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Volumn 10, Issue 24, 1996, Pages 3170-3182

SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins

Author keywords

extra cytoplasmic stress; LamB; outer membrane proteins; parvulins; Peptidyl prolyl isomerases; protein folding; SurA

Indexed keywords

BACTERIAL PROTEIN; CYTOPLASM PROTEIN; ISOMERASE; MALTODEXTRIN; OUTER MEMBRANE PROTEIN; PORIN;

EID: 0030476750     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.10.24.3170     Document Type: Article
Times cited : (258)

References (65)
  • 1
    • 0028143610 scopus 로고
    • The cyclophilin homolog NinaA functions as a chaperone, forming a stable complex in vivo with its protein target rhodopsin
    • Baker, E.K., N.J. Colley, and C.S. Zuker. 1994. The cyclophilin homolog NinaA functions as a chaperone, forming a stable complex in vivo with its protein target rhodopsin. EMBO J. 13: 4886-4895.
    • (1994) EMBO J. , vol.13 , pp. 4886-4895
    • Baker, E.K.1    Colley, N.J.2    Zuker, C.S.3
  • 2
    • 0026091179 scopus 로고
    • Identification of a protein required for disulfide bond formation in vivo
    • Bardwell, J.C, 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.1    McGovern, K.2    Beckwith, J.3
  • 3
    • 0019859523 scopus 로고
    • Regulation of the OmpA outer membrane protein of Escherichia coli
    • Beher, M.G. and C.A. Schnaitman. 1981. Regulation of the OmpA outer membrane protein of Escherichia coli. J. Bacteriol. 147: 972-985.
    • (1981) J. Bacteriol. , vol.147 , pp. 972-985
    • Beher, M.G.1    Schnaitman, C.A.2
  • 5
    • 0023404465 scopus 로고
    • Export of protein in Escherichia coli: A novel mutation in ompC affects expression of other major outer membrane proteins
    • Catron, K.M. and C.A. Schnaitman. 1987. Export of protein in Escherichia coli: A novel mutation in ompC affects expression of other major outer membrane proteins. J. Bacteriol. 169: 4327-4334.
    • (1987) J. Bacteriol. , vol.169 , pp. 4327-4334
    • Catron, K.M.1    Schnaitman, C.A.2
  • 7
    • 0029886388 scopus 로고    scopus 로고
    • A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins
    • Chen, R. and U. Henning. 1996. A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins. Mol. Microbiol. 19: 1287-1294.
    • (1996) Mol. Microbiol. , vol.19 , pp. 1287-1294
    • Chen, R.1    Henning, U.2
  • 8
    • 0024568867 scopus 로고
    • Export-defective lamB protein is a target for translation control caused by ompC porin overexpression
    • Click, E.M. and C.A. Schnaitman. 1989. Export-defective lamB protein is a target for translation control caused by ompC porin overexpression. J. Bacteriol. 171: 616-619.
    • (1989) J. Bacteriol. , vol.171 , pp. 616-619
    • Click, E.M.1    Schnaitman, C.A.2
  • 9
    • 0024009622 scopus 로고
    • Translation control of exported proteins that result from OmpC porin overexpression
    • Click, E.M., G.A. McDonald, and C.A. Schnaitman. 1988. Translation control of exported proteins that result from OmpC porin overexpression. J. Bacteriol. 170: 2005-2011.
    • (1988) J. Bacteriol. , vol.170 , pp. 2005-2011
    • Click, E.M.1    McDonald, G.A.2    Schnaitman, C.A.3
  • 10
    • 0025995535 scopus 로고
    • The cyclophilin homolog ninaA is required in the secretory pathway
    • Colley, N.J., E.K. Baker, M.A. Stamnes, and C.S. Zuker. 1991. The cyclophilin homolog ninaA is required in the secretory pathway. Cell 67: 255-263.
    • (1991) Cell , vol.67 , pp. 255-263
    • Colley, N.J.1    Baker, E.K.2    Stamnes, M.A.3    Zuker, C.S.4
  • 11
    • 0027323456 scopus 로고
    • Chaperones: Helpers along the pathways to protein folding
    • Craig, E.A. 1993. Chaperones: Helpers along the pathways to protein folding. Science 260: 1902-1903.
    • (1993) Science , vol.260 , pp. 1902-1903
    • Craig, E.A.1
  • 12
    • 0027300506 scopus 로고
    • Heat shock proteins: Molecular chaperones of protein biogenesis
    • Craig, E.A., B.D. Gambill, and R.J. Nelson. 1993. Heat shock proteins: Molecular chaperones of protein biogenesis. Microbiol Rev. 52: 402-414.
    • (1993) Microbiol Rev. , vol.52 , pp. 402-414
    • Craig, E.A.1    Gambill, B.D.2    Nelson, R.J.3
  • 13
    • 0025239037 scopus 로고
    • In vitro trimerization of outer membrane protein PhoE
    • De Cock, H., D. Hekstra, and J. Tommassen. 1990a. In vitro trimerization of outer membrane protein PhoE. Biochimie 72:177-182.
    • (1990) Biochimie , vol.72 , pp. 177-182
    • De Cock, H.1    Hekstra, D.2    Tommassen, J.3
  • 14
    • 0025214278 scopus 로고
    • Assembly of an in vitro synthesized Escherichia coli outer membrane porin into its stable trimeric configuration
    • De Cock, H., R. Hendriks, T. De Vrije, and J. Tommassen. 1990b. Assembly of an in vitro synthesized Escherichia coli outer membrane porin into its stable trimeric configuration. J. Biol. Chem. 265:4646-4651.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4646-4651
    • De Cock, H.1    Hendriks, R.2    De Vrije, T.3    Tommassen, J.4
  • 15
    • 0028981355 scopus 로고
    • A novel function of Escherichia coli chaperone DnaJ. Protein-disulfide isomerase
    • de Crouy-Chanel, A., M. Kohiyama, and G. Richarme. 1995. A novel function of Escherichia coli chaperone DnaJ. Protein-disulfide isomerase. J. Biol. Chem. 270: 22669-22672.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22669-22672
    • De Crouy-Chanel, A.1    Kohiyama, M.2    Richarme, G.3
  • 16
    • 0020052686 scopus 로고
    • Relationship between the OmpC and LamB proteins of Escherichia coli and its influence on the protein mass of the Outer Membrane
    • Diedrich, D.L. and J.A. Fralick. 1982. Relationship between the OmpC and LamB proteins of Escherichia coli and its influence on the protein mass of the Outer Membrane. J. Bacteriol. 149: 156-160.
    • (1982) J. Bacteriol. , vol.149 , pp. 156-160
    • Diedrich, D.L.1    Fralick, J.A.2
  • 17
    • 0024727149 scopus 로고
    • Identification of the sigma e subunit of Escherichia coli RNA polymerase: A second alternate sigma factor involved in high-temperture gene expression
    • Erikson, J.W. and C.A. Gross. 1989. Identification of the sigma E subunit of Escherichia coli RNA polymerase: A second alternate sigma factor involved in high-temperture gene expression. Genes & Dev. 3: 1462-1471.
    • (1989) Genes & Dev. , vol.3 , pp. 1462-1471
    • Erikson, J.W.1    Gross, C.A.2
  • 18
    • 0027940713 scopus 로고
    • Specific incorporation of cyclophilin A into HIV-1 virions
    • Franke, E.K., H.E. Yuan, and J. Luban. 1994. Specific incorporation of cyclophilin A into HIV-1 virions. Nature 372:359-362.
    • (1994) Nature , vol.372 , pp. 359-362
    • Franke, E.K.1    Yuan, H.E.2    Luban, J.3
  • 19
    • 0026499641 scopus 로고
    • Isomerase and chaperone activity of prolyl isomerase in the folding of carbonic anhydrase
    • Freskgard, P.O., N. Bergenhem, B.H. Jonsson, M. Svensson, and U. Carlsson. 1992. Isomerase and chaperone activity of prolyl isomerase in the folding of carbonic anhydrase. Science 258: 466-468.
    • (1992) Science , vol.258 , pp. 466-468
    • Freskgard, P.O.1    Bergenhem, N.2    Jonsson, B.H.3    Svensson, M.4    Carlsson, U.5
  • 21
    • 0019766123 scopus 로고
    • Genetic analysis of the major outer membrane proteins of Escherichia coli
    • Hall, M.N. and T.J. Silhavy. 1981. Genetic analysis of the major outer membrane proteins of Escherichia coli. Annu. Rev. Genet. 15:91-142.
    • (1981) Annu. Rev. Genet. , vol.15 , pp. 91-142
    • Hall, M.N.1    Silhavy, T.J.2
  • 22
    • 0029069724 scopus 로고
    • PTF1 encodes an essential protein in Saccharomyces cerevisiae, which shows strong homology with a new putative family of PPIases
    • Hani, J., G. Stumpf, and H. Domdey. 1995. PTF1 encodes an essential protein in Saccharomyces cerevisiae, which shows strong homology with a new putative family of PPIases. FEBS Lett. 365: 198-202.
    • (1995) FEBS Lett. , vol.365 , pp. 198-202
    • Hani, J.1    Stumpf, G.2    Domdey, H.3
  • 23
    • 0025033676 scopus 로고
    • Genes required for formation of the apoMoFe protein of Klebsiella pneumoniae nitrogenase in Escherichia coli
    • Harris, G.S., T.C. White, J.E. Flory, and W.H. Orme-Johnson. 1990. Genes required for formation of the apoMoFe protein of Klebsiella pneumoniae nitrogenase in Escherichia coli. J. Biol. Chem. 265: 15909-15919.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15909-15919
    • Harris, G.S.1    White, T.C.2    Flory, J.E.3    Orme-Johnson, W.H.4
  • 24
    • 0025756590 scopus 로고
    • Two distinct forms of peptidylprolyl-cis-trans-isomerase are expressed separately in periplasmic and cytoplasmic compartments of Escherichia coli cells
    • Hayano, T., N. Takahashi, S. Kato, N. Maki, and M. Suzuki. 1991. Two distinct forms of peptidylprolyl-cis-trans-isomerase are expressed separately in periplasmic and cytoplasmic compartments of Escherichia coli cells. Biochemistry 30: 3041-3048.
    • (1991) Biochemistry , vol.30 , pp. 3041-3048
    • Hayano, T.1    Takahashi, N.2    Kato, S.3    Maki, N.4    Suzuki, M.5
  • 25
    • 0026542814 scopus 로고
    • Notl genomic cleavage map of Escherichia coli K-12 strain MG1655
    • Heath, J.D, J.D. Perkin, B. Sharma, and G.M. Weinstock. 1992. Notl genomic cleavage map of Escherichia coli K-12 strain MG1655. J. Bacteriol. 174: 558-567.
    • (1992) J. Bacteriol. , vol.174 , pp. 558-567
    • Heath, J.D.1    Perkin, J.D.2    Sharma, B.3    Weinstock, G.M.4
  • 26
    • 0026012156 scopus 로고
    • FK 506-binding protein proline rotamase is a target for the immunosuppressive agent FK 506 in Saccharomyces cerevisiae
    • Heitman, J., N.R. Movva, P.C. Heistand, and M.N. Hall. 1991. FK 506-binding protein proline rotamase is a target for the immunosuppressive agent FK 506 in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. 88: 1948-1952.
    • (1991) Proc. Natl. Acad. Sci. , vol.88 , pp. 1948-1952
    • Heitman, J.1    Movva, N.R.2    Heistand, P.C.3    Hall, M.N.4
  • 27
    • 0000750468 scopus 로고
    • Identification of immunosuppressive drug targets in yeast
    • Heitman, J., A. Koller, M.E. Cardenas, and M.N. Hall. 1993. Identification of immunosuppressive drug targets in yeast. Methods 5: 176-187.
    • (1993) Methods , vol.5 , pp. 176-187
    • Heitman, J.1    Koller, A.2    Cardenas, M.E.3    Hall, M.N.4
  • 28
    • 0029064061 scopus 로고
    • Escherichia coli and other species of the Enterobacteriaceae encode a protein similar to the family of Mip-like FK506-binding proteins
    • Home, S.M. and K.D. Young. 1995. Escherichia coli and other species of the Enterobacteriaceae encode a protein similar to the family of Mip-like FK506-binding proteins. Arch. Microbiol. 163: 357-365.
    • (1995) Arch. Microbiol. , vol.163 , pp. 357-365
    • Home, S.M.1    Young, K.D.2
  • 29
    • 0022607892 scopus 로고
    • Klebsiella pneumoniae nifM gene product is required for stabilization and activation of nitrogenase iron protein in Escherichia coli
    • Howard, K.S., P.A. McLean, F.B. Hansen, P.V. Lemley, K.S. Koblan, and W.H. Orme-Johnson. 1986. Klebsiella pneumoniae nifM gene product is required for stabilization and activation of nitrogenase iron protein in Escherichia coli. J. Biol. Chem. 261: 772-778.
    • (1986) J. Biol. Chem. , vol.261 , pp. 772-778
    • Howard, K.S.1    McLean, P.A.2    Hansen, F.B.3    Lemley, P.V.4    Koblan, K.S.5    Orme-Johnson, W.H.6
  • 30
    • 0028278089 scopus 로고
    • Reassessment of the putative chaperone function of prolyl-cis/transisomerases
    • Kern, G., D. Kern, F.X. Schmid, and G. Fischer. 1994. Reassessment of the putative chaperone function of prolyl-cis/transisomerases. FEBS Lett. 348: 145-148.
    • (1994) FEBS Lett. , vol.348 , pp. 145-148
    • Kern, G.1    Kern, D.2    Schmid, F.X.3    Fischer, G.4
  • 31
    • 0028809455 scopus 로고
    • Characterization of an Escherichia coli rotA mutant, affected in periplasmic peptidyl-prolyl cis/trans isomerase
    • Kleerebezem, M., M. Heutink, and J. Tommassen. 1995. Characterization of an Escherichia coli rotA mutant, affected in periplasmic peptidyl-prolyl cis/trans isomerase. Mol Microbiol 18:313-320.
    • (1995) Mol Microbiol , vol.18 , pp. 313-320
    • Kleerebezem, M.1    Heutink, M.2    Tommassen, J.3
  • 33
    • 0027222723 scopus 로고
    • The PrsA lipoprotein is essential for protein secretion in Bacillus subtilis and sets a limit for high-level secretion
    • Kontinen, V.P. and M. Sarvas. 1993. The PrsA lipoprotein is essential for protein secretion in Bacillus subtilis and sets a limit for high-level secretion. Mol. Microbiol. 8: 727-737.
    • (1993) Mol. Microbiol. , vol.8 , pp. 727-737
    • Kontinen, V.P.1    Sarvas, M.2
  • 34
    • 0029918686 scopus 로고    scopus 로고
    • SurA assists the folding of E. coli outer membrane proteins
    • Lazar, S.W. and R. Kolter. 1996. SurA assists the folding of E. coli outer membrane proteins. J. Bacteriol. 178: 1770-1773.
    • (1996) J. Bacteriol. , vol.178 , pp. 1770-1773
    • Lazar, S.W.1    Kolter, R.2
  • 35
    • 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.T. 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. 87: 4028-4032.
    • (1990) Proc. Natl. Acad. Sci. , vol.87 , pp. 4028-4032
    • Liu, J.1    Walsh, C.T.2
  • 36
    • 0029916122 scopus 로고    scopus 로고
    • A human peptidyl-prolyl isomerase essential for regulation of mitosis
    • Lu, K.P., S.D. Hanes, and T. Hunter. 1996. A human peptidyl-prolyl isomerase essential for regulation of mitosis. Nature 380: 544-547.
    • (1996) Nature , vol.380 , pp. 544-547
    • Lu, K.P.1    Hanes, S.D.2    Hunter, T.3
  • 37
    • 0028077034 scopus 로고
    • The cellular response to unfolded proteins: Intercompartmental signaling
    • McMillan, D.R., M.J. Gething, and J. Sambrook. 1994. The cellular response to unfolded proteins: Intercompartmental signaling. Curr. Opin. Biotechnol. 5: 540-545.
    • (1994) Curr. Opin. Biotechnol. , vol.5 , pp. 540-545
    • McMillan, D.R.1    Gething, M.J.2    Sambrook, J.3
  • 39
    • 0027787823 scopus 로고
    • The activity of sigma E, an Escherichia coli heat-inducible sigma-factor, is modulated by expression of outer membrane proteins
    • Mecsas, J., P.E. Rouvière, J.W. Erikson, T.J. Donohue, and C.A. Gross. 1993. The activity of sigma E, an Escherichia coli heat-inducible sigma-factor, is modulated by expression of outer membrane proteins. Genes & Dev. 7: 2618-2628.
    • (1993) Genes & Dev. , vol.7 , pp. 2618-2628
    • Mecsas, J.1    Rouvière, P.E.2    Erikson, J.W.3    Donohue, T.J.4    Gross, C.A.5
  • 41
    • 0027208683 scopus 로고
    • OmpF assembly mutants of Escherichia coli K-12: Isolation, characterization, and suppressor analysis
    • Misra, R. 1993. OmpF assembly mutants of Escherichia coli K-12: Isolation, characterization, and suppressor analysis. J. Bacteriol. 175: 5049-5056.
    • (1993) J. Bacteriol. , vol.175 , pp. 5049-5056
    • Misra, R.1
  • 42
    • 0025768542 scopus 로고
    • A genetic approach for analyzing the pathway of LamB assembly into the outer membrane of Escherichia coli
    • Misra, R., A. Peterson, T. Ferenci, and T.J. Silhavy. 1991. A genetic approach for analyzing the pathway of LamB assembly into the outer membrane of Escherichia coli. J. Biol. Chem. 266: 13592-13597.
    • (1991) J. Biol. Chem. , vol.266 , pp. 13592-13597
    • Misra, R.1    Peterson, A.2    Ferenci, T.3    Silhavy, T.J.4
  • 43
    • 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
  • 44
    • 0029765609 scopus 로고    scopus 로고
    • New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH
    • Missiakas, D., J.-M. Betton, and S. Raina. 1996. New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH. Mol. Microbiol. 21:871-884.
    • (1996) Mol. Microbiol. , vol.21 , pp. 871-884
    • Missiakas, D.1    Betton, J.-M.2    Raina, S.3
  • 45
    • 0028025336 scopus 로고
    • Porins and specific diffusion channels in bacterial outer membranes
    • Nikaido, H. 1994. Porins and specific diffusion channels in bacterial outer membranes. J. Biol. Chem. 269: 3905-3908.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3905-3908
    • Nikaido, H.1
  • 46
    • 0028123018 scopus 로고
    • Streptomyces chrysomallus FKBP-33 is a novel immunophilin consisting of two FK506 binding domains; its gene is transcriptionally coupled to the FKBP-12 gene
    • Pahl, A. and U. Keller. 1994. Streptomyces chrysomallus FKBP-33 is a novel immunophilin consisting of two FK506 binding domains; its gene is transcriptionally coupled to the FKBP-12 gene. EMBO J. 13: 3472-3480.
    • (1994) EMBO J. , vol.13 , pp. 3472-3480
    • Pahl, A.1    Keller, U.2
  • 47
    • 0028124244 scopus 로고
    • Confirmation of the existence of a third family among peptidly-prolyl cis/trans isomerases. Amino acid sequence and recombinant production of parvulin
    • Rahfeld, J.U., K.P. Rucknagel, B. Schelbert, B. Ludwig, J. Hacker, K. Mann, and G. Fischer. 1994a. Confirmation of the existence of a third family among peptidly-prolyl cis/trans isomerases. Amino acid sequence and recombinant production of parvulin. FEBS Lett. 352: 180-184.
    • (1994) FEBS Lett. , vol.352 , pp. 180-184
    • Rahfeld, J.U.1    Rucknagel, K.P.2    Schelbert, B.3    Ludwig, B.4    Hacker, J.5    Mann, K.6    Fischer, G.7
  • 48
    • 0028349613 scopus 로고
    • A novel peptidyl-prolyl cis/trans isomerase from Escherichia coli
    • Rahfeld, J.U., A. Schierhorn, K. Mann, and G. Fischer. 1994b. A novel peptidyl-prolyl cis/trans isomerase from Escherichia coli. FEBS Lett. 343: 65-69.
    • (1994) FEBS Lett. , vol.343 , pp. 65-69
    • Rahfeld, J.U.1    Schierhorn, A.2    Mann, K.3    Fischer, G.4
  • 49
    • 0028948314 scopus 로고
    • Cyclophilin 20 is involved in mitochondrial protein folding in cooperation with molecular chaperones Hsp70 and Hsp60
    • Rassow, J., K. Mohrs, S. Koidl, I.B. Barthelmess, N. Pfanner, and M. Tropschug. 1995. Cyclophilin 20 is involved in mitochondrial protein folding in cooperation with molecular chaperones Hsp70 and Hsp60. Mol. Cell. Biol. 15: 2654-2662.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2654-2662
    • Rassow, J.1    Mohrs, K.2    Koidl, S.3    Barthelmess, I.B.4    Pfanner, N.5    Tropschug, M.6
  • 50
    • 0029131389 scopus 로고
    • Phi X174 lysis requires slyD, a host gene which is related to the FKB family of peptidyl-prolyl cis/trans isomerases
    • Roof, W.D. and R. Young. 1995. Phi X174 lysis requires slyD, a host gene which is related to the FKB family of peptidyl-prolyl cis/trans isomerases. FEMS Microbiol. Rev. 17: 213-218.
    • (1995) FEMS Microbiol. Rev. , vol.17 , pp. 213-218
    • Roof, W.D.1    Young, R.2
  • 51
    • 0028907529 scopus 로고
    • rpoE, the gene encoding the second heat-shock sigma factor, sigma E, in Escherichia coli
    • Rouvière, P.E., A. De Las Penas, J. Mecsas, C.Z. Lu, K.E. Rudd, and C.A. Gross. 1995. rpoE, the gene encoding the second heat-shock sigma factor, sigma E, in Escherichia coli. EMBO J. 14: 1032-1042.
    • (1995) EMBO J. , vol.14 , pp. 1032-1042
    • Rouvière, P.E.1    De Las Penas, A.2    Mecsas, J.3    Lu, C.Z.4    Rudd, K.E.5    Gross, C.A.6
  • 53
    • 0028946962 scopus 로고
    • Structural basis for sugar translocation through maltoporin channels at 3.1 A resolution
    • Schirmer, T., T.A. Keller, Y.F. Wang, and J.P. Rosenbusch. 1995. Structural basis for sugar translocation through maltoporin channels at 3.1 A resolution. Science 267: 512-514.
    • (1995) Science , vol.267 , pp. 512-514
    • Schirmer, T.1    Keller, T.A.2    Wang, Y.F.3    Rosenbusch, J.P.4
  • 54
    • 0027256737 scopus 로고
    • Prolyl isomerase: Enzymatic catalysis of slow protein-folding reactions
    • Schmid, F.X. 1993. Prolyl isomerase: Enzymatic catalysis of slow protein-folding reactions. Annu. Rev. Biophys. Biomol. Struct. 22: 123-142.
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 123-142
    • Schmid, F.X.1
  • 56
    • 0025970549 scopus 로고
    • Lipopolysaccharide structure required for in vitro trimerization of Escherichia coli OmpF porin
    • Sen, K. and H. Nikaido. 1991a. Lipopolysaccharide structure required for in vitro trimerization of Escherichia coli OmpF porin. J. Bacteriol. 173: 926-928.
    • (1991) J. Bacteriol. , vol.173 , pp. 926-928
    • Sen, K.1    Nikaido, H.2
  • 57
    • 0025833095 scopus 로고
    • Trimerization of an in vitro synthesized OmpF porin of Escherichia coli outer membrane
    • _. 1991b. Trimerization of an in vitro synthesized OmpF porin of Escherichia coli outer membrane. J. Biol. Chem. 266: 11295-11300.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11295-11300
  • 59
    • 0029058524 scopus 로고
    • Chaperone-like activity of protein disulfide-isomerase in the refolding of rhodanese
    • Song, J.L. and C.C. Wang. 1995. Chaperone-like activity of protein disulfide-isomerase in the refolding of rhodanese. Eur. J. Biochem. 231:312-316.
    • (1995) Eur. J. Biochem. , vol.231 , pp. 312-316
    • Song, J.L.1    Wang, C.C.2
  • 61
    • 0025309069 scopus 로고
    • surA, an Escherichia coli gene essential for survival in stationary phase
    • Tormo, A., M. Almiron, and R. Kolter. 1990. surA, an Escherichia coli gene essential for survival in stationary phase. J. Bacterial. 172: 4339-4347.
    • (1990) J. Bacterial. , vol.172 , pp. 4339-4347
    • Tormo, A.1    Almiron, M.2    Kolter, R.3
  • 62
    • 0028577268 scopus 로고
    • Detergent-induced folding of the outer-membrane protein PhoE, a pore protein induced by phosphate limitation
    • Van Der Gelder, P., H. De Cock, and J. Tommassen. 1994. Detergent-induced folding of the outer-membrane protein PhoE, a pore protein induced by phosphate limitation. Eur. J. Biochem. 226: 783-787.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 783-787
    • Van Der Gelder, P.1    De Cock, H.2    Tommassen, J.3
  • 63
    • 0021605388 scopus 로고
    • Assembly pathway of newly synthesized LamB protein an outer membrane protein of Escherichia coli K-12
    • Vos-Scheperkeuter, G.H. and B. Witholt. 1984. Assembly pathway of newly synthesized LamB protein an outer membrane protein of Escherichia coli K-12. J. Mol. Biol. 175: 511-528.
    • (1984) J. Mol. Biol. , vol.175 , pp. 511-528
    • Vos-Scheperkeuter, G.H.1    Witholt, B.2
  • 64
    • 0028286019 scopus 로고
    • Protein folding in the periplasm of Escherichia coli
    • Wulfing, C. and A. Pluckthun. 1994. Protein folding in the periplasm of Escherichia coli. Mol Microbiol. 12: 685-692.
    • (1994) Mol Microbiol. , vol.12 , pp. 685-692
    • Wulfing, C.1    Pluckthun, A.2


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