메뉴 건너뛰기




Volumn 21, Issue 6, 2004, Pages 351-359

Protein-lipid interactions of bacteriophage M13 gene 9 minor coat protein

Author keywords

Phage particle disassembly; Protein anchoring; Protein topology; Protein lipid interactions; Secondary structure; Spectroscopy

Indexed keywords

COAT PROTEIN; GENE 9 PROTEIN; UNCLASSIFIED DRUG;

EID: 11144349743     PISSN: 09687688     EISSN: None     Source Type: Journal    
DOI: 10.1080/09687860400012918     Document Type: Review
Times cited : (3)

References (79)
  • 1
  • 2
    • 0032406838 scopus 로고    scopus 로고
    • Statistical analysis of predicted transmembrane alpha-helices
    • Arkin, I. T. and Brunger, A. T., 1998, Statistical analysis of predicted transmembrane alpha-helices. Biochim. Biophys. Acta, 1429, 113-128.
    • (1998) Biochim. Biophys. Acta , vol.1429 , pp. 113-128
    • Arkin, I.T.1    Brunger, A.T.2
  • 4
    • 0024110756 scopus 로고
    • Filamentous phage morphogenetic signal sequence and orientation of DNA in the virion and gene V protein complex
    • Bauer, M. and Smith, G. P., 1988, Filamentous phage morphogenetic signal sequence and orientation of DNA in the virion and gene V protein complex. Virology, 167, 166-175.
    • (1988) Virology , vol.167 , pp. 166-175
    • Bauer, M.1    Smith, G.P.2
  • 5
    • 0017260974 scopus 로고
    • Mass, length, composition and structure of the filamentous bacterial virus fd
    • Berkowitz, S. and Day, L., 1976, Mass, length, composition and structure of the filamentous bacterial virus fd. J. Mol. Biol., 102, 531-547.
    • (1976) J. Mol. Biol. , vol.102 , pp. 531-547
    • Berkowitz, S.1    Day, L.2
  • 6
    • 0027942129 scopus 로고
    • Synergistic insertion of two hydrophobic regions drives Sec-independent membrane protein assembly
    • Cao, G., Cheng, S., Whitley, P., Von Heijne, G., Kuhn, A. and Dalbey, R. E., 1994, Synergistic insertion of two hydrophobic regions drives Sec-independent membrane protein assembly. J. Biol. Chem., 269, 26898-26903.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26898-26903
    • Cao, G.1    Cheng, S.2    Whitley, P.3    Von Heijne, G.4    Kuhn, A.5    Dalbey, R.E.6
  • 7
    • 0028935007 scopus 로고
    • The translocation of negatively charged residues across the membrane is driven by the electrochemical potential: Evidence for an electrophoresis-like membrane transfer mechanism
    • Cao, G., Kuhn, A. and Dalbey, R. E., 1995, The translocation of negatively charged residues across the membrane is driven by the electrochemical potential: evidence for an electrophoresis-like membrane transfer mechanism. EMBO J, 14, 866-875.
    • (1995) EMBO J. , vol.14 , pp. 866-875
    • Cao, G.1    Kuhn, A.2    Dalbey, R.E.3
  • 8
    • 0034525943 scopus 로고    scopus 로고
    • Evolutionarily related insertion pathways of bacterial, mitochondrial, and thylakoid membrane proteins
    • Dalbey, R. E. and Kuhn, A., 2000, Evolutionarily related insertion pathways of bacterial, mitochondrial, and thylakoid membrane proteins. Ann. Rev. Cell Dev. Biol., 16, 51-87.
    • (2000) Ann. Rev. Cell Dev. Biol. , vol.16 , pp. 51-87
    • Dalbey, R.E.1    Kuhn, A.2
  • 9
    • 0036301006 scopus 로고    scopus 로고
    • Motifs of serine and threonine can drive association of transmembrane helices
    • Dawson, J. P., Weinger, J. S. and Engelman, D. M., 2002, Motifs of serine and threonine can drive association of transmembrane helices. J. Mol. Biol., 316, 799-805.
    • (2002) J. Mol. Biol. , vol.316 , pp. 799-805
    • Dawson, J.P.1    Weinger, J.S.2    Engelman, D.M.3
  • 10
    • 0242659352 scopus 로고    scopus 로고
    • Protein-lipid interactions studied with designed transmembrane peptides: Role of hydrophobic matching and interfacial anchoring
    • De Planque, M. R. R. and Killian, J. A., 2003, Protein-lipid interactions studied with designed transmembrane peptides: role of hydrophobic matching and interfacial anchoring. Mol. Membr. Biol., 20, 271-284.
    • (2003) Mol. Membr. Biol. , vol.20 , pp. 271-284
    • De Planque, M.R.R.1    Killian, J.A.2
  • 12
    • 0029087064 scopus 로고
    • Location of filamentous phage minor coat proteins in phage and in infected cells
    • Endemann, H. and Model, P., 1995, Location of filamentous phage minor coat proteins in phage and in infected cells. J. Mol. Biol., 250, 496-506.
    • (1995) J. Mol. Biol. , vol.250 , pp. 496-506
    • Endemann, H.1    Model, P.2
  • 13
    • 8844231683 scopus 로고    scopus 로고
    • Membrane integration of E. coli model membrane proteins
    • Corrected Proof, Available online 26 June 2004
    • Facey, S. J. and Kuhn, A., 2004, Membrane integration of E. coli model membrane proteins. Biochim. Biophys. Acta, Corrected Proof, Available online 26 June 2004.
    • (2004) Biochim. Biophys. Acta
    • Facey, S.J.1    Kuhn, A.2
  • 14
    • 0343185890 scopus 로고    scopus 로고
    • Structural and orientational information of the membrane embedded M13 coat protein by 13C-MAS NMR spectroscopy
    • Glaubitz, C., Grobner, G. and Watts, A., 2000, Structural and orientational information of the membrane embedded M13 coat protein by 13C-MAS NMR spectroscopy. Biochem. Biophys. Acta, 1463, 151-161.
    • (2000) Biochem. Biophys. Acta , vol.1463 , pp. 151-161
    • Glaubitz, C.1    Grobner, G.2    Watts, A.3
  • 15
    • 0026638315 scopus 로고
    • 3-Dimensional structure of a cloning vector - X-ray diffraction studies of filamentous bacteriophage-M13 at 7-angstrom resolution
    • Glucksman, M. J., Bhattacharjee, S. and Makowski, L., 1992, 3-Dimensional structure of a cloning vector - X-ray diffraction studies of filamentous bacteriophage-M13 at 7-angstrom resolution. J. Mol. Biol., 226, 455-470.
    • (1992) J. Mol. Biol. , vol.226 , pp. 455-470
    • Glucksman, M.J.1    Bhattacharjee, S.2    Makowski, L.3
  • 16
    • 0019747710 scopus 로고
    • Structure of filamentous bacteriophage: Isolation, characterization, and localization of the minor coat proteins and orientation of the DNA
    • Grant, R. A., Lin, T.-C., Webster, R. E. and Konigsberg, W., 1981, Structure of filamentous bacteriophage: isolation, characterization, and localization of the minor coat proteins and orientation of the DNA. Prog. Clin. Biol. Res., 64, 413-428.
    • (1981) Prog. Clin. Biol. Res. , vol.64 , pp. 413-428
    • Grant, R.A.1    Lin, T.-C.2    Webster, R.E.3    Konigsberg, W.4
  • 17
    • 0021755525 scopus 로고
    • Intrahelical hydrogen bonding of serine, threonine and cysteine residues within alpha-helices and its relevance to membrane-bound proteins
    • Gray, T. M. and Matthews, B. W., 1984, Intrahelical hydrogen bonding of serine, threonine and cysteine residues within alpha-helices and its relevance to membrane-bound proteins. J. Mol. Biol., 175, 75-81.
    • (1984) J. Mol. Biol. , vol.175 , pp. 75-81
    • Gray, T.M.1    Matthews, B.W.2
  • 18
    • 0026723972 scopus 로고
    • Membrane localization and topology of a viral assembly protein
    • Guy-Caffey, J. K., Rapoza, M. P., Jolley, K. A. and Webster, R. E., 1992, Membrane localization and topology of a viral assembly protein. J. Bacteriol., 174, 2460-2465.
    • (1992) J. Bacteriol. , vol.174 , pp. 2460-2465
    • Guy-Caffey, J.K.1    Rapoza, M.P.2    Jolley, K.A.3    Webster, R.E.4
  • 19
    • 2942716977 scopus 로고    scopus 로고
    • Comprehensive mutational analysis of the M13 major coat protein: Improved scaffolds for C-terminal phage display
    • Held, H. A. and Sidhu, S. S., 2004, Comprehensive mutational analysis of the M13 major coat protein: improved scaffolds for C-terminal phage display. J. Mol. Biol., 340, 587-597.
    • (2004) J. Mol. Biol. , vol.340 , pp. 587-597
    • Held, H.A.1    Sidhu, S.S.2
  • 20
    • 0031568809 scopus 로고    scopus 로고
    • A conserved infection pathway for filamentous bacteriophages is suggested by the structure of the membrane penetration domain of the minor coat protein g3p from phage fd
    • Holliger, P. and Riechmann, L., 1997, A conserved infection pathway for filamentous bacteriophages is suggested by the structure of the membrane penetration domain of the minor coat protein g3p from phage fd. Structure, 5, 265-275.
    • (1997) Structure , vol.5 , pp. 265-275
    • Holliger, P.1    Riechmann, L.2
  • 21
    • 0035795118 scopus 로고    scopus 로고
    • Spontaneous insertion of gene 9 minor coat protein of bacteriophage M13 in model membranes
    • Houbiers, M. C., Spruijt, R. B., Demel, R. A., Hemminga, M. A. and Wolfs, C. J. A. M., 2001a, Spontaneous insertion of gene 9 minor coat protein of bacteriophage M13 in model membranes. Biochim. Biophys. Acta, 1511, 309-316.
    • (2001) Biochim. Biophys. Acta , vol.1511 , pp. 309-316
    • Houbiers, M.C.1    Spruijt, R.B.2    Demel, R.A.3    Hemminga, M.A.4    Wolfs, C.J.A.M.5
  • 22
    • 0033579802 scopus 로고    scopus 로고
    • Conformational and aggregational properties of the gene 9 minor coat protein of bacteriophage M13 in membrane-mimicking systems
    • Houbiers, M. C., Spruijt, R. B., Wolfs, C. J. A. M. and Hemminga, M. Á., 1999, Conformational and aggregational properties of the gene 9 minor coat protein of bacteriophage M13 in membrane-mimicking systems. Biochemistry, 38, 1128-1135.
    • (1999) Biochemistry , vol.38 , pp. 1128-1135
    • Houbiers, M.C.1    Spruijt, R.B.2    Wolfs, C.J.A.M.3    Hemminga, M.Á.4
  • 24
    • 0033571246 scopus 로고    scopus 로고
    • Hydrophobic forces drive spontaneous membrane insertion of the bacteriophage Pf3 coat protein without topological control
    • Kiefer, D. and Kuhn, A., 1999, Hydrophobic forces drive spontaneous membrane insertion of the bacteriophage Pf3 coat protein without topological control. EMBO J., 18, 6299-6306.
    • (1999) EMBO J. , vol.18 , pp. 6299-6306
    • Kiefer, D.1    Kuhn, A.2
  • 25
    • 0031740415 scopus 로고    scopus 로고
    • Hydrophobic mismatch between proteins and lipids in membranes
    • Killian, J. A., 1998, Hydrophobic mismatch between proteins and lipids in membranes. Biochim. Biophys. Acta, 1376, 401-416.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 401-416
    • Killian, J.A.1
  • 26
    • 0242405501 scopus 로고    scopus 로고
    • Synthetic peptides as models for intrinsic membrane proteins
    • Killian, J. A., 2003, Synthetic peptides as models for intrinsic membrane proteins. FEBS Lett., 555, 134-138.
    • (2003) FEBS Lett. , vol.555 , pp. 134-138
    • Killian, J.A.1
  • 27
    • 0034284386 scopus 로고    scopus 로고
    • How proteins adapt to a membrane-water interface
    • Killian, J. A. and Von Heijne, G., 2000, How proteins adapt to a membrane-water interface. Trends Biochem. Sci., 25, 429-434.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 429-434
    • Killian, J.A.1    Von Heijne, G.2
  • 28
    • 0023054119 scopus 로고
    • Both hydrophobic domains of M13 procoat are required to initiate membrane insertion
    • Kuhn, A., Kreil, G. and Wickner, W., 1986a, Both hydrophobic domains of M13 procoat are required to initiate membrane insertion. EMBO J., 5, 3681-3685.
    • (1986) EMBO J. , vol.5 , pp. 3681-3685
    • Kuhn, A.1    Kreil, G.2    Wickner, W.3
  • 29
    • 0022654552 scopus 로고
    • The cytoplasmic carboxy terminus of M13 procoat is required for the membrane insertion of its central domain
    • Kuhn, A., Wickner, W. and Kreil, G., 1986b, The cytoplasmic carboxy terminus of M13 procoat is required for the membrane insertion of its central domain. Nature, 322, 335-339.
    • (1986) Nature , vol.322 , pp. 335-339
    • Kuhn, A.1    Wickner, W.2    Kreil, G.3
  • 30
    • 0028047348 scopus 로고
    • A dual role for phosphatidylglycerol in protein translocatron across the Escherichia coli inner membrane
    • Kusters, R., Breukink, E., Gallusser, A., Kuhn, A. and De Kruijff, B., 1994, A dual role for phosphatidylglycerol in protein translocatron across the Escherichia coli inner membrane. J. Biol. Chem., 269, 1560-1563.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1560-1563
    • Kusters, R.1    Breukink, E.2    Gallusser, A.3    Kuhn, A.4    De Kruijff, B.5
  • 31
    • 1842293999 scopus 로고    scopus 로고
    • The filamentous phage pIV multimer visualized by scanning transmission electron microscopy
    • Linderoth, N. A., Simon, M. N. and Russel, M., 1997, The filamentous phage pIV multimer visualized by scanning transmission electron microscopy. Science, 278, 1635-1638.
    • (1997) Science , vol.278 , pp. 1635-1638
    • Linderoth, N.A.1    Simon, M.N.2    Russel, M.3
  • 32
    • 0020075898 scopus 로고
    • Minor coat protein composition and location of the A protein in bacteriophage f1 spheroids and I-forms
    • Lopez, J. and Webster, R. E., 1982, Minor coat protein composition and location of the A protein in bacteriophage f1 spheroids and I-forms. J. Virol., 42, 1099-1107.
    • (1982) J. Virol. , vol.42 , pp. 1099-1107
    • Lopez, J.1    Webster, R.E.2
  • 33
    • 0020619299 scopus 로고
    • Morphogenesis of filamentous bacteriophage f1: Orientation of extrusion and production of polyphage
    • Lopez, J. and Webster, R. E., 1983, Morphogenesis of filamentous bacteriophage f1: orientation of extrusion and production of polyphage. Virology, 127, 177-193.
    • (1983) Virology , vol.127 , pp. 177-193
    • Lopez, J.1    Webster, R.E.2
  • 34
    • 0022362701 scopus 로고
    • Assembly site of bacteriophage f1 corresponds to adhesion zones between the inner and outer membrane of the host cell
    • Lopez, J. and Webster, R. E., 1985, Assembly site of bacteriophage f1 corresponds to adhesion zones between the inner and outer membrane of the host cell. J. Bacteriol., 163, 1270-1274.
    • (1985) J. Bacteriol. , vol.163 , pp. 1270-1274
    • Lopez, J.1    Webster, R.E.2
  • 35
    • 0027080165 scopus 로고
    • Terminating a macromolecular helix - Structural model for the minor proteins of bacteriophage-M13
    • Makowski, L., 1992, Terminating a macromolecular helix - structural model for the minor proteins of bacteriophage-M13. J. Mol. Biol., 228, 885-892.
    • (1992) J. Mol. Biol. , vol.228 , pp. 885-892
    • Makowski, L.1
  • 36
    • 0028353665 scopus 로고
    • Phage display - Structure, assembly and engineering of filamentous bacteriophage M13
    • Makowski, L., 1994, Phage display - structure, assembly and engineering of filamentous bacteriophage M13. Curr. Opinion Struct. Biol., 4, 225-230.
    • (1994) Curr. Opinion Struct. Biol. , vol.4 , pp. 225-230
    • Makowski, L.1
  • 37
    • 0011248458 scopus 로고    scopus 로고
    • Structure and assembly of filamentous bacteriophages
    • W. Chui, M. Burnett and R. L. Garcea, eds (Oxford University Press, London)
    • Makowski, L. and Russel, M., 1997, Structure and assembly of filamentous bacteriophages, In Structural Biology of Viruses, W. Chui, M. Burnett and R. L. Garcea, eds (Oxford University Press, London), pp. 352-380.
    • (1997) Structural Biology of Viruses , pp. 352-380
    • Makowski, L.1    Russel, M.2
  • 38
    • 0018413794 scopus 로고
    • Translational and post-translational cleavage of M13 procoat protein: Extracts of both the cytoplasmic and outer membranes of Escherichia coli contain leader peptidase activity
    • Mandel, G. and Wickner, W., 1979, Translational and post-translational cleavage of M13 procoat protein: Extracts of both the cytoplasmic and outer membranes of Escherichia coli contain leader peptidase activity. Proc. Natl. Acad. Sci. USA, 76, 236-240.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 236-240
    • Mandel, G.1    Wickner, W.2
  • 39
    • 0037372352 scopus 로고    scopus 로고
    • Simultaneous assignment and structure determination of a membrane protein from NMR orientational restraints
    • Marassi, F. M. and Opella, S. J., 2003, Simultaneous assignment and structure determination of a membrane protein from NMR orientational restraints. Prot. Sci., 12, 403-411.
    • (2003) Prot. Sci. , vol.12 , pp. 403-411
    • Marassi, F.M.1    Opella, S.J.2
  • 40
    • 0032054113 scopus 로고    scopus 로고
    • Filamentous phage structure, infection and assembly
    • Marvin, D., 1998, Filamentous phage structure, infection and assembly. Curr. Opinion Struct. Biol., 8, 150-158.
    • (1998) Curr. Opinion Struct. Biol. , vol.8 , pp. 150-158
    • Marvin, D.1
  • 41
    • 0025036161 scopus 로고
    • Model-building studies of Inovirus: Genetic variations on a geometric theme
    • Marvin, D. A., 1990, Model-building studies of Inovirus: genetic variations on a geometric theme. Int. J. Biol. Macromol., 12, 125-138.
    • (1990) Int. J. Biol. Macromol. , vol.12 , pp. 125-138
    • Marvin, D.A.1
  • 42
    • 0028058295 scopus 로고
    • Molecular models and structural comparisons of native and mutant class-I filamentous bacteriophages Ff (fd, f1, M13), If1 and Ike
    • Marvin, D. A., Hale, R. D., Nave, C. and Citterich, M. H., 1994, Molecular models and structural comparisons of native and mutant class-I filamentous bacteriophages Ff (fd, f1, M13), If1 and Ike. J. Mol. Biol., 235, 260-286.
    • (1994) J. Mol. Biol. , vol.235 , pp. 260-286
    • Marvin, D.A.1    Hale, R.D.2    Nave, C.3    Citterich, M.H.4
  • 43
    • 0014530863 scopus 로고
    • Filamentous bacterial viruses
    • Marvin, D. A. and Hohn, B., 1969, Filamentous bacterial viruses. Bacteriol. Rev., 33, 172-209.
    • (1969) Bacteriol. Rev. , vol.33 , pp. 172-209
    • Marvin, D.A.1    Hohn, B.2
  • 44
    • 43949165935 scopus 로고
    • Effect of detergent concentration on multidimensional solution NMR spectra of membrane proteins in micelles
    • McDonnell, P. A. and Opella, S. J., 1993, Effect of detergent concentration on multidimensional solution NMR spectra of membrane proteins in micelles. J. Magn. Reson Ser. B, 102, 120-125.
    • (1993) J. Magn. Reson. Ser. B , vol.102 , pp. 120-125
    • McDonnell, P.A.1    Opella, S.J.2
  • 45
    • 0034705085 scopus 로고    scopus 로고
    • Membrane assembly of the bacteriophage Pf3 major coat protein
    • Meijer, A. B., Spruijt, R. B., Wolfs, C. J. A. M. and Hemminga, M. A., 2000, Membrane assembly of the bacteriophage Pf3 major coat protein. Biochemistry, 39, 6157-6163.
    • (2000) Biochemistry , vol.39 , pp. 6157-6163
    • Meijer, A.B.1    Spruijt, R.B.2    Wolfs, C.J.A.M.3    Hemminga, M.A.4
  • 46
    • 0035942345 scopus 로고    scopus 로고
    • Configurations of the N-terminal amphipathic domain of the membrane-bound M13 major coat protein
    • Meijer, A. B., Spruijt, R. B., Wolfs, C. J. A. M. and Hemminga, M. A., 2001 a, Configurations of the N-terminal amphipathic domain of the membrane-bound M13 major coat protein. Biochemistry, 40, 5081-5086.
    • (2001) Biochemistry , vol.40 , pp. 5081-5086
    • Meijer, A.B.1    Spruijt, R.B.2    Wolfs, C.J.A.M.3    Hemminga, M.A.4
  • 47
    • 0035979356 scopus 로고    scopus 로고
    • Membrane-anchoring interactions of M13 major coat protein
    • Meijer, A. B., Spruijt, R. B., Wolfs, C. J. A. M. and Hemminga, M. A., 2001b, Membrane-anchoring interactions of M13 major coat protein. Biochemistry, 40, 8815-8820.
    • (2001) Biochemistry , vol.40 , pp. 8815-8820
    • Meijer, A.B.1    Spruijt, R.B.2    Wolfs, C.J.A.M.3    Hemminga, M.A.4
  • 48
    • 0001654813 scopus 로고
    • Filamentous bacteriophage
    • R. Calender, ed. (Plenum Press, New York)
    • Model, P. and Russel, M., 1988, Filamentous bacteriophage, In The Bacteriophages, R. Calender, ed. (Plenum Press, New York) pp. 375-456.
    • (1988) The Bacteriophages , pp. 375-456
    • Model, P.1    Russel, M.2
  • 49
    • 0019799876 scopus 로고
    • The orientation of the major coat protein of bacteriophage f1 in the cytoplasmic membrane of Escherichia coli
    • Ohkawa, I. and Webster, R. E., 1981, The orientation of the major coat protein of bacteriophage f1 in the cytoplasmic membrane of Escherichia coli. J. Biol. Chem., 256, 9951-9958.
    • (1981) J. Biol. Chem. , vol.256 , pp. 9951-9958
    • Ohkawa, I.1    Webster, R.E.2
  • 50
    • 0019073186 scopus 로고
    • Nuclear magnetic resonance of the filamentous bacteriophage fd
    • Opella, S. J., Cross, T. A., DiVerdi, J. A. and Sturm, C. F., 1980, Nuclear magnetic resonance of the filamentous bacteriophage fd. Biophys. J., 32, 531-548.
    • (1980) Biophys. J. , vol.32 , pp. 531-548
    • Opella, S.J.1    Cross, T.A.2    DiVerdi, J.A.3    Sturm, C.F.4
  • 52
    • 0032544545 scopus 로고    scopus 로고
    • Solution structure of the M13 major coat protein in detergent micelles: A basis for a model of phage assembly involving specific residues
    • Papavoine, C. H. M., Christiaans, B. E. C., Folmer, R. H. A., Konings, R. N. H. and Hilbers, C. W., 1998, Solution structure of the M13 major coat protein in detergent micelles: A basis for a model of phage assembly involving specific residues. J. Mol. Biol., 282, 401-419.
    • (1998) J. Mol. Biol. , vol.282 , pp. 401-419
    • Papavoine, C.H.M.1    Christiaans, B.E.C.2    Folmer, R.H.A.3    Konings, R.N.H.4    Hilbers, C.W.5
  • 54
    • 0014575324 scopus 로고
    • Conditional lethal mutants of small filamentous coliphage M13. II. Two genes for coat proteins
    • Pratt, D., Tzagoloff, H. and Beaudoin, J., 1969, Conditional lethal mutants of small filamentous coliphage M13. II. Two genes for coat proteins. Virology, 39, 42-53.
    • (1969) Virology , vol.39 , pp. 42-53
    • Pratt, D.1    Tzagoloff, H.2    Beaudoin, J.3
  • 55
    • 0022969124 scopus 로고
    • Ff coliphages: Structural and functional relationships
    • Rasched, I. and Oberer, E., 1986, Ff coliphages: structural and functional relationships. Microbiol. Rev., 50, 401-427.
    • (1986) Microbiol. Rev. , vol.50 , pp. 401-427
    • Rasched, I.1    Oberer, E.2
  • 56
    • 0034732952 scopus 로고    scopus 로고
    • Analysis of the role of interfacial tryptophan residues in controlling the topology of membrane proteins
    • Ridder, A., Morein, S., Stam, J. G., Kuhn, A., De Kruijff, B. and Killian, J. A., 2000, Analysis of the role of interfacial tryptophan residues in controlling the topology of membrane proteins. Biochemistry, 39, 6521-6528.
    • (2000) Biochemistry , vol.39 , pp. 6521-6528
    • Ridder, A.1    Morein, S.2    Stam, J.G.3    Kuhn, A.4    De Kruijff, B.5    Killian, J.A.6
  • 57
    • 0030797114 scopus 로고    scopus 로고
    • The C terminal domain of TolA is the coreceptor for filamentous phage infection of E. Coli
    • Riechmann, L. and Holliger, P., 1997, The C terminal domain of TolA is the coreceptor for filamentous phage infection of E. Coli. Cell, 90, 351-360.
    • (1997) Cell , vol.90 , pp. 351-360
    • Riechmann, L.1    Holliger, P.2
  • 58
    • 0025734125 scopus 로고
    • Filamentous phage assembly
    • Russel, M., 1991, Filamentous phage assembly. Mol. Microbiol., 5, 1607-1613.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1607-1613
    • Russel, M.1
  • 59
    • 2042448583 scopus 로고
    • Thioredoxin is required for filamentous phage assembly
    • Russel, M. and Model, P., 1985, Thioredoxin is required for filamentous phage assembly. Proc. Natl. Acad. Sci. USA, 82, 29-33.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 29-33
    • Russel, M.1    Model, P.2
  • 60
    • 0023035960 scopus 로고
    • The role of thioredoxin in filamentous phage assembly. Construction, isolation, and characterization of mutant thioredoxins
    • Russel, M. and Model, P., 1986, The role of thioredoxin in filamentous phage assembly. Construction, isolation, and characterization of mutant thioredoxins. J. Biol. Chem., 261, 14997-15005.
    • (1986) J. Biol. Chem. , vol.261 , pp. 14997-15005
    • Russel, M.1    Model, P.2
  • 61
    • 0024384323 scopus 로고
    • Genetic analysis of the filamentous bacteriophage packaging signal and of the proteins that interact with it
    • Russel, M. and Model, P., 1989, Genetic analysis of the filamentous bacteriophage packaging signal and of the proteins that interact with it. J. Virol., 63, 3284-3295.
    • (1989) J. Virol. , vol.63 , pp. 3284-3295
    • Russel, M.1    Model, P.2
  • 62
    • 0032428794 scopus 로고    scopus 로고
    • Structures of membrane proteins determined at atomic resolution
    • Sakai, H. and 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
  • 64
    • 0026434565 scopus 로고
    • NMR studies of the structure and dynamics of membrane-bound bacteriophage-Pfl coat protein
    • Shon, K. J., Kim, Y. G., Colnago, L. A, and Opella, S. J., 1991, NMR studies of the structure and dynamics of membrane-bound bacteriophage-Pfl coat protein. Science, 252, 1303-1304.
    • (1991) Science , vol.252 , pp. 1303-1304
    • Shon, K.J.1    Kim, Y.G.2    Colnago, L.A.3    Opella, S.J.4
  • 66
    • 0019263093 scopus 로고
    • Reverse turns in peptides and proteins
    • Smith, J. and Pease, L., 1980, Reverse turns in peptides and proteins. CRC Crit. Rev. Biochem., 8, 315-399.
    • (1980) CRC Crit. Rev. Biochem. , vol.8 , pp. 315-399
    • Smith, J.1    Pease, L.2
  • 67
    • 0034694968 scopus 로고    scopus 로고
    • Localisation and rearrangement modulation of the N-terminal arm of hte membrane-bound major coat protein of bacteriophage M13
    • Spruijt, R. B., Meijer, A. B., Wolfs, C. J. A. M. and Hemminga, M. A., 2000, Localisation and rearrangement modulation of the N-terminal arm of hte membrane-bound major coat protein of bacteriophage M13. Biochim. Biophys. Acta, 1508, 311-323.
    • (2000) Biochim. Biophys. Acta , vol.1508 , pp. 311-323
    • Spruijt, R.B.1    Meijer, A.B.2    Wolfs, C.J.A.M.3    Hemminga, M.A.4
  • 71
    • 0032030962 scopus 로고    scopus 로고
    • The role of anionic lipids in protein insertion and translocation in bacterial membranes
    • Van Klompenburg, W. and De Kruijff, B., 1998, The role of anionic lipids in protein insertion and translocation in bacterial membranes. J. Membr. Biol., 162, 1-7.
    • (1998) J. Membr. Biol. , vol.162 , pp. 1-7
    • Van Klompenburg, W.1    De Kruijff, B.2
  • 72
    • 0030791975 scopus 로고    scopus 로고
    • Anionic phospholipids are determinants of membrane protein topology
    • Van Klompenburg, W., Nilsson, I., Von Heijne, G. and De Kruijff, B., 1997, Anionic phospholipids are determinants of membrane protein topology. EMBO J., 16, 4261-4266.
    • (1997) EMBO J. , vol.16 , pp. 4261-4266
    • Van Klompenburg, W.1    Nilsson, I.2    Von Heijne, G.3    De Kruijff, B.4
  • 73
    • 0019127851 scopus 로고
    • Nucleotide sequence of the filamentous bacteriophage M13 DNA genome: Comparison with phage fd
    • Van Wezenbeek, P., Hulsebos, T. and Schoenmakers, J., 1980, Nucleotide sequence of the filamentous bacteriophage M13 DNA genome: comparison with phage fd. Gene, 11, 129-148.
    • (1980) Gene , vol.11 , pp. 129-148
    • Van Wezenbeek, P.1    Hulsebos, T.2    Schoenmakers, J.3
  • 74
    • 0000651660 scopus 로고
    • The distribution of positively charged residues in bacterial inner membrane proteins correlates with the transmembrane topology
    • Von Heijne, G., 1986, The distribution of positively charged residues in bacterial inner membrane proteins correlates with the transmembrane topology. EMBO J., 5, 3021-3027.
    • (1986) EMBO J. , vol.5 , pp. 3021-3027
    • Von Heijne, G.1
  • 75
    • 0001873730 scopus 로고    scopus 로고
    • Biology of the filamentous phage
    • B. Kay, J. Winter and J. McCafferty, eds. (Academic Press, San Diego)
    • Webster, R. E., 1996, Biology of the filamentous phage, In Phage Display of Peptides and Proteins, B. Kay, J. Winter and J. McCafferty, eds. (Academic Press, San Diego), pp. 1-20.
    • (1996) Phage Display of Peptides and Proteins , pp. 1-20
    • Webster, R.E.1
  • 76
    • 0000398140 scopus 로고
    • Structure and assembly of the class I filamentous bacteriophage
    • S. Casjens, eds. (Jones and Bartelett Publishers Inc., Boston, MA)
    • Webster, R. E. and Lopez, J., 1985, Structure and assembly of the class I filamentous bacteriophage, In Virus Structure and Assembly, S. Casjens, eds. (Jones and Bartelett Publishers Inc., Boston, MA), pp. 235-267.
    • (1985) Virus Structure and Assembly , pp. 235-267
    • Webster, R.E.1    Lopez, J.2
  • 77
    • 0034733385 scopus 로고    scopus 로고
    • Design and evolution of artificial M13 coat proteins
    • Weiss, G. A. and Sidhu, S. S., 2000, Design and evolution of artificial M13 coat proteins. J. Mol. Biol. 300, 213-219.
    • (2000) J. Mol. Biol. , vol.300 , pp. 213-219
    • Weiss, G.A.1    Sidhu, S.S.2
  • 78
    • 0031740601 scopus 로고    scopus 로고
    • Hydrophobic interactions of peptides with membrane interfaces
    • White, S. H. and Wimley, W. C., 1998, Hydrophobic interactions of peptides with membrane interfaces. Biochim. Biophys. Acta, 1376, 339-352.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 339-352
    • White, S.H.1    Wimley, W.C.2
  • 79
    • 0036921994 scopus 로고    scopus 로고
    • Phage display: Practicalities and prospects
    • Willats, W. G. T., 2002, Phage display: practicalities and prospects. Plant Mol. Biol., 50, 837-854.
    • (2002) Plant Mol. Biol. , vol.50 , pp. 837-854
    • Willats, W.G.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.