메뉴 건너뛰기




Volumn 63, Issue , 2003, Pages 47-70

Transmembrane β-barrel proteins

Author keywords

[No Author keywords available]

Indexed keywords

BETA BARREL PROTEIN; CHAPERONE; CHYMOTRYPSIN; GRAMICIDIN A; LIPOCALIN; MEMBRANE PROTEIN; METALLOPROTEINASE; OUTER MEMBRANE PROTEIN A; OUTER MEMBRANE PROTEIN F; PECTATE LYASE; PHOSPHOLIPASE A; PORIN; PROTEIN OMPLA; PROTEIN OMPT; PROTEIN OMPX; PROTEINASE; STREPTAVIDIN; UNCLASSIFIED DRUG;

EID: 0037284970     PISSN: 00653233     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0065-3233(03)63003-2     Document Type: Review
Times cited : (46)

References (85)
  • 1
    • 0034695440 scopus 로고    scopus 로고
    • Refolded outer membrane protein A of Escherichia coli forms ion channels with two conductance states in planar lipid bilayers
    • Arora, A., Rinehart, D., Szabo, G., and Tamm, L. K. (2000). Refolded outer membrane protein A of Escherichia coli forms ion channels with two conductance states in planar lipid bilayers. J. Biol. Chem. 275, 1594-1600.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1594-1600
    • Arora, A.1    Rinehart, D.2    Szabo, G.3    Tamm, L.K.4
  • 2
    • 0035066331 scopus 로고    scopus 로고
    • Structure of outer membrane protein A transmembrane domain by NMR spectroscopy
    • Arora, A., Abildgaard, F., Bushweller, J. H., and Tamm, L. K. (2001). Structure of outer membrane protein A transmembrane domain by NMR spectroscopy. Nat. Struct. Biol. 8, 334-338.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 334-338
    • Arora, A.1    Abildgaard, F.2    Bushweller, J.H.3    Tamm, L.K.4
  • 4
    • 0027292152 scopus 로고
    • Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: A two-domain protein with a calcium binding parallel beta roll motif
    • Baumann, U., Wu, S., Flaherty, K. M., and McKay, D. B. (1993). Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: a two-domain protein with a calcium binding parallel beta roll motif. EMBO J. 12, 3357-3364.
    • (1993) EMBO J. , vol.12 , pp. 3357-3364
    • Baumann, U.1    Wu, S.2    Flaherty, K.M.3    McKay, D.B.4
  • 5
    • 0015518520 scopus 로고
    • Structure of crystalline α-chymotrypsin
    • Birktoft, J. J., and Blow, D. M. (1972). Structure of crystalline α-chymotrypsin. J. Mol. Biol. 68, 187-240.
    • (1972) J. Mol. Biol. , vol.68 , pp. 187-240
    • Birktoft, J.J.1    Blow, D.M.2
  • 6
    • 0033457943 scopus 로고    scopus 로고
    • Helix-bundle membrane protein fold templates
    • Bowie, J. U. (1999). Helix-bundle membrane protein fold templates. Protein Sci. 8, 2711-2719.
    • (1999) Protein Sci. , vol.8 , pp. 2711-2719
    • Bowie, J.U.1
  • 8
    • 0033970022 scopus 로고    scopus 로고
    • Expectations from structural genomics
    • Brenner, S. E., and Levitt, M. (2000). Expectations from structural genomics. Protein Sci. 9, 197-200.
    • (2000) Protein Sci. , vol.9 , pp. 197-200
    • Brenner, S.E.1    Levitt, M.2
  • 10
    • 0032993061 scopus 로고    scopus 로고
    • A functional protein pore with a "retro" transmembrane domain
    • Cheley, S., Braha, O., Lu, X., Conlan, S., and Bayley, H. (1999). A functional protein pore with a "retro" transmembrane domain. Protein Sci. 8, 1257-1267.
    • (1999) Protein Sci. , vol.8 , pp. 1257-1267
    • Cheley, S.1    Braha, O.2    Lu, X.3    Conlan, S.4    Bayley, H.5
  • 11
    • 0034601782 scopus 로고    scopus 로고
    • Biochemical and biophysical characterization of OmpG: A monomeric porin
    • Conlan, S., Zhang, Y., Cheley, S., and Bayley, H. (2000). Biochemical and biophysical characterization of OmpG: a monomeric porin. Biochemistry 39, 11845-11854.
    • (2000) Biochemistry , vol.39 , pp. 11845-11854
    • Conlan, S.1    Zhang, Y.2    Cheley, S.3    Bayley, H.4
  • 13
    • 0033556141 scopus 로고    scopus 로고
    • Affinity of the periplasmic chaperone Skp of Escherichia coli for phospholipids, lipopolysaccharides and non-native outer membrane proteins
    • DeCock, H., Schäfer, U., Potgeter, M., Demel, R., Müller, M., and Tommassen, J. (1999). Affinity of the periplasmic chaperone Skp of Escherichia coli for phospholipids, lipopolysaccharides and non-native outer membrane proteins. Eur. J. Biochem. 259, 96-103.
    • (1999) Eur. J. Biochem. , vol.259 , pp. 96-103
    • DeCock, H.1    Schäfer, U.2    Potgeter, M.3    Demel, R.4    Müller, M.5    Tommassen, J.6
  • 14
    • 0031791382 scopus 로고    scopus 로고
    • Prediction by a neural network of outer membrane β-strand protein topology
    • Diederichs, K., Freigang, J., Umhau, S., Zeth, K., and Breed, J. (1998). Prediction by a neural network of outer membrane β-strand protein topology. Protein Sci. 7, 2413-2420.
    • (1998) Protein Sci. , vol.7 , pp. 2413-2420
    • Diederichs, K.1    Freigang, J.2    Umhau, S.3    Zeth, K.4    Breed, J.5
  • 15
    • 0034733718 scopus 로고    scopus 로고
    • Sugar transport through maltoporin of Escherichia coli
    • Dumas, F., Koebnik, R., Winterhalter, M., and Van Gelder, P. (2000). Sugar transport through maltoporin of Escherichia coli. J. Biol. Chem. 275, 19747-19751.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19747-19751
    • Dumas, F.1    Koebnik, R.2    Winterhalter, M.3    Van Gelder, P.4
  • 17
    • 0032545324 scopus 로고    scopus 로고
    • Siderophore-mediated iron transport: Crystal structure of FhuA with bound lipopolysaccharide
    • Ferguson, A. D., Hofmann, E., Coulton, J. W., Diederichs, K., and Welte, W. (1998). Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide. Science 282, 2215-2220.
    • (1998) Science , vol.282 , pp. 2215-2220
    • Ferguson, A.D.1    Hofmann, E.2    Coulton, J.W.3    Diederichs, K.4    Welte, W.5
  • 18
    • 0035956956 scopus 로고    scopus 로고
    • Transverse relaxation-optimized NMR spectroscopy with the outer membrane protein OmpX in dihexanoyl phosphatidylcholine micelles
    • Fernández, C., Adeishvili, K., and Wüthrich, K. (2001a). Transverse relaxation-optimized NMR spectroscopy with the outer membrane protein OmpX in dihexanoyl phosphatidylcholine micelles. Proc. Natl. Acad. Sci. USA 98, 2358-2363.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2358-2363
    • Fernández, C.1    Adeishvili, K.2    Wüthrich, K.3
  • 19
    • 0035979788 scopus 로고    scopus 로고
    • Solution NMR studies of the integral membrane proteins OmpX and OmpA from Escherichia coli
    • Fernández, C., Hilty, C., Bonjour, S., Adeishvili, K., Pervushin, K., and Wüthrich, K. (2001b). Solution NMR studies of the integral membrane proteins OmpX and OmpA from Escherichia coli. FEBS Lett. 504, 173-178.
    • (2001) FEBS Lett. , vol.504 , pp. 173-178
    • Fernández, C.1    Hilty, C.2    Bonjour, S.3    Adeishvili, K.4    Pervushin, K.5    Wüthrich, K.6
  • 20
    • 0031985785 scopus 로고    scopus 로고
    • Structure of the sucrose-specific porin ScrY from Salmonella typhimurium and its complex with sucrose
    • Forst, D., Welte, W., Wacker, T., and Diederichs, K. (1998). Structure of the sucrose-specific porin ScrY from Salmonella typhimurium and its complex with sucrose. Nat. Struct. Biol. 5, 37-46.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 37-46
    • Forst, D.1    Welte, W.2    Wacker, T.3    Diederichs, K.4
  • 21
    • 0019036909 scopus 로고
    • Three-dimensional crystals of an integral membrane protein: An initial X-ray analysis
    • Garavito, R. M., and Rosenbusch, J. P. (1980). Three-dimensional crystals of an integral membrane protein: an initial X-ray analysis. J. Cell. Biol. 86, 327-329.
    • (1980) J. Cell. Biol. , vol.86 , pp. 327-329
    • Garavito, R.M.1    Rosenbusch, J.P.2
  • 22
    • 0028174318 scopus 로고
    • Artificial transmembrane ion channels from self-assembling peptide nanotubes
    • Ghadiri, M. R., Granja, J. R., and Buehler, L. K. (1994). Artificial transmembrane ion channels from self-assembling peptide nanotubes. Nature 369, 301-304.
    • (1994) Nature , vol.369 , pp. 301-304
    • Ghadiri, M.R.1    Granja, J.R.2    Buehler, L.K.3
  • 23
    • 0030958758 scopus 로고    scopus 로고
    • Identification of membrane spanning β-strands in bacterial porins
    • Gromiha, M. M., Majumdar, R., and Ponnuswamy, P. K. (1997). Identification of membrane spanning β-strands in bacterial porins. Protein Eng. 10, 497-500.
    • (1997) Protein Eng. , vol.10 , pp. 497-500
    • Gromiha, M.M.1    Majumdar, R.2    Ponnuswamy, P.K.3
  • 24
    • 0033594410 scopus 로고    scopus 로고
    • Stochastic sensing of organic analytes by a pore-forming protein containing a molecular adapter
    • Gu, L. Q., Braha, O., Conlan, S., Cheley, S., and Bayley, H. (1999). Stochastic sensing of organic analytes by a pore-forming protein containing a molecular adapter. Nature 398, 686-690.
    • (1999) Nature , vol.398 , pp. 686-690
    • Gu, L.Q.1    Braha, O.2    Conlan, S.3    Cheley, S.4    Bayley, H.5
  • 25
    • 0024653594 scopus 로고
    • Crystal structure of core streptavidin determined from multi-wavelength anomalous diffraction of synchrotron radiation
    • Hendrickson, W. A., Pähler, A., Smith, J. L., Satow, Y., Merritt, E. A., and Phizackerley, R. P. (1989). Crystal structure of core streptavidin determined from multi-wavelength anomalous diffraction of synchrotron radiation. Proc. Natl. Acad. Sci. USA 86, 2190-2194.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 2190-2194
    • Hendrickson, W.A.1    Pähler, A.2    Smith, J.L.3    Satow, Y.4    Merritt, E.A.5    Phizackerley, R.P.6
  • 26
    • 0032188847 scopus 로고    scopus 로고
    • Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins
    • Hill, K., Model, K., Ryan, M. T., Dietmeier, K., Martin, F., Wagner, R., and Pfanner, N. (1998). Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins. Nature 395, 516-521.
    • (1998) Nature , vol.395 , pp. 516-521
    • Hill, K.1    Model, K.2    Ryan, M.T.3    Dietmeier, K.4    Martin, F.5    Wagner, R.6    Pfanner, N.7
  • 28
    • 0035078840 scopus 로고    scopus 로고
    • Prediction of the transmembrane regions of β-barrel membrane proteins with a neural network-based predictor
    • Jacoboni, I., Martelli, P. L., Fariselli, P., de Pinto, V., and Casadio, R. (2001). Prediction of the transmembrane regions of β-barrel membrane proteins with a neural network-based predictor. Protein Sci. 10, 779-787.
    • (2001) Protein Sci. , vol.10 , pp. 779-787
    • Jacoboni, I.1    Martelli, P.L.2    Fariselli, P.3    De Pinto, V.4    Casadio, R.5
  • 29
    • 0024549593 scopus 로고
    • Molecular design of PhoE porin and its functional consequences
    • Jap, B. K. (1989). Molecular design of PhoE porin and its functional consequences. J. Mol. Biol. 205, 407-419.
    • (1989) J. Mol. Biol. , vol.205 , pp. 407-419
    • Jap, B.K.1
  • 30
    • 0027360175 scopus 로고
    • High-resolution conformation of gramicidin A in a lipid bilayer by solid-state NMR
    • Ketchem, R. R., Hu, W., and Cross, T. A. (1993). High-resolution conformation of gramicidin A in a lipid bilayer by solid-state NMR. Science 261, 1457-1460.
    • (1993) Science , vol.261 , pp. 1457-1460
    • Ketchem, R.R.1    Hu, W.2    Cross, T.A.3
  • 31
    • 0033052932 scopus 로고    scopus 로고
    • Structural and functional roles of the surface-exposed loops of the β-barrel membrane protein OmpA from Escherichia coli
    • Koebnik, R. (1999). Structural and functional roles of the surface-exposed loops of the β-barrel membrane protein OmpA from Escherichia coli. J. Bacteriol. 181, 3688-3694.
    • (1999) J. Bacteriol. , vol.181 , pp. 3688-3694
    • Koebnik, R.1
  • 32
    • 0034702177 scopus 로고    scopus 로고
    • Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export
    • Koronakis, V., Sharff, A., Koronakis, E., Luisi, B., and Hughes, C. (2000). Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export. Nature 405, 914-919.
    • (2000) Nature , vol.405 , pp. 914-919
    • Koronakis, V.1    Sharff, A.2    Koronakis, E.3    Luisi, B.4    Hughes, C.5
  • 33
    • 0028153088 scopus 로고
    • Refined structure of the porin from Rhodopseudomonas blastica: Comparison with the porin from Rhodobacter capsulatus
    • Kreusch, A., and Schulz, G. E. (1994). Refined structure of the porin from Rhodopseudomonas blastica: comparison with the porin from Rhodobacter capsulatus. J. Mol. Biol. 243, 891-905.
    • (1994) J. Mol. Biol. , vol.243 , pp. 891-905
    • Kreusch, A.1    Schulz, G.E.2
  • 34
    • 0024281641 scopus 로고
    • Three-dimensional structure at 0.86 Å of the uncomplexed form of the transmembrane ion channel peptide gramicidin A
    • Langs, D. A. (1988). Three-dimensional structure at 0.86 Å of the uncomplexed form of the transmembrane ion channel peptide gramicidin A. Science 241, 188-191.
    • (1988) Science , vol.241 , pp. 188-191
    • Langs, D.A.1
  • 35
    • 0032991467 scopus 로고    scopus 로고
    • Protonmotive force, ExbB and ligand-bound FepA drive conformational changes in TonB
    • Larsen, R. A., Thomas, M. G., and Postle, K. (1999). Protonmotive force, ExbB and ligand-bound FepA drive conformational changes in TonB. Mol. Microbiol. 31, 1809-1824.
    • (1999) Mol. Microbiol. , vol.31 , pp. 1809-1824
    • Larsen, R.A.1    Thomas, M.G.2    Postle, K.3
  • 36
    • 0034808117 scopus 로고    scopus 로고
    • Comparing function and structure between entire proteomes
    • Liu, J., and Rost, B. (2001). Comparing function and structure between entire proteomes. Protein Sci. 10, 1970-1979.
    • (2001) Protein Sci. , vol.10 , pp. 1970-1979
    • Liu, J.1    Rost, B.2
  • 37
    • 0031668883 scopus 로고    scopus 로고
    • The spontaneous gating activity of OmpC porin is affected by mutations of a putative hydrogen bond network or of a salt bridge between the L3 loop and the barrel
    • Liu, N., and Delcour, A. H. (1998). The spontaneous gating activity of OmpC porin is affected by mutations of a putative hydrogen bond network or of a salt bridge between the L3 loop and the barrel. Protein Eng. 11, 797-802.
    • (1998) Protein Eng. , vol.11 , pp. 797-802
    • Liu, N.1    Delcour, A.H.2
  • 38
    • 0032579317 scopus 로고    scopus 로고
    • Shear numbers of protein β-barrels: Definition, refinements and statistics
    • Liu, W. M. (1998). Shear numbers of protein β-barrels: definition, refinements and statistics. J. Mol. Biol. 275, 541-545.
    • (1998) J. Mol. Biol. , vol.275 , pp. 541-545
    • Liu, W.M.1
  • 39
    • 0032414254 scopus 로고    scopus 로고
    • Transmembrane signaling across the ligand-gated FhuA receptor: Crystal structures of free and ferrichrome-bound states reveal allosteric changes
    • Locher, K. P., Rees, B., Koebnik, R., Mitschler, A., Moulinier, L., Rosenbusch, J. P., and Moras, D. (1998). Transmembrane signaling across the ligand-gated FhuA receptor: crystal structures of free and ferrichrome-bound states reveal allosteric changes. Cell 95, 771-778.
    • (1998) Cell , vol.95 , pp. 771-778
    • Locher, K.P.1    Rees, B.2    Koebnik, R.3    Mitschler, A.4    Moulinier, L.5    Rosenbusch, J.P.6    Moras, D.7
  • 40
    • 0031448082 scopus 로고    scopus 로고
    • On the structure and gating mechanism of the mitochondrial channel, VDAC
    • Mannella, C. A. (1997). On the structure and gating mechanism of the mitochondrial channel, VDAC. J. Bioenerg. Biomembr. 29, 525-531.
    • (1997) J. Bioenerg. Biomembr. , vol.29 , pp. 525-531
    • Mannella, C.A.1
  • 41
    • 0031857554 scopus 로고    scopus 로고
    • Conformational changes in the mitochondrial channel protein, VDAC, and their functional implications
    • Mannella, C. A. (1998). Conformational changes in the mitochondrial channel protein, VDAC, and their functional implications. J. Struct. Biol. 121, 207-218.
    • (1998) J. Struct. Biol. , vol.121 , pp. 207-218
    • Mannella, C.A.1
  • 42
    • 0030902082 scopus 로고    scopus 로고
    • Energy profile of maltooligosaccharide permeation through maltoporin as derived from the structure and from a statistical analysis of saccharide-protein interactions
    • Meyer, J. E. W., and Schulz, G. E. (1997). Energy profile of maltooligosaccharide permeation through maltoporin as derived from the structure and from a statistical analysis of saccharide-protein interactions. Protein Sci. 6, 1084-1091.
    • (1997) Protein Sci. , vol.6 , pp. 1084-1091
    • Meyer, J.E.W.1    Schulz, G.E.2
  • 43
    • 0031557404 scopus 로고    scopus 로고
    • Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl-maltotrioside
    • Meyer, J. E. W., Hofnung, M., and Schulz, G. E. (1997). Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl-maltotrioside. J. Mol. Biol. 266, 761-775.
    • (1997) J. Mol. Biol. , vol.266 , pp. 761-775
    • Meyer, J.E.W.1    Hofnung, M.2    Schulz, G.E.3
  • 44
    • 0021213980 scopus 로고
    • Escherichia coli K-12 outer membrane protein (OmpA) as a bacteriophage receptor: Analysis of mutant genes expressing altered proteins
    • Morona, R., Klose, M., and Henning, U. (1984). Escherichia coli K-12 outer membrane protein (OmpA) as a bacteriophage receptor: analysis of mutant genes expressing altered proteins. J. Bacteriol. 159, 570-578.
    • (1984) J. Bacteriol. , vol.159 , pp. 570-578
    • Morona, R.1    Klose, M.2    Henning, U.3
  • 45
    • 0037666544 scopus 로고    scopus 로고
    • Voltage and pH-induced channel closure of porin OmpF visualized by atomic force microscopy
    • Müller, D. J., and Engel, A. (1999). Voltage and pH-induced channel closure of porin OmpF visualized by atomic force microscopy. J. Mol. Biol. 285, 1347-1351.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1347-1351
    • Müller, D.J.1    Engel, A.2
  • 46
    • 0028348081 scopus 로고
    • Principles determining the structure of β-sheet barrels in proteins. I. A theoretical analysis
    • Murzin, A. G., Lesk, A. M., and Chothia, C. (1994a). Principles determining the structure of β-sheet barrels in proteins. I. A theoretical analysis. J. Mol. Biol. 236, 1369-1381.
    • (1994) J. Mol. Biol. , vol.236 , pp. 1369-1381
    • Murzin, A.G.1    Lesk, A.M.2    Chothia, C.3
  • 47
    • 0028330220 scopus 로고
    • Principles determining the structure of β-sheet barrels in proteins. II. The observed structures
    • Murzin, A. G., Lesk, A. M., and Chothia, C. (1994b). Principles determining the structure of β-sheet barrels in proteins. II. The observed structures. J. Mol. Biol. 236, 1382-1400.
    • (1994) J. Mol. Biol. , vol.236 , pp. 1382-1400
    • Murzin, A.G.1    Lesk, A.M.2    Chothia, C.3
  • 48
    • 0024006622 scopus 로고
    • The orientation of β-sheets in porin. A polarized Fourier transform infrared spectroscopic investigation
    • Nabedryk, E., Garavito, R. M., and Breton, J. (1988). The orientation of β-sheets in porin. A polarized Fourier transform infrared spectroscopic investigation. Biophys. J. 53, 671-676.
    • (1988) Biophys. J. , vol.53 , pp. 671-676
    • Nabedryk, E.1    Garavito, R.M.2    Breton, J.3
  • 50
    • 23444456920 scopus 로고
    • Prevention of drug access to bacterial targets: Permeability barriers and active efflux
    • Nikaido, H. (1994). Prevention of drug access to bacterial targets: permeability barriers and active efflux. Science 264, 382-388.
    • (1994) Science , vol.264 , pp. 382-388
    • Nikaido, H.1
  • 51
    • 0032932083 scopus 로고    scopus 로고
    • Crystal structure of staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel
    • Olson, R., Nariya, H., Yokota, K., Kamio, Y., and Gouaux, E. (1999). Crystal structure of staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel. Nat. Struct. Biol. 6, 134-140.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 134-140
    • Olson, R.1    Nariya, H.2    Yokota, K.3    Kamio, Y.4    Gouaux, E.5
  • 52
    • 0031733336 scopus 로고    scopus 로고
    • Structure of the outer membrane protein A transmembrane domain
    • Pautsch, A., and Schulz, G. E. (1998). Structure of the outer membrane protein A transmembrane domain. Nat. Struct. Biol. 5, 1013-1017.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 1013-1017
    • Pautsch, A.1    Schulz, G.E.2
  • 53
    • 0034724567 scopus 로고    scopus 로고
    • High resolution structure of the OmpA membrane domain
    • Pautsch, A., and Schulz, G. E. (2000). High resolution structure of the OmpA membrane domain. J. Mol. Biol. 298, 273-282.
    • (2000) J. Mol. Biol. , vol.298 , pp. 273-282
    • Pautsch, A.1    Schulz, G.E.2
  • 55
    • 0028844306 scopus 로고
    • A left-handed parallel β-helix in the structure of UDP-N-acetylglucosamine acyltransferase
    • Raetz, C. R. H., and Roderick, S. L. (1995). A left-handed parallel β-helix in the structure of UDP-N-acetylglucosamine acyltransferase. Science 270, 997-1000.
    • (1995) Science , vol.270 , pp. 997-1000
    • Raetz, C.R.H.1    Roderick, S.L.2
  • 56
    • 0033582158 scopus 로고    scopus 로고
    • The evolutionary origin of the protein-translocating channel of chloroplastic envelope membranes: Identification of a cyanobacterial homolog
    • Reumann, S., Davila-Aponte, J., and Keegstra, K. (1999). The evolutionary origin of the protein-translocating channel of chloroplastic envelope membranes: identification of a cyanobacterial homolog. Proc. Natl. Acad. Sci. USA 96, 784-789.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 784-789
    • Reumann, S.1    Davila-Aponte, J.2    Keegstra, K.3
  • 57
    • 0026545681 scopus 로고
    • Formation of a gated channel by a ligand-specific transport protein in the bacterial outer membrane
    • Rutz, J. M., Liu, J., Lyons, A. J., Goranson, J., Armstrong, S. K., McIntosh, M. A., Feix, J. B., and Klebba, P. E. (1992). Formation of a gated channel by a ligand-specific transport protein in the bacterial outer membrane. Science 258, 471-475.
    • (1992) Science , vol.258 , pp. 471-475
    • Rutz, J.M.1    Liu, J.2    Lyons, A.J.3    Goranson, J.4    Armstrong, S.K.5    McIntosh, M.A.6    Feix, J.B.7    Klebba, P.E.8
  • 58
    • 0033573851 scopus 로고    scopus 로고
    • Ion selectivity reversal and induction of voltage-gating by site-directed mutations in the Paracoccus denitrificans porin
    • Saxena, K., Drosou, V., Maier, E., Benz, R., and Ludwig, B. (1999). Ion selectivity reversal and induction of voltage-gating by site-directed mutations in the Paracoccus denitrificans porin. Biochemistry 38, 2206-2212.
    • (1999) Biochemistry , vol.38 , pp. 2206-2212
    • Saxena, K.1    Drosou, V.2    Maier, E.3    Benz, R.4    Ludwig, B.5
  • 59
    • 0038105593 scopus 로고    scopus 로고
    • Skp, a molecular chaperone of gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins
    • Schäfer, U., Beck, K., and Müller M. (1999). Skp, a molecular chaperone of gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins. J. Biol. Chem. 274, 24567-24574.
    • (1999) J. Biol. Chem. , vol.274 , pp. 24567-24574
    • Schäfer, U.1    Beck, K.2    Müller, M.3
  • 60
    • 0027161268 scopus 로고
    • Prediction of membrane-spanning β-strands and its application to maltoporin
    • Schirmer, T., and Cowan, S. W. (1993). Prediction of membrane-spanning β-strands and its application to maltoporin. Protein Sci. 2, 1361-1363.
    • (1993) Protein Sci. , vol.2 , pp. 1361-1363
    • Schirmer, T.1    Cowan, S.W.2
  • 61
    • 0033579482 scopus 로고    scopus 로고
    • Brownian dynamics simulation of ion flow through porin channels
    • Schirmer, T., and Phale, P. S. (1999). Brownian dynamics simulation of ion flow through porin channels. J. Mol. Biol. 294, 1159-1167.
    • (1999) J. Mol. Biol. , vol.294 , pp. 1159-1167
    • Schirmer, T.1    Phale, P.S.2
  • 62
    • 0028946962 scopus 로고
    • Structural basis for sugar translocation through maltoporin channels at 3.1 Å resolution
    • Schirmer, T., Keller, T. A., Wang, Y. F., and Rosenbusch, J. P. (1995). Structural basis for sugar translocation through maltoporin channels at 3.1 Å resolution. Science 267, 512-514.
    • (1995) Science , vol.267 , pp. 512-514
    • Schirmer, T.1    Keller, T.A.2    Wang, Y.F.3    Rosenbusch, J.P.4
  • 63
    • 18744422713 scopus 로고    scopus 로고
    • Expression of porin from Rhodopseudomonas blastica in Escherichia coli inclusion bodies and folding into exact native structure
    • Schmid, B., Krömer, M., and Schulz, G. E. (1996). Expression of porin from Rhodopseudomonas blastica in Escherichia coli inclusion bodies and folding into exact native structure. FEBS Lett. 381, 111-114.
    • (1996) FEBS Lett. , vol.381 , pp. 111-114
    • Schmid, B.1    Krömer, M.2    Schulz, G.E.3
  • 65
    • 0019528471 scopus 로고
    • Protein differentiation: Emergence of novel proteins during evolution
    • Schulz, G. E. (1981). Protein differentiation: emergence of novel proteins during evolution. Angew. Chem. Int. Ed. Engl. 20, 143-151.
    • (1981) Angew. Chem. Int. Ed. Engl. , vol.20 , pp. 143-151
    • Schulz, G.E.1
  • 66
    • 0001761402 scopus 로고
    • Structure-function relationships in the membrane channel porin as based on a 1.8 Å resolution crystal structure
    • A. Pullman, J. Jortner, and B. Pullman, Eds. Kluwer Academic, Dordrecht
    • Schulz, G. E. (1992). Structure-function relationships in the membrane channel porin as based on a 1.8 Å resolution crystal structure. In: Membrane Proteins: Structures, Interactions and Models (A. Pullman, J. Jortner, and B. Pullman, Eds.), pp. 403-412. Kluwer Academic, Dordrecht.
    • (1992) Membrane Proteins: Structures, Interactions and Models , pp. 403-412
    • Schulz, G.E.1
  • 67
    • 0042050648 scopus 로고
    • Structure-function relationships in porins as derived from a 1.8 Å resolution crystal structure
    • J. M. Ghuysen, and R. Hakenbeck, Eds. Elsevier, Amsterdam
    • Schulz, G. E. (1994). Structure-function relationships in porins as derived from a 1.8 Å resolution crystal structure. In: New Comprehensive Biochemistry: Bacterial Cell Wall (J. M. Ghuysen, and R. Hakenbeck, Eds.), vol. 27, pp. 343-352. Elsevier, Amsterdam.
    • (1994) New Comprehensive Biochemistry: Bacterial Cell Wall , vol.27 , pp. 343-352
    • Schulz, G.E.1
  • 69
    • 0031716791 scopus 로고    scopus 로고
    • Architecture of β-barrel membrane proteins: Analysis of trimeric porins
    • Seshadri, K., Garemyr, R., Wallin, E., von Heijne, G., and Elofsson, A. (1998). Architecture of β-barrel membrane proteins: analysis of trimeric porins. Protein Sci. 7, 2026-2032.
    • (1998) Protein Sci. , vol.7 , pp. 2026-2032
    • Seshadri, K.1    Garemyr, R.2    Wallin, E.3    Von Heijne, G.4    Elofsson, A.5
  • 70
    • 0027264995 scopus 로고
    • Predicting the topology of eukaryotic membrane proteins
    • Sipos, L., and von Heijne, G. (1993). Predicting the topology of eukaryotic membrane proteins. Eur. J. Biochem. 213, 1333-1340.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 1333-1340
    • Sipos, L.1    Von Heijne, G.2
  • 72
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal ct-hemolysin, a heptameric transmembrane pore
    • Song, L., Hobaugh, M. R., Shustak, C., Cheley, S., Bayley, H., and Gouaux, J. E. (1996). Structure of staphylococcal ct-hemolysin, a heptameric transmembrane pore. Science 274, 1859-1865.
    • (1996) Science , vol.274 , pp. 1859-1865
    • Song, L.1    Hobaugh, M.R.2    Shustak, C.3    Cheley, S.4    Bayley, H.5    Gouaux, J.E.6
  • 73
    • 0028321391 scopus 로고
    • OmpA protein of Escherichia coli outer membrane occurs in open and closed channel forms
    • Sugawara, E., and Nikaido, H. (1994). OmpA protein of Escherichia coli outer membrane occurs in open and closed channel forms. J. Biol. Chem. 269, 17981-17987.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17981-17987
    • Sugawara, E.1    Nikaido, H.2
  • 74
    • 0032987970 scopus 로고    scopus 로고
    • Site-directed mutagenesis of loop L3 of sucrose porin ScrYleads to changes in substrate selectivity
    • Ulmke, D., Kreth, J., Lengeler, J. W., Welte, W., and Schmid, T. (1999). Site-directed mutagenesis of loop L3 of sucrose porin ScrYleads to changes in substrate selectivity. J. Bacteriol. 181, 1920-1923.
    • (1999) J. Bacteriol. , vol.181 , pp. 1920-1923
    • Ulmke, D.1    Kreth, J.2    Lengeler, J.W.3    Welte, W.4    Schmid, T.5
  • 75
    • 0035903650 scopus 로고    scopus 로고
    • Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site
    • Vandeputte-Rutten, L., Kramer, R. A., Kroon, J., Dekker, N., Egmond, M. R., and Gros, P. (2001). Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site. EMBO J. 20, 5033-5039.
    • (2001) EMBO J. , vol.20 , pp. 5033-5039
    • Vandeputte-Rutten, L.1    Kramer, R.A.2    Kroon, J.3    Dekker, N.4    Egmond, M.R.5    Gros, P.6
  • 76
    • 0030759550 scopus 로고    scopus 로고
    • Pore functioning of outer membrane protein PhoE of Escherichia coli: Mutagenesis of the constriction loop L3
    • VanGelder, P., Saint, N., van Boxtel, R., Rosenbusch, J. P., and Tommassen, J. (1997). Pore functioning of outer membrane protein PhoE of Escherichia coli: mutagenesis of the constriction loop L3. Protein Eng. 10, 699-706.
    • (1997) Protein Eng. , vol.10 , pp. 699-706
    • VanGelder, P.1    Saint, N.2    Van Boxtel, R.3    Rosenbusch, J.P.4    Tommassen, J.5
  • 77
    • 0033570111 scopus 로고    scopus 로고
    • The structure of the outer membrane protein OmpX from Escherichia coli reveals possible mechanisms of virulence
    • Vogt, J., and Schulz, G. E. (1999). The structure of the outer membrane protein OmpX from Escherichia coli reveals possible mechanisms of virulence. Structure 7, 1301-1309.
    • (1999) Structure , vol.7 , pp. 1301-1309
    • Vogt, J.1    Schulz, G.E.2
  • 78
    • 0024281633 scopus 로고
    • The gramicidin pore: Crystal structure of a cesium complex
    • Wallace, B. A., and Ravikumar, K. (1988). The gramicidin pore: crystal structure of a cesium complex. Science 241, 182-187.
    • (1988) Science , vol.241 , pp. 182-187
    • Wallace, B.A.1    Ravikumar, K.2
  • 79
    • 0026737314 scopus 로고
    • Structure of porin refined at 1.8 Å resolution
    • Weiss, M. S., and Schulz, G. E. (1992). Structure of porin refined at 1.8 Å resolution. J. Mol. Biol. 227, 493-509.
    • (1992) J. Mol. Biol. , vol.227 , pp. 493-509
    • Weiss, M.S.1    Schulz, G.E.2
  • 80
    • 0025345316 scopus 로고
    • The three-dimensional structure of porin from Rhodobacter capsulatus at 3 Å resolution
    • Weiss, M. S., Wacker, T., Weckesser, J., Welte, W., and Schulz, G. E. (1990). The three-dimensional structure of porin from Rhodobacter capsulatus at 3 Å resolution. FEBS Lett. 267, 268-272.
    • (1990) FEBS Lett. , vol.267 , pp. 268-272
    • Weiss, M.S.1    Wacker, T.2    Weckesser, J.3    Welte, W.4    Schulz, G.E.5
  • 81
    • 0026046174 scopus 로고
    • Prediction of the general structure of OmpF and PhoE from the sequence and structure of porin from Rhodobacter capsulatus. Orientation of porin in the membrane
    • Welte, W., Weiss, M. S., Nestel, U., Weckesser, J., Schiltz, E., and Schulz, G. E. (1991). Prediction of the general structure of OmpF and PhoE from the sequence and structure of porin from Rhodobacter capsulatus. Orientation of porin in the membrane. Biochim. Biophys. Acta 1080, 271-274.
    • (1991) Biochim. Biophys. Acta , vol.1080 , pp. 271-274
    • Welte, W.1    Weiss, M.S.2    Nestel, U.3    Weckesser, J.4    Schiltz, E.5    Schulz, G.E.6
  • 82
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley, W. C., and White, S. H. (1996). Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat. Struct. Biol. 3, 842-848.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 83
    • 0032552880 scopus 로고    scopus 로고
    • The preference of tryptophan for membrane interfaces
    • Yau, W. M., Wimley, W. C., Gawrisch, K., and White, S. H. (1998). The preference of tryptophan for membrane interfaces. Biochemistry 37, 14713-14718.
    • (1998) Biochemistry , vol.37 , pp. 14713-14718
    • Yau, W.M.1    Wimley, W.C.2    Gawrisch, K.3    White, S.H.4
  • 84
    • 0027329090 scopus 로고
    • New domain motif: The structure of pectate lyase C, a secreted plant virulence factor
    • Yoder, M. D., Keen, N. T., and Jurnak, F. (1993). New domain motif: the structure of pectate lyase C, a secreted plant virulence factor. Science 260, 1503-1507.
    • (1993) Science , vol.260 , pp. 1503-1507
    • Yoder, M.D.1    Keen, N.T.2    Jurnak, F.3
  • 85
    • 0034665240 scopus 로고    scopus 로고
    • Crystal structure of Omp32, the anion-selective porin from Comamonas acidovorans, in complex with a periplasmic peptide at 2.1 Å resolution
    • Zeth, K., Diederichs, K., Welte, W., and Engelhardt, H. (2000). Crystal structure of Omp32, the anion-selective porin from Comamonas acidovorans, in complex with a periplasmic peptide at 2.1 Å resolution. Structure 8, 981-992.
    • (2000) Structure , vol.8 , pp. 981-992
    • Zeth, K.1    Diederichs, K.2    Welte, W.3    Engelhardt, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.