메뉴 건너뛰기




Volumn 38, Issue 4, 2004, Pages 482-493

Bacterial and archaeal S-layers as a subject of nanobiotechnology

Author keywords

biosensors; cell S layer; nanotechnology; vaccines

Indexed keywords

ADJUVANT; ANTIINFECTIVE AGENT; ANTINEOPLASTIC AGENT; BACTERIAL ANTIGEN; BACTERIAL POLYSACCHARIDE; BACTERIAL PROTEIN; BACTERIAL VACCINE; BETV 1 ANTIGEN; CANCER VACCINE; GLYCOPROTEIN; HAPTEN; ISOPROTEIN; POLLEN ANTIGEN; UNCLASSIFIED DRUG;

EID: 4444354681     PISSN: 00268933     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:MBIL.0000036999.77762.6a     Document Type: Review
Times cited : (19)

References (106)
  • 1
    • 0141431019 scopus 로고    scopus 로고
    • Commercializing nanotechnology
    • Mazzola L. 2003. Commercializing nanotechnology. Nature Biotechnol. 21, 1137-1143.
    • (2003) Nature Biotechnol. , vol.21 , pp. 1137-1143
    • Mazzola, L.1
  • 2
    • 85015106657 scopus 로고    scopus 로고
    • DNA in a material world
    • Seeman N.C. 2003. DNA in a material world. Nature. 421, 427-431.
    • (2003) Nature , vol.421 , pp. 427-431
    • Seeman, N.C.1
  • 4
    • 0141534348 scopus 로고    scopus 로고
    • DNA-templated self-assembly of protein arrays and highly conductive nanowires
    • Yan H., Ha Park S., Finkelstein G., Peif J.H., La Bean T.H. 2003. DNA-templated self-assembly of protein arrays and highly conductive nanowires. Science. 301, 1882-1884.
    • (2003) Science , vol.301 , pp. 1882-1884
    • Yan, H.1    Ha Park, S.2    Finkelstein, G.3    Peif, J.H.4    La Bean, T.H.5
  • 5
    • 0018195592 scopus 로고
    • Regular arrays of macromolecules on bacterial cell walls: Structure, chemistry, assembly and function
    • Sleytr U.B. 1978. Regular arrays of macromolecules on bacterial cell walls: Structure, chemistry, assembly and function. Int. Rev.Cytol. 53, 1-64.
    • (1978) Int. Rev.Cytol. , vol.53 , pp. 1-64
    • Sleytr, U.B.1
  • 6
    • 0026587424 scopus 로고
    • Crystalline bacterial cell surface layers
    • Messner P., Sleytr U.B. 1992. Crystalline bacterial cell surface layers. Adv. Microbiol. Physiol. 33, 213-275.
    • (1992) Adv. Microbiol. Physiol. , vol.33 , pp. 213-275
    • Messner, P.1    Sleytr, U.B.2
  • 9
    • 77956828123 scopus 로고
    • Analysis of crystalline bacterial surface layers by freeze-etching, metal shadowing, negative staining and ultrathin sectioning methods
    • Sleytr U.B., Messner P., Pum D. 1988. Analysis of crystalline bacterial surface layers by freeze-etching, metal shadowing, negative staining and ultrathin sectioning methods. Microbiology. 20, 29-60.
    • (1988) Microbiology , vol.20 , pp. 29-60
    • Sleytr, U.B.1    Messner, P.2    Pum, D.3
  • 11
    • 0032464347 scopus 로고    scopus 로고
    • Structure research on surface layers: A focus on stability, surface layer homology domains, and surface layer-cell wall interaction
    • Engelhardt H., Peters J. 1998. Structure research on surface layers: A focus on stability, surface layer homology domains, and surface layer-cell wall interaction. J. Struct. Biol. 124, 276-302.
    • (1998) J. Struct. Biol. , vol.124 , pp. 276-302
    • Engelhardt, H.1    Peters, J.2
  • 12
    • 0030058166 scopus 로고    scopus 로고
    • Conformational change of the hexagonally packed intermediate layer of Deinococcus radiodurans imaged by atomic force microscopy
    • Müller D.J., Baumeister W., Engel A. 1996. Conformational change of the hexagonally packed intermediate layer of Deinococcus radiodurans imaged by atomic force microscopy. J. Bacteriol. 178, 3025-3030.
    • (1996) J. Bacteriol. , vol.178 , pp. 3025-3030
    • Müller, D.J.1    Baumeister, W.2    Engel, A.3
  • 13
    • 0033539578 scopus 로고    scopus 로고
    • Controlled unzipping of a bacterial surface layer with atomic force microcopy
    • Muller D.J., Baumeister W., Engel A. 1999. Controlled unzipping of a bacterial surface layer with atomic force microcopy. Proc. Natl. Acad. Sci. USA. 96, 13170-13174.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13170-13174
    • Muller, D.J.1    Baumeister, W.2    Engel, A.3
  • 16
    • 0000013061 scopus 로고
    • Paracrystalline protein surface arrays on bacteria
    • Kova S.F. 1988. Paracrystalline protein surface arrays on bacteria. Can. J. Microbiol. 34, 407-414.
    • (1988) Can. J. Microbiol. , vol.34 , pp. 407-414
    • Kova, S.F.1
  • 18
    • 0031047960 scopus 로고    scopus 로고
    • Bacterial glycoproteins
    • Messner P. 1997. Bacterial glycoproteins. Glycoconj. J. 14, 3-11.
    • (1997) Glycoconj. J. , vol.14 , pp. 3-11
    • Messner, P.1
  • 19
    • 0032766054 scopus 로고    scopus 로고
    • Structural heterogeneity in the core oligosaccharide of the S-layer glycoprotein from Aneurinibacillus thermoaerophylus DSM1055
    • Wugedtisch T., Zacchara N.E., Puchberger M., et al. 1999. Structural heterogeneity in the core oligosaccharide of the S-layer glycoprotein from Aneurinibacillus thermoaerophylus DSM1055. Glycobiology. 9, 787-795.
    • (1999) Glycobiology , vol.9 , pp. 787-795
    • Wugedtisch, T.1    Zacchara, N.E.2    Puchberger, M.3
  • 20
    • 0031029608 scopus 로고    scopus 로고
    • Linker mutagenesis of the Canlobacter crescentus S-layer protein: Toward a definition of an N-terminal anchoring region and C-terminal secretion signal and the potential for heterologous protein secretion
    • Bingll W.H., Nomellini J.F., Smith J. 1997. Linker mutagenesis of the Canlobacter crescentus S-layer protein: Toward a definition of an N-terminal anchoring region and C-terminal secretion signal and the potential for heterologous protein secretion. J. Bacteriol. 179, 601-611.
    • (1997) J. Bacteriol. , vol.179 , pp. 601-611
    • Bingll, W.H.1    Nomellini, J.F.2    Smith, J.3
  • 21
    • 0032425549 scopus 로고    scopus 로고
    • Campylobacter fetus surface layer proteins are transported by a type I secretion system
    • Thompson S.A., Shedd O.L., Ray K.C., et al. 1998. Campylobacter fetus surface layer proteins are transported by a type I secretion system. J. Bacteriol. 180, 6450-6458.
    • (1998) J. Bacteriol. , vol.180 , pp. 6450-6458
    • Thompson, S.A.1    Shedd, O.L.2    Ray, K.C.3
  • 22
    • 0020671471 scopus 로고
    • Crystalline surface layers on bacteria
    • Sleytr U.B., Messner P. 1983. Crystalline surface layers on bacteria. Annu. Rev. Microbiol. 37, 311-339.
    • (1983) Annu. Rev. Microbiol. , vol.37 , pp. 311-339
    • Sleytr, U.B.1    Messner, P.2
  • 23
    • 0029812726 scopus 로고    scopus 로고
    • The Lactobacillus acidophylus S-layer protein gene expression site comprises two consensus promoter sequences, one of which directs transcription of stable mRNA
    • Boot H.J, Kolen C.P.A.M., Andreadaki F.J., et al. 1996. The Lactobacillus acidophylus S-layer protein gene expression site comprises two consensus promoter sequences, one of which directs transcription of stable mRNA. J. Bacteriol. 178, 5388-5394.
    • (1996) J. Bacteriol. , vol.178 , pp. 5388-5394
    • Boot, H.J.1    Kolen, C.P.A.M.2    Andreadaki, F.J.3
  • 24
    • 0242444555 scopus 로고    scopus 로고
    • Molecular biology of the Lactobacillus brevis S-layer gene (slpA)
    • Palva A. 1997. Molecular biology of the Lactobacillus brevis S-layer gene (slpA). FEMS Microbiol. Rev. 20, 83-88.
    • (1997) FEMS Microbiol. Rev. , vol.20 , pp. 83-88
    • Palva, A.1
  • 25
    • 0242696936 scopus 로고    scopus 로고
    • The S-layer of Thermus thermophylus HB8: Structure and genetic regulation
    • Fernandez-Herrero L.A., Olabarria G., Berengner J. 1997. The S-layer of Thermus thermophylus HB8: structure and genetic regulation. FEMS Microbiol. Rev. 20, 64-67.
    • (1997) FEMS Microbiol. Rev. , vol.20 , pp. 64-67
    • Fernandez-Herrero, L.A.1    Olabarria, G.2    Berengner, J.3
  • 26
    • 0030889859 scopus 로고    scopus 로고
    • Surface proteins and a novel transcription factor regulate the expression of the S-layer gene in Thermus thermophylus HB8
    • Fernandez-Herrero L.A., Olabarria G., Berengner J. 1997. Surface proteins and a novel transcription factor regulate the expression of the S-layer gene in Thermus thermophylus HB8. Mol. Microbiol. 24, 61-72.
    • (1997) Mol. Microbiol. , vol.24 , pp. 61-72
    • Fernandez-Herrero, L.A.1    Olabarria, G.2    Berengner, J.3
  • 27
    • 0035253107 scopus 로고    scopus 로고
    • Conserved anchoring mechanisms between crystalline cell surface S-layer proteins and secondary cell wall polymers in Gram-positive bacteria
    • Sara M. 2001. Conserved anchoring mechanisms between crystalline cell surface S-layer proteins and secondary cell wall polymers in Gram-positive bacteria. Trends Microbiol. 9, 47-49.
    • (2001) Trends Microbiol. , vol.9 , pp. 47-49
    • Sara, M.1
  • 28
    • 0028262129 scopus 로고
    • Domain structure of the Acetogenium kivui surface layer revealed by electron crystallography and sequence analysis
    • Lupas A., Engelhardt H., Peters J., et al. 1994. Domain structure of the Acetogenium kivui surface layer revealed by electron crystallography and sequence analysis. J. Bacteriol. 176, 1224-1233.
    • (1994) J. Bacteriol. , vol.176 , pp. 1224-1233
    • Lupas, A.1    Engelhardt, H.2    Peters, J.3
  • 29
    • 0029000658 scopus 로고
    • OlpB, a new outer layer protein of Clostridium thermocellum, and binding of its S-layer-like domains to component of the cell envelope
    • Lemaire M., Ohayon H., Gounon P., Fujino P., et al. 1995. OlpB, a new outer layer protein of Clostridium thermocellum, and binding of its S-layer-like domains to component of the cell envelope. J. Bacteriol. 177, 2451-2459.
    • (1995) J. Bacteriol. , vol.177 , pp. 2451-2459
    • Lemaire, M.1    Ohayon, H.2    Gounon, P.3    Fujino, P.4
  • 30
    • 10144222885 scopus 로고    scopus 로고
    • A conserved motif in S-layer proteins is involved in peptidoglycan binding in Thermus thermophilus
    • Olabarria G., Carrascosa J., De Pedro J. et al. 1996. A conserved motif in S-layer proteins is involved in peptidoglycan binding in Thermus thermophilus. J. Bacteriol. 178, 4765-4772.
    • (1996) J. Bacteriol. , vol.178 , pp. 4765-4772
    • Olabarria, G.1    Carrascosa, J.2    De Pedro, J.3
  • 32
    • 0001442107 scopus 로고    scopus 로고
    • Occurrence and function of a common domain in S-layer and other exocellular proteins
    • Leibovitz E., Lemaire M., Miras I., et al. 1997. Occurrence and function of a common domain in S-layer and other exocellular proteins. FEMS Microbiol. Rev. 20, 127-133.
    • (1997) FEMS Microbiol. Rev. , vol.20 , pp. 127-133
    • Leibovitz, E.1    Lemaire, M.2    Miras, I.3
  • 33
    • 0031038990 scopus 로고    scopus 로고
    • Molecular characterization of the second S-layer gene sbsB of Bacillus stearothermophilus PV72 expressed by oxidative stress
    • Kuen B., Koch A., Asenbauer E. et al. 1997. Molecular characterization of the second S-layer gene sbsB of Bacillus stearothermophilus PV72 expressed by oxidative stress. J. Bacteriol. 179, 1664-1670.
    • (1997) J. Bacteriol. , vol.179 , pp. 1664-1670
    • Kuen, B.1    Koch, A.2    Asenbauer, E.3
  • 34
    • 0031931533 scopus 로고    scopus 로고
    • The S-layer gene of Lactobacillus helveticus CNRZ892: Cloning, sequencing and heterologous expression
    • Callegari L., Riboli B., Sanders W., et al. 1998. The S-layer gene of Lactobacillus helveticus CNRZ892: Cloning, sequencing and heterologous expression. Microbiology. 144, 719-726.
    • (1998) Microbiology , vol.144 , pp. 719-726
    • Callegari, L.1    Riboli, B.2    Sanders, W.3
  • 35
    • 0026564244 scopus 로고
    • S-layer protein gene of Lactobacillus brevis cloning by polymerase chain reaction and determination of nucleotide sequence
    • Vidgren G., Pabva I., Pakkanen R., Lounatmaa K., Palva A. 1992. S-layer protein gene of Lactobacillus brevis cloning by polymerase chain reaction and determination of nucleotide sequence. J. Bacteriol. 174, 7419-7427.
    • (1992) J. Bacteriol. , vol.174 , pp. 7419-7427
    • Vidgren, G.1    Pabva, I.2    Pakkanen, R.3    Lounatmaa, K.4    Palva, A.5
  • 36
    • 0031014881 scopus 로고    scopus 로고
    • The S-layer protein of Corenebacterium glutamicum is anchored to the cell wall by its C-terminal hydrophobic domain
    • Chami M., Bayan N., Peyret J.L., et al. 1997. The S-layer protein of Corenebacterium glutamicum is anchored to the cell wall by its C-terminal hydrophobic domain. Mol. Microbiol. 23, 483-492.
    • (1997) Mol. Microbiol. , vol.23 , pp. 483-492
    • Chami, M.1    Bayan, N.2    Peyret, J.L.3
  • 37
    • 0030700288 scopus 로고    scopus 로고
    • Molecular mechanism of Campylobacter fetus surface layer protein expression
    • Dworkin J., Blaser M.J. 1997. Molecular mechanism of Campylobacter fetus surface layer protein expression. Mol. Microbiol. 26, 433-440.
    • (1997) Mol. Microbiol. , vol.26 , pp. 433-440
    • Dworkin, J.1    Blaser, M.J.2
  • 39
    • 3543055396 scopus 로고    scopus 로고
    • The response S-layered bacteria to the Gram stain
    • Beveridge T.J. 1997. The response S-layered bacteria to the Gram stain. FEMS Microbiol. Rev. 20, 101-114.
    • (1997) FEMS Microbiol. Rev. , vol.20 , pp. 101-114
    • Beveridge, T.J.1
  • 40
    • 0023655597 scopus 로고
    • The primary structure of a prokaryotic glycoprotein. Cloning and sequencing of the cell surface gene of Halobacteria
    • Lechner J., Sumper M. 1987. The primary structure of a prokaryotic glycoprotein. Cloning and sequencing of the cell surface gene of Halobacteria. J. Biol. Chem. 262, 9724-9729.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9724-9729
    • Lechner, J.1    Sumper, M.2
  • 41
    • 0032969566 scopus 로고    scopus 로고
    • Surface protein of Gram-positive bacteria and mechanisms of their targeting to the cell envelope
    • Navarre W.W., Schneewind O. 1999. Surface protein of Gram-positive bacteria and mechanisms of their targeting to the cell envelope. Microbiol. Mol. Biol. Rev. 63, 174-229.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 174-229
    • Navarre, W.W.1    Schneewind, O.2
  • 42
    • 0031010863 scopus 로고    scopus 로고
    • Evidence that a secondary cell wall polymer recognizes the N-terminal part of the S-layer protein from Bacillus stearothermophilus PV72/p2
    • Ries W., Hotzy C., Schoches I., Sleytr U.B., Sara M. 1997. Evidence that a secondary cell wall polymer recognizes the N-terminal part of the S-layer protein from Bacillus stearothermophilus PV72/p2. J. Bacteriol. 179, 3892-3898.
    • (1997) J. Bacteriol. , vol.179 , pp. 3892-3898
    • Ries, W.1    Hotzy, C.2    Schoches, I.3    Sleytr, U.B.4    Sara, M.5
  • 43
    • 0032786249 scopus 로고    scopus 로고
    • Structural and functional analyses of the secondary cell wall polymer of Bacillus sphaericus CCM2177 serving an S-layer-specific anchor
    • Ilk N., Kosma P., Puchberger M., et al. 1999. Structural and functional analyses of the secondary cell wall polymer of Bacillus sphaericus CCM2177 serving an S-layer-specific anchor. J. Bacteriol. 181, 7643-7646.
    • (1999) J. Bacteriol. , vol.181 , pp. 7643-7646
    • Ilk, N.1    Kosma, P.2    Puchberger, M.3
  • 44
    • 0030867822 scopus 로고    scopus 로고
    • Basic and applied S-layer research: An overview
    • Sleytr U.B. 1997. Basic and applied S-layer research: An overview. FEMS Microbiol. Rev. 20, 5-12.
    • (1997) FEMS Microbiol. Rev. , vol.20 , pp. 5-12
    • Sleytr, U.B.1
  • 45
    • 0026099178 scopus 로고
    • The cell envelope of the hyperthermophilic Archaebacterium pyrobacillum organothrophum consist of two regularly arrayed protein layers: Three-dimension structure of the outer layer
    • Phipps B., Huber R., Baumeister W. 1991. The cell envelope of the hyperthermophilic Archaebacterium pyrobacillum organothrophum consist of two regularly arrayed protein layers: Three-dimension structure of the outer layer. Mol. Microbiol. 5, 523-528.
    • (1991) Mol. Microbiol. , vol.5 , pp. 523-528
    • Phipps, B.1    Huber, R.2    Baumeister, W.3
  • 46
    • 0025731018 scopus 로고
    • The effect of paracrystalline protein surface layers on predation by Bdellovibrio bacteriovorous
    • Koval S.F., Hynes S.H. 1991. The effect of paracrystalline protein surface layers on predation by Bdellovibrio bacteriovorous. J. Bacteriol. 173, 2244-2249.
    • (1991) J. Bacteriol. , vol.173 , pp. 2244-2249
    • Koval, S.F.1    Hynes, S.H.2
  • 47
    • 0013622235 scopus 로고    scopus 로고
    • The effect of S-layers and cell surface hydrophobicity on prey selection by bacteriovorous protozoa
    • Koval S.F. 1997. The effect of S-layers and cell surface hydrophobicity on prey selection by bacteriovorous protozoa. FEMS Microbiol. Rev. 20, 138-142.
    • (1997) FEMS Microbiol. Rev. , vol.20 , pp. 138-142
    • Koval, S.F.1
  • 48
    • 0029025393 scopus 로고
    • A collagen-binding S-layer protein in Lactobacillus crispatus
    • Toba T., Varkola R., Westerlund B., et al. 1995. A collagen-binding S-layer protein in Lactobacillus crispatus. Appl. Environ. Microbiol. 61, 2467-2471.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 2467-2471
    • Toba, T.1    Varkola, R.2    Westerlund, B.3
  • 49
    • 0033754371 scopus 로고    scopus 로고
    • Characterization of the collagen-binding S-layer protein CbsA of Lactobacillus crispatus
    • Sillanpää J., Martinez B., Antikainen J., et al. 2000. Characterization of the collagen-binding S-layer protein CbsA of Lactobacillus crispatus. J. Bacteriol. 182, 6440-6450.
    • (2000) J. Bacteriol. , vol.182 , pp. 6440-6450
    • Sillanpää, J.1    Martinez, B.2    Antikainen, J.3
  • 50
    • 0036430117 scopus 로고    scopus 로고
    • Domain in the S-layer protein CbsA of Lactobacillus crispatus involved in adherence collagens, laminin and lipotechoic acids and self assembly
    • Antikainen J., Anton L., Sillanpaa J., et al. 2002. Domain in the S-layer protein CbsA of Lactobacillus crispatus involved in adherence collagens, laminin and lipotechoic acids and self assembly. Mol. Microbiol. 46, 381-394.
    • (2002) Mol. Microbiol. , vol.46 , pp. 381-394
    • Antikainen, J.1    Anton, L.2    Sillanpaa, J.3
  • 51
    • 0036267352 scopus 로고    scopus 로고
    • Identification by flagellum display of an epithelial cell and fibronectin-binding function in the SlpA surface protein of Lactobacillus brevis
    • Hynönen U., Westerlund-Wikstrom B., Palva A., et al. 2002. Identification by flagellum display of an epithelial cell and fibronectin-binding function in the SlpA surface protein of Lactobacillus brevis. J. Bacteriol. 184, 3360-3367.
    • (2002) J. Bacteriol. , vol.184 , pp. 3360-3367
    • Hynönen, U.1    Westerlund-Wikstrom, B.2    Palva, A.3
  • 52
    • 0037005874 scopus 로고    scopus 로고
    • Lactobacillus express cell surface proteins which mediate binding of immobilized collagen and fibronectin
    • Lorea G., Torino M.J., Font de Valdez G., Ljungh A. 2002. Lactobacillus express cell surface proteins which mediate binding of immobilized collagen and fibronectin. FEMS Microbiol. Lett. 206, 31-37.
    • (2002) FEMS Microbiol. Lett. , vol.206 , pp. 31-37
    • Lorea, G.1    Torino, M.J.2    Font De Valdez, G.3    Ljungh, A.4
  • 53
    • 0030928054 scopus 로고    scopus 로고
    • The synthesis, secretion and role in virulence of the paracrystalline surface protein layers of Aeromonas salmonicida and Aeromonas hydrophila
    • Noonan B., Trust T.J. 1997. The synthesis, secretion and role in virulence of the paracrystalline surface protein layers of Aeromonas salmonicida and Aeromonas hydrophila. FEMS Microbiol. Lett. 154, 1-7.
    • (1997) FEMS Microbiol. Lett. , vol.154 , pp. 1-7
    • Noonan, B.1    Trust, T.J.2
  • 54
    • 0027407983 scopus 로고
    • Adhesion of Lactobacillus acidophilus to avian intestinal epithelial cells mediated by the crystalline bacterial cell surface layer (S-layer)
    • Schneitz C., Nuotioo L., Lounatmaa K. 1992. Adhesion of Lactobacillus acidophilus to avian intestinal epithelial cells mediated by the crystalline bacterial cell surface layer (S-layer). J. Appl. Bacteriol. 74, 290-299.
    • (1992) J. Appl. Bacteriol. , vol.74 , pp. 290-299
    • Schneitz, C.1    Nuotioo, L.2    Lounatmaa, K.3
  • 55
    • 0026621322 scopus 로고
    • Participation of a cyanobacterial S-layer in fine-grain mineral formation
    • Schultze-Lam S., Haranz G., Beveridge T.J. 1992. Participation of a cyanobacterial S-layer in fine-grain mineral formation. J. Bacteriol. 74, 7971-7981.
    • (1992) J. Bacteriol. , vol.74 , pp. 7971-7981
    • Schultze-Lam, S.1    Haranz, G.2    Beveridge, T.J.3
  • 56
    • 0023406967 scopus 로고
    • Molecular sieving through S-layers of Bacillus stearothermophilus strain
    • Sara M., Sleytr U.B. 1987. Molecular sieving through S-layers of Bacillus stearothermophilus strain. J. Bacteriol. 169, 4092-4098.
    • (1987) J. Bacteriol. , vol.169 , pp. 4092-4098
    • Sara, M.1    Sleytr, U.B.2
  • 57
    • 0022904865 scopus 로고
    • Ultrafiltration membranes with uniform pores from crystalline bacterial cell envelope layers
    • Sleytr U.B., Sara M. 1987. Ultrafiltration membranes with uniform pores from crystalline bacterial cell envelope layers. Appl. Microbiol. Biotechnol. 25, 83-90.
    • (1987) Appl. Microbiol. Biotechnol. , vol.25 , pp. 83-90
    • Sleytr, U.B.1    Sara, M.2
  • 58
    • 0023399734 scopus 로고
    • Production and characteristics of ultrafiltration membranes with uniform pores from two-dimensional arrays of protein
    • Sara M., Sleytr U.B. 1987. Production and characteristics of ultrafiltration membranes with uniform pores from two-dimensional arrays of protein. J. Membrane Sci. 33, 27-49.
    • (1987) J. Membrane Sci. , vol.33 , pp. 27-49
    • Sara, M.1    Sleytr, U.B.2
  • 59
    • 4444329087 scopus 로고
    • US Patent 4.752.395
    • Sleytr U.B., Sara M. 1988. US Patent 4.752.395.
    • (1988)
    • Sleytr, U.B.1    Sara, M.2
  • 60
    • 4444341676 scopus 로고
    • US Patent 4.886.604
    • Sleytr U.B., Sara M. 1989. US Patent 4.886.604.
    • (1989)
    • Sleytr, U.B.1    Sara, M.2
  • 61
    • 0030580469 scopus 로고    scopus 로고
    • Ultrafiltration membranes prepared from crystalline bacterial cell surface layers as model system for studying the influence of surface properties on protein adsorption
    • Weigert S., Sara M. 1996. Ultrafiltration membranes prepared from crystalline bacterial cell surface layers as model system for studying the influence of surface properties on protein adsorption. J. Membr. Sci. 121, 185-196.
    • (1996) J. Membr. Sci. , vol.121 , pp. 185-196
    • Weigert, S.1    Sara, M.2
  • 62
    • 0027507214 scopus 로고
    • Pathogenesis of Campylobacter fetus infection. Critical role of high molecular mass S-layer proteins in virulence
    • Blaser M.J., Pai Z. 1993. Pathogenesis of Campylobacter fetus infection. Critical role of high molecular mass S-layer proteins in virulence. J. Infect. Dis. 167, 372-377.
    • (1993) J. Infect. Dis. , vol.167 , pp. 372-377
    • Blaser, M.J.1    Pai, Z.2
  • 64
    • 0342703215 scopus 로고    scopus 로고
    • The role of S-layer proteins in ovine Campylobacter abortion
    • Grogono-Thomas R., Dworkin J., Blaser M.J. 1997. The role of S-layer proteins in ovine Campylobacter abortion. FEMS Microbiol. Rev. 20, 133-135.
    • (1997) FEMS Microbiol. Rev. , vol.20 , pp. 133-135
    • Grogono-Thomas, R.1    Dworkin, J.2    Blaser, M.J.3
  • 65
    • 0002801697 scopus 로고
    • Surface layers from Bacillus alvei as a carrier for a Streptococcus pneumoniae conjugate vaccine
    • Eds. Breveridge T.J., Roval S.F. N.Y.: Plenum Press
    • Malcolm A.J., Best M.W., Szarka R.J., et al. 1993. Surface layers from Bacillus alvei as a carrier for a Streptococcus pneumoniae conjugate vaccine. In: Advances in Paracrystalline Bacterial Surface Layers. Eds. Breveridge T.J., Roval S.F. N.Y.: Plenum Press, 219-233.
    • (1993) Advances in Paracrystalline Bacterial Surface Layers , pp. 219-233
    • Malcolm, A.J.1    Best, M.W.2    Szarka, R.J.3
  • 66
    • 0029664728 scopus 로고    scopus 로고
    • nI-controlled vaccination responses: Vaccine application of bacterial surface layer proteins
    • nI-controlled vaccination responses: Vaccine application of bacterial surface layer proteins. J. Biotechnol. 44, 225-231.
    • (1996) J. Biotechnol. , vol.44 , pp. 225-231
    • Smid, B.J.1    Messner, P.2    Unger, F.M.3
  • 67
    • 4444229959 scopus 로고    scopus 로고
    • Vaccine application of crystalline bacterial surface layer proteins (S-layers)
    • Unger F.M., Messner P., Smid B.J., Sleytr U.B. 1997. Vaccine application of crystalline bacterial surface layer proteins (S-layers). FEMS Microbiol. Rev. 20, 157-158.
    • (1997) FEMS Microbiol. Rev. , vol.20 , pp. 157-158
    • Unger, F.M.1    Messner, P.2    Smid, B.J.3    Sleytr, U.B.4
  • 68
    • 0030432302 scopus 로고    scopus 로고
    • Crystalline bacterial cell surface layers (S-layers) from cell structure to biomimetics
    • Sara M., Sleytr U.B. 1996. Crystalline bacterial cell surface layers (S-layers) from cell structure to biomimetics. Prog. Biophys. Mol. Biol. 65, 83-111.
    • (1996) Prog. Biophys. Mol. Biol. , vol.65 , pp. 83-111
    • Sara, M.1    Sleytr, U.B.2
  • 69
    • 4444246533 scopus 로고
    • Immunogenic composition containing ordered carriers. US Patent 5.043.158
    • Sleytr U.B., Mundt W., Messner P., Smith R.H., Unger F.M. 1991. Immunogenic composition containing ordered carriers. US Patent 5.043.158.
    • (1991)
    • Sleytr, U.B.1    Mundt, W.2    Messner, P.3    Smith, R.H.4    Unger, F.M.5
  • 70
    • 0028031306 scopus 로고
    • A potential vaccine strategy for asthma and allied atopic diseases during early childhood
    • Holt P.G. 1994. A potential vaccine strategy for asthma and allied atopic diseases during early childhood. Lancet. 344, 456-458.
    • (1994) Lancet , vol.344 , pp. 456-458
    • Holt, P.G.1
  • 72
    • 0024555905 scopus 로고
    • Use of regularly structured bacterial cell surface layers as matrix for immobilizing macromolecules
    • Sara M., Sleytr U.B. 1989. Use of regularly structured bacterial cell surface layers as matrix for immobilizing macromolecules. Appl. Microbiol. Biotechnol. 30, 184-189.
    • (1989) Appl. Microbiol. Biotechnol. , vol.30 , pp. 184-189
    • Sara, M.1    Sleytr, U.B.2
  • 73
    • 0030114743 scopus 로고    scopus 로고
    • Biotechnology and biomimetic with crystalline bacterial cell surface layers (S-layers)
    • Sara M., Sleytr U.B. 1996. Biotechnology and biomimetic with crystalline bacterial cell surface layers (S-layers). Micron. 27, 141-156.
    • (1996) Micron , vol.27 , pp. 141-156
    • Sara, M.1    Sleytr, U.B.2
  • 74
    • 0029067275 scopus 로고
    • The crystalline cell surface layer from Thermoanaerobacter thermohydrosulfuricum LIII-69 as an immobilization matrix: Influence of the morphological properties and the pore size of the matrix on loss of activity of covalently bound enzymes
    • Kupcu S., Mader C., Sara M. 1995. The crystalline cell surface layer from Thermoanaerobacter thermohydrosulfuricum LIII-69 as an immobilization matrix: Influence of the morphological properties and the pore size of the matrix on loss of activity of covalently bound enzymes. Biotechnol. Appl. Biochem. 21, 275-286.
    • (1995) Biotechnol. Appl. Biochem. , vol.21 , pp. 275-286
    • Kupcu, S.1    Mader, C.2    Sara, M.3
  • 75
    • 0000528333 scopus 로고
    • An amperometric glucose sensor based on isoporous crystalline protein membranes as immobilization matrix
    • Neubauer A., Pum D., Sleytr U.B. 1993. An amperometric glucose sensor based on isoporous crystalline protein membranes as immobilization matrix. Anal. Lett. 26, 1347-1360.
    • (1993) Anal. Lett. , vol.26 , pp. 1347-1360
    • Neubauer, A.1    Pum, D.2    Sleytr, U.B.3
  • 76
    • 0027950481 scopus 로고
    • A multistep enzyme sensor for sucrose based on S-layers microparticles as immobilization matrix
    • Neubauer A., Hodl C., Pum D., Sleytr U.B. 1994. A multistep enzyme sensor for sucrose based on S-layers microparticles as immobilization matrix. Anal. Lett. 27, 849-865.
    • (1994) Anal. Lett. , vol.27 , pp. 849-865
    • Neubauer, A.1    Hodl, C.2    Pum, D.3    Sleytr, U.B.4
  • 77
    • 0343586524 scopus 로고    scopus 로고
    • Fibreoptic sensor using enzyme membrane with 2D crystalline structure
    • Neubauer A., Pum D., Sleytr U.B., et al. 1996. Fibreoptic sensor using enzyme membrane with 2D crystalline structure. Biosensors Bioelectronics. 113, 317-325.
    • (1996) Biosensors Bioelectronics , vol.113 , pp. 317-325
    • Neubauer, A.1    Pum, D.2    Sleytr, U.B.3
  • 78
    • 0033026971 scopus 로고    scopus 로고
    • The application of bacterial S-layers in molecular nanotechnology
    • Pum D., Sleytr U.B. 1999. The application of bacterial S-layers in molecular nanotechnology. Trends Biotechnol. 17, 8-12.
    • (1999) Trends Biotechnol. , vol.17 , pp. 8-12
    • Pum, D.1    Sleytr, U.B.2
  • 79
    • 0036308492 scopus 로고    scopus 로고
    • Molecular characterization of the S-layer gene, sbpA, of Bacillus sphaericus CCM2177 and production of functional S-layer fusion protein with ability to recrystallize in a definite orientation while presented the fused allergen
    • Ilk N., Völlenkle C., Edelseer E.M., et al. 2002. Molecular characterization of the S-layer gene, sbpA, of Bacillus sphaericus CCM2177 and production of functional S-layer fusion protein with ability to recrystallize in a definite orientation while presented the fused allergen. Appl. Environ. Microbiol. 68, 3251-3260.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 3251-3260
    • Ilk, N.1    Völlenkle, C.2    Edelseer, E.M.3
  • 80
    • 0029876584 scopus 로고    scopus 로고
    • Dynamics in oxygen-induced changes in S-layer protein synthesis from Bacillus stearothermophilus PV72 and the S-layer-deficient variant T5 in continuous culture, and studies of the cell wall composition
    • Sara M., Kuen B., Mayer N.F., et al. 1996. Dynamics in oxygen-induced changes in S-layer protein synthesis from Bacillus stearothermophilus PV72 and the S-layer-deficient variant T5 in continuous culture, and studies of the cell wall composition. J. Bacteriol. 178, 2108-2117.
    • (1996) J. Bacteriol. , vol.178 , pp. 2108-2117
    • Sara, M.1    Kuen, B.2    Mayer, N.F.3
  • 81
    • 0037069325 scopus 로고    scopus 로고
    • S-layer-streptavidin fusion proteins as template for nanopatterned molecular arrays
    • Moll D., Huber C., Schlegel B., et al. 2001. S-layer-streptavidin fusion proteins as template for nanopatterned molecular arrays. Proc. Natl. Acad. USA. 99, 14646-14651.
    • (2001) Proc. Natl. Acad. USA , vol.99 , pp. 14646-14651
    • Moll, D.1    Huber, C.2    Schlegel, B.3
  • 82
    • 0242669327 scopus 로고    scopus 로고
    • Surface display of foreign epitopes on the Lactobacillus brevis S-layer
    • Avall-Jaaskelainen S., Kylä-Nikkilä., Kahala M., et al. 2002. Surface display of foreign epitopes on the Lactobacillus brevis S-layer. Appl. Environ. Microbiol. 68, 5943-5951.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 5943-5951
    • Avall-Jaaskelainen, S.1    Kylä-Nikkilä2    Kahala, M.3
  • 84
    • 0030569732 scopus 로고    scopus 로고
    • Supported membranes: Scientific and practical application
    • Sackmann E. 1996. Supported membranes: Scientific and practical application. Science. 271, 43-48.
    • (1996) Science , vol.271 , pp. 43-48
    • Sackmann, E.1
  • 85
    • 0024351124 scopus 로고
    • Planar lipid-protein membranes: Strategies of formation and detecting dependencies of ion transport functions on membrane conditions
    • Schindler H. 1989. Planar lipid-protein membranes: Strategies of formation and detecting dependencies of ion transport functions on membrane conditions. Methods Enzymol. 171, 225-253.
    • (1989) Methods Enzymol. , vol.171 , pp. 225-253
    • Schindler, H.1
  • 86
    • 0027189904 scopus 로고
    • Large-scale recrystallization of the S-layer of Bacillus coagulans E-3866 at the air-water interface and on lipid films
    • Pum D., Weinhand M., Hodl C., Sleytr U.B. 1993. Large-scale recrystallization of the S-layer of Bacillus coagulans E-3866 at the air-water interface and on lipid films. J. Bacteriol. 175, 2762-2766.
    • (1993) J. Bacteriol. , vol.175 , pp. 2762-2766
    • Pum, D.1    Weinhand, M.2    Hodl, C.3    Sleytr, U.B.4
  • 87
    • 0343145679 scopus 로고    scopus 로고
    • Bacterial and archaeal S-layer proteins: Structure-function relationships and their biotechnological applications
    • Sleytr U.B., Sara M. 1997. Bacterial and archaeal S-layer proteins: Structure-function relationships and their biotechnological applications. Trends Biotechnol. 15, 20-26.
    • (1997) Trends Biotechnol. , vol.15 , pp. 20-26
    • Sleytr, U.B.1    Sara, M.2
  • 88
    • 0032513080 scopus 로고    scopus 로고
    • Self assembled α-hemolysin pores in an S-layer-supported lipid bilayer
    • Schuster B., Pun D., Braha O., et al. 1998. Self assembled α-hemolysin pores in an S-layer-supported lipid bilayer. Biochim. Biophys. Acta. 1370, 280-288.
    • (1998) Biochim. Biophys. Acta , vol.1370 , pp. 280-288
    • Schuster, B.1    Pun, D.2    Braha, O.3
  • 89
    • 0032206180 scopus 로고    scopus 로고
    • S-layer reconstitution at phospholipid monolayers
    • Wetzer B., Pfandler A., Gyozvary E., et al. 1998. S-layer reconstitution at phospholipid monolayers. Langmuir. 14, 6899-6906.
    • (1998) Langmuir , vol.14 , pp. 6899-6906
    • Wetzer, B.1    Pfandler, A.2    Gyozvary, E.3
  • 90
    • 0029040954 scopus 로고
    • Liposomes coated with crystalline bacterial cell surface protein (S-layer) as immobilization structures for macromolecules
    • Kupcu S., Sara M., Sleytr U.B. 1995. Liposomes coated with crystalline bacterial cell surface protein (S-layer) as immobilization structures for macromolecules. Biochim. Biophys. Acta. 1235, 263-269.
    • (1995) Biochim. Biophys. Acta , vol.1235 , pp. 263-269
    • Kupcu, S.1    Sara, M.2    Sleytr, U.B.3
  • 91
    • 0345435047 scopus 로고    scopus 로고
    • Stabilizing effect of an S-layer on liposomes towards thermal or mechanical stress
    • Mader C., Kupcu S., Sara M., Sleytr U.B. 1999. Stabilizing effect of an S-layer on liposomes towards thermal or mechanical stress. Biochim. Biophys. Acta. 1418, 106-116.
    • (1999) Biochim. Biophys. Acta , vol.1418 , pp. 106-116
    • Mader, C.1    Kupcu, S.2    Sara, M.3    Sleytr, U.B.4
  • 92
    • 0028433572 scopus 로고
    • Large-scale reconstitution of crystalline bacterial surface layer proteins at the air-water interface and on lipid films
    • Pum D., Sleytr U.B. 1994. Large-scale reconstitution of crystalline bacterial surface layer proteins at the air-water interface and on lipid films. Thin Solid Films. 244, 882-886.
    • (1994) Thin Solid Films , vol.244 , pp. 882-886
    • Pum, D.1    Sleytr, U.B.2
  • 93
    • 0033583512 scopus 로고    scopus 로고
    • Crystalline bacterial cell surface layers (S-layers): From supramolecular cell structure to biomimetic and nanotechnology
    • Sleytr U.B., Messner P., Pum D., Sara M. 1999. Crystalline bacterial cell surface layers (S-layers): from supramolecular cell structure to biomimetic and nanotechnology. Angew. Chem. Int. Ed. 38, 1034-1054.
    • (1999) Angew. Chem. Int. Ed. , vol.38 , pp. 1034-1054
    • Sleytr, U.B.1    Messner, P.2    Pum, D.3    Sara, M.4
  • 94
    • 0038233833 scopus 로고    scopus 로고
    • Nanotechnology goals and challenges for electronic application
    • Bohr M.T. 2002. Nanotechnology goals and challenges for electronic application. IEEE Trans. Nanotechnol. 1, 56-62.
    • (2002) IEEE Trans. Nanotechnol. , vol.1 , pp. 56-62
    • Bohr, M.T.1
  • 95
    • 0030773829 scopus 로고    scopus 로고
    • Synthesis of cadmium sulphide superlattices using bacterial S-layers
    • Shenton W., Pum D., Sleytr U.B., Mann S. 1997. Synthesis of cadmium sulphide superlattices using bacterial S-layers. Nature. 389, 585-587.
    • (1997) Nature , vol.389 , pp. 585-587
    • Shenton, W.1    Pum, D.2    Sleytr, U.B.3    Mann, S.4
  • 96
    • 0032019299 scopus 로고    scopus 로고
    • Formation of a gold superlattice on an S-layer with square lattice symmetry
    • Dielnweit S., Pum D., Sleytr U.B. 1998. Formation of a gold superlattice on an S-layer with square lattice symmetry. Supramol. Sci. 5, 15-19.
    • (1998) Supramol. Sci. , vol.5 , pp. 15-19
    • Dielnweit, S.1    Pum, D.2    Sleytr, U.B.3
  • 97
    • 0029367707 scopus 로고    scopus 로고
    • Mononuclear reassembly of a crystalline bacterial cell surface (S-layer) on untreated and modified silicon surface
    • Pum D., Sleytr U.B. 1996. Mononuclear reassembly of a crystalline bacterial cell surface (S-layer) on untreated and modified silicon surface. Supramol. Sci. 2, 193-197.
    • (1996) Supramol. Sci. , vol.2 , pp. 193-197
    • Pum, D.1    Sleytr, U.B.2
  • 98
    • 3042995316 scopus 로고
    • Transfer of biologically derived nanometer-scale patterns to smooth substrates
    • Douglas K., Devand G., Clark N.A. 1992. Transfer of biologically derived nanometer-scale patterns to smooth substrates. Science. 257, 642-644.
    • (1992) Science , vol.257 , pp. 642-644
    • Douglas, K.1    Devand, G.2    Clark, N.A.3
  • 99
    • 0342663053 scopus 로고    scopus 로고
    • Biomimetic approaches to nanostructural fabrication
    • Ed. Mann S. N.Y.: VCY
    • Douglas K. 1996. Biomimetic approaches to nanostructural fabrication. In: Biomimetic Materials Chemistry. Ed. Mann S. N.Y.: VCY, 117-142.
    • (1996) Biomimetic Materials Chemistry , pp. 117-142
    • Douglas, K.1
  • 100
    • 0026036332 scopus 로고
    • Image analysis and processing of an imperfect two dimensional crystal: The surface layer of the archaebacterium Sulfjlobus acidocalgarius reinvestigated
    • Lembcke G., Durr R., Hegerl R., et al. 1991. Image analysis and processing of an imperfect two dimensional crystal: The surface layer of the archaebacterium Sulfjlobus acidocalgarius reinvestigated. J. Microsc. 161, 263-278.
    • (1991) J. Microsc. , vol.161 , pp. 263-278
    • Lembcke, G.1    Durr, R.2    Hegerl, R.3
  • 101
    • 0342663051 scopus 로고
    • Low-energy electron beam enhanced etching of Si (100) (2x1) by molecular hydrogen
    • Gillis H.P., Clemons J.L., Chamberlain J.P. 1992. Low-energy electron beam enhanced etching of Si (100) (2x1) by molecular hydrogen. J. Vac. Sci. Technol. B10, 2729-2732.
    • (1992) J. Vac. Sci. Technol. , vol.B10 , pp. 2729-2732
    • Gillis, H.P.1    Clemons, J.L.2    Chamberlain, J.P.3
  • 102
    • 36449001266 scopus 로고
    • Low-energy electron-enhanced etching of Si (100) in hydrogen/helium direct-current plasma
    • Gillis H.P., Chontov D.A., Steiner I.V., et al. 1995. Low-energy electron-enhanced etching of Si (100) in hydrogen/helium direct-current plasma. Appl. Phys. Lett. 66, 2475-2477.
    • (1995) Appl. Phys. Lett. , vol.66 , pp. 2475-2477
    • Gillis, H.P.1    Chontov, D.A.2    Steiner, I.V.3
  • 103
    • 20244364178 scopus 로고    scopus 로고
    • Low-energy electron-enhanced etching of GaAs (100) in a clorine/hydrogen PC plasma
    • Gillis H.P., Chontov D.A., Martin K.P., et al. Low-energy electron-enhanced etching of GaAs (100) in a clorine/hydrogen PC plasma. Appl. Phys. Lett. 68, 2255-2257.
    • Appl. Phys. Lett. , vol.68 , pp. 2255-2257
    • Gillis, H.P.1    Chontov, D.A.2    Martin, K.P.3
  • 104
    • 4444221216 scopus 로고    scopus 로고
    • US Patent Application 20020123227; 2003. US Patent 65.518.194
    • Winningham T.A., Douglas K. 2002. US Patent Application 20020123227; 2003. US Patent 65.518.194.
    • (2002)
    • Winningham, T.A.1    Douglas, K.2
  • 105
    • 0031069380 scopus 로고    scopus 로고
    • Patterning of monolayers of crystalline S-layer proteins on a silicon surface by deep ultraviolet radiation
    • Pum D., Stangl G., Sponer C., et al. 1997. Patterning of monolayers of crystalline S-layer proteins on a silicon surface by deep ultraviolet radiation. Microelectron. Eng. 35. 297-300.
    • (1997) Microelectron. Eng. , vol.35 , pp. 297-300
    • Pum, D.1    Stangl, G.2    Sponer, C.3
  • 106
    • 0141780801 scopus 로고    scopus 로고
    • Molecular biomimetics: Nanotechnology through biology
    • Sarikaya M., Tamerler C., Jen A.R.Y., et al. 2003. Molecular biomimetics: Nanotechnology through biology. Nature Materials. 2, 577-585.
    • (2003) Nature Materials , vol.2 , pp. 577-585
    • Sarikaya, M.1    Tamerler, C.2    Jen, A.R.Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.