메뉴 건너뛰기




Volumn 266, Issue 5, 1997, Pages 978-992

Module swaps between related translocator proteins pIV(f1), pIV(IKe) and PulD: Identification of a specificity domain

Author keywords

Extra cellular secretion; Filamentous phage assembly; Protein export; Pullulanase secretion

Indexed keywords

AMINO ACID; CARRIER PROTEIN;

EID: 0031567136     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0866     Document Type: Article
Times cited : (34)

References (62)
  • 1
    • 33745466322 scopus 로고
    • Pullulan, ein extracelullaeres Glucan von Pullularia pullulans
    • Bender, S., Lehman, J. & Wallenfels, K. (1959). Pullulan, ein extracelullaeres Glucan von Pullularia pullulans. Biochim. Biophys. Acta, 36, 309-316.
    • (1959) Biochim. Biophys. Acta , vol.36 , pp. 309-316
    • Bender, S.1    Lehman, J.2    Wallenfels, K.3
  • 2
    • 0019185349 scopus 로고
    • Processing of filamentous phage pre-coat protein. Effect of sequence variations near the signal peptidase cleavage site
    • Boeke, J. D., Russel, M. & Model, P. (1980). Processing of filamentous phage pre-coat protein. Effect of sequence variations near the signal peptidase cleavage site. J. Mol. Biol. 144, 103-116.
    • (1980) J. Mol. Biol. , vol.144 , pp. 103-116
    • Boeke, J.D.1    Russel, M.2    Model, P.3
  • 3
    • 0018961637 scopus 로고
    • Morphological and serological relationships of conjugative pili
    • Bradley, D. E. (1980). Morphological and serological relationships of conjugative pili. Plasmid, 4, 155-169.
    • (1980) Plasmid , vol.4 , pp. 155-169
    • Bradley, D.E.1
  • 4
    • 0025230537 scopus 로고
    • Secretion and membrane integration of a filamentous phage-encoded morphogenetic protein
    • Brissette, J. L. & Russel, M. (1990). Secretion and membrane integration of a filamentous phage-encoded morphogenetic protein. J. Mol. Biol. 211, 565-580.
    • (1990) J. Mol. Biol. , vol.211 , pp. 565-580
    • Brissette, J.L.1    Russel, M.2
  • 6
    • 0023956658 scopus 로고
    • Functional analysis of the adsorption protein of two filamentous phages with different host specificities
    • Bross, P., Bussmann, K., Keppner, W. & Rasched, I. (1988). Functional analysis of the adsorption protein of two filamentous phages with different host specificities. J. Gen. Microbiol. 134, 461-471.
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 461-471
    • Bross, P.1    Bussmann, K.2    Keppner, W.3    Rasched, I.4
  • 7
    • 0027285690 scopus 로고
    • Signal sequence processing is required for the assembly of LamB trimers in the outer membrane of Escherichia coli
    • Carlson, J. H. & Silhavy, T. J. (1993). Signal sequence processing is required for the assembly of LamB trimers in the outer membrane of Escherichia coli. J. Bacteriol. 175, 3327-3334.
    • (1993) J. Bacteriol. , vol.175 , pp. 3327-3334
    • Carlson, J.H.1    Silhavy, T.J.2
  • 8
    • 0017807890 scopus 로고
    • Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid
    • Chang, A. C. & Cohen, S. N. (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.C.1    Cohen, S.N.2
  • 9
    • 0017868338 scopus 로고
    • Empirical predictions of protein conformation
    • Chou, P. Y. & Fasman, G. D. (1978). Empirical predictions of protein conformation. Annu. Rev. Biochem. 47, 251-276.
    • (1978) Annu. Rev. Biochem. , vol.47 , pp. 251-276
    • Chou, P.Y.1    Fasman, G.D.2
  • 10
    • 0028568176 scopus 로고
    • TopPred II: An improved software for membrane protein structure predictions
    • Claros, M. G. & von Heijne, G. (1994). TopPred II: an improved software for membrane protein structure predictions. CABIOS, 10, 685-686.
    • (1994) CABIOS , vol.10 , pp. 685-686
    • Claros, M.G.1    Von Heijne, G.2
  • 12
    • 0024384953 scopus 로고
    • Klebsiella pneumoniae pulS gene encodes an outer membrane lipoprotein required for pullulanase secretion
    • d'Enfert, C. & Pugsley, A. P. (1989). Klebsiella pneumoniae pulS gene encodes an outer membrane lipoprotein required for pullulanase secretion. J. Bacteriol. 171, 3673-3679.
    • (1989) J. Bacteriol. , vol.171 , pp. 3673-3679
    • D'Enfert, C.1    Pugsley, A.P.2
  • 13
    • 0024341985 scopus 로고
    • Protein secretion by Gram-negative bacteria. Characterization of two membrane proteins required for pullulanase secretion by Escherichia coli K-12
    • d'Enfert, C., Reyss, I., Wandersman, C. & Pugsley, A. P. (1989). Protein secretion by Gram-negative bacteria. Characterization of two membrane proteins required for pullulanase secretion by Escherichia coli K-12. J. Biol. Chem. 264, 17462-17468.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17462-17468
    • D'Enfert, C.1    Reyss, I.2    Wandersman, C.3    Pugsley, A.P.4
  • 14
    • 0027522531 scopus 로고
    • Specificity domains distinguish the Ras-related GTPases Ypt1 and Sec4
    • Dunn, B., Stearns, T. & Botstein, D. (1993). Specificity domains distinguish the Ras-related GTPases Ypt1 and Sec4. Nature, 362, 563-565.
    • (1993) Nature , vol.362 , pp. 563-565
    • Dunn, B.1    Stearns, T.2    Botstein, D.3
  • 15
    • 0027772476 scopus 로고
    • Chimaeric nicotinic-serotonergic receptor combines distinct ligand binding and channel specificities
    • Eisele, J. L., Bertrand, S., Galzi, J. L., Devillers-Thiery, A., Changeux, J. P. & Bertrand, D. (1993). Chimaeric nicotinic-serotonergic receptor combines distinct ligand binding and channel specificities. Nature, 366, 479-483.
    • (1993) Nature , vol.366 , pp. 479-483
    • Eisele, J.L.1    Bertrand, S.2    Galzi, J.L.3    Devillers-Thiery, A.4    Changeux, J.P.5    Bertrand, D.6
  • 16
    • 0028353854 scopus 로고
    • A superfamily of proteins involved in different secretion pathways in Gram-negative bacteria: Modular structure and specificity of the N-terminal domain
    • Genin, S. & Boucher, C. A. (1994). A superfamily of proteins involved in different secretion pathways in Gram-negative bacteria: modular structure and specificity of the N-terminal domain. Mol. Gen. Genet. 243, 112-118.
    • (1994) Mol. Gen. Genet. , vol.243 , pp. 112-118
    • Genin, S.1    Boucher, C.A.2
  • 17
    • 0029870545 scopus 로고    scopus 로고
    • Insertion of an outer membrane protein in Escherichia coli requires a chaperone-like protein
    • Hardie, K. R., Lory, S. & Pugsley, A. P. (1996). Insertion of an outer membrane protein in Escherichia coli requires a chaperone-like protein. EMBO J. 15, 978-988.
    • (1996) EMBO J. , vol.15 , pp. 978-988
    • Hardie, K.R.1    Lory, S.2    Pugsley, A.P.3
  • 19
    • 0019952423 scopus 로고
    • Nucleotide sequence of bacteriophage f1 DNA
    • Hill, D. F. & Petersen, G. B. (1982). Nucleotide sequence of bacteriophage f1 DNA. J. Virol. 44, 32-46.
    • (1982) J. Virol. , vol.44 , pp. 32-46
    • Hill, D.F.1    Petersen, G.B.2
  • 20
    • 0016289862 scopus 로고
    • Pullulanase synthesis in Klebsiella (aerobacter) aerogenes strains growing in continuous culture
    • Hope, G. C. & Dean, A. C. (1974). Pullulanase synthesis in Klebsiella (aerobacter) aerogenes strains growing in continuous culture. Biochem. J. 144, 403-411.
    • (1974) Biochem. J. , vol.144 , pp. 403-411
    • Hope, G.C.1    Dean, A.C.2
  • 21
    • 0023042015 scopus 로고
    • Morphogenesis of f1 filamentous bacteriophage. Increased expression of gene I inhibits bacterial growth
    • Horabin, J. I. & Webster, R. E. (1986). Morphogenesis of f1 filamentous bacteriophage. Increased expression of gene I inhibits bacterial growth. J. Mol. Biol. 188, 403-413.
    • (1986) J. Mol. Biol. , vol.188 , pp. 403-413
    • Horabin, J.I.1    Webster, R.E.2
  • 22
    • 0028167849 scopus 로고
    • Beta-structure in the membrane-spanning part of the nicotinic acetylcholine receptor (or how helical are transmembrane helices?)
    • Hucho, F., Gorne-Tschelnokow, U. & Strecker, A. (1994). Beta-structure in the membrane-spanning part of the nicotinic acetylcholine receptor (or how helical are transmembrane helices?). Trends Biochem. Sci. 19, 383-387.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 383-387
    • Hucho, F.1    Gorne-Tschelnokow, U.2    Strecker, A.3
  • 23
    • 0025190086 scopus 로고
    • Structure predictions of membrane proteins are not that bad
    • Jahnig, F. (1990). Structure predictions of membrane proteins are not that bad. Trends Biochem. Sci. 15, 93-95.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 93-95
    • Jahnig, F.1
  • 24
    • 0026690571 scopus 로고
    • A new approach to protein fold recognition
    • Jones, D. T., Taylor, W. R. & Thornton, J. M. (1992). A new approach to protein fold recognition. Nature, 358, 86-89.
    • (1992) Nature , vol.358 , pp. 86-89
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 25
    • 0028363816 scopus 로고
    • pIV, a filamentous phage protein that mediates phage export across the bacterial cell envelope, forms a multimer
    • Kazmierczak, B. I., Mielke, D. L., Russel, M. & Model, P. (1994). pIV, a filamentous phage protein that mediates phage export across the bacterial cell envelope, forms a multimer. J. Mol, Biol. 238, 187-198.
    • (1994) J. Mol, Biol. , vol.238 , pp. 187-198
    • Kazmierczak, B.I.1    Mielke, D.L.2    Russel, M.3    Model, P.4
  • 26
    • 0027751445 scopus 로고
    • The secretion pathway of IgA protease-type proteins in Gram-negative bacteria
    • Klauser, T., Pohlner, J. & Meyer, T. F. (1993). The secretion pathway of IgA protease-type proteins in Gram-negative bacteria. Bioessays, 15, 799-805.
    • (1993) Bioessays , vol.15 , pp. 799-805
    • Klauser, T.1    Pohlner, J.2    Meyer, T.F.3
  • 27
    • 0027522364 scopus 로고
    • Expression of the pspA gene stimulates efficient protein export in Escherichia coli
    • Kleerebezem, M. & Tommassen, J. (1993). Expression of the pspA gene stimulates efficient protein export in Escherichia coli. Mol. Microbiol. 7, 947-956.
    • (1993) Mol. Microbiol. , vol.7 , pp. 947-956
    • Kleerebezem, M.1    Tommassen, J.2
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 0026680833 scopus 로고
    • Dissection of IncP conjugative plasmid transfer: Definition of the transfer region Tra2 by mobilization of the Tra1 region in trans
    • Lessl, M., Balzer, D., Lurz, R., Waters, V. L., Guiney, D. G. & Lanka, E. (1992). Dissection of IncP conjugative plasmid transfer: definition of the transfer region Tra2 by mobilization of the Tra1 region in trans. J. Bacteriol. 174, 2493-2500.
    • (1992) J. Bacteriol. , vol.174 , pp. 2493-2500
    • Lessl, M.1    Balzer, D.2    Lurz, R.3    Waters, V.L.4    Guiney, D.G.5    Lanka, E.6
  • 30
    • 0029927929 scopus 로고    scopus 로고
    • Complementation of deletion mutations in a cloned functional cluster of Erwinia chrysanthemi out genes with Erwinia carotovora out homologues revels OutC and OutD as candidate gatekeepers of species-specific secretion of proteins via the type II pathway
    • Lindeberg, M., Salmond, G. P. C. & Collmer, A. (1996). Complementation of deletion mutations in a cloned functional cluster of Erwinia chrysanthemi out genes with Erwinia carotovora out homologues revels OutC and OutD as candidate gatekeepers of species-specific secretion of proteins via the type II pathway. Mol. Microbiol. 20, 175-190.
    • (1996) Mol. Microbiol. , vol.20 , pp. 175-190
    • Lindeberg, M.1    Salmond, G.P.C.2    Collmer, A.3
  • 31
    • 0023245373 scopus 로고
    • Construction of a series of ompC-ompF chimeric genes by in vivo homologous recombination in Escherichia coli and characterization of their translational products
    • Mizuno, T., Kasai, H. & Mizushima, S. (1987). Construction of a series of ompC-ompF chimeric genes by in vivo homologous recombination in Escherichia coli and characterization of their translational products. Mol. Gen. Genet. 207, 217-223.
    • (1987) Mol. Gen. Genet. , vol.207 , pp. 217-223
    • Mizuno, T.1    Kasai, H.2    Mizushima, S.3
  • 32
    • 0001654813 scopus 로고
    • Filamentous bacteriophage
    • (Calendar, R., ed.), Plenum Publishing Corporation, New York
    • Model, P. & Russel, M. (1988). Filamentous bacteriophage. In The Bacteriophages (Calendar, R., ed.), vol. 2, pp. 375-456. Plenum Publishing Corporation, New York.
    • (1988) The Bacteriophages , vol.2 , pp. 375-456
    • Model, P.1    Russel, M.2
  • 33
    • 0022397969 scopus 로고
    • Nucleotide sequence and genetic organization of the genome of the N-specific filamentous bacteriophage IKe. Comparison with the genome of the F-specific filamentous phages M13, fd and f1
    • Peeters, B. P., Peters, R. M., Schoenmakers, J. G. & Konings, R. N. (1985). Nucleotide sequence and genetic organization of the genome of the N-specific filamentous bacteriophage IKe. Comparison with the genome of the F-specific filamentous phages M13, fd and f1. J. Mol. Biol. 181, 27-39.
    • (1985) J. Mol. Biol. , vol.181 , pp. 27-39
    • Peeters, B.P.1    Peters, R.M.2    Schoenmakers, J.G.3    Konings, R.N.4
  • 34
    • 0023056798 scopus 로고
    • The gene II proteins of the filamentous phages IKe and Ff (M13, fd and f1) are not functionally interchangeable during viral strand replication
    • Peeters, B. P., Schoenmakers, J. G. & Konings, R. N. (1986). The gene II proteins of the filamentous phages IKe and Ff (M13, fd and f1) are not functionally interchangeable during viral strand replication. Nucl. Acids Res. 14, 5067-5080.
    • (1986) Nucl. Acids Res. , vol.14 , pp. 5067-5080
    • Peeters, B.P.1    Schoenmakers, J.G.2    Konings, R.N.3
  • 35
    • 0028279520 scopus 로고
    • Prediction of transmembrane segments in proteins utilising multiple sequence alignments
    • Persson, B. & Argos, P. (1994). Prediction of transmembrane segments in proteins utilising multiple sequence alignments. J. Mol. Biol. 237, 182-192.
    • (1994) J. Mol. Biol. , vol.237 , pp. 182-192
    • Persson, B.1    Argos, P.2
  • 36
    • 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
  • 37
    • 0025678539 scopus 로고
    • Genetics of extracellular protein secretion by Gram-negative bacteria
    • Pugsley, A. P., d'Enfert, C., Reyss, I. & Kornacker, M. G. (1990). Genetics of extracellular protein secretion by Gram-negative bacteria. Annu. Rev. Genet. 24, 67-90.
    • (1990) Annu. Rev. Genet. , vol.24 , pp. 67-90
    • Pugsley, A.P.1    D'Enfert, C.2    Reyss, I.3    Kornacker, M.G.4
  • 38
    • 0014206950 scopus 로고
    • A new method for the determination of alpha-amylase
    • Rinderknecht, H., Wilding, P. & Haverback, B. J. (1967). A new method for the determination of alpha-amylase. Experientia, 23, 805.
    • (1967) Experientia , vol.23 , pp. 805
    • Rinderknecht, H.1    Wilding, P.2    Haverback, B.J.3
  • 39
    • 0015294972 scopus 로고
    • Reducing value methods for maltodextrins. I. Chain-length dependence of alkaline 3,5-dinitrosalicylate and chain-length independence of alkaline copper
    • Robyt, J. F. & Whelan, W. J. (1972). Reducing value methods for maltodextrins. I. Chain-length dependence of alkaline 3,5-dinitrosalicylate and chain-length independence of alkaline copper. Anal. Biochem. 45, 510-516.
    • (1972) Anal. Biochem. , vol.45 , pp. 510-516
    • Robyt, J.F.1    Whelan, W.J.2
  • 40
    • 0026706335 scopus 로고
    • Interchangeability of related proteins and autonomy of function. The morphogenetic proteins of filamentous phage f1 and IKe cannot replace one another
    • Russel, M. (1992). Interchangeability of related proteins and autonomy of function. The morphogenetic proteins of filamentous phage f1 and IKe cannot replace one another. J. Mol. Biol. 227, 453-462.
    • (1992) J. Mol. Biol. , vol.227 , pp. 453-462
    • Russel, M.1
  • 41
    • 0027337983 scopus 로고
    • Protein-protein interactions during filamentous phage assembly
    • Russel, M. (1993). Protein-protein interactions during filamentous phage assembly. J. Mol. Biol. 231, 689-697.
    • (1993) J. Mol. Biol. , vol.231 , pp. 689-697
    • Russel, M.1
  • 42
    • 0027986656 scopus 로고
    • Mutants at conserved positions in gene IV, a gene required for assembly and secretion of filamentous phages
    • Russel, M. (1994a). Mutants at conserved positions in gene IV, a gene required for assembly and secretion of filamentous phages. Mol. Microbiol. 14, 357-369.
    • (1994) Mol. Microbiol. , vol.14 , pp. 357-369
    • Russel, M.1
  • 43
    • 0027982566 scopus 로고
    • Phage assembly: A paradigm for bacterial virulence factor export?
    • Russel, M. (1994b). Phage assembly: a paradigm for bacterial virulence factor export? Science, 265, 612-614.
    • (1994) Science , vol.265 , pp. 612-614
    • Russel, M.1
  • 44
    • 0028999019 scopus 로고
    • Moving through the membrane with filamentous phages
    • Russel, M. (1995). Moving through the membrane with filamentous phages. Trends Microbiol. 3, 223-228.
    • (1995) Trends Microbiol. , vol.3 , pp. 223-228
    • Russel, M.1
  • 45
    • 0027293725 scopus 로고
    • Analysis of the structure and subcellular location of filamentous phage pIV
    • Russel, M. & Kazmierczak, B. (1993). Analysis of the structure and subcellular location of filamentous phage pIV. J. Bacteriol. 175, 3998-4007.
    • (1993) J. Bacteriol. , vol.175 , pp. 3998-4007
    • Russel, M.1    Kazmierczak, B.2
  • 46
    • 0022372670 scopus 로고
    • Enzymatic amplification of beta-globin genomic sequences and restriction site analysis for diagnosis of sickle cell anemia
    • Saiki, R. K., Scharf, S., Faloona, F., Mullis, K. B., Horn, G. T., Erlich, H. A. & Arnheim, N. (1985). Enzymatic amplification of beta-globin genomic sequences and restriction site analysis for diagnosis of sickle cell anemia. Science, 230, 1350-1354.
    • (1985) Science , vol.230 , pp. 1350-1354
    • Saiki, R.K.1    Scharf, S.2    Faloona, F.3    Mullis, K.B.4    Horn, G.T.5    Erlich, H.A.6    Arnheim, N.7
  • 47
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Šali, A. & Blundell, T. L. (1993). Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234, 779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Šali, A.1    Blundell, T.L.2
  • 48
    • 0027434697 scopus 로고
    • Membrane traffic wardens and proteins secretion in Gram-negative bacteria
    • Salmond, G. P. & Reeves, P. J. (1993). Membrane traffic wardens and proteins secretion in Gram-negative bacteria. Trends Biochem. Sci. 18, 7-12.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 7-12
    • Salmond, G.P.1    Reeves, P.J.2
  • 51
    • 0025694884 scopus 로고
    • Genetic analysis of protein export in Escherichia coli
    • Schatz, P. J. & Beckwith, J. (1990). Genetic analysis of protein export in Escherichia coli. Annu. Rev. Genet. 24, 215-248.
    • (1990) Annu. Rev. Genet. , vol.24 , pp. 215-248
    • Schatz, P.J.1    Beckwith, J.2
  • 52
    • 0028946962 scopus 로고
    • Structural basis for sugar translocation through maltoporin channels at 3.1 Å resolution
    • Schirmer, T., Keller, T. A., Wang, Y. F. & Rosenbusch, J. P. (1995). Structural basis for sugar translocation through maltoporin channels at 3.1 Å 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
    • 0023571657 scopus 로고
    • High-copy-number and low-copy-number plasmid vectors for lacZ alpha-complementation and chloramphenicol-or kanamycin-resistance selection
    • Takeshita, S., Sato, M., Toba, M., Masahashi, W. & Hashimoto-Gotoh, T. (1987). High-copy-number and low-copy-number plasmid vectors for lacZ alpha-complementation and chloramphenicol-or kanamycin-resistance selection. Gene, 61, 63-74.
    • (1987) Gene , vol.61 , pp. 63-74
    • Takeshita, S.1    Sato, M.2    Toba, M.3    Masahashi, W.4    Hashimoto-Gotoh, T.5
  • 55
    • 0025899909 scopus 로고
    • Nucleotide sequence of a cluster of genes involved in the transformation of Haemophilus influenzae Rd
    • Tomb, J. F., el-Hajj, H. & Smith, H. O. (1991). Nucleotide sequence of a cluster of genes involved in the transformation of Haemophilus influenzae Rd. Gene, 104, 1-10.
    • (1991) Gene , vol.104 , pp. 1-10
    • Tomb, J.F.1    El-Hajj, H.2    Smith, H.O.3
  • 56
    • 0022085069 scopus 로고
    • Localization of functional domains in E. coli K-12 outer membrane porins
    • Tommassen, J., van der Ley, P., van Zeijl, M. & Agterberg, M. (1985). Localization of functional domains in E. coli K-12 outer membrane porins. EMBO J. 4, 1583-1587.
    • (1985) EMBO J. , vol.4 , pp. 1583-1587
    • Tommassen, J.1    Van Der Ley, P.2    Van Zeijl, M.3    Agterberg, M.4
  • 57
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T. & Gordon, J. (1979). Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl Acad. Sci. USA, 76, 4350-4354.
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 58
    • 0029984543 scopus 로고    scopus 로고
    • Projection structure of the nicotinic acetylcholine receptor. Distinct conformations of the alpha subunits
    • Unwin, N. (1996). Projection structure of the nicotinic acetylcholine receptor. Distinct conformations of the alpha subunits. J. Mol. Biol. 257, 586-596.
    • (1996) J. Mol. Biol. , vol.257 , pp. 586-596
    • Unwin, N.1
  • 59
    • 0023429366 scopus 로고
    • Analysis of structure-function relationships in Escherichia coli K12 outer membrane porins with the aid of ompC-phoE and phoE-ompC hybrid genes
    • van der Ley, P., Burm, P., Agterberg, M., van Meersbergen, J. & Tommassen, J. (1987). Analysis of structure-function relationships in Escherichia coli K12 outer membrane porins with the aid of ompC-phoE and phoE-ompC hybrid genes. Mol. Gen. Genet. 209, 585-591.
    • (1987) Mol. Gen. Genet. , vol.209 , pp. 585-591
    • Van Der Ley, P.1    Burm, P.2    Agterberg, M.3    Van Meersbergen, J.4    Tommassen, J.5
  • 60
    • 0026716643 scopus 로고
    • Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule
    • von Heijne, G. (1992). Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule. J. Mol. Biol. 225, 487-494.
    • (1992) J. Mol. Biol. , vol.225 , pp. 487-494
    • Von Heijne, G.1
  • 61
    • 0026669327 scopus 로고
    • Secretion across the bacterial outer membrane
    • Wandersman, C. (1992). Secretion across the bacterial outer membrane. Trends Genet. 8, 317-322.
    • (1992) Trends Genet. , vol.8 , pp. 317-322
    • Wandersman, C.1
  • 62
    • 0025885002 scopus 로고
    • The enzymology of protein translocation across the Escherichia coli plasma membrane
    • Wickner, W., Driessen, A. J. & Hartl, F. U. (1991). The enzymology of protein translocation across the Escherichia coli plasma membrane. Annu. Rev. Biochem. 60, 101-124.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 101-124
    • Wickner, W.1    Driessen, A.J.2    Hartl, F.U.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.