메뉴 건너뛰기




Volumn 124, Issue 2-3, 1998, Pages 276-302

Structural research on surface layers: A focus on stability, surface layer homology domains, and surface layer-cell wall interactions

Author keywords

Electron crystallography; Electron microscopy; Electron tomography; High resolution structure of S layers; S layer homology domain; S layer structure; S layer cell wall interactions; SLH domain; Stability of S layer proteins; Surface layer proteins from Bacteria and Archaea

Indexed keywords

ARTICLE; CELL INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN CROSS LINKING; PROTEIN GLYCOSYLATION; PROTEIN ISOLATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY; UNINDEXED SEQUENCE;

EID: 0032464347     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.1998.4070     Document Type: Article
Times cited : (199)

References (181)
  • 1
    • 0021892611 scopus 로고
    • The mechanism of irreversible enzyme inactivation at 100°C
    • Ahern T. J., Klibanov A. M. The mechanism of irreversible enzyme inactivation at 100°C. Science. 228:1985;1280-1284.
    • (1985) Science , vol.228 , pp. 1280-1284
    • Ahern, T.J.1    Klibanov, A.M.2
  • 6
    • 0031831035 scopus 로고    scopus 로고
    • The regulated outer membrane protein Omp21 formComamonas acidovorans
    • Baldermann C., Lupas A., Lubieniecki J., Engelhardt H. The regulated outer membrane protein Omp21 formComamonas acidovorans. J. Bacteriol. 180:1998;3741-3749.
    • (1998) J. Bacteriol. , vol.180 , pp. 3741-3749
    • Baldermann, C.1    Lupas, A.2    Lubieniecki, J.3    Engelhardt, H.4
  • 7
    • 0023053025 scopus 로고
    • The three-dimensional structure of the regular surface layer (HPI-layer) ofDeinococcus radiodurans
    • Baumeister W., Barth M., Hegerl R., Guckenberger R., Hahn M., Saxton W. O. The three-dimensional structure of the regular surface layer (HPI-layer) ofDeinococcus radiodurans. J. Mol. Biol. 187:1986;241-253.
    • (1986) J. Mol. Biol. , vol.187 , pp. 241-253
    • Baumeister, W.1    Barth, M.2    Hegerl, R.3    Guckenberger, R.4    Hahn, M.5    Saxton, W.O.6
  • 8
    • 0000493109 scopus 로고
    • Three-dimensional structure of bacterial surface layers
    • London: Academic Press. p. 109-145
    • Baumeister W., Engelhardt H. Three-dimensional structure of bacterial surface layers. Membranous Structures. 1987;Academic Press, London. p. 109-145.
    • (1987) Membranous Structures
    • Baumeister, W.1    Engelhardt, H.2
  • 9
  • 10
    • 0026467758 scopus 로고
    • Structural features of archaebacterial cell envelopes
    • Baumeister W., Lembcke G. Structural features of archaebacterial cell envelopes. J. Bioenerg. Biomembr. 24:1992;567-575.
    • (1992) J. Bioenerg. Biomembr. , vol.24 , pp. 567-575
    • Baumeister, W.1    Lembcke, G.2
  • 13
    • 0023953848 scopus 로고
    • Bacterial surface proteins. Some structural, functional and evolutionary aspects
    • Baumeister W., Wildhaber I., Engelhardt H. Bacterial surface proteins. Some structural, functional and evolutionary aspects. Biophys. Chem. 29:1988;39-49.
    • (1988) Biophys. Chem. , vol.29 , pp. 39-49
    • Baumeister, W.1    Wildhaber, I.2    Engelhardt, H.3
  • 14
    • 0024523934 scopus 로고
    • Principles of organization in eubacterial and archaebacterial surface proteins
    • Baumeister W., Wildhaber I., Phipps B. M. Principles of organization in eubacterial and archaebacterial surface proteins. Can. J. Microbiol. 35:1989;215-227.
    • (1989) Can. J. Microbiol. , vol.35 , pp. 215-227
    • Baumeister, W.1    Wildhaber, I.2    Phipps, B.M.3
  • 18
    • 0018678010 scopus 로고
    • Surface arrays on the wall ofSporosarcina ureae
    • Beveridge T. J. Surface arrays on the wall ofSporosarcina ureae. J. Bacteriol. 139:1979;1039-1048.
    • (1979) J. Bacteriol. , vol.139 , pp. 1039-1048
    • Beveridge, T.J.1
  • 19
    • 0019395615 scopus 로고
    • Ultrastructure, chemistry, and function of the bacterial wall
    • Beveridge T. J. Ultrastructure, chemistry, and function of the bacterial wall. Intl. Rev. Cytol. 72:1981;229-317.
    • (1981) Intl. Rev. Cytol. , vol.72 , pp. 229-317
    • Beveridge, T.J.1
  • 20
    • 0016262987 scopus 로고
    • Superficial macromolecular array on the cell wall ofSpirillum putridiconchylium
    • Beveridge T. J., Murray R. E. G. Superficial macromolecular array on the cell wall ofSpirillum putridiconchylium. J. Bacteriol. 119:1974;1019-1038.
    • (1974) J. Bacteriol. , vol.119 , pp. 1019-1038
    • Beveridge, T.J.1    Murray, R.E.G.2
  • 21
    • 0016622401 scopus 로고
    • Surface arrays on the cell wall ofSpirillum metamorphum
    • Beveridge T. J., Murray R. E. G. Surface arrays on the cell wall ofSpirillum metamorphum. J. Bacteriol. 124:1975;1529-1544.
    • (1975) J. Bacteriol. , vol.124 , pp. 1529-1544
    • Beveridge, T.J.1    Murray, R.E.G.2
  • 23
    • 0017098791 scopus 로고
    • Superficial cell-wall layers onSpirillum
    • Beveridge T. J., Murray R. E. G. Superficial cell-wall layers onSpirillum. Can. J. Microbiol. 22:1976b;567-582.
    • (1976) Can. J. Microbiol. , vol.22 , pp. 567-582
    • Beveridge, T.J.1    Murray, R.E.G.2
  • 26
    • 0021270996 scopus 로고
    • Regular surface layer ofAzotobacter vinelandii
    • Bingle W. H., Doran J. L., Page W. J. Regular surface layer ofAzotobacter vinelandii. J. Bacteriol. 159:1984;251-259.
    • (1984) J. Bacteriol. , vol.159 , pp. 251-259
    • Bingle, W.H.1    Doran, J.L.2    Page, W.J.3
  • 27
    • 0023445512 scopus 로고
    • Three-dimensional structure of the regular tetragonal surface layer ofAzotobacter vinelandii
    • Bingle W. H., Engelhardt H., Page W. J., Baumeister W. Three-dimensional structure of the regular tetragonal surface layer ofAzotobacter vinelandii. J. Bacteriol. 169:1987;5008-5015.
    • (1987) J. Bacteriol. , vol.169 , pp. 5008-5015
    • Bingle, W.H.1    Engelhardt, H.2    Page, W.J.3    Baumeister, W.4
  • 28
    • 0025063349 scopus 로고
    • Surface array protein ofCampylobacter fetus
    • Blaser M. J., Gotschlich E. C. Surface array protein ofCampylobacter fetus. J. Biol. Chem. 265:1990;14529-14535.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14529-14535
    • Blaser, M.J.1    Gotschlich, E.C.2
  • 30
    • 0024720358 scopus 로고
    • Cloning and sequencing of the gene encoding a 125-kilodalton surface-layer protein fromBacillus sphaericus
    • Bowditch R. D., Baumann P., Yousten A. A. Cloning and sequencing of the gene encoding a 125-kilodalton surface-layer protein fromBacillus sphaericus. J. Bacteriol. 171:1989;4178-4188.
    • (1989) J. Bacteriol. , vol.171 , pp. 4178-4188
    • Bowditch, R.D.1    Baumann, P.2    Yousten, A.A.3
  • 31
    • 0026620295 scopus 로고
    • Evidence for an S-layer protein pool in the peptidoglycan ofBacillus stearothermophilus
    • Breitwieser A., Gruber K., Sleytr U. B. Evidence for an S-layer protein pool in the peptidoglycan ofBacillus stearothermophilus. J. Bacteriol. 174:1992;8008-8015.
    • (1992) J. Bacteriol. , vol.174 , pp. 8008-8015
    • Breitwieser, A.1    Gruber, K.2    Sleytr, U.B.3
  • 32
    • 0027476160 scopus 로고
    • Assymmetry of orientation and voltage gating of theAcidovorax delafieldii
    • Brunen M., Engelhardt H. Assymmetry of orientation and voltage gating of theAcidovorax delafieldii. Eur. J. Biochem. 212:1993;129-135.
    • (1993) Eur. J. Biochem. , vol.212 , pp. 129-135
    • Brunen, M.1    Engelhardt, H.2
  • 34
    • 0025066725 scopus 로고
    • Characterization of the gene encoding the protective paracrystalline surface-layer protein ofRickettsia prowazekii:Rickettsia typhi
    • Carl M., Dobson M. E., Ching W.-M., Dasch G. A. Characterization of the gene encoding the protective paracrystalline surface-layer protein ofRickettsia prowazekii:Rickettsia typhi. Proc. Natl. Acad. Sci. USA. 87:1990;8237-8241.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 8237-8241
    • Carl, M.1    Dobson, M.E.2    Ching, W.-M.3    Dasch, G.A.4
  • 35
    • 85030356674 scopus 로고
    • Description of two regular structures associated to the cell envelope ofThermus thermophilus:
    • in, Peachey, L. D.Williams, D. B. 269, San Francisco Press, San Francisco
    • Carrascosa, J. L. Castón, J. R. Faraldo, M. M. Berenguer, J. de Pedro, M. A. 1990, Description of two regular structures associated to the cell envelope ofThermus thermophilus:, in, Peachey, L. D.Williams, D. B. Proc. XIIth Int. Congress Electron Microscopy, 1, 268, 269, San Francisco Press, San Francisco.
    • (1990) Proc. XIIth Int. Congress Electron Microscopy , vol.1 , pp. 268
    • Carrascosa, J.L.1    Castón, J.R.2    Faraldo, M.M.3    Berenguer, J.4    De Pedro, M.A.5
  • 40
    • 0020394274 scopus 로고
    • A correlation between protein thermostability and resistance to proteolysis
    • Daniel R. M., Cowan D. A., Morgan H. W., Curran M. P. A correlation between protein thermostability and resistance to proteolysis. Biochem. J. 207:1982;641-644.
    • (1982) Biochem. J. , vol.207 , pp. 641-644
    • Daniel, R.M.1    Cowan, D.A.2    Morgan, H.W.3    Curran, M.P.4
  • 41
    • 0342875445 scopus 로고
    • The stability of proteins from extreme thermophiles
    • D.L. Oxeder. New York: A. R. Liss
    • Daniel R. M. The stability of proteins from extreme thermophiles. Oxeder D. L. Protein Structure, Folding and Design. 1986;291-296 A. R. Liss, New York.
    • (1986) Protein Structure, Folding and Design , pp. 291-296
    • Daniel, R.M.1
  • 42
    • 0031580211 scopus 로고    scopus 로고
    • Role of the carboxy-terminal phenylalanine in the biogenesis of outer membrane protein PhoE ofEscherichia coli
    • de Cock H., Struyve M., Kleerebezem M., van der Krift T., Tommassen J. Role of the carboxy-terminal phenylalanine in the biogenesis of outer membrane protein PhoE ofEscherichia coli. J. Mol. Biol. 269:1997;473-478.
    • (1997) J. Mol. Biol. , vol.269 , pp. 473-478
    • De Cock, H.1    Struyve, M.2    Kleerebezem, M.3    Van Der Krift, T.4    Tommassen, J.5
  • 43
    • 0022578265 scopus 로고
    • Structure, biosynthesis, and physicochemical properties of archaebacterial lipids
    • de Rosa M., Gambacorta A., Gliozzi A. Structure, biosynthesis, and physicochemical properties of archaebacterial lipids. Microbiol. Rev. 50:1986;70-80.
    • (1986) Microbiol. Rev. , vol.50 , pp. 70-80
    • De Rosa, M.1    Gambacorta, A.2    Gliozzi, A.3
  • 44
    • 0024485484 scopus 로고
    • Three-dimensional structure of an open form of the surface layer from the fish pathogenAeromonas salmonicida
    • Dooley J. S. G., Engelhardt H., Baumeister W., Kay W. W., Trust T. J. Three-dimensional structure of an open form of the surface layer from the fish pathogenAeromonas salmonicida. J. Bacteriol. 171:1989;190-197.
    • (1989) J. Bacteriol. , vol.171 , pp. 190-197
    • Dooley, J.S.G.1    Engelhardt, H.2    Baumeister, W.3    Kay, W.W.4    Trust, T.J.5
  • 45
    • 0023112774 scopus 로고
    • Role of calcium in assembly of theAzotobacter vinelandii
    • Doran J. L., Bingle W. H., Page W. J. Role of calcium in assembly of theAzotobacter vinelandii. J. Gen. Microbiol. 133:1987;399-413.
    • (1987) J. Gen. Microbiol. , vol.133 , pp. 399-413
    • Doran, J.L.1    Bingle, W.H.2    Page, W.J.3
  • 46
    • 0031569879 scopus 로고    scopus 로고
    • Making a fitting choice: Common aspects of sugar-binding sites in plant and animal lectins
    • Drickamer K. Making a fitting choice: Common aspects of sugar-binding sites in plant and animal lectins. Structure. 5:1997;465-468.
    • (1997) Structure , vol.5 , pp. 465-468
    • Drickamer, K.1
  • 47
    • 0025733570 scopus 로고
    • Three-dimensional reconstruction of the surface protein ofPyrodictium brockii:
    • Dürr R., Hegerl R., Volker S., Santarius U., Baumeister W. Three-dimensional reconstruction of the surface protein ofPyrodictium brockii: J. Struct. Biol. 106:1991;181-190.
    • (1991) J. Struct. Biol. , vol.106 , pp. 181-190
    • Dürr, R.1    Hegerl, R.2    Volker, S.3    Santarius, U.4    Baumeister, W.5
  • 48
    • 0029644059 scopus 로고    scopus 로고
    • Crystal strutures of various maltooligosaccharides bound to maltoporin reveal a specific sugar translocation pathway
    • Dutzler R., Wang Y.-F., Rizkallah P. J., Rosenbusch J. P., Schirmer T. Crystal strutures of various maltooligosaccharides bound to maltoporin reveal a specific sugar translocation pathway. Structure. 4:1996;127-134.
    • (1996) Structure , vol.4 , pp. 127-134
    • Dutzler, R.1    Wang, Y.-F.2    Rizkallah, P.J.3    Rosenbusch, J.P.4    Schirmer, T.5
  • 49
    • 0029819431 scopus 로고    scopus 로고
    • Evidence that an N-terminal S-layer protein fragment triggers the release of a cell-associated high-molecular-weight amylase inBacillus stearothermophilus
    • Egelseer E. M., Schocher I., Sleytr U. B., Sára M. Evidence that an N-terminal S-layer protein fragment triggers the release of a cell-associated high-molecular-weight amylase inBacillus stearothermophilus. J. Bacteriol. 178:1996;5602-5609.
    • (1996) J. Bacteriol. , vol.178 , pp. 5602-5609
    • Egelseer, E.M.1    Schocher, I.2    Sleytr, U.B.3    Sára, M.4
  • 51
    • 0023224783 scopus 로고
    • Outer membrane-bound protease ofDeinococcus radiodurans
    • Emde-Kamola B., Karrenberg F. H. Outer membrane-bound protease ofDeinococcus radiodurans. FEMS Microbiol. Lett. 42:1987;69-74.
    • (1987) FEMS Microbiol. Lett. , vol.42 , pp. 69-74
    • Emde-Kamola, B.1    Karrenberg, F.H.2
  • 52
    • 0022380710 scopus 로고
    • Porin channel triplets merge into single outlets inEscherichia coli
    • Engel A., Massalski A., Schindler H., Dorset D. L., Rosenbusch J. P. Porin channel triplets merge into single outlets inEscherichia coli. Nature. 317:1985;643-645.
    • (1985) Nature , vol.317 , pp. 643-645
    • Engel, A.1    Massalski, A.2    Schindler, H.3    Dorset, D.L.4    Rosenbusch, J.P.5
  • 53
    • 0026439779 scopus 로고
    • Isolation and cloning of Ompα, a coiled-coil protein spanning the periplasmic space of the ancestral eubacteriumThermotoga maritima
    • Engel A. M., Cejka Z., Lupas A., Lottspeich F., Baumeister W. Isolation and cloning of Ompα, a coiled-coil protein spanning the periplasmic space of the ancestral eubacteriumThermotoga maritima. EMBO J. 11:1992;4369-4378.
    • (1992) EMBO J. , vol.11 , pp. 4369-4378
    • Engel, A.M.1    Cejka, Z.2    Lupas, A.3    Lottspeich, F.4    Baumeister, W.5
  • 54
    • 0022520187 scopus 로고
    • Three-dimensional structure of the tetragonal surface layer ofSporosarcina ureae
    • Engelhardt H., Saxton O. W., Baumeister W. Three-dimensional structure of the tetragonal surface layer ofSporosarcina ureae. J. Bacteriol. 168:1986;309-317.
    • (1986) J. Bacteriol. , vol.168 , pp. 309-317
    • Engelhardt, H.1    Saxton, O.W.2    Baumeister, W.3
  • 56
    • 0025734127 scopus 로고
    • The three-dimensional structure of the regular surface protein ofComamonas acidovorans
    • Engelhardt H., Gerbl-Rieger S., Santarius U., Baumeister W. The three-dimensional structure of the regular surface protein ofComamonas acidovorans. Mol. Microbiol. 5:1991;1695-1702.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1695-1702
    • Engelhardt, H.1    Gerbl-Rieger, S.2    Santarius, U.3    Baumeister, W.4
  • 57
    • 38249027644 scopus 로고
    • Purification, composition and Ca2+-binding properties of the monomeric protein of the S-layer ofThermus thermophilus
    • Faraldo M. L. M., de Pedro M. A., Berenguer J. Purification, composition and Ca2+-binding properties of the monomeric protein of the S-layer ofThermus thermophilus. FEBS Lett. 235:1988;117-121.
    • (1988) FEBS Lett. , vol.235 , pp. 117-121
    • Faraldo, M.L.M.1    De Pedro, M.A.2    Berenguer, J.3
  • 58
    • 0030889859 scopus 로고    scopus 로고
    • Surface properties and a novel transcription factor regulate the expression of the S-layer ofThermus thermophilus
    • Fernandez-Herrero L. A., Olabarría G., Berenguer J. Surface properties and a novel transcription factor regulate the expression of the S-layer ofThermus thermophilus. Mol. Microbiol. 24:1997;61-72.
    • (1997) Mol. Microbiol. , vol.24 , pp. 61-72
    • Fernandez-Herrero, L.A.1    Olabarría, G.2    Berenguer, J.3
  • 60
    • 0028276244 scopus 로고
    • The organization of the paracrystalline multilayered spacer-plugs ofMethanospirillum hungatei
    • Firtel M., Southam G., Harauz G., Beveridge T. J. The organization of the paracrystalline multilayered spacer-plugs ofMethanospirillum hungatei. J. Struct. Biol. 112:1994;160-172.
    • (1994) J. Struct. Biol. , vol.112 , pp. 160-172
    • Firtel, M.1    Southam, G.2    Harauz, G.3    Beveridge, T.J.4
  • 61
    • 0031985785 scopus 로고    scopus 로고
    • Structure of the sucrose-specific porin ScrY fromSalmonella typhimurium
    • Forst D., Welte W., Wacker T., Diederichs K. Structure of the sucrose-specific porin ScrY fromSalmonella typhimurium. Nat. Struct. Biol. 5:1998;37-46.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 37-46
    • Forst, D.1    Welte, W.2    Wacker, T.3    Diederichs, K.4
  • 62
    • 0026984730 scopus 로고
    • Novel structural patterns in divalent cation-depleted surface layers ofAeromonas salmonicida
    • Garduño R. A., Phipps B. M., Baumeister W., Kay W. W. Novel structural patterns in divalent cation-depleted surface layers ofAeromonas salmonicida. J. Struct. Biol. 109:1992;184-195.
    • (1992) J. Struct. Biol. , vol.109 , pp. 184-195
    • Garduño, R.A.1    Phipps, B.M.2    Baumeister, W.3    Kay, W.W.4
  • 63
    • 0021112470 scopus 로고
    • DNA sequences, gene regulation and modular protein evolution in theDrosophila
    • Garfinkel M. D., Pruitt R. E., Meyerowitz E. M. DNA sequences, gene regulation and modular protein evolution in theDrosophila. J. Mol. Biol. 168:1983;765-789.
    • (1983) J. Mol. Biol. , vol.168 , pp. 765-789
    • Garfinkel, M.D.1    Pruitt, R.E.2    Meyerowitz, E.M.3
  • 65
    • 0026716013 scopus 로고
    • Nucleotide sequence analysis of the gene encoding theCaulobacter crescentus
    • Gilchrist A., Fisher J. A., Smit J. Nucleotide sequence analysis of the gene encoding theCaulobacter crescentus. Can. J. Microbiol. 38:1992;193-202.
    • (1992) Can. J. Microbiol. , vol.38 , pp. 193-202
    • Gilchrist, A.1    Fisher, J.A.2    Smit, J.3
  • 66
    • 0024644887 scopus 로고
    • Three-dimensional reconstructions from incomplete data: Interpretability of density maps at "atomic" resolution
    • Glaeser R. M., Tong L., Kim S.-H. Three-dimensional reconstructions from incomplete data: Interpretability of density maps at "atomic" resolution. Ultramicroscopy. 27:1989;307-318.
    • (1989) Ultramicroscopy , vol.27 , pp. 307-318
    • Glaeser, R.M.1    Tong, L.2    Kim, S.-H.3
  • 67
    • 0020675618 scopus 로고
    • Monolayer black membranes from bipolar lipids of archaebacteria and their temperature-induced structural changes
    • Gliozzi A., Rolandi R., De Rosa M., Gambacorta A. Monolayer black membranes from bipolar lipids of archaebacteria and their temperature-induced structural changes. J. Membr. Biol. 75:1983;45-56.
    • (1983) J. Membr. Biol. , vol.75 , pp. 45-56
    • Gliozzi, A.1    Rolandi, R.2    De Rosa, M.3    Gambacorta, A.4
  • 70
    • 0023708875 scopus 로고
    • Localized insertion of new S-layer during growth ofBacillus stearothermophilus
    • Gruber K., Sleytr U. B. Localized insertion of new S-layer during growth ofBacillus stearothermophilus. Arch. Microbiol. 149:1988;485-491.
    • (1988) Arch. Microbiol. , vol.149 , pp. 485-491
    • Gruber, K.1    Sleytr, U.B.2
  • 71
    • 0032007853 scopus 로고    scopus 로고
    • Strategies for optimizing protein expression inE. coli
    • Hannig G., Makrides S. C. Strategies for optimizing protein expression inE. coli. Trends Biotechnol. 16:1998;54-60.
    • (1998) Trends Biotechnol. , vol.16 , pp. 54-60
    • Hannig, G.1    Makrides, S.C.2
  • 72
    • 0032581675 scopus 로고    scopus 로고
    • Cloning and characterization of the genes coding for two porins in the unicellular cyanobacteriumSynechococcus
    • Hansel A., Pattus F., Jürgens U. J., Tadros M. H. Cloning and characterization of the genes coding for two porins in the unicellular cyanobacteriumSynechococcus. Biochim. Biophys. Acta. 1399:1998;31-39.
    • (1998) Biochim. Biophys. Acta , vol.1399 , pp. 31-39
    • Hansel, A.1    Pattus, F.2    Jürgens, U.J.3    Tadros, M.H.4
  • 73
    • 0031966135 scopus 로고    scopus 로고
    • Characterization of two pore-forming proteins isolated from the outer membrane ofSynechococcus
    • Hansel A., Tadros M. H. Characterization of two pore-forming proteins isolated from the outer membrane ofSynechococcus. Curr. Microbiol. 36:1998;321-326.
    • (1998) Curr. Microbiol. , vol.36 , pp. 321-326
    • Hansel, A.1    Tadros, M.H.2
  • 74
    • 0027756896 scopus 로고
    • A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants
    • Harbury P. B., Zhang T., Kim P. S., Alber T. A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants. Science. 262:1993;1401-1407.
    • (1993) Science , vol.262 , pp. 1401-1407
    • Harbury, P.B.1    Zhang, T.2    Kim, P.S.3    Alber, T.4
  • 75
    • 0018361068 scopus 로고
    • Isolation, characterization, and in vitro assembly of the tetragonally arrayed layer ofBacillus sphaericus
    • Hastie A. T., Brinton C. C. Jr. Isolation, characterization, and in vitro assembly of the tetragonally arrayed layer ofBacillus sphaericus. J. Bacteriol. 138:1979;999-1009.
    • (1979) J. Bacteriol. , vol.138 , pp. 999-1009
    • Hastie, A.T.1    Brinton C.C., Jr.2
  • 76
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson R., Baldwin J. M., Ceska T. A., Zemlin F., Beckmann E., Downing K. H. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 213:1990;899-929.
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 77
    • 0025351922 scopus 로고
    • Proteins under extreme physical conditions
    • Jaenicke R., Závodszky P. Proteins under extreme physical conditions. FEBS Lett. 268:1990;344-349.
    • (1990) FEBS Lett. , vol.268 , pp. 344-349
    • Jaenicke, R.1    Závodszky, P.2
  • 79
    • 0032493739 scopus 로고    scopus 로고
    • Investigation of the structural basis for thermostability of DNA-binding protein HU fromBacillus stearothermophilus
    • Kawamura S., Abe Y., Ueda T., Masumoto K., Imoto T., Yamasaki N., Kimura M. Investigation of the structural basis for thermostability of DNA-binding protein HU fromBacillus stearothermophilus. J. Biol. Chem. 273:1998;19982-19987.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19982-19987
    • Kawamura, S.1    Abe, Y.2    Ueda, T.3    Masumoto, K.4    Imoto, T.5    Yamasaki, N.6    Kimura, M.7
  • 80
    • 0022376557 scopus 로고
    • Purification and disposition of a surface protein associated with virulence ofAeromonas salmonicida
    • Kay W. W., Bucklex J. T., Ishiguro E. E., Phipps B. M., Monette J. P. L., Trust T. J. Purification and disposition of a surface protein associated with virulence ofAeromonas salmonicida. J. Bacteriol. 164:1985a;1332-1336.
    • (1985) J. Bacteriol. , vol.164 , pp. 1332-1336
    • Kay, W.W.1    Bucklex, J.T.2    Ishiguro, E.E.3    Phipps, B.M.4    Monette, J.P.L.5    Trust, T.J.6
  • 81
    • 0022376557 scopus 로고
    • Prophyrin binding by the surface array virulence protein ofAeromonas salmonicida
    • Kay W. W., Phipps B., Ishiguro E. E., Trust T. J. Prophyrin binding by the surface array virulence protein ofAeromonas salmonicida. J. Bacteriol. 164:1985b;1332-1336.
    • (1985) J. Bacteriol. , vol.164 , pp. 1332-1336
    • Kay, W.W.1    Phipps, B.2    Ishiguro, E.E.3    Trust, T.J.4
  • 83
    • 0024279245 scopus 로고
    • Naturally crystalline porin in the outer membrane ofBordetella pertussis
    • Kessel M., Brennan M. J., Trus B. L., Bisher M. E., Steven A. C. Naturally crystalline porin in the outer membrane ofBordetella pertussis. J. Mol. Biol. 203:1988a;275-278.
    • (1988) J. Mol. Biol. , vol.203 , pp. 275-278
    • Kessel, M.1    Brennan, M.J.2    Trus, B.L.3    Bisher, M.E.4    Steven, A.C.5
  • 84
    • 84985269049 scopus 로고
    • The structure of the stalk surface layer of a brine pond microorganism: Correlation averaging applied to a double layered lattice structure
    • Kessel M., Radermacher M., Frank J. The structure of the stalk surface layer of a brine pond microorganism: Correlation averaging applied to a double layered lattice structure. J. Microsc. (Oxford. 139:1985;63-74.
    • (1985) J. Microsc. (Oxford , vol.139 , pp. 63-74
    • Kessel, M.1    Radermacher, M.2    Frank, J.3
  • 85
    • 0000499006 scopus 로고
    • Three-dimensional structure of the regular surface glycoprotein layer ofHalobacterium volcanii
    • Kessel M., Wildhaber I., Cohen S., Baumeister W. Three-dimensional structure of the regular surface glycoprotein layer ofHalobacterium volcanii. EMBO J. 7:1988b;1549-1554.
    • (1988) EMBO J. , vol.7 , pp. 1549-1554
    • Kessel, M.1    Wildhaber, I.2    Cohen, S.3    Baumeister, W.4
  • 87
    • 0029092472 scopus 로고
    • MicroCorrespondence. Proposal for a peptidoglycan-associating alpha-helical motif in the C-terminal regions of some bacterial cell-surface proteins
    • Koebnik R. MicroCorrespondence. Proposal for a peptidoglycan-associating alpha-helical motif in the C-terminal regions of some bacterial cell-surface proteins. Mol. Microbiol. 16:1995;1269-1270.
    • (1995) Mol. Microbiol. , vol.16 , pp. 1269-1270
    • Koebnik, R.1
  • 89
    • 0021843326 scopus 로고
    • Effect of calcium on thein vivoAquaspirillum serpens
    • Koval S. F., Murray R. G. E. Effect of calcium on thein vivoAquaspirillum serpens. Can. J. Microbiol. 31:1985;261-267.
    • (1985) Can. J. Microbiol. , vol.31 , pp. 261-267
    • Koval, S.F.1    Murray, R.G.E.2
  • 90
    • 0030054098 scopus 로고    scopus 로고
    • Heterologous expression and self-assembly of the S-layer protein SbsA ofBacillus stearothermophilusEscherichia coli.
    • Kuen B., Sará M., Lubitz W. Heterologous expression and self-assembly of the S-layer protein SbsA ofBacillus stearothermophilusEscherichia coli. Mol. Microbiol. 19:1996;495-503.
    • (1996) Mol. Microbiol. , vol.19 , pp. 495-503
    • Kuen, B.1    Sará, M.2    Lubitz, W.3
  • 91
    • 0028147508 scopus 로고
    • Atomic model of plant light-harvesting complex by electron crystallography
    • Kühlbrandt W., Wang D. N., Fujioshi Y. Atomic model of plant light-harvesting complex by electron crystallography. Nature. 367:1994;614-621.
    • (1994) Nature , vol.367 , pp. 614-621
    • Kühlbrandt, W.1    Wang, D.N.2    Fujioshi, Y.3
  • 92
    • 0018383067 scopus 로고
    • Regularly arranged structures on the surface of somePseudomonas
    • Lapchine L. Regularly arranged structures on the surface of somePseudomonas. FEMS Microbiol. Lett. 5:1979;223-225.
    • (1979) FEMS Microbiol. Lett. , vol.5 , pp. 223-225
    • Lapchine, L.1
  • 93
  • 94
    • 0023655597 scopus 로고
    • The primary structure of a procaryotic glycoprotein
    • Lechner J., Sumper M. The primary structure of a procaryotic glycoprotein. J. Biol. Chem. 262:1987;9724-9729.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9724-9729
    • Lechner, J.1    Sumper, M.2
  • 96
    • 0027540622 scopus 로고
    • Cryo-electron microscopy of the surface protein ofSulfolobus shibatae
    • Lembcke G., Baumeister W., Beckmann E., Zemlin F. Cryo-electron microscopy of the surface protein ofSulfolobus shibatae. Ultramicroscopy. 49:1993;397-406.
    • (1993) Ultramicroscopy , vol.49 , pp. 397-406
    • Lembcke, G.1    Baumeister, W.2    Beckmann, E.3    Zemlin, F.4
  • 97
    • 0022528232 scopus 로고
    • Three-dimensional structure of the T-layer ofBacillus sphaericus
    • Lepault J., Martin N., Leonard K. Three-dimensional structure of the T-layer ofBacillus sphaericus. J. Bacteriol. 168:1986;303-308.
    • (1986) J. Bacteriol. , vol.168 , pp. 303-308
    • Lepault, J.1    Martin, N.2    Leonard, K.3
  • 98
    • 0025159447 scopus 로고
    • Purification, characterization, and gene cloning of thermopsin, a thermostable acid protease fromSulfolobus acidocaldarius
    • Lin X., Tang J. Purification, characterization, and gene cloning of thermopsin, a thermostable acid protease fromSulfolobus acidocaldarius. J. Biol. Chem. 265:1990;1490-1495.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1490-1495
    • Lin, X.1    Tang, J.2
  • 100
    • 0000230584 scopus 로고    scopus 로고
    • MicroCorrespondence. A circular permutation event in the evolution of the SLH domain
    • Lupas A. MicroCorrespondence. A circular permutation event in the evolution of the SLH domain. Mol. Microbiol. 20:1996;895-900.
    • (1996) Mol. Microbiol. , vol.20 , pp. 895-900
    • Lupas, A.1
  • 102
    • 0028987628 scopus 로고
    • Model structure of the Ompα rod, a parallel four-stranded coiled coil from the hyperthermophilic eubacteriumThermotoga maritima
    • Lupas A., Müller S., Goldie K., Engel A., Baumeister W. Model structure of the Ompα rod, a parallel four-stranded coiled coil from the hyperthermophilic eubacteriumThermotoga maritima. J. Mol. Biol. 248:1995;180-189.
    • (1995) J. Mol. Biol. , vol.248 , pp. 180-189
    • Lupas, A.1    Müller, S.2    Goldie, K.3    Engel, A.4    Baumeister, W.5
  • 103
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas A., van Dyke M., Stock J. Predicting coiled coils from protein sequences. Science. 252:1991;1162-1164.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 104
    • 0031658512 scopus 로고    scopus 로고
    • Nonlinear and asymmetric open channel characteristics of an ion-selective porin in planar membranes
    • Mathes A., Engelhardt H. Nonlinear and asymmetric open channel characteristics of an ion-selective porin in planar membranes. Biophys. J. 75:1998;1255-1262.
    • (1998) Biophys. J. , vol.75 , pp. 1255-1262
    • Mathes, A.1    Engelhardt, H.2
  • 105
    • 0029853345 scopus 로고    scopus 로고
    • Characterization of genes fromThermoanaerobacterium thermosulfurigenes
    • Matuschek M., Sahm K., Zibat A., Bahl H. Characterization of genes fromThermoanaerobacterium thermosulfurigenes. Mol. Gen. Genet. 252:1996;493-496.
    • (1996) Mol. Gen. Genet. , vol.252 , pp. 493-496
    • Matuschek, M.1    Sahm, K.2    Zibat, A.3    Bahl, H.4
  • 106
    • 0030156252 scopus 로고    scopus 로고
    • A hyperthermostable protease of the subtilisin family bound to the surface layer of the archaeonStaphylothermus marinus
    • Mayr J., Lupas A., Kellermann J., Eckerskorn C., Baumeister W., Peters J. A hyperthermostable protease of the subtilisin family bound to the surface layer of the archaeonStaphylothermus marinus. Curr. Biol. 6:1996;739-749.
    • (1996) Curr. Biol. , vol.6 , pp. 739-749
    • Mayr, J.1    Lupas, A.2    Kellermann, J.3    Eckerskorn, C.4    Baumeister, W.5    Peters, J.6
  • 108
    • 0021261426 scopus 로고
    • Paracrystalline cell wall surface layers of differentBacillus stearothermophilus
    • Messner P., Hollaus F., Sleytr U. B. Paracrystalline cell wall surface layers of differentBacillus stearothermophilus. Intl. J. Syst. Bacteriol. 34:1984;202-210.
    • (1984) Intl. J. Syst. Bacteriol. , vol.34 , pp. 202-210
    • Messner, P.1    Hollaus, F.2    Sleytr, U.B.3
  • 109
    • 0022639502 scopus 로고
    • Ultrastructure of the cell envelope of the archaeabacteriaThermoproteus tenaxThermoproteus neutrophilus
    • Messner P., Pum D., Sára M., Stetter K. O., Sleytr U. B. Ultrastructure of the cell envelope of the archaeabacteriaThermoproteus tenaxThermoproteus neutrophilus. J. Bacteriol. 166:1986;1046-1054.
    • (1986) J. Bacteriol. , vol.166 , pp. 1046-1054
    • Messner, P.1    Pum, D.2    Sára, M.3    Stetter, K.O.4    Sleytr, U.B.5
  • 110
    • 0030058166 scopus 로고    scopus 로고
    • Conformational change of the hexagonally packed intermediate layer ofDeinococcus radiodurans
    • Müller D. J., Baumeister W., Engel A. Conformational change of the hexagonally packed intermediate layer ofDeinococcus radiodurans. J. Bacteriol. 178:1996;3025-3030.
    • (1996) J. Bacteriol. , vol.178 , pp. 3025-3030
    • Müller, D.J.1    Baumeister, W.2    Engel, A.3
  • 111
    • 0031194365 scopus 로고    scopus 로고
    • Structural changes in native membrane proteins monitored at subnanometer resolution with the atomic force microscope: A Review
    • Müller D. J., Schoenenberger C.-A., Schabert F., Engel A. Structural changes in native membrane proteins monitored at subnanometer resolution with the atomic force microscope: A Review. J. Struct. Biol. 119:1997;149-157.
    • (1997) J. Struct. Biol. , vol.119 , pp. 149-157
    • Müller, D.J.1    Schoenenberger, C.-A.2    Schabert, F.3    Engel, A.4
  • 112
    • 0030882980 scopus 로고    scopus 로고
    • Characterization of a porin fromMycobacterium smegmatis
    • Mukhopadhyay S., Basu D., Chakrabarti P. Characterization of a porin fromMycobacterium smegmatis. J. Bacteriol. 179:1997;6205-6207.
    • (1997) J. Bacteriol. , vol.179 , pp. 6205-6207
    • Mukhopadhyay, S.1    Basu, D.2    Chakrabarti, P.3
  • 114
    • 0024571246 scopus 로고
    • Crystallization and preliminary X-ray analysis of porin fromRhodobacter capsulatus
    • Nestel U., Wacker T., Woitzik D., Weckesser J., Kreutz W., Welte W. Crystallization and preliminary X-ray analysis of porin fromRhodobacter capsulatus. FEBS Lett. 242:1989;405-408.
    • (1989) FEBS Lett. , vol.242 , pp. 405-408
    • Nestel, U.1    Wacker, T.2    Woitzik, D.3    Weckesser, J.4    Kreutz, W.5    Welte, W.6
  • 115
    • 0029560316 scopus 로고
    • Identification of channel-froming activity in the cell wall ofCorynebacterium glutamicum
    • Niederweis M., Meier E., Lichtinger T., Benz R., Kramer R. Identification of channel-froming activity in the cell wall ofCorynebacterium glutamicum. J. Bacteriol. 177:1995;5716-5718.
    • (1995) J. Bacteriol. , vol.177 , pp. 5716-5718
    • Niederweis, M.1    Meier, E.2    Lichtinger, T.3    Benz, R.4    Kramer, R.5
  • 116
    • 0020597554 scopus 로고
    • Porin channels inEscherichia coli.
    • Nikaido H., Rosenberg E. Y. Porin channels inEscherichia coli. J. Bacteriol. 153:1983;241-252.
    • (1983) J. Bacteriol. , vol.153 , pp. 241-252
    • Nikaido, H.1    Rosenberg, E.Y.2
  • 117
    • 0001373925 scopus 로고
    • Complete sequence and transcript regulation of a cell adhesion protein from aggregatingDictyostelium
    • Noegel A., Gerisch G., Stadler J., Westphal M. Complete sequence and transcript regulation of a cell adhesion protein from aggregatingDictyostelium. EMBO J. 5:1986;1473-1476.
    • (1986) EMBO J. , vol.5 , pp. 1473-1476
    • Noegel, A.1    Gerisch, G.2    Stadler, J.3    Westphal, M.4
  • 118
    • 0030928054 scopus 로고    scopus 로고
    • The synthesis, secretion and role in virulence of the paracrystalline surface protein layers ofAeromonas salmonicidaA. hydrophila
    • Noonan B., Trust T. J. The synthesis, secretion and role in virulence of the paracrystalline surface protein layers ofAeromonas salmonicidaA. hydrophila. FEMS Lett. 154:1997;1-7.
    • (1997) FEMS Lett. , vol.154 , pp. 1-7
    • Noonan, B.1    Trust, T.J.2
  • 119
    • 10144222885 scopus 로고    scopus 로고
    • A conserved motif in S-layer proteins is involved in peptidoglycan binding inThermus thermophilus
    • Olabarría G., Carrascosa J. L., de Pedro M. A., Berenguer J. A conserved motif in S-layer proteins is involved in peptidoglycan binding inThermus thermophilus. J. Bacteriol. 178:1996a;4765-4772.
    • (1996) J. Bacteriol. , vol.178 , pp. 4765-4772
    • Olabarría, G.1    Carrascosa, J.L.2    De Pedro, M.A.3    Berenguer, J.4
  • 120
    • 0030045981 scopus 로고    scopus 로고
    • SlpM, a gene coding for an "s-layer-like array" overexpressed in S-layer mutants ofThermus thermophilus
    • Olabarría G., Fernández-Herrero L. A., Carrascosa J. L., Berenguer J. slpM, a gene coding for an "S-layer-like array" overexpressed in S-layer mutants ofThermus thermophilus. J. Bacteriol. 178:1996b;357-365.
    • (1996) J. Bacteriol. , vol.178 , pp. 357-365
    • Olabarría, G.1    Fernández-Herrero, L.A.2    Carrascosa, J.L.3    Berenguer, J.4
  • 121
    • 0024195466 scopus 로고
    • Modification of proteins with covalent lipids
    • Olson E. N. Modification of proteins with covalent lipids. Prog. Lipid Res. 27:1988;177-197.
    • (1988) Prog. Lipid Res. , vol.27 , pp. 177-197
    • Olson, E.N.1
  • 122
    • 0019513289 scopus 로고
    • Recovery of competence in calcium-limitedAzotobacter vinelandii
    • Page W. J., Doran J. L. Recovery of competence in calcium-limitedAzotobacter vinelandii. J. Bacteriol. 146:1981;33-40.
    • (1981) J. Bacteriol. , vol.146 , pp. 33-40
    • Page, W.J.1    Doran, J.L.2
  • 123
    • 0026557660 scopus 로고
    • Two-dimensional crystallization of a bacterial surface protein on lipid vesicles under controlled conditions
    • Paul A., Engelhardt H., Jakubowski U., Baumeister W. Two-dimensional crystallization of a bacterial surface protein on lipid vesicles under controlled conditions. Biophys. J. 61:1992;172-188.
    • (1992) Biophys. J. , vol.61 , pp. 172-188
    • Paul, A.1    Engelhardt, H.2    Jakubowski, U.3    Baumeister, W.4
  • 124
    • 0022534712 scopus 로고
    • Molecular cloning, expression, and characterization of the gene for the surface (HPI)-layer protein ofDeinococcus radioduransEscherichia coli
    • Peters J., Baumeister W. Molecular cloning, expression, and characterization of the gene for the surface (HPI)-layer protein ofDeinococcus radioduransEscherichia coli. J. Bacteriol. 167:1986;1048-1054.
    • (1986) J. Bacteriol. , vol.167 , pp. 1048-1054
    • Peters, J.1    Baumeister, W.2
  • 125
    • 0029942482 scopus 로고    scopus 로고
    • Hyperthermostable surface layer protein tetrabrachion from the archaebacteriumStaphylothermus marinus:
    • Peters J., Baumeister W., Lupas A. Hyperthermostable surface layer protein tetrabrachion from the archaebacteriumStaphylothermus marinus: J. Mol. Biol. 257:1996;1031-1041.
    • (1996) J. Mol. Biol. , vol.257 , pp. 1031-1041
    • Peters, J.1    Baumeister, W.2    Lupas, A.3
  • 127
    • 0024467302 scopus 로고
    • S-layer protein gene ofAcetogenium kivui:Escherichia coli
    • Peters J., Peters M., Lottspeich F., Baumeister W. S-layer protein gene ofAcetogenium kivui:Escherichia coli. J. Bacteriol. 171:1989;6307-63115.
    • (1989) J. Bacteriol. , vol.171 , pp. 6307-63115
    • Peters, J.1    Peters, M.2    Lottspeich, F.3    Baumeister, W.4
  • 128
    • 0023448994 scopus 로고
    • Nucleotide sequence analysis of the gene encoding theDeinococcus radiodurans
    • Peters J., Peters M., Lottspeich F., Schäfer W., Baumeister W. Nucleotide sequence analysis of the gene encoding theDeinococcus radiodurans. J. Bacteriol. 169:1987;5216-5223.
    • (1987) J. Bacteriol. , vol.169 , pp. 5216-5223
    • Peters, J.1    Peters, M.2    Lottspeich, F.3    Schäfer, W.4    Baumeister, W.5
  • 130
    • 0023915405 scopus 로고
    • Purification and characterization of a family of high molecular weight surface-array proteins fromCampylobacter fetus
    • Pei Z., Ellison R., Lewis R., Blaser. Purification and characterization of a family of high molecular weight surface-array proteins fromCampylobacter fetus. J. Biol. Chem. 263:1988;6416-6420.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6416-6420
    • Pei, Z.1    Ellison, R.2    Lewis, R.3    Blaser4
  • 132
    • 0025143711 scopus 로고
    • Three-dimensional structure of the crystalline protein envelope layer of the hyperthermophilic archaebacteriaumPyrobaculum islandicum
    • Phipps B. M., Engelhardt H., Huber R., Baumeister W. Three-dimensional structure of the crystalline protein envelope layer of the hyperthermophilic archaebacteriaumPyrobaculum islandicum. J. Struct. Biol. 103:1990;152-163.
    • (1990) J. Struct. Biol. , vol.103 , pp. 152-163
    • Phipps, B.M.1    Engelhardt, H.2    Huber, R.3    Baumeister, W.4
  • 133
    • 0026099178 scopus 로고
    • The cell envelope of the hyperthermophilic archaebacteriumPyrobaculum organotrophum
    • Phipps B. M., Huber R., Baumeister W. The cell envelope of the hyperthermophilic archaebacteriumPyrobaculum organotrophum. Mol. Microbiol. 5:1991;253-265.
    • (1991) Mol. Microbiol. , vol.5 , pp. 253-265
    • Phipps, B.M.1    Huber, R.2    Baumeister, W.3
  • 134
    • 0025246062 scopus 로고
    • A porin-type protein is the main constituent of the cell envelope of the ancestral eubacteriumThermotoga maritima
    • Rachel R., Engel A. M., Huber R., Stetter K.-O., Baumeister W. A porin-type protein is the main constituent of the cell envelope of the ancestral eubacteriumThermotoga maritima. FEBS Lett. 262:1990;64-68.
    • (1990) FEBS Lett. , vol.262 , pp. 64-68
    • Rachel, R.1    Engel, A.M.2    Huber, R.3    Stetter, K.-O.4    Baumeister, W.5
  • 137
    • 0022368577 scopus 로고
    • Freeze-fracture observations ofCorynebacterium glutamicum:
    • Richter W., Hänel F., Hilligier M. Freeze-fracture observations ofCorynebacterium glutamicum: J. Basic Microbiol. 25:1985;527-536.
    • (1985) J. Basic Microbiol. , vol.25 , pp. 527-536
    • Richter, W.1    Hänel, F.2    Hilligier, M.3
  • 138
    • 0027169638 scopus 로고
    • Improved prediction of protein secondary structure by use of sequence profiles and neural networks
    • Rost B., Sander C. Improved prediction of protein secondary structure by use of sequence profiles and neural networks. Proc. Natl. Acad. Sci. USA. 90:1993;7558-7562.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7558-7562
    • Rost, B.1    Sander, C.2
  • 139
    • 0017105764 scopus 로고
    • Elastin structure in health and disease
    • Sandberg L. B. Elastin structure in health and disease. Int. Rev. Connect. Tissue Res. 7:1976;159-210.
    • (1976) Int. Rev. Connect. Tissue Res. , vol.7 , pp. 159-210
    • Sandberg, L.B.1
  • 140
    • 0032472790 scopus 로고    scopus 로고
    • Voltage clamp studies on S-layer-supported tetraether lipid membranes
    • Schuster B., Pum D., Sleytr U. B. Voltage clamp studies on S-layer-supported tetraether lipid membranes. Biochim. Biophys. Acta. 1369:1998;51-60.
    • (1998) Biochim. Biophys. Acta , vol.1369 , pp. 51-60
    • Schuster, B.1    Pum, D.2    Sleytr, U.B.3
  • 141
    • 0027367345 scopus 로고
    • Stabilization of the membrane protein bacteriorhodopsin to 140°C in two-dimensional films
    • Shen Y., Safinya C. R., Liang K. S., Ruppert A. F., Rothschild K. J. Stabilization of the membrane protein bacteriorhodopsin to 140°C in two-dimensional films. Nature. 366:1993;48-50.
    • (1993) Nature , vol.366 , pp. 48-50
    • Shen, Y.1    Safinya, C.R.2    Liang, K.S.3    Ruppert, A.F.4    Rothschild, K.J.5
  • 142
    • 0029987201 scopus 로고    scopus 로고
    • Characterization of a porin from the outer membrane ofVibrio anguillarum
    • Simón M., Mathes A., Blanch A., Engelhardt H. Characterization of a porin from the outer membrane ofVibrio anguillarum. J. Bacteriol. 178:1996;4182-4188.
    • (1996) J. Bacteriol. , vol.178 , pp. 4182-4188
    • Simón, M.1    Mathes, A.2    Blanch, A.3    Engelhardt, H.4
  • 143
    • 0018195592 scopus 로고
    • Regular arrays of macromolecules on bacterial cell walls: Structure, chemistry, assembly, and function
    • Sleytr U. B. Regular arrays of macromolecules on bacterial cell walls: Structure, chemistry, assembly, and function. Int. Rev. Cytol. 53:1978;1-64.
    • (1978) Int. Rev. Cytol. , vol.53 , pp. 1-64
    • Sleytr, U.B.1
  • 144
    • 0030867822 scopus 로고    scopus 로고
    • Basic and applied S-layers, an overview
    • Sleytr U. B. Basic and applied S-layers, an overview. FEMS Lett. 20:1997;5-12.
    • (1997) FEMS Lett. , vol.20 , pp. 5-12
    • Sleytr, U.B.1
  • 147
    • 0022885348 scopus 로고
    • Structural and chamical characterization of S-layers of selected strains ofBacillus stearothermophilusDesulfotomaculum nigrificans
    • Sleytr U. B., Sára M., Küpcü Z., Messner P. Structural and chamical characterization of S-layers of selected strains ofBacillus stearothermophilusDesulfotomaculum nigrificans. Arch. Microbiol. 146:1986;19-24.
    • (1986) Arch. Microbiol. , vol.146 , pp. 19-24
    • Sleytr, U.B.1    Sára, M.2    Küpcü, Z.3    Messner, P.4
  • 148
    • 0028075732 scopus 로고
    • Two-dimensional protein crystals (S-layers): Fundamentals and applications
    • Sleytr U. B., Sára M., Messner P., Pum D. Two-dimensional protein crystals (S-layers): Fundamentals and applications. J. Cell. Biochem. 56:1994;171-176.
    • (1994) J. Cell. Biochem. , vol.56 , pp. 171-176
    • Sleytr, U.B.1    Sára, M.2    Messner, P.3    Pum, D.4
  • 149
    • 0025331070 scopus 로고
    • The structure and associations of the double S layer on the cell wall ofAquaspirillum sinuosum
    • Smith S. H., Murray R. G. E. The structure and associations of the double S layer on the cell wall ofAquaspirillum sinuosum. Can. J. Microbiol. 36:1990;327-335.
    • (1990) Can. J. Microbiol. , vol.36 , pp. 327-335
    • Smith, S.H.1    Murray, R.G.E.2
  • 151
    • 0029991767 scopus 로고    scopus 로고
    • Hyperthermopholic procaryotes
    • Stetter K. O. Hyperthermopholic procaryotes. FEMS. Microbiol. Rev. 18:1996;149-158.
    • (1996) FEMS. Microbiol. Rev. , vol.18 , pp. 149-158
    • Stetter, K.O.1
  • 154
    • 0019984815 scopus 로고
    • Structure of the regular surface layer ofAquaspirillum serpens
    • Stewart M., Murray R. G. E. Structure of the regular surface layer ofAquaspirillum serpens. J. Bacteriol. 150:1982;348-357.
    • (1982) J. Bacteriol. , vol.150 , pp. 348-357
    • Stewart, M.1    Murray, R.G.E.2
  • 155
    • 0023235232 scopus 로고
    • Halobacterial glycoprotein biosynthesis
    • Sumper M. Halobacterial glycoprotein biosynthesis. Biochim. Biophys. Acta. 906:1987;69-79.
    • (1987) Biochim. Biophys. Acta , vol.906 , pp. 69-79
    • Sumper, M.1
  • 156
    • 0025605636 scopus 로고
    • Primary structure and glycosylation of the S-layer protein ofHaloferax volcanii
    • Sumper M., Berg E., Mengele R., Strobel I. Primary structure and glycosylation of the S-layer protein ofHaloferax volcanii. J. Bacteriol. 172:1990;7111-7118.
    • (1990) J. Bacteriol. , vol.172 , pp. 7111-7118
    • Sumper, M.1    Berg, E.2    Mengele, R.3    Strobel, I.4
  • 157
    • 0029955959 scopus 로고    scopus 로고
    • Crystal structure of a bacterial family-III cellulose-binding domain: A general mechanism for attachment to cellulose
    • Tormo J., Lamed R., Chirino A. J., Morage E., Bayer E. A., Shoham Y., Steitz T. A. Crystal structure of a bacterial family-III cellulose-binding domain: A general mechanism for attachment to cellulose. EMBO J. 15:1996;6739-5751.
    • (1996) EMBO J. , vol.15 , pp. 6739-5751
    • Tormo, J.1    Lamed, R.2    Chirino, A.J.3    Morage, E.4    Bayer, E.A.5    Shoham, Y.6    Steitz, T.A.7
  • 159
    • 0020429578 scopus 로고
    • Reassembly in vitro of hexagonal surface arrays in a protein-producing bacterium,Bacillus brevis
    • Tsuboi A., Tsukagoschi N., Udaka S. Reassembly in vitro of hexagonal surface arrays in a protein-producing bacterium,Bacillus brevis. J. Bacteriol. 151:1982;1285-1297.
    • (1982) J. Bacteriol. , vol.151 , pp. 1285-1297
    • Tsuboi, A.1    Tsukagoschi, N.2    Udaka, S.3
  • 162
    • 0023557882 scopus 로고
    • Relationship of protein flexibility to thermostability
    • Vihinen M. Relationship of protein flexibility to thermostability. Protein Eng. 1:1987;477-480.
    • (1987) Protein Eng. , vol.1 , pp. 477-480
    • Vihinen, M.1
  • 163
    • 0022517918 scopus 로고
    • Models for the structure of outer membrane proteins ofEscherichia coli
    • Vogel H., Jähnig F. Models for the structure of outer membrane proteins ofEscherichia coli. J. Mol. Biol. 190:1986;191-199.
    • (1986) J. Mol. Biol. , vol.190 , pp. 191-199
    • Vogel, H.1    Jähnig, F.2
  • 164
    • 0029609070 scopus 로고
    • The structure and characterization of the surface protein layer of aComamonas
    • Wai S. N., Takade A., Fujimoto S., Amako K. The structure and characterization of the surface protein layer of aComamonas. Microbiol. Immunol. 39:1995;943-949.
    • (1995) Microbiol. Immunol. , vol.39 , pp. 943-949
    • Wai, S.N.1    Takade, A.2    Fujimoto, S.3    Amako, K.4
  • 165
    • 0019499337 scopus 로고
    • Polyphenolic substance ofMytilus edulis:
    • Waite J. H., Tanzer M. L. Polyphenolic substance ofMytilus edulis: Science. 212:1981;1038-1039.
    • (1981) Science , vol.212 , pp. 1038-1039
    • Waite, J.H.1    Tanzer, M.L.2
  • 167
    • 0031877370 scopus 로고    scopus 로고
    • Electron crystallography of two-dimensional crystals of membrane proteins
    • Walz T., Grigorieff N. Electron crystallography of two-dimensional crystals of membrane proteins. J. Struct. Biol. 121:1998;142-161.
    • (1998) J. Struct. Biol. , vol.121 , pp. 142-161
    • Walz, T.1    Grigorieff, N.2
  • 169
    • 0010518516 scopus 로고    scopus 로고
    • Engineering cellulases: Catalysis, binding, and modules
    • Warren R. A. J. Engineering cellulases: Catalysis, binding, and modules. Am. Soc. Microbiol. News. 62:1996;85-88.
    • (1996) Am. Soc. Microbiol. News , vol.62 , pp. 85-88
    • Warren, R.A.J.1
  • 170
    • 0029952519 scopus 로고    scopus 로고
    • Structural basis of lectin-carbohydrate recognition
    • Weis W. I., Drickamer K. Structural basis of lectin-carbohydrate recognition. Annu. Rev. Biochem. 65:1996;441-473.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 441-473
    • Weis, W.I.1    Drickamer, K.2
  • 171
    • 0026331041 scopus 로고
    • Molecular architecture and electrostatic properties of a bacterial porin
    • Weiss M. S., Abele U., Weckesser J., Welte W., Schlitz E., Schulz G. E. Molecular architecture and electrostatic properties of a bacterial porin. Science. 254:1991;1627-1630.
    • (1991) Science , vol.254 , pp. 1627-1630
    • Weiss, M.S.1    Abele, U.2    Weckesser, J.3    Welte, W.4    Schlitz, E.5    Schulz, G.E.6
  • 172
    • 0020580697 scopus 로고
    • The ultrastructure ofPseudomonas avenae.
    • Wells B., Horne R. W., Lund B. M., King N. R. The ultrastructure ofPseudomonas avenae. Micron. 14:1983;11-28.
    • (1983) Micron , vol.14 , pp. 11-28
    • Wells, B.1    Horne, R.W.2    Lund, B.M.3    King, N.R.4
  • 173
    • 0021753827 scopus 로고
    • Hydrolytic stability of biomolecules at high temperatures and its implication for life at 250°C
    • White R. H. Hydrolytic stability of biomolecules at high temperatures and its implication for life at 250°C. Nature. 310:1984;430-432.
    • (1984) Nature , vol.310 , pp. 430-432
    • White, R.H.1
  • 174
    • 0001177791 scopus 로고
    • The cell envelope ofThermoproteus tenax:
    • Wildhaber I., Baumeister W. The cell envelope ofThermoproteus tenax: EMBO J. 6:1987;1475-1480.
    • (1987) EMBO J. , vol.6 , pp. 1475-1480
    • Wildhaber, I.1    Baumeister, W.2
  • 175
    • 0023464761 scopus 로고
    • Three-dimensional structure of the surface protein ofDesulfurococcus mobilis
    • Wildhaber I., Santarius U., Baumeister W. Three-dimensional structure of the surface protein ofDesulfurococcus mobilis. J. Bacteriol. 169:1987;5563-5568.
    • (1987) J. Bacteriol. , vol.169 , pp. 5563-5568
    • Wildhaber, I.1    Santarius, U.2    Baumeister, W.3
  • 176
    • 0022896329 scopus 로고
    • The tetragonal surface layer ofClostridium aceticum:Clostridium thermohydrosulfuricum
    • Woodcock C. L. F., Engelhardt H., Baumeister W. The tetragonal surface layer ofClostridium aceticum:Clostridium thermohydrosulfuricum. Eur. J. Cell Biol. 42:1986;211-217.
    • (1986) Eur. J. Cell Biol. , vol.42 , pp. 211-217
    • Woodcock, C.L.F.1    Engelhardt, H.2    Baumeister, W.3
  • 177
    • 0030220095 scopus 로고    scopus 로고
    • The structural role of sugars in glycoproteins
    • Wyss D. F., Wagner. The structural role of sugars in glycoproteins. Curr. Opin. Biotechnol. 7:1996;409-416.
    • (1996) Curr. Opin. Biotechnol. , vol.7 , pp. 409-416
    • Wyss, D.F.1    Wagner2
  • 178
    • 0031856212 scopus 로고    scopus 로고
    • The second decade - Into the new millenium
    • Wüthrich K. The second decade - into the new millenium. Nat. Struct. Biol. NMR. 5:1998;492-495.
    • (1998) Nat. Struct. Biol. NMR , vol.5 , pp. 492-495
    • Wüthrich, K.1
  • 179
    • 0026565859 scopus 로고
    • Reattachment of surface array proteins toCampylobacter fetus
    • Yang L., Pei Z., Fujimoto S., Blaser M. J. Reattachment of surface array proteins toCampylobacter fetus. J. Bacteriol. 174:1992;1258-1267.
    • (1992) J. Bacteriol. , vol.174 , pp. 1258-1267
    • Yang, L.1    Pei, Z.2    Fujimoto, S.3    Blaser, M.J.4
  • 180
    • 0021763770 scopus 로고
    • Enzymatic catalysis in organic media at 100°C
    • Zaks A., Klibanov A. M. Enzymatic catalysis in organic media at 100°C. Science. 224:1984;1249-1251.
    • (1984) Science , vol.224 , pp. 1249-1251
    • Zaks, A.1    Klibanov, A.M.2
  • 181
    • 0023055754 scopus 로고
    • Why does ribonuclease irreversibly inactivate at high temperatures
    • Zale S. E., Klibanov A. M. Why does ribonuclease irreversibly inactivate at high temperatures. Biochem. 25:1986;5432-5444.
    • (1986) Biochem. , vol.25 , pp. 5432-5444
    • Zale, S.E.1    Klibanov, A.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.