메뉴 건너뛰기




Volumn 175, Issue 3, 2000, Pages 165-180

Families of proteins forming transmembrane channels

Author keywords

Bacteriocins; Channels; Holins; Membranes; Porins; Toxins; Transport

Indexed keywords

BACTERIOCIN; CARRIER PROTEIN; PORIN;

EID: 0033917333     PISSN: 00222631     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00232001065     Document Type: Review
Times cited : (78)

References (99)
  • 1
    • 0032806872 scopus 로고    scopus 로고
    • Identification of three novel members of the calcium-dependent chloride channel (CaCC) family predominantly expressed in the digestive tract and trachea
    • Agnel, M., Vermat, T., Culouscou, J. 1999. Identification of three novel members of the calcium-dependent chloride channel (CaCC) family predominantly expressed in the digestive tract and trachea. FEBS Lett. 455:295-301
    • (1999) FEBS Lett. , vol.455 , pp. 295-301
    • Agnel, M.1    Vermat, T.2    Culouscou, J.3
  • 3
    • 0028220778 scopus 로고
    • Expansion of bacteriocin activity and host range upon complementation of two peptides encoded within the lactacin F operon
    • Allison, G.E., Fremaux, C., Klaenhammer, T.R. 1994. Expansion of bacteriocin activity and host range upon complementation of two peptides encoded within the lactacin F operon. J. Bacteriol. 176:2235-2241
    • (1994) J. Bacteriol. , vol.176 , pp. 2235-2241
    • Allison, G.E.1    Fremaux, C.2    Klaenhammer, T.R.3
  • 4
    • 0024044243 scopus 로고
    • Extracellular proteins of Vibrio cholerae: Nucleotide sequence of the structural gene (hlyA) for the hemolysin of the hemolytic EI tor strain 017 and characterization of the hlyA mutation in the nonhemolytic classical strain 569B
    • Alm, R.A., Stroeher, U.H., Manning, P.A. 1988. Extracellular proteins of Vibrio cholerae: Nucleotide sequence of the structural gene (hlyA) for the hemolysin of the hemolytic EI Tor strain 017 and characterization of the hlyA mutation in the nonhemolytic classical strain 569B. Mol. Microbiol. 2:481-488
    • (1988) Mol. Microbiol. , vol.2 , pp. 481-488
    • Alm, R.A.1    Stroeher, U.H.2    Manning, P.A.3
  • 5
    • 0027528983 scopus 로고
    • The two faces of Bacillus thuringiensis: Insecticidal proteins and postexponential survival
    • Aronson, A.I. 1993. The two faces of Bacillus thuringiensis: Insecticidal proteins and postexponential survival. Mol. Microbiol. 7:489-496
    • (1993) Mol. Microbiol. , vol.7 , pp. 489-496
    • Aronson, A.I.1
  • 6
    • 0033043978 scopus 로고    scopus 로고
    • Characterization of the dual start motif of a class II holin gene
    • Barenboim, M., Chang, C.-Y., dib Hajj, F., Young, R. 1999. Characterization of the dual start motif of a class II holin gene. Mol. Microbiol. 32:715-727
    • (1999) Mol. Microbiol. , vol.32 , pp. 715-727
    • Barenboim, M.1    Chang, C.-Y.2    Dib Hajj, F.3    Young, R.4
  • 7
    • 0030981655 scopus 로고    scopus 로고
    • Structure and functions of channel-forming peptides: Magainins, cecropins, melittin and alamethicin
    • Bechinger, B. 1997. Structure and functions of channel-forming peptides: Magainins, cecropins, melittin and alamethicin. J. Membrane Biol. 156:197-211
    • (1997) J. Membrane Biol. , vol.156 , pp. 197-211
    • Bechinger, B.1
  • 8
    • 0033028398 scopus 로고    scopus 로고
    • Pseudomonas syringae phytotoxins: Mode of action, regulation and biosynthesis by peptide and polyketide synthetases
    • Bender, C.L., Alarcón-Chaidez, F., Gross, D.C. 1999. Pseudomonas syringae phytotoxins: Mode of action, regulation and biosynthesis by peptide and polyketide synthetases. Microbiol. Mol. Biol. Rev. 63:266-292
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 266-292
    • Bender, C.L.1    Alarcón-Chaidez, F.2    Gross, D.C.3
  • 10
    • 0037513862 scopus 로고    scopus 로고
    • The C-terminal sequence of the λ holin constitutes a cytoplasmic regulatory domain
    • Bläsi, U., Fraisl, P., Chang, C.-Y., Zhang, N., Young, R. 1999. The C-terminal sequence of the λ holin constitutes a cytoplasmic regulatory domain. J. Bacteriol. 181:2922-2929
    • (1999) J. Bacteriol. , vol.181 , pp. 2922-2929
    • Bläsi, U.1    Fraisl, P.2    Chang, C.-Y.3    Zhang, N.4    Young, R.5
  • 11
    • 0028325274 scopus 로고
    • Colicins: Structures, modes of action, transfer through membranes and evolution
    • Braun, V., Pilsl, H., Gross, P. 1994. Colicins: Structures, modes of action, transfer through membranes and evolution. Arch. Microbiol. 161:199-206
    • (1994) Arch. Microbiol. , vol.161 , pp. 199-206
    • Braun, V.1    Pilsl, H.2    Gross, P.3
  • 12
    • 0030903162 scopus 로고    scopus 로고
    • Phylogenetic relationships of Bacillus thuringiensis δ-endotoxin family proteins and their functional domains
    • Bravo, A. 1997. Phylogenetic relationships of Bacillus thuringiensis δ-endotoxin family proteins and their functional domains. J. Bacteriol. 179:2793-2801
    • (1997) J. Bacteriol. , vol.179 , pp. 2793-2801
    • Bravo, A.1
  • 13
    • 0032573081 scopus 로고    scopus 로고
    • The conducting form of gramicidin A is a right-handed double-stranded double helix
    • Burkhart, B.M., Li, N., Langs, D.A., Pangborn, W.A., Duax, W.L. 1998. The conducting form of gramicidin A is a right-handed double-stranded double helix. Proc. Natl. Acad. Sci. USA 95:12950-12955
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12950-12955
    • Burkhart, B.M.1    Li, N.2    Langs, D.A.3    Pangborn, W.A.4    Duax, W.L.5
  • 14
    • 17544382882 scopus 로고    scopus 로고
    • Unusual amino acid determinants of host range in the Mtx2 family of mosquitocidal toxins
    • Chan, S.W., Thanabalu, T., Wee, B.Y., Porter, A.G. 1996. Unusual amino acid determinants of host range in the Mtx2 family of mosquitocidal toxins. J. Biol. Chem. 271:14183-14187
    • (1996) J. Biol. Chem. , vol.271 , pp. 14183-14187
    • Chan, S.W.1    Thanabalu, T.2    Wee, B.Y.3    Porter, A.G.4
  • 17
    • 0033515072 scopus 로고    scopus 로고
    • The vacuolating toxin from Helicobacter pylori forms hexameric pores in lipid bilayers at low pH
    • Czajkowsky, D.W., Iwanoto, H., Cover, T.L., Shao, Z. 1999. The vacuolating toxin from Helicobacter pylori forms hexameric pores in lipid bilayers at low pH. Proc. Natl. Acad. Sci. USA 96:2001-2006
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 2001-2006
    • Czajkowsky, D.W.1    Iwanoto, H.2    Cover, T.L.3    Shao, Z.4
  • 18
    • 0025170604 scopus 로고
    • The mitochondrial aspartate/glutamate and ADP/ATP carrier switch from obligate counterexchange to unidirectional transport after modification by SH-reagents
    • Dierks, T., Salentin, A., Heberger, C., Krämer, R. 1990a. The mitochondrial aspartate/glutamate and ADP/ATP carrier switch from obligate counterexchange to unidirectional transport after modification by SH-reagents. Biochim. Biophys. Acta 1028:268-280
    • (1990) Biochim. Biophys. Acta , vol.1028 , pp. 268-280
    • Dierks, T.1    Salentin, A.2    Heberger, C.3    Krämer, R.4
  • 19
    • 0025126060 scopus 로고
    • Pore-like and carrier-like properties of the mitochondrial aspartate/glutamate carrier after modification by SH-reagents: Evidence for a preformed channel as a structural requirement of carrier-mediated transport
    • Dierks, T., Salentin, A., Heberger, C., Krämer, R. 1990b. Pore-like and carrier-like properties of the mitochondrial aspartate/glutamate carrier after modification by SH-reagents: Evidence for a preformed channel as a structural requirement of carrier-mediated transport. Biochim. Biophys. Acta 1028:281-288
    • (1990) Biochim. Biophys. Acta , vol.1028 , pp. 281-288
    • Dierks, T.1    Salentin, A.2    Heberger, C.3    Krämer, R.4
  • 22
    • 0031627534 scopus 로고    scopus 로고
    • CIC and CFTR chloride channel gating
    • Foskett, J.K. 1998. CIC and CFTR chloride channel gating. Annu. Rev. Physiol. 60:689-717
    • (1998) Annu. Rev. Physiol. , vol.60 , pp. 689-717
    • Foskett, J.K.1
  • 23
    • 0025134451 scopus 로고
    • Genetic analysis of an MDR-like export system: The secretion of colicin V
    • Gilson, L., Mahanty, H.K., Kolter, R. 1990. Genetic analysis of an MDR-like export system: The secretion of colicin V. EMBO J. 9:3875-3894
    • (1990) EMBO J. , vol.9 , pp. 3875-3894
    • Gilson, L.1    Mahanty, H.K.2    Kolter, R.3
  • 24
    • 0031569404 scopus 로고    scopus 로고
    • The long and short of colicin action: The molecular basis for the biological activity of channel-forming colicins
    • Gonaux, E. 1997. The long and short of colicin action: The molecular basis for the biological activity of channel-forming colicins. Structure 5:313-317
    • (1997) Structure , vol.5 , pp. 313-317
    • Gonaux, E.1
  • 25
    • 0026047489 scopus 로고
    • The cecropin locus-cloning and expression of a gene cluster encoding 3 antibacterial peptides in Hyalophora cecropia
    • Gudmundsson, G.H., Lidholm, D.A., Asling, B., Gan, R.B., Boman, H.G. 1991. The cecropin locus-cloning and expression of a gene cluster encoding 3 antibacterial peptides in Hyalophora cecropia. J. Biol. Chem. 266:11510-11517
    • (1991) J. Biol. Chem. , vol.266 , pp. 11510-11517
    • Gudmundsson, G.H.1    Lidholm, D.A.2    Asling, B.3    Gan, R.B.4    Boman, H.G.5
  • 27
    • 0030862762 scopus 로고    scopus 로고
    • + channel is contained within the multi-membrane-spanning N-terminal region of gp91-phox
    • + channel is contained within the multi-membrane-spanning N-terminal region of gp91-phox. Biochem. J. 325:701-705
    • (1997) Biochem. J. , vol.325 , pp. 701-705
    • Henderson, L.M.1    Thomas, S.2    Banting, G.3    Chappell, J.B.4
  • 28
    • 0025903814 scopus 로고
    • Crystal structure of defensin HNP-3, an amphiphilic dimer: Mechanisms of membrane permeabilization
    • Hill, C.P., Yee, J., Selsted, M.E., Eisenberg, D. 1991. Crystal structure of defensin HNP-3, an amphiphilic dimer: Mechanisms of membrane permeabilization. Science 251:1481-1485
    • (1991) Science , vol.251 , pp. 1481-1485
    • Hill, C.P.1    Yee, J.2    Selsted, M.E.3    Eisenberg, D.4
  • 29
    • 0008549004 scopus 로고
    • Chapter 9: Structure of channel proteins; chapter 20: Evolution and diversity
    • Sinauer Associates, Sunderland, MA
    • Hille, B. 1992. Chapter 9: Structure of channel proteins; Chapter 20: Evolution and diversity. In: Ionic Channels of Excitable Membranes. (2nd Ed). Sinauer Associates, Sunderland, MA
    • (1992) Ionic Channels of Excitable Membranes. (2nd Ed)
    • Hille, B.1
  • 30
    • 0032483451 scopus 로고    scopus 로고
    • Identifying transmembrane states and defining the membrane insertion boundaries of hydrophobic helices in membrane-inserted diphtheria toxin T domain
    • Kachel, K., Ren, J., Collier, R.J., London, E. 1998. Identifying transmembrane states and defining the membrane insertion boundaries of hydrophobic helices in membrane-inserted diphtheria toxin T domain. J. Biol. Chem. 273:22950-22956
    • (1998) J. Biol. Chem. , vol.273 , pp. 22950-22956
    • Kachel, K.1    Ren, J.2    Collier, R.J.3    London, E.4
  • 31
    • 0032718515 scopus 로고    scopus 로고
    • Porins in the cell wall of Mycobacterium tuberculosis
    • Kartmann, B., Stengler, S., Neiderweis, M. 1999. Porins in the cell wall of Mycobacterium tuberculosis. J. Bacteriol. 181:6543-6546
    • (1999) J. Bacteriol. , vol.181 , pp. 6543-6546
    • Kartmann, B.1    Stengler, S.2    Neiderweis, M.3
  • 33
    • 0031896999 scopus 로고    scopus 로고
    • Functional properties and physiological roles of organic solute channels
    • Kirk, K., Strange, K. 1998. Functional properties and physiological roles of organic solute channels. Annu. Rev. Physiol. 60:719-739
    • (1998) Annu. Rev. Physiol. , vol.60 , pp. 719-739
    • Kirk, K.1    Strange, K.2
  • 34
    • 0027199706 scopus 로고
    • Genetics of bacteriocins produced by lactic acid bacteria
    • Klaenhammer, T.R. 1993. Genetics of bacteriocins produced by lactic acid bacteria. FEMS Microbiol. Rev. 12:39-85
    • (1993) FEMS Microbiol. Rev. , vol.12 , pp. 39-85
    • Klaenhammer, T.R.1
  • 35
    • 4244144005 scopus 로고
    • The crystal δ-endotoxins of Bacillus thuringiensis: Models for their mechanisms of action on the insect gut
    • Knowles, B.H., Dow, J.A.T. 1993. The crystal δ-endotoxins of Bacillus thuringiensis: Models for their mechanisms of action on the insect gut. BioEssays 15:469-476
    • (1993) BioEssays , vol.15 , pp. 469-476
    • Knowles, B.H.1    Dow, J.A.T.2
  • 36
    • 0027160122 scopus 로고
    • The mitochondrial carrier family of transport proteins: Structural, functional and evolutionary relationships
    • Kuan, J., Saier, M.H., Jr. 1993. The mitochondrial carrier family of transport proteins: structural, functional and evolutionary relationships. Crit. Rev. Biochem. Mol. Biol. 28:209-233
    • (1993) Crit. Rev. Biochem. Mol. Biol. , vol.28 , pp. 209-233
    • Kuan, J.1    Saier M.H., Jr.2
  • 37
    • 0032441768 scopus 로고    scopus 로고
    • Unraveling the structures and modes of action of bacterial toxins
    • Lacy, D.B., Stevens, R.C. 1998. Unraveling the structures and modes of action of bacterial toxins. Curr. Opin. Struct. Biol. 8:778-784
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 778-784
    • Lacy, D.B.1    Stevens, R.C.2
  • 39
    • 0032991467 scopus 로고    scopus 로고
    • Protonmotive force, ExbB and ligand-bound FepA drive conformational changes in TonB
    • Larsen, R.A., Thomas, M.G., 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
  • 42
    • 0345196593 scopus 로고    scopus 로고
    • Protection of E. Coli cells against extreme turgor by activation of MscS and MscL mechanosensitive channels: Identification of genes required for MscS activity
    • Levina, N., Tötemeyer, S., Stokes, N.R., Louis, P., Jones, M.A., Booth, I.R. 1999. Protection of E. coli cells against extreme turgor by activation of MscS and MscL mechanosensitive channels: Identification of genes required for MscS activity. EMBO J. 18:1730-1737
    • (1999) EMBO J. , vol.18 , pp. 1730-1737
    • Levina, N.1    Tötemeyer, S.2    Stokes, N.R.3    Louis, P.4    Jones, M.A.5    Booth, I.R.6
  • 43
    • 0032973863 scopus 로고    scopus 로고
    • Evidence for a small anion-selective channel in the cell wall of Mycobacterium bovis BCG besides a wide cation-selective pore
    • Lichtinger, T., Heym, B., Maier, E., Eichner, H., Cole, S.T., Benz, R. 1999. Evidence for a small anion-selective channel in the cell wall of Mycobacterium bovis BCG besides a wide cation-selective pore. FEBS Lett. 454:349-355
    • (1999) FEBS Lett. , vol.454 , pp. 349-355
    • Lichtinger, T.1    Heym, B.2    Maier, E.3    Eichner, H.4    Cole, S.T.5    Benz, R.6
  • 44
    • 0033979868 scopus 로고    scopus 로고
    • Biochemical identification and biophysical characterization of a channel-forming protein from Rhodococcus erythropolis
    • Lichtinger, T., Reiss, G., Benz, R. 2000. Biochemical identification and biophysical characterization of a channel-forming protein from Rhodococcus erythropolis. J. Bacteriol. 182:764-770
    • (2000) J. Bacteriol. , vol.182 , pp. 764-770
    • Lichtinger, T.1    Reiss, G.2    Benz, R.3
  • 46
    • 0029949981 scopus 로고    scopus 로고
    • New gene from nine Bacillus sphaericus strains encoding highly conserved 35.8 kilodalton mosquitocidal toxins
    • Liu, J.W., Porter, A.G., Wee, B.Y., Thanabalu, T. 1996. New gene from nine Bacillus sphaericus strains encoding highly conserved 35.8 kilodalton mosquitocidal toxins. Appl. Environ. Microbiol. 62:2174-2176
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 2174-2176
    • Liu, J.W.1    Porter, A.G.2    Wee, B.Y.3    Thanabalu, T.4
  • 47
    • 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., 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
  • 48
    • 0026574178 scopus 로고
    • Diphtheria toxin: Membrane interaction and membrane translocation
    • London, E. 1992. Diphtheria toxin: Membrane interaction and membrane translocation. Biochim. Biophys. Acta 1113:25-51
    • (1992) Biochim. Biophys. Acta , vol.1113 , pp. 25-51
    • London, E.1
  • 49
    • 0032927728 scopus 로고    scopus 로고
    • Analysis of the SlyA-controlled expression, subcellular localization and pore-forming activity of a 34 kDa hemolysin (ClyA) from Escherichia coli K-12
    • Ludwig, A., Bauer, S., Benz, R., Bergmann, B., Goebel, W. 1999. Analysis of the SlyA-controlled expression, subcellular localization and pore-forming activity of a 34 kDa hemolysin (ClyA) from Escherichia coli K-12. Mol. Microbiol. 31:557-567
    • (1999) Mol. Microbiol. , vol.31 , pp. 557-567
    • Ludwig, A.1    Bauer, S.2    Benz, R.3    Bergmann, B.4    Goebel, W.5
  • 50
    • 0025369033 scopus 로고
    • A consensus structure for membrane transport
    • Maloney, P.C. 1990. A consensus structure for membrane transport. Res. Microbiol. 141:374-383
    • (1990) Res. Microbiol. , vol.141 , pp. 374-383
    • Maloney, P.C.1
  • 51
    • 0033985403 scopus 로고    scopus 로고
    • Crosstalk between ammonium transporters in yeast and interference by the soybean SAT1 protein
    • Marini, A.-M., Spingael, J.-Y., Frommer, W.B., André, B. 2000. Crosstalk between ammonium transporters in yeast and interference by the soybean SAT1 protein. Mol. Microbiol. 35:378-385
    • (2000) Mol. Microbiol. , vol.35 , pp. 378-385
    • Marini, A.-M.1    Spingael, J.-Y.2    Frommer, W.B.3    André, B.4
  • 52
    • 0029870676 scopus 로고    scopus 로고
    • Peptide models for membrane channels
    • Marsh, D. 1996. Peptide models for membrane channels. Biochem. J. 315:345-361
    • (1996) Biochem. J. , vol.315 , pp. 345-361
    • Marsh, D.1
  • 53
    • 0031912599 scopus 로고    scopus 로고
    • Functional analysis of the two-gene lysis system of the Pneumococcal phage Cp-1 in homologous and heterologous host cells
    • Martín, A.C., López, R., García, P. 1998. Functional analysis of the two-gene lysis system of the Pneumococcal phage Cp-1 in homologous and heterologous host cells. J. Bacteriol. 180:210-217
    • (1998) J. Bacteriol. , vol.180 , pp. 210-217
    • Martín, A.C.1    López, R.2    García, P.3
  • 55
    • 0025114667 scopus 로고
    • Mechanosensitive channels of E. Coli activated by amphipaths
    • Martinac, B., Adler, J., Kung, C. 1990. Mechanosensitive channels of E. coli activated by amphipaths. Nature 348:261-263
    • (1990) Nature , vol.348 , pp. 261-263
    • Martinac, B.1    Adler, J.2    Kung, C.3
  • 56
    • 0031962435 scopus 로고    scopus 로고
    • Analysis of the gene cluster involved in production and immunity of the peptide antibiotic AS-48 in Enterococcus faecalis
    • Martínez-Bueno, M., Valdivia, E., Gálvez, A., Coyette, J., Maqueda, M. 1998. Analysis of the gene cluster involved in production and immunity of the peptide antibiotic AS-48 in Enterococcus faecalis. Mol. Microbiol. 27:347-358
    • (1998) Mol. Microbiol. , vol.27 , pp. 347-358
    • Martínez-Bueno, M.1    Valdivia, E.2    Gálvez, A.3    Coyette, J.4    Maqueda, M.5
  • 57
    • 0031740520 scopus 로고    scopus 로고
    • Magainins as paradigm for the mode of action of pore forming polypeptides
    • Matsuzaki, K. 1998. Magainins as paradigm for the mode of action of pore forming polypeptides. Biochim. Biophys. Acta 1376:391-400
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 391-400
    • Matsuzaki, K.1
  • 58
    • 0032145173 scopus 로고    scopus 로고
    • Protein toxins and membrane transport
    • Montecucco, C. 1998. Protein toxins and membrane transport. Curr. Opin. Cell Biol. 10:530-536
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 530-536
    • Montecucco, C.1
  • 59
    • 0033222872 scopus 로고    scopus 로고
    • Modular assembly of voltage-gated channel proteins: A sequence analysis and phylogenetic study
    • Nelson, R.D., Kuan, G., Saier, M.H., Jr., Montal, M. 1999. Modular assembly of voltage-gated channel proteins: A sequence analysis and phylogenetic study. J. Mol. Microbiol. Biotechnol. 1:281-287
    • (1999) J. Mol. Microbiol. Biotechnol. , vol.1 , pp. 281-287
    • Nelson, R.D.1    Kuan, G.2    Saier M.H., Jr.3    Montal, M.4
  • 62
    • 0028055018 scopus 로고
    • The winds of (evolutionary) change: Breathing new life into microbiology
    • Olsen, G.J., Woese, C.R., Overbeek, R. 1994. The winds of (evolutionary) change: breathing new life into microbiology. J. Bacteriol. 176:1-6
    • (1994) J. Bacteriol. , vol.176 , pp. 1-6
    • Olsen, G.J.1    Woese, C.R.2    Overbeek, R.3
  • 64
    • 0026468973 scopus 로고
    • NMR studies of defensin antimicrobial peptides. 2. Three-dimensional structures of rabbit NP-2 and human HNP-1
    • Pardi, A., Zhang, X.L., Selsted, M.E., Skalicky, J.J., Yip, P.F. 1992. NMR studies of defensin antimicrobial peptides. 2. Three-dimensional structures of rabbit NP-2 and human HNP-1. Biochemistry 31:11357-11364
    • (1992) Biochemistry , vol.31 , pp. 11357-11364
    • Pardi, A.1    Zhang, X.L.2    Selsted, M.E.3    Skalicky, J.J.4    Yip, P.F.5
  • 65
    • 0029910115 scopus 로고    scopus 로고
    • Phylogenetic characterization of the MIP family of transmembrane channel proteins
    • Park, J.H., Saier, M.H., Jr. 1996. Phylogenetic characterization of the MIP family of transmembrane channel proteins. J. Membrane Biol. 153:171-180
    • (1996) J. Membrane Biol. , vol.153 , pp. 171-180
    • Park, J.H.1    Saier M.H., Jr.2
  • 66
    • 0030043134 scopus 로고    scopus 로고
    • Aerolysin - the ins and outs of a model channel-forming toxin
    • Parker, M.W., van der Goot, F.G., Buckley, J.T. 1996. Aerolysin - the ins and outs of a model channel-forming toxin. Mol. Microbiol. 19:205-212
    • (1996) Mol. Microbiol. , vol.19 , pp. 205-212
    • Parker, M.W.1    Van Der Goot, F.G.2    Buckley, J.T.3
  • 67
    • 0030769466 scopus 로고    scopus 로고
    • Clostridium perfringens epsilon-toxin acts on MDCK cells by forming a large membrane complex
    • Petit, L., Gibert, M., Gillet, D., Laurent-Winter, C., Boquet, P., Popoff, M.R. 1997. Clostridium perfringens epsilon-toxin acts on MDCK cells by forming a large membrane complex. J. Bacteriol. 179:6480-6487
    • (1997) J. Bacteriol. , vol.179 , pp. 6480-6487
    • Petit, L.1    Gibert, M.2    Gillet, D.3    Laurent-Winter, C.4    Boquet, P.5    Popoff, M.R.6
  • 69
    • 0026782824 scopus 로고
    • - channel protein isolated from bovine trachea
    • - channel protein isolated from bovine trachea. J. Biol. Chem. 267:3618-3625
    • (1992) J. Biol. Chem. , vol.267 , pp. 3618-3625
    • Ran, S.1    Benos, D.J.2
  • 70
    • 0043284551 scopus 로고    scopus 로고
    • Mechanisms of pyrazinamide resistance in mycobacteria: Importance of lack of uptake in addition to lack of pyrazinamide activity
    • Raynaud, C., Lanéelle, M.-A., Senaratne, R.H., Draper, P., Lanéelle, G., Daffé, M. 1999. Mechanisms of pyrazinamide resistance in mycobacteria: importance of lack of uptake in addition to lack of pyrazinamide activity. Microbiology 145:1359-1367
    • (1999) Microbiology , vol.145 , pp. 1359-1367
    • Raynaud, C.1    Lanéelle, M.-A.2    Senaratne, R.H.3    Draper, P.4    Lanéelle, G.5    Daffé, M.6
  • 71
    • 0031824098 scopus 로고    scopus 로고
    • The cell wall porin of Nocardia farcinica: Biochemical identification of the channel-forming protein and biophysical characterization of the channel properties
    • Riess, F.G., Lichtinger, T., Cseh, R., Yassin, A.F., Schaal, K.P., Benz, R. 1998. The cell wall porin of Nocardia farcinica: biochemical identification of the channel-forming protein and biophysical characterization of the channel properties. Mol. Microbiol. 29:139-150
    • (1998) Mol. Microbiol. , vol.29 , pp. 139-150
    • Riess, F.G.1    Lichtinger, T.2    Cseh, R.3    Yassin, A.F.4    Schaal, K.P.5    Benz, R.6
  • 72
    • 0007871410 scopus 로고    scopus 로고
    • The cell wall porin of the gram-positive bacterium Nocardia asteriodes forms cation-selective channels that exhibit asymmetric voltage dependence
    • Riess, F.G., Lichtinger, T., Yassin, A.F., Schaal, K.P., Benz, R. 1999. The cell wall porin of the gram-positive bacterium Nocardia asteriodes forms cation-selective channels that exhibit asymmetric voltage dependence. Arch. Microbiol. 171:173-182
    • (1999) Arch. Microbiol. , vol.171 , pp. 173-182
    • Riess, F.G.1    Lichtinger, T.2    Yassin, A.F.3    Schaal, K.P.4    Benz, R.5
  • 73
    • 0032425481 scopus 로고    scopus 로고
    • Molecular mechanisms of bacteriocin evolution
    • Riley, M.A. 1998. Molecular mechanisms of bacteriocin evolution. Annu. Rev. Genet. 32:255-278
    • (1998) Annu. Rev. Genet. , vol.32 , pp. 255-278
    • Riley, M.A.1
  • 74
    • 0030666371 scopus 로고    scopus 로고
    • Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form
    • Rossjohn, J., Feil, S.C., McKinstry, W.J., Tweten, R.K., Parker, M.W. 1997. Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form. Cell 89:685-692
    • (1997) Cell , vol.89 , pp. 685-692
    • Rossjohn, J.1    Feil, S.C.2    McKinstry, W.J.3    Tweten, R.K.4    Parker, M.W.5
  • 75
    • 0031782954 scopus 로고    scopus 로고
    • Lantibiotics: Biosynthesis and biological activities of uniquely modified peptides from Gram-positive bacteria
    • Sahl, H.-G., Bierbaum, G. 1998. Lantibiotics: Biosynthesis and biological activities of uniquely modified peptides from Gram-positive bacteria. Annu. Rev. Microbiol. 52:41-79
    • (1998) Annu. Rev. Microbiol. , vol.52 , pp. 41-79
    • Sahl, H.-G.1    Bierbaum, G.2
  • 76
    • 0028345374 scopus 로고
    • Computer-aided analyses of transport protein sequences: Gleaning evidence concerning function, structure, biogenesis, and evolution
    • Saier, M.H., Jr. 1994. Computer-aided analyses of transport protein sequences: gleaning evidence concerning function, structure, biogenesis, and evolution. Microbiol. Rev. 58:71-93
    • (1994) Microbiol. Rev. , vol.58 , pp. 71-93
    • Saier M.H., Jr.1
  • 77
    • 0031733149 scopus 로고    scopus 로고
    • Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya
    • R.K. Poole, editor. Academic Press San Diego, CA
    • Saier, M.H., Jr. 1998. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. In: Advances in Microbial Physiology. R.K. Poole, editor. pp. 81-136. Academic Press San Diego, CA.
    • (1998) Advances in Microbial Physiology , pp. 81-136
    • Saier M.H., Jr.1
  • 78
    • 0344172785 scopus 로고    scopus 로고
    • Genome archeology leading to the characterization and classification of transport proteins
    • Saier, M.H., Jr. 1999. Genome archeology leading to the characterization and classification of transport proteins. Curr. Opin. Microbiol. 2:555-561
    • (1999) Curr. Opin. Microbiol. , vol.2 , pp. 555-561
    • Saier M.H., Jr.1
  • 79
    • 0032428794 scopus 로고    scopus 로고
    • Structures of membrane proteins determined at atomic resolution
    • Sakai, H., Tsukihara, T. 1998. Structures of membrane proteins determined at atomic resolution. J. Biochem. 124:1051-1059
    • (1998) J. Biochem. , vol.124 , pp. 1051-1059
    • Sakai, H.1    Tsukihara, T.2
  • 80
    • 0032543554 scopus 로고    scopus 로고
    • + channels in atomic glory
    • + channels in atomic glory. Curr. Biol. 8:R450-R452
    • (1998) Curr. Biol. , vol.8
    • Sansom, M.S.P.1
  • 82
    • 0030220261 scopus 로고    scopus 로고
    • Porins: General to specific, native to engineered passive pores
    • Schulz, G.E. 1996. Porins: General to specific, native to engineered passive pores. Curr. Opin. Struct. Biol. 6:485-490
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 485-490
    • Schulz, G.E.1
  • 83
    • 0028149758 scopus 로고
    • Ion channel properties of the reconstituted chloroplast triose phosphate/phosphate translocator
    • Schwarz, M., Gross, A., Steinkamp, T., Flügge, U.-I., Wagner, R. 1994. Ion channel properties of the reconstituted chloroplast triose phosphate/phosphate translocator. J. Biol. Chem. 269:29481-29489
    • (1994) J. Biol. Chem. , vol.269 , pp. 29481-29489
    • Schwarz, M.1    Gross, A.2    Steinkamp, T.3    Flügge, U.-I.4    Wagner, R.5
  • 84
    • 0032457522 scopus 로고    scopus 로고
    • Expression of a gene for a porin-like protein of the OmpA family from Mycobacterium tuberculosis H37Rv
    • Senaratne, R.H., Mobasheri, H., Papavinasasundaram, K.G., Jenner, P., Lea, E.J.A., Draper, P. 1998. Expression of a gene for a porin-like protein of the OmpA family from Mycobacterium tuberculosis H37Rv. J. Bacteriol. 180:3541-3547
    • (1998) J. Bacteriol. , vol.180 , pp. 3541-3547
    • Senaratne, R.H.1    Mobasheri, H.2    Papavinasasundaram, K.G.3    Jenner, P.4    Lea, E.J.A.5    Draper, P.6
  • 85
    • 0031920998 scopus 로고    scopus 로고
    • Microbial magnesium transport: Unusual transporters searching for identity
    • Smith, R.L., Maguire, M.E. 1998. Microbial magnesium transport: Unusual transporters searching for identity. Mol. Microbiol. 28:217-226
    • (1998) Mol. Microbiol. , vol.28 , pp. 217-226
    • Smith, R.L.1    Maguire, M.E.2
  • 86
    • 0031946779 scopus 로고    scopus 로고
    • Functional similarity between archaeal and bacterial CorA magnesium transporters
    • Smith, R.L., Gottlieb, E., Kucharski, L.M., Maguire, M.E. 1998a. Functional similarity between archaeal and bacterial CorA magnesium transporters. J. Bacteriol. 180:2788-2791
    • (1998) J. Bacteriol. , vol.180 , pp. 2788-2791
    • Smith, R.L.1    Gottlieb, E.2    Kucharski, L.M.3    Maguire, M.E.4
  • 88
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore
    • Song, L., Hobaugh, M.R., Shustak, C., Cheley, S., Bayley, H., Gouaux, J.E. 1996. Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore. Science 274:1859-1866
    • (1996) Science , vol.274 , pp. 1859-1866
    • Song, L.1    Hobaugh, M.R.2    Shustak, C.3    Cheley, S.4    Bayley, H.5    Gouaux, J.E.6
  • 91
    • 0029681356 scopus 로고    scopus 로고
    • MscL: A mechanosensitive channel in Escherichia coli
    • D.E. Clapham and B.E. Ehrlich, editors, Rockefeller University Press, New York
    • Sukharev, S.I., Blount, P., Martinac, B., Guy, H.R., Kung, C. 1996. MscL: A mechanosensitive channel in Escherichia coli. In: Organellar Ion Channels and Transporters. D.E. Clapham and B.E. Ehrlich, editors, pp. 133-141 Rockefeller University Press, New York
    • (1996) Organellar Ion Channels and Transporters , pp. 133-141
    • Sukharev, S.I.1    Blount, P.2    Martinac, B.3    Guy, H.R.4    Kung, C.5
  • 92
    • 0020479123 scopus 로고
    • The structure of melittin. II. Interpretation of the structure
    • Terwilliger, T.C., Eisenberg, D. 1982. The structure of melittin. II. Interpretation of the structure. J. Biol. Chem. 257:6016-6022
    • (1982) J. Biol. Chem. , vol.257 , pp. 6016-6022
    • Terwilliger, T.C.1    Eisenberg, D.2
  • 94
    • 0029074843 scopus 로고
    • Functional analysis of the pediocin operon of Pediococcus acidilactici PAC1.0: PedB is the immunity protein and PedD is the precursor processing enzyme
    • Venema, K., Kok, J., Marugg, J.D., Toonen, M.Y., Ledeboer, A.M., Venema, G., Chikindas, M.L. 1995a. Functional analysis of the pediocin operon of Pediococcus acidilactici PAC1.0: PedB is the immunity protein and PedD is the precursor processing enzyme. Mol. Microbiol. 17:515-522
    • (1995) Mol. Microbiol. , vol.17 , pp. 515-522
    • Venema, K.1    Kok, J.2    Marugg, J.D.3    Toonen, M.Y.4    Ledeboer, A.M.5    Venema, G.6    Chikindas, M.L.7
  • 95
    • 0029100551 scopus 로고
    • Lactococcal bacteriocins: Mode of action and immunity
    • Venema, K., Venema, G., Kok, J. 1995b. Lactococcal bacteriocins: Mode of action and immunity. Trends Microbiol. 3:299-304
    • (1995) Trends Microbiol. , vol.3 , pp. 299-304
    • Venema, K.1    Venema, G.2    Kok, J.3
  • 96
    • 0031458238 scopus 로고    scopus 로고
    • Ligand conduction and the gated-pore mechanism of transmembrane transport
    • West, I.C. 1997. Ligand conduction and the gated-pore mechanism of transmembrane transport. Biochim. Biophys. Acta 1331:213-234
    • (1997) Biochim. Biophys. Acta , vol.1331 , pp. 213-234
    • West, I.C.1
  • 97
    • 0031033823 scopus 로고    scopus 로고
    • Structure-function studies of the adenylate cyclase toxin of Bordetella pertussis and the leukotoxin of Pasteurella haemolytica by heterologous C protein activation and construction of hybrid proteins
    • Westrop, G., Hormozi, K., da Costa, N., Parton, R., Coote, J. 1997. Structure-function studies of the adenylate cyclase toxin of Bordetella pertussis and the leukotoxin of Pasteurella haemolytica by heterologous C protein activation and construction of hybrid proteins. J. Bacteriol. 179:871-879
    • (1997) J. Bacteriol. , vol.179 , pp. 871-879
    • Westrop, G.1    Hormozi, K.2    Da Costa, N.3    Parton, R.4    Coote, J.5
  • 98
    • 0029097918 scopus 로고
    • Holins: Form and function in bacteriophage lysis
    • Young, R., Bläsi, U. 1995. Holins: Form and function in bacteriophage lysis. FEMS Microbiol. Rev. 17:191-205
    • (1995) FEMS Microbiol. Rev. , vol.17 , pp. 191-205
    • Young, R.1    Bläsi, U.2
  • 99
    • 0033556418 scopus 로고    scopus 로고
    • Oligomerization of Vibrio cholerae cytolysin yields a pentameric pore and has a dual specificity for cholesterol and sphingolipids in the target membrane
    • Zitzer, A., Zitzer, O., Bhakdi, S., Palmer, M. 1999. Oligomerization of Vibrio cholerae cytolysin yields a pentameric pore and has a dual specificity for cholesterol and sphingolipids in the target membrane. J. Biol. Chem. 274:1375-1380
    • (1999) J. Biol. Chem. , vol.274 , pp. 1375-1380
    • Zitzer, A.1    Zitzer, O.2    Bhakdi, S.3    Palmer, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.