and ribonucleotide reductase in cells: immunohistochemical aspects, p. 177-187. In A. Holmgren, C.-I. Brändén, H. Jörnvall, and B.-M. Sjöberg (ed.), Thioredoxin and glutaredoxin systems. Raven Press, New York, N.Y.
    • (1986) Thioredoxin and Glutaredoxin Systems , pp. 177-187
    • Hansson, H.1    Holmgren, A.2    Rozell, B.3    Stemme, S.4
  • 31
    • 0029043218 scopus 로고
    • Suppression of signal sequence defects and azide resistance in Escherichia coli commonly result from the same mutations in secA
    • Huie, J. L., and T. J. Silhavy. 1995. Suppression of signal sequence defects and azide resistance in Escherichia coli commonly result from the same mutations in secA. J. Bacteriol. 177:3518-3526.
    • (1995) J. Bacteriol. , vol.177 , pp. 3518-3526
    • Huie, J.L.1    Silhavy, T.J.2
  • 33
    • 0017065028 scopus 로고
    • Properties of a major protein released from Escherichia coli by osmotic shock
    • Jacobson, G. R., B. J. Takacs, and J. P. Rosenbusch. 1976. Properties of a major protein released from Escherichia coli by osmotic shock. Biochemistry 15:2297-2303.
    • (1976) Biochemistry , vol.15 , pp. 2297-2303
    • Jacobson, G.R.1    Takacs, B.J.2    Rosenbusch, J.P.3
  • 34
    • 0027251266 scopus 로고
    • The Escherichia coli K-12 "wild types" W3110 and MG1655 have an rph frameshift mutation that leads to pyrimidine starvation due to low pyrE expression levels
    • Jensen, K. F. 1993. The Escherichia coli K-12 "wild types" W3110 and MG1655 have an rph frameshift mutation that leads to pyrimidine starvation due to low pyrE expression levels. J. Bacteriol. 175:3401-3407.
    • (1993) J. Bacteriol. , vol.175 , pp. 3401-3407
    • Jensen, K.F.1
  • 35
    • 0028583118 scopus 로고
    • Recombinant proteins can be isolated from E. coli cells by repeated cycles of freezing and thawing
    • Johnson, B. H., and M. H. Hecht. 1994. Recombinant proteins can be isolated from E. coli cells by repeated cycles of freezing and thawing. Bio/ Technology 12:1357-1360.
    • (1994) Bio/ Technology , vol.12 , pp. 1357-1360
    • Johnson, B.H.1    Hecht, M.H.2
  • 36
    • 0025133455 scopus 로고
    • Biosynthesis of a membrane adhesion zone fraction throughout the cell cycle of Escherichia coli
    • Joseleau-Petit, D., F. Kepes, L. Peutat, R. D'Ari, and L. I. Rothfield. 1990. Biosynthesis of a membrane adhesion zone fraction throughout the cell cycle of Escherichia coli. J. Bacteriol. 172:6573-6575.
    • (1990) J. Bacteriol. , vol.172 , pp. 6573-6575
    • Joseleau-Petit, D.1    Kepes, F.2    Peutat, L.3    D'Ari, R.4    Rothfield, L.I.5
  • 37
    • 0025303732 scopus 로고
    • Human recombinant interleukin-1β isolated from Escherichia coli by simple osmotic shock
    • Joseph-Liauzun, E., P. Leplatois, R. Legoux, V. Guerveno, E. Marchese, and P. Ferrara. 1990. Human recombinant interleukin-1β isolated from Escherichia coli by simple osmotic shock. Gene 86:291-295.
    • (1990) Gene , vol.86 , pp. 291-295
    • Joseph-Liauzun, E.1    Leplatois, P.2    Legoux, R.3    Guerveno, V.4    Marchese, E.5    Ferrara, P.6
  • 38
    • 0029016348 scopus 로고
    • Physiological and biochemical analysis of the effects of alkaline phosphatase overproduction in Escherichia coli
    • Kadokura, H., K. Watanabe, K. Tsuneizumi, K. Yoda, and M. Yamasaki. 1995. Physiological and biochemical analysis of the effects of alkaline phosphatase overproduction in Escherichia coli. J. Bacteriol. 177:3596-3600.
    • (1995) J. Bacteriol. , vol.177 , pp. 3596-3600
    • Kadokura, H.1    Watanabe, K.2    Tsuneizumi, K.3    Yoda, K.4    Yamasaki, M.5
  • 39
    • 0026567097 scopus 로고
    • Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme
    • Kamitani, S., Y. Akiyama, and K. Ito. 1991. Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme. EMBO J. 11:57-62.
    • (1991) EMBO J. , vol.11 , pp. 57-62
    • Kamitani, S.1    Akiyama, Y.2    Ito, K.3
  • 40
    • 0025314999 scopus 로고
    • The 'Bayer bridges' confronted with results from improved electron microscopy methods
    • Kelenberger, E. 1990. The 'Bayer bridges' confronted with results from improved electron microscopy methods. Mol. Microbiol. 4:697-705.
    • (1990) Mol. Microbiol. , vol.4 , pp. 697-705
    • Kelenberger, E.1
  • 41
    • 0027551081 scopus 로고
    • Bacterial signal peptide-independent protein export: Hylβ-directed secretion of hemolysin
    • Koronakis, V., and C. Hughes. 1993. Bacterial signal peptide-independent protein export: hylβ-directed secretion of hemolysin. Semin. Cell Biol. 4:7-15.
    • (1993) Semin. Cell Biol. , vol.4 , pp. 7-15
    • Koronakis, V.1    Hughes, C.2
  • 42
    • 0026728215 scopus 로고
    • Secretion of peptides and proteins lacking hydrophobic signal sequences: The role of adenosine triphosphate-driven membrane translocators
    • Kuchler, K., and J. Thorner. 1992. Secretion of peptides and proteins lacking hydrophobic signal sequences: the role of adenosine triphosphate-driven membrane translocators. Endocrine Rev. 13:499-514.
    • (1992) Endocrine Rev. , vol.13 , pp. 499-514
    • Kuchler, K.1    Thorner, J.2
  • 43
    • 0025325366 scopus 로고
    • Peptidyl-prolyl cis-trans-isomerase from Escherichia coli: A periplasmic homolog of cyclophilin that is not inhibited by cyclosporin A
    • Liu, J., and C. Walsh. 1990. Peptidyl-prolyl cis-trans-isomerase from Escherichia coli: a periplasmic homolog of cyclophilin that is not inhibited by cyclosporin A. Proc. Natl. Acad. Sci. USA 87:4028-4032.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4028-4032
    • Liu, J.1    Walsh, C.2
  • 44
    • 0026024747 scopus 로고
    • Nucleotide sequence of the Escherichia coli recJ chromosomal region and construction of RecJ-overexpression plasmids
    • Lovett, S. T., and R. D. Kolodner. 1991. Nucleotide sequence of the Escherichia coli recJ chromosomal region and construction of RecJ-overexpression plasmids. J. Bacteriol. 173:353-364.
    • (1991) J. Bacteriol. , vol.173 , pp. 353-364
    • Lovett, S.T.1    Kolodner, R.D.2
  • 45
    • 0020448702 scopus 로고
    • Localization of thioredoxin from Escherichia coli in an osmotically sensitive compartment
    • Lunn, C. A., and V. P. Pigiet. 1982. Localization of thioredoxin from Escherichia coli in an osmotically sensitive compartment. J. Biol. Chem. 257: 11424-11430.
    • (1982) J. Biol. Chem. , vol.257 , pp. 11424-11430
    • Lunn, C.A.1    Pigiet, V.P.2
  • 46
    • 0027373949 scopus 로고
    • Crystal structure of the DsbA protein required for disulphide bond formation in vivo
    • Martin, J. L., C. A. Bardwell, and J. Kuryan. 1993. Crystal structure of the DsbA protein required for disulphide bond formation in vivo. Nature 365: 464-468.
    • (1993) Nature , vol.365 , pp. 464-468
    • Martin, J.L.1    Bardwell, C.A.2    Kuryan, J.3
  • 47
    • 0020581487 scopus 로고
    • Mutations that alter the signal sequence of alkaline phosphatase in Escherichia coli
    • Michaelis, S., H. Inouye, D. Oliver, and J. Beckwith. 1983. Mutations that alter the signal sequence of alkaline phosphatase in Escherichia coli. J. Bacteriol. 154:366-374.
    • (1983) J. Bacteriol. , vol.154 , pp. 366-374
    • Michaelis, S.1    Inouye, H.2    Oliver, D.3    Beckwith, J.4
  • 48
  • 49
    • 0028296940 scopus 로고
    • The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation
    • Missiakas, D., C. Georgopoulos, and S. Raina. 1994. The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation. EMBO J. 13:2013-2020.
    • (1994) EMBO J. , vol.13 , pp. 2013-2020
    • Missiakas, D.1    Georgopoulos, C.2    Raina, S.3
  • 50
    • 76549170704 scopus 로고
    • The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts
    • Neu, H. C., and L. A. Heppel. 1965. The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts. J. Biol. Chem. 240:3685-3691.
    • (1965) J. Biol. Chem. , vol.240 , pp. 3685-3691
    • Neu, H.C.1    Heppel, L.A.2
  • 51
    • 0026668342 scopus 로고
    • Characterization of a periplasmic thiol: Disulfide interchange protein required for the functional maturation of secreted virulence factors of Vibrio cholerae
    • Peek, J. A., and R. K. Taylor. 1992. Characterization of a periplasmic thiol: disulfide interchange protein required for the functional maturation of secreted virulence factors of Vibrio cholerae. Proc. Natl. Acad. Sci. USA 89: 6210-6214.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6210-6214
    • Peek, J.A.1    Taylor, R.K.2
  • 52
    • 0024804106 scopus 로고
    • Crystallographic refinement of interleukin-1β at 2.0 Å resolution
    • Priestle, J. P., H. Schär, and M. G. Grütter. 1989. Crystallographic refinement of interleukin-1β at 2.0 Å resolution. Proc. Natl. Acad. Sci. USA 86:9667-9671.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9667-9671
    • Priestle, J.P.1    Schär, H.2    Grütter, M.G.3
  • 53
    • 0027450561 scopus 로고
    • The complete general secretory pathway in gram-negative bacteria
    • Pugsley, A. P. 1993. The complete general secretory pathway in gram-negative bacteria. Microbiol. Rev. 57:50-108.
    • (1993) Microbiol. Rev. , vol.57 , pp. 50-108
    • Pugsley, A.P.1
  • 54
    • 0022002006 scopus 로고
    • Location of some proteins involved in peptidoglycan synthesis and cell division in the inner and outer membranes of Escherichia coli
    • Rodríguez-Tébar, A., J. A. Barbas, and D. Vázguez. 1985. Location of some proteins involved in peptidoglycan synthesis and cell division in the inner and outer membranes of Escherichia coli. J. Bacteriol. 161:243-248.
    • (1985) J. Bacteriol. , vol.161 , pp. 243-248
    • Rodríguez-Tébar, A.1    Barbas, J.A.2    Vázguez, D.3
  • 55
    • 0023464708 scopus 로고
    • Vectors for selective expression of cloned DNAs by T7 RNA polymerase
    • Rosenberg, A., B. Lade, D. Chui, S. Lin, J. Dunn, and F. Studier. 1987. Vectors for selective expression of cloned DNAs by T7 RNA polymerase. Gene 56:125-135.
    • (1987) Gene , vol.56 , pp. 125-135
    • Rosenberg, A.1    Lade, B.2    Chui, D.3    Lin, S.4    Dunn, J.5    Studier, F.6
  • 57
    • 0026443077 scopus 로고
    • Secretion of thioredoxin by normal and neoplastic cells through a leaderless secretory pathway
    • Rubartelli, A., A. Bajetto, G. Allavena, E. Wollman, and R. Sitia. 1992. Secretion of thioredoxin by normal and neoplastic cells through a leaderless secretory pathway. J. Biol. Chem. 267:24161-24164.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24161-24164
    • Rubartelli, A.1    Bajetto, A.2    Allavena, G.3    Wollman, E.4    Sitia, R.5
  • 58
    • 0025255629 scopus 로고
    • A novel secretory pathway for interleukin-1b, a protein lacking a signal sequence
    • Rubartelli, A., F. Cozzolino, M. Talio, and R. Sitia. 1990. A novel secretory pathway for interleukin-1b, a protein lacking a signal sequence. EMBO J. 9:1503-1510.
    • (1990) EMBO J. , vol.9 , pp. 1503-1510
    • Rubartelli, A.1    Cozzolino, F.2    Talio, M.3    Sitia, R.4
  • 59
    • 0039310043 scopus 로고
    • Use of peptide libraries to map the substrate specificity of a peptide-modifying enzyme: A 13 residue consensus peptide specificities biotinylation in Escherichia coli
    • Schatz, P. J. 1993. Use of peptide libraries to map the substrate specificity of a peptide-modifying enzyme: a 13 residue consensus peptide specificities biotinylation in Escherichia coli. Bio/Technology 11:1138-1143.
    • (1993) Bio/Technology , vol.11 , pp. 1138-1143
    • Schatz, P.J.1
  • 60
    • 0027156394 scopus 로고
    • Protein localization and asymmetry in the bacterial cell
    • Shapiro, L. 1993. Protein localization and asymmetry in the bacterial cell. Cell 73:841-855.
    • (1993) Cell , vol.73 , pp. 841-855
    • Shapiro, L.1
  • 61
    • 0028215226 scopus 로고
    • Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity
    • Shevchik, V. E., G. Condemine, and J. Robert-Baudouy. 1994. Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity. EMBO J. 13:2007-2012.
    • (1994) EMBO J. , vol.13 , pp. 2007-2012
    • Shevchik, V.E.1    Condemine, G.2    Robert-Baudouy, J.3
  • 62
    • 1842301899 scopus 로고
    • Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • Silhavy, T. J. 1984. Experiments in molecular genetics, p. xi-xii. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • (1984) Experiments in Molecular Genetics
    • Silhavy, T.J.1
  • 63
    • 0023845961 scopus 로고
    • Interleukin-1β is localized in the cytoplasmic ground substance but is largely absent from the Golgi apparatus and plasma membranes of stimulated human monocytes
    • Singer, I. I., S. Scott, G. L. Hall, G. Limjuco, J. Chin, and J. A. Schmidt. 1988. Interleukin-1β is localized in the cytoplasmic ground substance but is largely absent from the Golgi apparatus and plasma membranes of stimulated human monocytes. J. Exp. Med. 167:389-407.
    • (1988) J. Exp. Med. , vol.167 , pp. 389-407
    • Singer, I.I.1    Scott, S.2    Hall, G.L.3    Limjuco, G.4    Chin, J.5    Schmidt, J.A.6
  • 64
    • 0028983021 scopus 로고
    • β-Galactosidase is inactivated by intermolecular disulfide bonds and is toxic when secreted to the periplasm of Escherichia coli
    • Snyder, W. B., and T. J. Silhavy. 1995. β-Galactosidase is inactivated by intermolecular disulfide bonds and is toxic when secreted to the periplasm of Escherichia coli. J. Bacteriol. 177:953-63.
    • (1995) J. Bacteriol. , vol.177 , pp. 953-963
    • Snyder, W.B.1    Silhavy, T.J.2
  • 65
    • 0023738918 scopus 로고
    • Production and characterization of human basic fibroblast growth factor from Escherichia coli
    • Squires, C. H., J. Childs, S. P. Eisenberg, P. J. Polverini, and A. Sommer. 1988. Production and characterization of human basic fibroblast growth factor from Escherichia coli. J. Biol. Chem. 263:16297-16302.
    • (1988) J. Biol. Chem. , vol.263 , pp. 16297-16302
    • Squires, C.H.1    Childs, J.2    Eisenberg, S.P.3    Polverini, P.J.4    Sommer, A.5
  • 66
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier, F. W., and B. A. Moffatt. 1986. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189:113-130.
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 67
    • 0028170807 scopus 로고
    • Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane
    • Walter, P., and A. E. Johnson. 1994. Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane. Annu. Rev. Cell Biol. 10:87-119.
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 87-119
    • Walter, P.1    Johnson, A.E.2
  • 68
    • 0024360758 scopus 로고
    • The sequence of the mouse 14kDa β-galactoside-binding lectin and evidence for its synthesis on free cytoplasmic ribosomes
    • Wilson, T. J. G., M. N. Firth, J. T. Powell, and R. L. Harrison. 1989. The sequence of the mouse 14kDa β-galactoside-binding lectin and evidence for its synthesis on free cytoplasmic ribosomes. Biochem. J. 261:847-852.
    • (1989) Biochem. J. , vol.261 , pp. 847-852
    • Wilson, T.J.G.1    Firth, M.N.2    Powell, J.T.3    Harrison, R.L.4
  • 69
    • 84886622040 scopus 로고
    • An efficient and reproducible procedure for the formation of spheroplasts from variously grown Escherichia coli
    • Wiltholt, B., M. Boekhout, M. Brock, J. Kingma, H. Van Heerikhuizen, and L. De Leij. 1976. An efficient and reproducible procedure for the formation of spheroplasts from variously grown Escherichia coli. Anal. Biochem. 74: 160-170.
    • (1976) Anal. Biochem. , vol.74 , pp. 160-170
    • Wiltholt, B.1    Boekhout, M.2    Brock, M.3    Kingma, J.4    Van Heerikhuizen, H.5    De Leij, L.6
  • 70
    • 0028153243 scopus 로고
    • Localization of DnaK (chaperone 70) from Escherichia coli in an osmotic-shock-sensitive compartment of the cytoplasm
    • Yaagoubi, A. E., M. Kohiyama, and G. Richarme. 1994. Localization of DnaK (chaperone 70) from Escherichia coli in an osmotic-shock-sensitive compartment of the cytoplasm. J. Bacteriol. 176:7074-7078.
    • (1994) J. Bacteriol. , vol.176 , pp. 7074-7078
    • Yaagoubi, A.E.1    Kohiyama, M.2    Richarme, G.3
  • 71
    • 0026323941 scopus 로고
    • Three-dimensional structure of human basic fibroblast growth factor, a structural homolog of interleukin-1β
    • Zhang, J., L. S. Cousens, P. J. Barr, and S. R. Sprang. 1991. Three-dimensional structure of human basic fibroblast growth factor, a structural homolog of interleukin-1β. Proc. Natl. Acad. Sci. USA 88:3446-3450.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3446-3450
    • Zhang, J.1    Cousens, L.S.2    Barr, P.J.3    Sprang, S.R.4


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