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Volumn 1, Issue 2, 2008, Pages 177-190

Development of a LytE-based high-density surface display system in Bacillus subtilis

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; BETA LACTAMASE; HYBRID PROTEIN; HYDROLASE; PROTEIN LYTE; UNCLASSIFIED DRUG;

EID: 77953557660     PISSN: 17517907     EISSN: 17517915     Source Type: Journal    
DOI: 10.1111/j.1751-7915.2007.00017.x     Document Type: Article
Times cited : (17)

References (52)
  • 1
    • 0001524630 scopus 로고    scopus 로고
    • Heat-stable spore-based vaccines: Surface expression of invasin-cell wall fusion proteins in Bacillus subtilis
    • Brown, F, Burton, D, Doherty, P, Mekalanos, J, and Norrby, E, eds, Cold Spring Harbor, NY, USA: Cold Spring Harbor Laboratory Press, pp
    • Acheson, D.W.K., Sonenshein, A.L., Leong, J.M., Keusch, G.T., and Norrby, E. (1997) Heat-stable spore-based vaccines: surface expression of invasin-cell wall fusion proteins in Bacillus subtilis. In Vaccines 97: Molecular Approaches to the Control of Infectious Diseases. Brown, F., Burton, D., Doherty, P., Mekalanos, J., and Norrby, E. (eds). Cold Spring Harbor, NY, USA: Cold Spring Harbor Laboratory Press, pp. 179-184.
    • (1997) Vaccines 97: Molecular Approaches to the Control of Infectious Diseases , pp. 179-184
    • Acheson, D.W.K.1    Sonenshein, A.L.2    Leong, J.M.3    Keusch, G.T.4    Norrby, E.5
  • 2
    • 0036244046 scopus 로고    scopus 로고
    • Stabilization of cell wall proteins in Bacillus subtilis: A proteomic approach
    • Antelmann, H., Yamamoto, H., Sekiguchi, J., and Hecker, M. (2002) Stabilization of cell wall proteins in Bacillus subtilis: a proteomic approach. Proteomics 2: 591-602.
    • (2002) Proteomics , vol.2 , pp. 591-602
    • Antelmann, H.1    Yamamoto, H.2    Sekiguchi, J.3    Hecker, M.4
  • 3
    • 0034674162 scopus 로고    scopus 로고
    • The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD)
    • Bateman, A., and Bycroft, M. (2000) The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD). J Mol Biol 299: 1113-1119.
    • (2000) J Mol Biol , vol.299 , pp. 1113-1119
    • Bateman, A.1    Bycroft, M.2
  • 4
    • 0031963480 scopus 로고    scopus 로고
    • The role of autolysins during vegetative growth of Bacillus subtilis 168
    • Blackman, S.A., Smith, T.J., and Foster, S.J. (1998) The role of autolysins during vegetative growth of Bacillus subtilis 168. Microbiology 144: 73-82.
    • (1998) Microbiology , vol.144 , pp. 73-82
    • Blackman, S.A.1    Smith, T.J.2    Foster, S.J.3
  • 5
    • 31544432925 scopus 로고    scopus 로고
    • Novel surface display system for proteins on non-genetically modified gram-positive bacteria
    • Bosma, T., Kanninga, R., Neef, J., Audouy, S.A., van Roosmalen, M.L., Steen, A., et al. (2006) Novel surface display system for proteins on non-genetically modified gram-positive bacteria. Appl Environ Microbiol 72: 880-889.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 880-889
    • Bosma, T.1    Kanninga, R.2    Neef, J.3    Audouy, S.A.4    van Roosmalen, M.L.5    Steen, A.6
  • 6
    • 0030047151 scopus 로고    scopus 로고
    • The permeability of the wall fabric of Escherichia coli and Bacillus subtilis
    • Demchick, P., and Koch, A.L. (1996) The permeability of the wall fabric of Escherichia coli and Bacillus subtilis. J Bacteriol 178: 768-773.
    • (1996) J Bacteriol , vol.178 , pp. 768-773
    • Demchick, P.1    Koch, A.L.2
  • 7
    • 33645049557 scopus 로고    scopus 로고
    • Protein cell surface display in Gram-positive bacteria: From single protein to macromolecular protein structure
    • Desvaux, M., Dumas, E., Chafsey, I., and Hebraud, M. (2006) Protein cell surface display in Gram-positive bacteria: from single protein to macromolecular protein structure. FEMS Microbiol Lett 256: 1-15.
    • (2006) FEMS Microbiol Lett , vol.256 , pp. 1-15
    • Desvaux, M.1    Dumas, E.2    Chafsey, I.3    Hebraud, M.4
  • 8
    • 0026512822 scopus 로고
    • Analysis of the autolysins of Bacillus subtilis 168 during vegetative growth and differentiation by using renaturing polyacrylamide gel electrophoresis
    • Foster, S.J. (1992) Analysis of the autolysins of Bacillus subtilis 168 during vegetative growth and differentiation by using renaturing polyacrylamide gel electrophoresis. J Bacteriol 174: 464-470.
    • (1992) J Bacteriol , vol.174 , pp. 464-470
    • Foster, S.J.1
  • 9
    • 0027154835 scopus 로고
    • Molecular analysis of three major wall-associated proteins of Bacillus subtilis 168: Evidence for processing of the product of a gene encoding a 258 kDa precursor two-domain ligand-binding protein
    • Foster, S.J. (1993) Molecular analysis of three major wall-associated proteins of Bacillus subtilis 168: evidence for processing of the product of a gene encoding a 258 kDa precursor two-domain ligand-binding protein. Mol Microbiol 8: 299-310.
    • (1993) Mol Microbiol , vol.8 , pp. 299-310
    • Foster, S.J.1
  • 10
    • 0001904527 scopus 로고    scopus 로고
    • Structure and synthesis of cell wall, spore cortex, teichoic acids, S-layers and capsules
    • Sonenshein, A.L, Hoch, J.A, and Losick, R, eds, Washington, DC, USA: ASM Press, pp
    • Foster, S.J., and Popham, D.L. (2002) Structure and synthesis of cell wall, spore cortex, teichoic acids, S-layers and capsules. In Bacillus subtilis and Its Closest Relatives. Sonenshein, A.L., Hoch, J.A., and Losick, R. (eds). Washington, DC, USA: ASM Press, pp. 21-41.
    • (2002) Bacillus subtilis and Its Closest Relatives , pp. 21-41
    • Foster, S.J.1    Popham, D.L.2
  • 11
    • 33751381791 scopus 로고    scopus 로고
    • FoldUnfold: Web server for the prediction of disordered regions in protein chain
    • Galzitskaya, O.V., Garbuzynskiy, S.O., and Lobanov, M.Y. (2006) FoldUnfold: web server for the prediction of disordered regions in protein chain. Bioinformatics 22: 2948-2949.
    • (2006) Bioinformatics , vol.22 , pp. 2948-2949
    • Galzitskaya, O.V.1    Garbuzynskiy, S.O.2    Lobanov, M.Y.3
  • 12
    • 0031012062 scopus 로고    scopus 로고
    • Display of heterologous proteins on the surface of microorganisms: From the screening of combinatorial libraries to live recombinant vaccines
    • Georgiou, G., Stathopoulos, C., Daugherty, P.S., Nayak, A.R., Iverson, B.L., and Curtiss, R. (1997) Display of heterologous proteins on the surface of microorganisms: from the screening of combinatorial libraries to live recombinant vaccines. Nat Biotechnol 15: 29-34.
    • (1997) Nat Biotechnol , vol.15 , pp. 29-34
    • Georgiou, G.1    Stathopoulos, C.2    Daugherty, P.S.3    Nayak, A.R.4    Iverson, B.L.5    Curtiss, R.6
  • 13
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S.C., and Von Hippel, P.H. (1989) Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem 182: 319-326.
    • (1989) Anal Biochem , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 14
    • 0017698858 scopus 로고
    • Zinc is associated with the beta subunit of DNA dependent RNA polymerase of Bacillus subtilis
    • Halling, S.M., Sanchez-Anzaldo, F.J., Fukuda, R., Doi, R.H., and Meares, C.F. (1977) Zinc is associated with the beta subunit of DNA dependent RNA polymerase of Bacillus subtilis. Biochemistry 16: 2880-2884.
    • (1977) Biochemistry , vol.16 , pp. 2880-2884
    • Halling, S.M.1    Sanchez-Anzaldo, F.J.2    Fukuda, R.3    Doi, R.H.4    Meares, C.F.5
  • 15
    • 0016688222 scopus 로고
    • Estimates of the porosity of Bacillus licheniformis and Bacillus subtilis cell walls
    • Hughes, R.C., Thurman, P.F., and Stokes, E. (1975) Estimates of the porosity of Bacillus licheniformis and Bacillus subtilis cell walls. Z Immunitatsforsch Exp Klin Immunol 149: 126-135.
    • (1975) Z Immunitatsforsch Exp Klin Immunol , vol.149 , pp. 126-135
    • Hughes, R.C.1    Thurman, P.F.2    Stokes, E.3
  • 17
    • 0031978461 scopus 로고    scopus 로고
    • Regulation of a new cell wall hydrolase gene, cwlF, which affects cell separation in Bacillus subtilis
    • Ishikawa, S., Hara, Y., Ohnishi, R., and Sekiguchi, J. (1998) Regulation of a new cell wall hydrolase gene, cwlF, which affects cell separation in Bacillus subtilis. J Bacteriol 180: 2549-2555.
    • (1998) J Bacteriol , vol.180 , pp. 2549-2555
    • Ishikawa, S.1    Hara, Y.2    Ohnishi, R.3    Sekiguchi, J.4
  • 19
    • 0034662487 scopus 로고    scopus 로고
    • Accumulation of an artificial cell wall-binding lipase by Bacillus subtilis wprA and/or sigD mutants
    • Kabayashi, G., Toida, J., Akamatsu, T., Yamamoto, H., Shida, T., and Sekiguchi, J. (2000) Accumulation of an artificial cell wall-binding lipase by Bacillus subtilis wprA and/or sigD mutants. FEMS Microbiol Lett 188: 165-169.
    • (2000) FEMS Microbiol Lett , vol.188 , pp. 165-169
    • Kabayashi, G.1    Toida, J.2    Akamatsu, T.3    Yamamoto, H.4    Shida, T.5    Sekiguchi, J.6
  • 20
    • 17444367302 scopus 로고    scopus 로고
    • Spore-displayed streptavidin: A live diagnostic tool in biotechnology
    • Kim, J.H., Lee, C.S., and Kim, B.G. (2005a) Spore-displayed streptavidin: a live diagnostic tool in biotechnology. Biochem Biophys Res Commun 331: 210-214.
    • (2005) Biochem Biophys Res Commun , vol.331 , pp. 210-214
    • Kim, J.H.1    Lee, C.S.2    Kim, B.G.3
  • 21
    • 23044500836 scopus 로고    scopus 로고
    • Development and characterization of membrane surface display system using molecular chaperon, PrsA, of Bacillus subtilis
    • Kim, J.H., Park, I.S., and Kim, B.G. (2005b) Development and characterization of membrane surface display system using molecular chaperon, PrsA, of Bacillus subtilis. Biochem Biophys Res Commun 334: 1248-1253.
    • (2005) Biochem Biophys Res Commun , vol.334 , pp. 1248-1253
    • Kim, J.H.1    Park, I.S.2    Kim, B.G.3
  • 23
    • 0034302315 scopus 로고    scopus 로고
    • Accumulation of a recombinant Aspergillus oryzae lipase artificially localized on the Bacillus subtilis cell surface
    • Kobayashi, G., Toida, J., Akamatsu, T., Yamamoto, H., Shida, T., and Sekiguchi, J. (2000) Accumulation of a recombinant Aspergillus oryzae lipase artificially localized on the Bacillus subtilis cell surface. J Biosci Bioeng 90: 422-425.
    • (2000) J Biosci Bioeng , vol.90 , pp. 422-425
    • Kobayashi, G.1    Toida, J.2    Akamatsu, T.3    Yamamoto, H.4    Shida, T.5    Sekiguchi, J.6
  • 24
    • 0025011966 scopus 로고
    • Cloning, sequencing and genetic mapping of a Bacillus subtilis cell wall hydrolase gene
    • Kuroda, A., and Sekiguchi, J. (1990) Cloning, sequencing and genetic mapping of a Bacillus subtilis cell wall hydrolase gene. J Gen Microbiol 136: 2209-2216.
    • (1990) J Gen Microbiol , vol.136 , pp. 2209-2216
    • Kuroda, A.1    Sekiguchi, J.2
  • 25
    • 0032925064 scopus 로고    scopus 로고
    • Biochemical characterization of the Pseudomonas aeruginosa 101/1477 metallo-beta-lactamase IMP-1 produced by Escherichia coli
    • Laraki, N., Franceschini, N., Rossolini, G.M., Santucci, P., Meunier, C., de Pauw, E., et al. (1999) Biochemical characterization of the Pseudomonas aeruginosa 101/1477 metallo-beta-lactamase IMP-1 produced by Escherichia coli. Antimicrob Agents Chemother 43: 902-906.
    • (1999) Antimicrob Agents Chemother , vol.43 , pp. 902-906
    • Laraki, N.1    Franceschini, N.2    Rossolini, G.M.3    Santucci, P.4    Meunier, C.5    de Pauw, E.6
  • 26
    • 0034051291 scopus 로고    scopus 로고
    • Autodisplay: Functional display of active beta-lactamase on the surface of Escherichia coli by the AIDA-I autotransporter
    • Lattemann, C.T., Maurer, J., Gerland, E., and Meyer, T.F. (2000) Autodisplay: functional display of active beta-lactamase on the surface of Escherichia coli by the AIDA-I autotransporter. J Bacteriol 182: 3726-3733.
    • (2000) J Bacteriol , vol.182 , pp. 3726-3733
    • Lattemann, C.T.1    Maurer, J.2    Gerland, E.3    Meyer, T.F.4
  • 27
    • 0026673165 scopus 로고
    • Sequencing and analysis of the Bacillus subtilis lytRABC divergon: A regulatory unit encompassing the structural genes of the N-acetylmuramoyl-L- alanine amidase and its modifier
    • Lazarevic, V., Margot, P., Soldo, B., and Karamata, D. (1992) Sequencing and analysis of the Bacillus subtilis lytRABC divergon: a regulatory unit encompassing the structural genes of the N-acetylmuramoyl-L- alanine amidase and its modifier. J Gen Microbiol 138: 1949-1961.
    • (1992) J Gen Microbiol , vol.138 , pp. 1949-1961
    • Lazarevic, V.1    Margot, P.2    Soldo, B.3    Karamata, D.4
  • 28
    • 0042622240 scopus 로고    scopus 로고
    • GlobPlot: Exploring protein sequences for globularity and disorder
    • Linding, R., Russell, R.B., Neduva, V., and Gibson, T.J. (2003) GlobPlot: exploring protein sequences for globularity and disorder. Nucleic Acids Res 31: 3701-3708.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3701-3708
    • Linding, R.1    Russell, R.B.2    Neduva, V.3    Gibson, T.J.4
  • 29
    • 0036231904 scopus 로고    scopus 로고
    • C-terminal domains of Listeria monocytogenes bacteriophage murein hydrolases determine specific recognition and high-affinity binding to bacterial cell wall carbohydrates
    • Loessner, M.J., Kramer, K., Ebel, F., and Scherer, S. (2002) C-terminal domains of Listeria monocytogenes bacteriophage murein hydrolases determine specific recognition and high-affinity binding to bacterial cell wall carbohydrates. Mol Microbiol 44: 335-349.
    • (2002) Mol Microbiol , vol.44 , pp. 335-349
    • Loessner, M.J.1    Kramer, K.2    Ebel, F.3    Scherer, S.4
  • 30
    • 0030444419 scopus 로고    scopus 로고
    • The wprA gene of Bacillus subtilis 168, expressed during exponential growth, encodes a cell-wall-associated protease
    • Margot, P., and Karamata, D. (1996) The wprA gene of Bacillus subtilis 168, expressed during exponential growth, encodes a cell-wall-associated protease. Microbiology (UK) 142: 3437-3444.
    • (1996) Microbiology (UK) , vol.142 , pp. 3437-3444
    • Margot, P.1    Karamata, D.2
  • 31
    • 0028291159 scopus 로고
    • The gene of the N-acetylglucosaminidase, a Bacillus subtilis 168 cell wall hydrolase not involved in vegetative cell autolysis
    • Margot, P., Mauel, C., and Karamata, D. (1994) The gene of the N-acetylglucosaminidase, a Bacillus subtilis 168 cell wall hydrolase not involved in vegetative cell autolysis. Mol Microbiol 12: 535-545.
    • (1994) Mol Microbiol , vol.12 , pp. 535-545
    • Margot, P.1    Mauel, C.2    Karamata, D.3
  • 33
    • 16244387909 scopus 로고    scopus 로고
    • Cryo-electron microscopy reveals native polymeric cell wall structure in Bacillus subtilis 168 and the existence of a periplasmic space
    • Matias, V.R., and Beveridge, T.J. (2005) Cryo-electron microscopy reveals native polymeric cell wall structure in Bacillus subtilis 168 and the existence of a periplasmic space. Mol Microbiol 56: 240-251.
    • (2005) Mol Microbiol , vol.56 , pp. 240-251
    • Matias, V.R.1    Beveridge, T.J.2
  • 34
  • 35
    • 0026491205 scopus 로고
    • Sorbitol dehydrogenase from Bacillus subtilis. Purification, characterization, and gene cloning
    • Ng, K., Ye, R., Wu, X.-C., and Wong, S.-L. (1992) Sorbitol dehydrogenase from Bacillus subtilis. Purification, characterization, and gene cloning. J Biol Chem 267: 24989-24994.
    • (1992) J Biol Chem , vol.267 , pp. 24989-24994
    • Ng, K.1    Ye, R.2    Wu, X.-C.3    Wong, S.-L.4
  • 36
    • 33645333138 scopus 로고    scopus 로고
    • Establishment of an experimental system allowing immobilization of proteins on the surface of Bacillus subtilis cells
    • Nguyen, H.D., and Schumann,W. (2006) Establishment of an experimental system allowing immobilization of proteins on the surface of Bacillus subtilis cells. J Biotechnol 122: 473-482.
    • (2006) J Biotechnol , vol.122 , pp. 473-482
    • Nguyen, H.D.1    Schumann, W.2
  • 37
    • 0014381393 scopus 로고
    • Conformation of polypeptides and proteins
    • Ramachandran, G.N., and Sasisekharan, V. (1968) Conformation of polypeptides and proteins. Adv Protein Chem 23: 283-438.
    • (1968) Adv Protein Chem , vol.23 , pp. 283-438
    • Ramachandran, G.N.1    Sasisekharan, V.2
  • 38
    • 0018999186 scopus 로고
    • Methods for ligand-receptor assays in clinical chemistry
    • Smith, R.G., and Sestili, M.A. (1980) Methods for ligand-receptor assays in clinical chemistry. Clin Chem 26: 543-550.
    • (1980) Clin Chem , vol.26 , pp. 543-550
    • Smith, R.G.1    Sestili, M.A.2
  • 39
    • 0033950951 scopus 로고    scopus 로고
    • Autolysins of Bacillus subtilis: Multiple enzymes with multiple functions
    • Smith, T.J., Blackman, S.A., and Foster, S.J. (2000) Autolysins of Bacillus subtilis: multiple enzymes with multiple functions. Microbiology 146: 249-262.
    • (2000) Microbiology , vol.146 , pp. 249-262
    • Smith, T.J.1    Blackman, S.A.2    Foster, S.J.3
  • 40
    • 0342710346 scopus 로고    scopus 로고
    • Bacterial surface display: Trends and progress
    • Stahl, S., and Uhlen, M. (1997) Bacterial surface display: trends and progress. Trends Biotechnol 15: 185-192.
    • (1997) Trends Biotechnol , vol.15 , pp. 185-192
    • Stahl, S.1    Uhlen, M.2
  • 41
    • 0037930133 scopus 로고    scopus 로고
    • Cell wall attachment of a widely distributed peptidoglycan binding domain is hindered by cell wall constituents
    • Steen, A., Buist, G., Leenhouts, K.J., El Khattabi, M., Grijpstra, F., Zomer, A.L., et al. (2003) Cell wall attachment of a widely distributed peptidoglycan binding domain is hindered by cell wall constituents. J Biol Chem 278: 23874-23881.
    • (2003) J Biol Chem , vol.278 , pp. 23874-23881
    • Steen, A.1    Buist, G.2    Leenhouts, K.J.3    El Khattabi, M.4    Grijpstra, F.5    Zomer, A.L.6
  • 42
    • 0021829611 scopus 로고
    • The DNA sequence of the secreted Bacillus subtilis enzyme levansucrase and its genetic control sites
    • Steinmetz, M., LeCoq, D., Aymerich, S., Gonzy-Treboul, G., and Gay, P. (1985) The DNA sequence of the secreted Bacillus subtilis enzyme levansucrase and its genetic control sites. Mol Gen Genet 200: 220-228.
    • (1985) Mol Gen Genet , vol.200 , pp. 220-228
    • Steinmetz, M.1    LeCoq, D.2    Aymerich, S.3    Gonzy-Treboul, G.4    Gay, P.5
  • 43
    • 0029808395 scopus 로고    scopus 로고
    • In vivo immobilization of enzymatically active polypeptides on the cell surface of Staphylococcus carnosus
    • Strauss, A., and Gotz, F. (1996) In vivo immobilization of enzymatically active polypeptides on the cell surface of Staphylococcus carnosus. Mol Microbiol 21: 491-500.
    • (1996) Mol Microbiol , vol.21 , pp. 491-500
    • Strauss, A.1    Gotz, F.2
  • 44
  • 45
    • 2942584912 scopus 로고    scopus 로고
    • Identification and characterization of the novel LysM domain-containing surface protein Sep from Lactobacillus fermentum BR11 and its use as a peptide fusion partner in Lactobacillus and Lactococcus
    • Turner, M.S., Hafner, L.M., Walsh, T., and Giffard, P.M. (2004) Identification and characterization of the novel LysM domain-containing surface protein Sep from Lactobacillus fermentum BR11 and its use as a peptide fusion partner in Lactobacillus and Lactococcus. Appl Environ Microbiol 70: 3673-3680.
    • (2004) Appl Environ Microbiol , vol.70 , pp. 3673-3680
    • Turner, M.S.1    Hafner, L.M.2    Walsh, T.3    Giffard, P.M.4
  • 46
    • 33845225226 scopus 로고    scopus 로고
    • Enhanced immunisation and expression strategies using bacterial spores as heat-stable vaccine delivery vehicles
    • Uyen, N.Q., Hong, H.A., and Cutting, S.M. (2007) Enhanced immunisation and expression strategies using bacterial spores as heat-stable vaccine delivery vehicles. Vaccine 25: 356-365.
    • (2007) Vaccine , vol.25 , pp. 356-365
    • Uyen, N.Q.1    Hong, H.A.2    Cutting, S.M.3
  • 47
    • 0021243550 scopus 로고
    • 37 RNA polymerase holoenzymes during growth and stationary phases
    • 37 RNA polymerase holoenzymes during growth and stationary phases. J Biol Chem 259: 8619-8625.
    • (1984) J Biol Chem , vol.259 , pp. 8619-8625
    • Wang, P.-Z.1    Doi, R.H.2
  • 48
    • 10444241949 scopus 로고    scopus 로고
    • Biotechnological applications for surface-engineered bacteria
    • Wernerus, H., and Stahl, S. (2004) Biotechnological applications for surface-engineered bacteria. Biotechnol Appl Biochem 40: 209-228.
    • (2004) Biotechnol Appl Biochem , vol.40 , pp. 209-228
    • Wernerus, H.1    Stahl, S.2
  • 49
    • 0022848673 scopus 로고
    • Determination of the signal peptidase cleavage site in the preprosubtilisin of Bacillus subtilis
    • Wong, S.-L., and Doi, R.H. (1986) Determination of the signal peptidase cleavage site in the preprosubtilisin of Bacillus subtilis. J Biol Chem 261: 10176-10181.
    • (1986) J Biol Chem , vol.261 , pp. 10176-10181
    • Wong, S.-L.1    Doi, R.H.2
  • 50
    • 0036307716 scopus 로고    scopus 로고
    • Functional production and characterization of a fibrin-specific single-chain antibody fragment from Bacillus subtilis: Effects of molecular chaperones and a wall-bound protease on antibody fragment production
    • Wu, S.-C., Yeung, J.C., Duan, Y., Ye, R., Szarka, S.J., Habibi, H.R., and Wong, S.-L. (2002) Functional production and characterization of a fibrin-specific single-chain antibody fragment from Bacillus subtilis: effects of molecular chaperones and a wall-bound protease on antibody fragment production. Appl Environ Microbiol 68: 3261-3269.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 3261-3269
    • Wu, S.-C.1    Yeung, J.C.2    Duan, Y.3    Ye, R.4    Szarka, S.J.5    Habibi, H.R.6    Wong, S.-L.7
  • 51
    • 0242575014 scopus 로고    scopus 로고
    • Localization of the vegetative cell wall hydrolases LytC, LytE, and LytF on the Bacillus subtilis cell surface and stability of these enzymes to cell wall-bound or extracellular proteases
    • Yamamoto, H., Kurosawa, S., and Sekiguchi, J. (2003) Localization of the vegetative cell wall hydrolases LytC, LytE, and LytF on the Bacillus subtilis cell surface and stability of these enzymes to cell wall-bound or extracellular proteases. J Bacteriol 185: 6666-6677.
    • (2003) J Bacteriol , vol.185 , pp. 6666-6677
    • Yamamoto, H.1    Kurosawa, S.2    Sekiguchi, J.3
  • 52
    • 0032472195 scopus 로고    scopus 로고
    • Quantitation of transcription and clonal selection of single living cells with beta-lactamase as reporter
    • Zlokarnik, G., Negulescu, P.A., Knapp, T.E., Mere, L., Burres, N., Feng, L., et al. (1998) Quantitation of transcription and clonal selection of single living cells with beta-lactamase as reporter. Science 279: 84-88.
    • (1998) Science , vol.279 , pp. 84-88
    • Zlokarnik, G.1    Negulescu, P.A.2    Knapp, T.E.3    Mere, L.4    Burres, N.5    Feng, L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.