메뉴 건너뛰기




Volumn 114, Issue 2, 2014, Pages 80-122

Structure and assembly of filamentous bacteriophages

Author keywords

Fibre diffraction; Inovirus; Membrane transport; Phage display; Phyllotaxis; Solid state NMR

Indexed keywords

BACTERIA (MICROORGANISMS); FILAMENTOUS BACTERIOPHAGE; INOVIRIDAE; INOVIRUS;

EID: 84899092430     PISSN: 00796107     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pbiomolbio.2014.02.003     Document Type: Review
Times cited : (102)

References (406)
  • 1
    • 33847697902 scopus 로고    scopus 로고
    • Classification of bacteriophages
    • Oxford University Press, New York, R. Calendar (Ed.)
    • Ackermann H.-W. Classification of bacteriophages. The Bacteriophages 2006, 8-16. Oxford University Press, New York. second ed. R. Calendar (Ed.).
    • (2006) The Bacteriophages , pp. 8-16
    • Ackermann, H.-W.1
  • 2
    • 33846269602 scopus 로고    scopus 로고
    • TRNA's wobble decoding of the genome: 40 years of modification
    • Agris P.F., Vendeix F.A.P., Graham W.D. tRNA's wobble decoding of the genome: 40 years of modification. J.Mol. Biol. 2007, 366:1-13.
    • (2007) J.Mol. Biol. , vol.366 , pp. 1-13
    • Agris, P.F.1    Vendeix, F.A.P.2    Graham, W.D.3
  • 4
    • 0015505976 scopus 로고
    • Isolation and characterization of gene 5 protein of filamentous bacterial viruses
    • Alberts B., Frey L., Delius H. Isolation and characterization of gene 5 protein of filamentous bacterial viruses. J.Mol. Biol. 1972, 68:139-152.
    • (1972) J.Mol. Biol. , vol.68 , pp. 139-152
    • Alberts, B.1    Frey, L.2    Delius, H.3
  • 5
    • 0031577283 scopus 로고    scopus 로고
    • Fd coat protein structure in membrane environments: structural dynamics of the loop between the hydrophobic trans-membrane helix and the amphipathic in-plane helix
    • Almeida F.C.L., Opella S.J. fd coat protein structure in membrane environments: structural dynamics of the loop between the hydrophobic trans-membrane helix and the amphipathic in-plane helix. J.Mol. Biol. 1997, 270:481-495.
    • (1997) J.Mol. Biol. , vol.270 , pp. 481-495
    • Almeida, F.C.L.1    Opella, S.J.2
  • 6
    • 0017379292 scopus 로고
    • Ether induced morphological alteration of Pf1 filamentous phage
    • Amako K., Yasunaka K. Ether induced morphological alteration of Pf1 filamentous phage. Nature 1977, 267:862-863.
    • (1977) Nature , vol.267 , pp. 862-863
    • Amako, K.1    Yasunaka, K.2
  • 7
    • 0038902602 scopus 로고
    • Aserological screening method for detection of free C-terminal amino acids in virus coat proteins
    • Anderer F.A., Schlumberger H.D., Frank H. Aserological screening method for detection of free C-terminal amino acids in virus coat proteins. Biochim. Biophys. Acta 1967, 140:80-92.
    • (1967) Biochim. Biophys. Acta , vol.140 , pp. 80-92
    • Anderer, F.A.1    Schlumberger, H.D.2    Frank, H.3
  • 9
    • 0036913982 scopus 로고    scopus 로고
    • OB-fold domains: a snapshot of the evolution of sequence, structure and function
    • Arcus V. OB-fold domains: a snapshot of the evolution of sequence, structure and function. Curr. Opin. Struct. Biol. 2002, 12:794-801.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 794-801
    • Arcus, V.1
  • 10
    • 84864810701 scopus 로고    scopus 로고
    • Site-specific recombination systems in filamentous phages
    • Askora A., Abdel-Haliem M.E.F., Yamada T. Site-specific recombination systems in filamentous phages. Mol. Genet. Genomics 2012, 287:525-530.
    • (2012) Mol. Genet. Genomics , vol.287 , pp. 525-530
    • Askora, A.1    Abdel-Haliem, M.E.F.2    Yamada, T.3
  • 11
    • 0021111683 scopus 로고
    • The complete DNA sequence of minute virus of mice, an autonomous parvovirus
    • Astell C.R., Thomson M., Merchlinsky M., Ward D.C. The complete DNA sequence of minute virus of mice, an autonomous parvovirus. Nucl. Acids Res. 1983, 11:999-1018.
    • (1983) Nucl. Acids Res. , vol.11 , pp. 999-1018
    • Astell, C.R.1    Thomson, M.2    Merchlinsky, M.3    Ward, D.C.4
  • 13
    • 0019405446 scopus 로고
    • Structure of the protein and DNA in fd filamentous bacterial virus
    • Banner D.W., Nave C., Marvin D.A. Structure of the protein and DNA in fd filamentous bacterial virus. Nature 1981, 289:814-816.
    • (1981) Nature , vol.289 , pp. 814-816
    • Banner, D.W.1    Nave, C.2    Marvin, D.A.3
  • 14
    • 0003400039 scopus 로고    scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor,NY, C.F. Barbas, D.R. Burton, J.K. Scott, G.J. Silverman (Eds.)
    • Phage Display: ALaboratory Manual 2001, Cold Spring Harbor Laboratory Press, Cold Spring Harbor,NY. C.F. Barbas, D.R. Burton, J.K. Scott, G.J. Silverman (Eds.).
    • (2001) Phage Display: ALaboratory Manual
  • 15
    • 70349290626 scopus 로고    scopus 로고
    • Amodel liquid crystalline system based on rodlike viruses with variable chirality and persistence length
    • Barry E., Beller D., Dogic Z. Amodel liquid crystalline system based on rodlike viruses with variable chirality and persistence length. Soft Matter 2009, 5:2563-2570.
    • (2009) Soft Matter , vol.5 , pp. 2563-2570
    • Barry, E.1    Beller, D.2    Dogic, Z.3
  • 16
    • 0024110756 scopus 로고
    • Filamentous phage morphogenetic signal sequence and orientation of DNA in the virion and gene V complex
    • Bauer M., Smith G.P. Filamentous phage morphogenetic signal sequence and orientation of DNA in the virion and gene V complex. Virology 1988, 167:166-175.
    • (1988) Virology , vol.167 , pp. 166-175
    • Bauer, M.1    Smith, G.P.2
  • 17
    • 0019439126 scopus 로고
    • Structural and functional evidence of cooperativity between membranes and cell wall in bacteria
    • Academic Press, New York, A.L. Muggleton-Harris (Ed.) Membrane Research. Classic Origins and Current Concepts
    • Bayer M.E. Structural and functional evidence of cooperativity between membranes and cell wall in bacteria. Int. Rev. Cytol. Suppl 1981, 12:39-70. Academic Press, New York. A.L. Muggleton-Harris (Ed.).
    • (1981) Int. Rev. Cytol. Suppl , vol.12 , pp. 39-70
    • Bayer, M.E.1
  • 18
    • 0022656413 scopus 로고
    • Effects of bacteriophage fd infection on Escherichiacoli HB11 envelope: a morphological and biochemical study
    • Bayer M.E., Bayer M.H. Effects of bacteriophage fd infection on Escherichiacoli HB11 envelope: a morphological and biochemical study. J.Virol. 1986, 57:258-266.
    • (1986) J.Virol. , vol.57 , pp. 258-266
    • Bayer, M.E.1    Bayer, M.H.2
  • 19
    • 0021847025 scopus 로고
    • Reconstitution of M13 bacteriophage coat protein. A new strategy to analyze configuration of the protein in the membrane
    • Bayer R., Feigenson G.W. Reconstitution of M13 bacteriophage coat protein. A new strategy to analyze configuration of the protein in the membrane. Biochim. Biophys. Acta 1985, 81:369-379.
    • (1985) Biochim. Biophys. Acta , vol.81 , pp. 369-379
    • Bayer, R.1    Feigenson, G.W.2
  • 21
    • 0029777441 scopus 로고    scopus 로고
    • Raman spectroscopy of the Ff gene V protein and complexes with poly(dA): nonspecific DNA recognition and binding
    • Benevides J.M., Terwilliger T.C., Vohnik S., Thomas G.J. Raman spectroscopy of the Ff gene V protein and complexes with poly(dA): nonspecific DNA recognition and binding. Biochemistry 1996, 35:9603-9609.
    • (1996) Biochemistry , vol.35 , pp. 9603-9609
    • Benevides, J.M.1    Terwilliger, T.C.2    Vohnik, S.3    Thomas, G.J.4
  • 22
    • 80051671357 scopus 로고    scopus 로고
    • Characterization of a dual-function domain that mediates membrane insertion and excision of Ff filamentous bacteriophage
    • Bennett N.J., Gagic D., Sutherland-Smith A.J., Rakonjac J. Characterization of a dual-function domain that mediates membrane insertion and excision of Ff filamentous bacteriophage. J.Mol. Biol. 2011, 411:972-985.
    • (2011) J.Mol. Biol. , vol.411 , pp. 972-985
    • Bennett, N.J.1    Gagic, D.2    Sutherland-Smith, A.J.3    Rakonjac, J.4
  • 23
    • 0024991453 scopus 로고
    • Parvovirus replication
    • Berns K.I. Parvovirus replication. Microbiol. Rev. 1990, 54:316-329.
    • (1990) Microbiol. Rev. , vol.54 , pp. 316-329
    • Berns, K.I.1
  • 25
    • 0026538698 scopus 로고
    • Structural polymorphism correlated to surface charge in filamentous bacteriophage
    • Bhattacharjee S., Glucksman M.J., Makowski L. Structural polymorphism correlated to surface charge in filamentous bacteriophage. Biophys. J. 1992, 61:725-735.
    • (1992) Biophys. J. , vol.61 , pp. 725-735
    • Bhattacharjee, S.1    Glucksman, M.J.2    Makowski, L.3
  • 27
    • 0033516702 scopus 로고    scopus 로고
    • Raman optical activity of filamentous bacteriophages: hydration of α-helices
    • Blanch E.W., Bell A.F., Hecht L., Day L.A., Barron L.D. Raman optical activity of filamentous bacteriophages: hydration of α-helices. J.Mol. Biol. 1999, 290:1-7.
    • (1999) J.Mol. Biol. , vol.290 , pp. 1-7
    • Blanch, E.W.1    Bell, A.F.2    Hecht, L.3    Day, L.A.4    Barron, L.D.5
  • 28
    • 0034827721 scopus 로고    scopus 로고
    • Tryptophan absolute stereochemistry in viral coat proteins from Raman optical activity
    • Blanch E.W., Hecht L., Day L.A., Pederson D.M., Barron L.D. Tryptophan absolute stereochemistry in viral coat proteins from Raman optical activity. J.Am. Chem. Soc. 2001, 123:4863-4864.
    • (2001) J.Am. Chem. Soc. , vol.123 , pp. 4863-4864
    • Blanch, E.W.1    Hecht, L.2    Day, L.A.3    Pederson, D.M.4    Barron, L.D.5
  • 29
    • 0025993884 scopus 로고
    • Physical properties of the fluid lipid-bilayer component of cell membranes: a perspective
    • Bloom M., Evans E., Mouritsen O.G. Physical properties of the fluid lipid-bilayer component of cell membranes: a perspective. Quart. Rev. Biophys. 1991, 24:293-397.
    • (1991) Quart. Rev. Biophys. , vol.24 , pp. 293-397
    • Bloom, M.1    Evans, E.2    Mouritsen, O.G.3
  • 30
    • 0035253862 scopus 로고    scopus 로고
    • Structure of the major single-stranded DNA-binding domain of replication protein A suggests a dynamic mechanism for DNA binding
    • Bochkareva E., Belegu V., Korolev S., Bochkarev A. Structure of the major single-stranded DNA-binding domain of replication protein A suggests a dynamic mechanism for DNA binding. EMBO J. 2001, 20:612-618.
    • (2001) EMBO J. , vol.20 , pp. 612-618
    • Bochkareva, E.1    Belegu, V.2    Korolev, S.3    Bochkarev, A.4
  • 31
    • 51649107357 scopus 로고    scopus 로고
    • To flip or not to flip: lipid-protein charge interactions are a determinant of final membrane protein topology
    • Bogdanov M., Xie J., Heacock P., Dowhan W. To flip or not to flip: lipid-protein charge interactions are a determinant of final membrane protein topology. J.Cell. Biol. 2008, 182:925-935.
    • (2008) J.Cell. Biol. , vol.182 , pp. 925-935
    • Bogdanov, M.1    Xie, J.2    Heacock, P.3    Dowhan, W.4
  • 32
    • 0032559425 scopus 로고    scopus 로고
    • Equilibrium and kinetic binding analysis of the N-terminal domain of the Pf1 gene 5 protein and its interaction with single-stranded DNA
    • Bogdarina I., Fox D.G., Kneale G.G. Equilibrium and kinetic binding analysis of the N-terminal domain of the Pf1 gene 5 protein and its interaction with single-stranded DNA. J.Mol. Biol. 1998, 275:443-452.
    • (1998) J.Mol. Biol. , vol.275 , pp. 443-452
    • Bogdarina, I.1    Fox, D.G.2    Kneale, G.G.3
  • 33
    • 0023755798 scopus 로고
    • Comparison of the dynamics of the membrane bound form of fd coat protein in micelles and in bilayers
    • Bogusky M.J., Leo G.C., Opella S.J. Comparison of the dynamics of the membrane bound form of fd coat protein in micelles and in bilayers. Proteins: Struct. Funct. Genet. 1988, 4:123-130.
    • (1988) Proteins: Struct. Funct. Genet. , vol.4 , pp. 123-130
    • Bogusky, M.J.1    Leo, G.C.2    Opella, S.J.3
  • 34
    • 0017133211 scopus 로고
    • DNA of minute virus of mice: self-priming, nonpermuted, single-stranded genome with a 5'-terminal hairpin duplex
    • Bourguignon G.J., Tattersall P.J., Ward D.C. DNA of minute virus of mice: self-priming, nonpermuted, single-stranded genome with a 5'-terminal hairpin duplex. J.Virol. 1976, 20:290-306.
    • (1976) J.Virol. , vol.20 , pp. 290-306
    • Bourguignon, G.J.1    Tattersall, P.J.2    Ward, D.C.3
  • 35
    • 79952399087 scopus 로고    scopus 로고
    • Beyond natural antibodies: the power of invitro display technologies
    • Bradbury A.R.M., Sidhu S., Dübel S., McCafferty J. Beyond natural antibodies: the power of invitro display technologies. Nat. Biotech. 2011, 29:245-254.
    • (2011) Nat. Biotech. , vol.29 , pp. 245-254
    • Bradbury, A.R.M.1    Sidhu, S.2    Dübel, S.3    McCafferty, J.4
  • 36
    • 33645028167 scopus 로고
    • The structure of some bacteriophages associated with male strains of Escherichia coli
    • Bradley D.E. The structure of some bacteriophages associated with male strains of Escherichia coli. J.Gen. Microbiol. 1964, 35:471-482.
    • (1964) J.Gen. Microbiol. , vol.35 , pp. 471-482
    • Bradley, D.E.1
  • 37
    • 0021104997 scopus 로고
    • Refined structure of the gene 5 DNA binding protein from bacteriophage fd
    • Brayer G.D., McPherson A. Refined structure of the gene 5 DNA binding protein from bacteriophage fd. J.Mol. Biol. 1983, 169:565-596.
    • (1983) J.Mol. Biol. , vol.169 , pp. 565-596
    • Brayer, G.D.1    McPherson, A.2
  • 40
    • 0031031841 scopus 로고    scopus 로고
    • Anatural longer glycine-rich region in IKe filamentous phage confers no selective advantage
    • Bruno R., Bradbury A. Anatural longer glycine-rich region in IKe filamentous phage confers no selective advantage. Gene 1997, 184:121-123.
    • (1997) Gene , vol.184 , pp. 121-123
    • Bruno, R.1    Bradbury, A.2
  • 41
    • 0343462480 scopus 로고
    • Maximum entropy in structural molecular biology: the fiber diffraction phase problem
    • D. Reidel Publishing Company, Dordrecht, C.R. Smith, G.J. Erickson (Eds.)
    • Bryan R.K. Maximum entropy in structural molecular biology: the fiber diffraction phase problem. Maximum-Entropy and Bayesian Spectral Analysis and Estimation Problems 1987, 207-228. D. Reidel Publishing Company, Dordrecht. C.R. Smith, G.J. Erickson (Eds.).
    • (1987) Maximum-Entropy and Bayesian Spectral Analysis and Estimation Problems , pp. 207-228
    • Bryan, R.K.1
  • 42
    • 0020805510 scopus 로고
    • Maximum-entropy calculation of the electron density at 4 Å resolution of Pf1 filamentous bacteriophage
    • Bryan R.K., Bansal M., Folkhard W., Nave C., Marvin D.A. Maximum-entropy calculation of the electron density at 4 Å resolution of Pf1 filamentous bacteriophage. Proc. Natl. Acad. Sci. U.S.A. 1983, 80:4728-4731.
    • (1983) Proc. Natl. Acad. Sci. U.S.A. , vol.80 , pp. 4728-4731
    • Bryan, R.K.1    Bansal, M.2    Folkhard, W.3    Nave, C.4    Marvin, D.A.5
  • 43
    • 0019230178 scopus 로고
    • 31P nuclear magnetic resonance and freeze-fracture electron microscopy studies on Escherichia coli. I. Cytoplasmic membrane and total phospholipids
    • 31P nuclear magnetic resonance and freeze-fracture electron microscopy studies on Escherichia coli. I. Cytoplasmic membrane and total phospholipids. Biochim. Biophys. Acta 1980, 597:492-501.
    • (1980) Biochim. Biophys. Acta , vol.597 , pp. 492-501
    • Burnell, E.1    van Alphen, L.2    Verkleij, A.3    de Kruijff, B.4
  • 44
    • 84858215567 scopus 로고    scopus 로고
    • Chaperone-usher pathways: diversity and pilus assembly mechanism
    • Busch A., Waksman G. Chaperone-usher pathways: diversity and pilus assembly mechanism. Phil. Trans. R. Soc. B 2012, 367:1112-1122.
    • (2012) Phil. Trans. R. Soc. B , vol.367 , pp. 1112-1122
    • Busch, A.1    Waksman, G.2
  • 45
    • 0023710642 scopus 로고
    • The 'molten globule' state is involved in the translocation of proteins across membranes?
    • Bychkova V.E., Pain R.H., Ptitsyn O.B. The 'molten globule' state is involved in the translocation of proteins across membranes?. FEBS Lett. 1988, 238:231-234.
    • (1988) FEBS Lett. , vol.238 , pp. 231-234
    • Bychkova, V.E.1    Pain, R.H.2    Ptitsyn, O.B.3
  • 47
    • 84872876822 scopus 로고    scopus 로고
    • Base composition and translational selection are insufficient to explain codon usage bias in plant viruses
    • Cardinale D.J., DeRosa D., Duffy S. Base composition and translational selection are insufficient to explain codon usage bias in plant viruses. Viruses 2013, 5:162-181.
    • (2013) Viruses , vol.5 , pp. 162-181
    • Cardinale, D.J.1    DeRosa, D.2    Duffy, S.3
  • 48
    • 0025917105 scopus 로고
    • The putative single-stranded DNA-binding protein of the filamentous bacteriophage, Ifl. Amino acid sequence of theprotein and structure of the gene
    • Carne A., Hill D.F., Stockwell P.A., Hughes G., Petersen G.B. The putative single-stranded DNA-binding protein of the filamentous bacteriophage, Ifl. Amino acid sequence of theprotein and structure of the gene. Proc. R. Soc. Lond. B 1991, 245:23-30.
    • (1991) Proc. R. Soc. Lond. B , vol.245 , pp. 23-30
    • Carne, A.1    Hill, D.F.2    Stockwell, P.A.3    Hughes, G.4    Petersen, G.B.5
  • 49
    • 0025975541 scopus 로고
    • Circular dichroism and fluorescence analysis of the interaction of Pfl gene 5 protein with poly dT
    • Carpenter M.L., Kneale G.G. Circular dichroism and fluorescence analysis of the interaction of Pfl gene 5 protein with poly dT. J.Mol. Biol. 1991, 217:681-689.
    • (1991) J.Mol. Biol. , vol.217 , pp. 681-689
    • Carpenter, M.L.1    Kneale, G.G.2
  • 50
    • 0021875052 scopus 로고
    • The precursor complex of Pf3 bacteriophage
    • Casadevall A., Day L.A. The precursor complex of Pf3 bacteriophage. Virology 1985, 145:260-272.
    • (1985) Virology , vol.145 , pp. 260-272
    • Casadevall, A.1    Day, L.A.2
  • 51
    • 0019887666 scopus 로고
    • The symmetries of filamentous phage particles
    • Caspar D.L., Makowski L. The symmetries of filamentous phage particles. J.Mol. Biol. 1981, 145:611-617.
    • (1981) J.Mol. Biol. , vol.145 , pp. 611-617
    • Caspar, D.L.1    Makowski, L.2
  • 52
    • 61549106933 scopus 로고    scopus 로고
    • Thermus thermophilus as biological model
    • Cava F., Hidalgo A., Berenguer J. Thermus thermophilus as biological model. Extremophiles 2009, 13:213-231.
    • (2009) Extremophiles , vol.13 , pp. 213-231
    • Cava, F.1    Hidalgo, A.2    Berenguer, J.3
  • 53
    • 34848842845 scopus 로고    scopus 로고
    • Geometry of nonbonded interactions involving planar groups in proteins
    • Chakrabarti P., Bhattacharyya R. Geometry of nonbonded interactions involving planar groups in proteins. Prog. Biophys. Mol. Biol. 2007, 95:83-137.
    • (2007) Prog. Biophys. Mol. Biol. , vol.95 , pp. 83-137
    • Chakrabarti, P.1    Bhattacharyya, R.2
  • 54
    • 0018122841 scopus 로고
    • Effect of membrane-associated f1 bacteriophage coat protein upon the activity of Escherichia coli phosphatidylserine synthetase
    • Chamberlain B.K., Webster R.E. Effect of membrane-associated f1 bacteriophage coat protein upon the activity of Escherichia coli phosphatidylserine synthetase. J.Bacteriol. 1978, 135:883-887.
    • (1978) J.Bacteriol. , vol.135 , pp. 883-887
    • Chamberlain, B.K.1    Webster, R.E.2
  • 55
    • 0032540092 scopus 로고    scopus 로고
    • Sequence analysis and expression of the filamentous phage φLf gene I encoding a 48-kDa protein associated with host cell membrane
    • Chang K.-H., Wen F.-S., Tseng T.-T., Lin N.-T., Yang M.-T., Tseng Y.-H. Sequence analysis and expression of the filamentous phage φLf gene I encoding a 48-kDa protein associated with host cell membrane. Biochem. Biophys. Res. Commun. 1998, 245:313-318.
    • (1998) Biochem. Biophys. Res. Commun. , vol.245 , pp. 313-318
    • Chang, K.-H.1    Wen, F.-S.2    Tseng, T.-T.3    Lin, N.-T.4    Yang, M.-T.5    Tseng, Y.-H.6
  • 57
    • 0030580355 scopus 로고    scopus 로고
    • Single-stranded DNA binding protein from bacteriophage cf: characterization, gene localization and protein-ssDNA complex
    • Chen W.P., Cheng C.M., Wang A.H., Kuo T.T. Single-stranded DNA binding protein from bacteriophage cf: characterization, gene localization and protein-ssDNA complex. Biochim. Biophys. Acta 1996, 1309:147-155.
    • (1996) Biochim. Biophys. Acta , vol.1309 , pp. 147-155
    • Chen, W.P.1    Cheng, C.M.2    Wang, A.H.3    Kuo, T.T.4
  • 58
    • 58949093974 scopus 로고    scopus 로고
    • Effect of membrane composition on antimicrobial peptides aurein 2.2 and 2.3 from Australian Southern Bell frogs
    • Cheng J.T.J., Hale J.D., Elliot M., Hancock R.E.W., Straus S.K. Effect of membrane composition on antimicrobial peptides aurein 2.2 and 2.3 from Australian Southern Bell frogs. Biophys. J. 2009, 96:552-565.
    • (2009) Biophys. J. , vol.96 , pp. 552-565
    • Cheng, J.T.J.1    Hale, J.D.2    Elliot, M.3    Hancock, R.E.W.4    Straus, S.K.5
  • 59
    • 78650624171 scopus 로고    scopus 로고
    • The importance of bacterial membrane composition in the structure and function of aurein 2.2 and selected variants
    • Cheng J.T.J., Hale J.D., Elliott M., Hancock R.E.W., Straus S.K. The importance of bacterial membrane composition in the structure and function of aurein 2.2 and selected variants. Biochim. Biophys. Acta Biomembranes 2011, 1808:622-633.
    • (2011) Biochim. Biophys. Acta Biomembranes , vol.1808 , pp. 622-633
    • Cheng, J.T.J.1    Hale, J.D.2    Elliott, M.3    Hancock, R.E.W.4    Straus, S.K.5
  • 60
    • 78349238929 scopus 로고    scopus 로고
    • Importance of residue 13 and the C-terminus for the structure and activity of the antimicrobial peptide aurein 2.2
    • Cheng J.T.J., Hale J.D., Kindrachuk J., Jessen H., Elliott M., Hancock R.E.W., Straus S.K. Importance of residue 13 and the C-terminus for the structure and activity of the antimicrobial peptide aurein 2.2. Biophys. J. 2010, 99:2926-2935.
    • (2010) Biophys. J. , vol.99 , pp. 2926-2935
    • Cheng, J.T.J.1    Hale, J.D.2    Kindrachuk, J.3    Jessen, H.4    Elliott, M.5    Hancock, R.E.W.6    Straus, S.K.7
  • 62
    • 0036203064 scopus 로고    scopus 로고
    • Filamentous phage active on the gram-positive bacterium Propionibacterium freuden- reichii
    • Chopin M.C., Rouault A., Ehrlich S.D., Gautier M. Filamentous phage active on the gram-positive bacterium Propionibacterium freuden- reichii. J.Bacteriol. 2002, 184:2030-2033.
    • (2002) J.Bacteriol. , vol.184 , pp. 2030-2033
    • Chopin, M.C.1    Rouault, A.2    Ehrlich, S.D.3    Gautier, M.4
  • 63
    • 0035965121 scopus 로고    scopus 로고
    • Zipper-like Watson-Crick base-pairs
    • Chou S.-H., Chin K.-H. Zipper-like Watson-Crick base-pairs. J.Mol. Biol. 2001, 312:753-768.
    • (2001) J.Mol. Biol. , vol.312 , pp. 753-768
    • Chou, S.-H.1    Chin, K.-H.2
  • 64
    • 77956943704 scopus 로고    scopus 로고
    • Insights into the infective properties of YpfΦ, the Yersinia pestis filamentous phage
    • Chouikha I., Charrier L., Filali S., Derbise A., Carniel E. Insights into the infective properties of YpfΦ, the Yersinia pestis filamentous phage. Virology 2010, 407:43-52.
    • (2010) Virology , vol.407 , pp. 43-52
    • Chouikha, I.1    Charrier, L.2    Filali, S.3    Derbise, A.4    Carniel, E.5
  • 65
    • 0026899228 scopus 로고
    • Flow linear dichroism spectra of four filamentous bacteriophages: DNA and coat protein contributions
    • Clack B.A., Gray D.M. Flow linear dichroism spectra of four filamentous bacteriophages: DNA and coat protein contributions. Biopolymers 1992, 32:795-810.
    • (1992) Biopolymers , vol.32 , pp. 795-810
    • Clack, B.A.1    Gray, D.M.2
  • 66
    • 0031894126 scopus 로고    scopus 로고
    • The TolQRA proteins are required for membrane insertion of the major capsid protein of the filamentous phage f1 during infection
    • Click E.M., Webster R.E. The TolQRA proteins are required for membrane insertion of the major capsid protein of the filamentous phage f1 during infection. J.Bacteriol. 1998, 180:1723-1728.
    • (1998) J.Bacteriol. , vol.180 , pp. 1723-1728
    • Click, E.M.1    Webster, R.E.2
  • 67
    • 0032517327 scopus 로고    scopus 로고
    • Measurement of residual dipolar couplings of macromolecules aligned in the nematic phase of a colloidal suspension of rod-shaped viruses
    • Clore G.M., Starich M.R., Gronenborn A.M. Measurement of residual dipolar couplings of macromolecules aligned in the nematic phase of a colloidal suspension of rod-shaped viruses. J.Am. Chem. Soc. 1998, 120:10571-10572.
    • (1998) J.Am. Chem. Soc. , vol.120 , pp. 10571-10572
    • Clore, G.M.1    Starich, M.R.2    Gronenborn, A.M.3
  • 68
    • 0023106948 scopus 로고
    • Dynamics of fd coat protein in the bacteriophage
    • Colnago L.A., Valentine K.G., Opella S.J. Dynamics of fd coat protein in the bacteriophage. Biochemistry 1987, 26:847-854.
    • (1987) Biochemistry , vol.26 , pp. 847-854
    • Colnago, L.A.1    Valentine, K.G.2    Opella, S.J.3
  • 69
    • 2442589577 scopus 로고    scopus 로고
    • Type IV pilus structure and bacterial pathogenicity
    • Craig L., Pique M.E., Tainer J.A. Type IV pilus structure and bacterial pathogenicity. Nat. Rev. Microbiol. 2004, 2:363-378.
    • (2004) Nat. Rev. Microbiol. , vol.2 , pp. 363-378
    • Craig, L.1    Pique, M.E.2    Tainer, J.A.3
  • 70
    • 0000920828 scopus 로고
    • The packing of α-helices: simple coiled-coils
    • Crick F.H.C. The packing of α-helices: simple coiled-coils. Acta Crystallogr. 1953, 6:689-697.
    • (1953) Acta Crystallogr. , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 72
    • 0019884742 scopus 로고
    • Hydrogen-1 and carbon-13 nuclear magnetic resonance of the aromatic residues of fd coat protein
    • Cross T.A., Opella S.J. Hydrogen-1 and carbon-13 nuclear magnetic resonance of the aromatic residues of fd coat protein. Biochemistry 1981, 20:290-297.
    • (1981) Biochemistry , vol.20 , pp. 290-297
    • Cross, T.A.1    Opella, S.J.2
  • 73
    • 0000397184 scopus 로고
    • Protein structure by solid-state NMR
    • Cross T.A., Opella S.J. Protein structure by solid-state NMR. J.Am. Chem. Soc. 1983, 105:306-308.
    • (1983) J.Am. Chem. Soc. , vol.105 , pp. 306-308
    • Cross, T.A.1    Opella, S.J.2
  • 74
    • 0022342799 scopus 로고
    • Protein structure by solid state nuclear magnetic resonance. Residues 40 to 45 of bacteriophage fd coat protein
    • Cross T.A., Opella S.J. Protein structure by solid state nuclear magnetic resonance. Residues 40 to 45 of bacteriophage fd coat protein. J.Mol. Biol. 1985, 182:367-381.
    • (1985) J.Mol. Biol. , vol.182 , pp. 367-381
    • Cross, T.A.1    Opella, S.J.2
  • 75
    • 0020639043 scopus 로고
    • Comparison of protein and DNA backbone structures in fd and Pf1 bacteriophages
    • Cross T.A., Tsang P., Opella S.J. Comparison of protein and DNA backbone structures in fd and Pf1 bacteriophages. Biochemistry 1983, 22:721-726.
    • (1983) Biochemistry , vol.22 , pp. 721-726
    • Cross, T.A.1    Tsang, P.2    Opella, S.J.3
  • 76
    • 0031567136 scopus 로고    scopus 로고
    • IKe and PulD: identification of a specificity domain
    • IKe and PulD: identification of a specificity domain. J.Mol. Biol. 1997, 266:978-992.
    • (1997) J.Mol. Biol. , vol.266 , pp. 978-992
    • Daefler, S.1    Russel, M.2    Model, P.3
  • 77
    • 4544233713 scopus 로고    scopus 로고
    • YidC family members are involved in the membrane insertion, lateral integration, folding, and assembly of membrane proteins
    • Dalbey R.E., Kuhn A. YidC family members are involved in the membrane insertion, lateral integration, folding, and assembly of membrane proteins. J.Cell. Biol. 2004, 166:769-774.
    • (2004) J.Cell. Biol. , vol.166 , pp. 769-774
    • Dalbey, R.E.1    Kuhn, A.2
  • 78
    • 84866912780 scopus 로고    scopus 로고
    • Protein traffic in Gram-negative bacteria - how exported and secreted proteins find their way
    • Dalbey R.E., Kuhn A. Protein traffic in Gram-negative bacteria - how exported and secreted proteins find their way. FEMS Microbiol. Rev. 2012, 36:1023-1045.
    • (2012) FEMS Microbiol. Rev. , vol.36 , pp. 1023-1045
    • Dalbey, R.E.1    Kuhn, A.2
  • 79
    • 79959435716 scopus 로고    scopus 로고
    • Assembly of bacterial inner membrane proteins
    • Dalbey R.E., Wang P., Kuhn A. Assembly of bacterial inner membrane proteins. Annu. Rev. Biochem. 2011, 80:161-187.
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 161-187
    • Dalbey, R.E.1    Wang, P.2    Kuhn, A.3
  • 80
    • 79960117044 scopus 로고    scopus 로고
    • Virus-templated self-assembled single-walled carbon nanotubes for highly efficient electron collection in photovoltaic devices
    • Dang X., Yi H., Ham M.H., Qi J., Yun D.S., Ladewski R., Strano M.S., Hammond P.T., Belcher A.M. Virus-templated self-assembled single-walled carbon nanotubes for highly efficient electron collection in photovoltaic devices. Nat. Nanotechnol. 2011, 6:377-384.
    • (2011) Nat. Nanotechnol. , vol.6 , pp. 377-384
    • Dang, X.1    Yi, H.2    Ham, M.H.3    Qi, J.4    Yun, D.S.5    Ladewski, R.6    Strano, M.S.7    Hammond, P.T.8    Belcher, A.M.9
  • 81
    • 0019050907 scopus 로고
    • Procoat, the precursor of M13 coat protein, requires an electrochemical potential for membrane insertion
    • Date T., Goodman J.M., Wickner W.T. Procoat, the precursor of M13 coat protein, requires an electrochemical potential for membrane insertion. Proc. Natl. Acad. Sci. U.S.A. 1980, 77:4669-4673.
    • (1980) Proc. Natl. Acad. Sci. U.S.A. , vol.77 , pp. 4669-4673
    • Date, T.1    Goodman, J.M.2    Wickner, W.T.3
  • 82
    • 0037325258 scopus 로고    scopus 로고
    • Filamentous phages linked to virulence of Vibrio cholerae
    • Davis B.M., Waldor M.K. Filamentous phages linked to virulence of Vibrio cholerae. Curr. Opin. Microbiol. 2003, 6:35-42.
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 35-42
    • Davis, B.M.1    Waldor, M.K.2
  • 83
    • 0028917692 scopus 로고
    • Comparison of Pf1 and fd gene 5proteins and their single-stranded DNA complexes by NMR spectroscopy and differential scanning calorimetry
    • Davis K.G., Plyte S.E., Robertson S.R., Cooper A., Kneale G.G. Comparison of Pf1 and fd gene 5proteins and their single-stranded DNA complexes by NMR spectroscopy and differential scanning calorimetry. Biochemistry 1995, 34:148-154.
    • (1995) Biochemistry , vol.34 , pp. 148-154
    • Davis, K.G.1    Plyte, S.E.2    Robertson, S.R.3    Cooper, A.4    Kneale, G.G.5
  • 84
    • 0013866084 scopus 로고
    • Protein conformation in fd bacteriophage as investigated by optical rotatory dispersion
    • Day L.A. Protein conformation in fd bacteriophage as investigated by optical rotatory dispersion. J.Mol. Biol. 1966, 15:395-398.
    • (1966) J.Mol. Biol. , vol.15 , pp. 395-398
    • Day, L.A.1
  • 85
    • 0018716751 scopus 로고
    • Structural models for DNA in filamentous viruses with phosphates near the center
    • Day L.A., Wiseman R.L., Marzec C.J. Structural models for DNA in filamentous viruses with phosphates near the center. Nuclear Acids Res. 1979, 7:1393-1403.
    • (1979) Nuclear Acids Res. , vol.7 , pp. 1393-1403
    • Day, L.A.1    Wiseman, R.L.2    Marzec, C.J.3
  • 87
    • 0036301383 scopus 로고    scopus 로고
    • Delineating the site of interaction on the pIII protein of filamentous bacteriophage fd with the F-pilus of Escherichia coli
    • Deng L.-W., Perham R.N. Delineating the site of interaction on the pIII protein of filamentous bacteriophage fd with the F-pilus of Escherichia coli. J.Mol. Biol. 2002, 319:603-614.
    • (2002) J.Mol. Biol. , vol.319 , pp. 603-614
    • Deng, L.-W.1    Perham, R.N.2
  • 88
    • 0014687173 scopus 로고
    • Altered coding in single stranded DNA viruses?
    • Denhardt D.T., Marvin D.A. Altered coding in single stranded DNA viruses?. Nature 1969, 221:769-770.
    • (1969) Nature , vol.221 , pp. 769-770
    • Denhardt, D.T.1    Marvin, D.A.2
  • 90
    • 0020005862 scopus 로고
    • 19F nuclear magnetic resonance studies of the coat protein of bacteriophage M13 in synthetic phospholipid vesicles and deoxycholate micelles
    • 19F nuclear magnetic resonance studies of the coat protein of bacteriophage M13 in synthetic phospholipid vesicles and deoxycholate micelles. Biophys. J. 1982, 37:243-251.
    • (1982) Biophys. J. , vol.37 , pp. 243-251
    • Dettman, H.D.1    Weiner, J.H.2    Sykes, B.D.3
  • 91
    • 77952474083 scopus 로고    scopus 로고
    • Phage display in molecular imaging and diagnosis of cancer
    • Deutscher S.L. Phage display in molecular imaging and diagnosis of cancer. Chem. Rev. 2010, 110:3196-3211.
    • (2010) Chem. Rev. , vol.110 , pp. 3196-3211
    • Deutscher, S.L.1
  • 92
    • 34249856814 scopus 로고    scopus 로고
    • DNA-nanotube-induced alignment of membrane proteins for NMR structure determination
    • Douglas S.M., Chou J.J., Shih W.M. DNA-nanotube-induced alignment of membrane proteins for NMR structure determination. Proc. Natl. Acad. Sci. U.S.A. 2007, 104:6644-6648.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 6644-6648
    • Douglas, S.M.1    Chou, J.J.2    Shih, W.M.3
  • 93
    • 79957459665 scopus 로고    scopus 로고
    • Lipid-protein interactions as determinants of membrane protein structure and function
    • Dowhan W., Bogdanov M. Lipid-protein interactions as determinants of membrane protein structure and function. Biochem. Soc. Trans. 2011, 39:767-774.
    • (2011) Biochem. Soc. Trans. , vol.39 , pp. 767-774
    • Dowhan, W.1    Bogdanov, M.2
  • 94
    • 0025938928 scopus 로고
    • Proposed molten globule intermediates in fd phage penetration and assembly
    • Dunker A.K., Ensign L.D., Arnold G.E., Roberts L.M. Proposed molten globule intermediates in fd phage penetration and assembly. FEBS Lett. 1991, 292:275-278.
    • (1991) FEBS Lett. , vol.292 , pp. 275-278
    • Dunker, A.K.1    Ensign, L.D.2    Arnold, G.E.3    Roberts, L.M.4
  • 95
    • 34548827056 scopus 로고    scopus 로고
    • Aconformational unfolding reaction activates phage fd for the infection of Escherichia coli
    • Eckert B., Schmid F.X. Aconformational unfolding reaction activates phage fd for the infection of Escherichia coli. J.Mol. Biol. 2007, 373:452-461.
    • (2007) J.Mol. Biol. , vol.373 , pp. 452-461
    • Eckert, B.1    Schmid, F.X.2
  • 96
    • 33845305513 scopus 로고    scopus 로고
    • The iterative helical real space reconstruction method: surmounting the problems posed by real polymers
    • Egelman E.H. The iterative helical real space reconstruction method: surmounting the problems posed by real polymers. J.Struct. Biol. 2007, 157:83-94.
    • (2007) J.Struct. Biol. , vol.157 , pp. 83-94
    • Egelman, E.H.1
  • 97
  • 98
    • 77952898456 scopus 로고    scopus 로고
    • Phase separation in biological membranes: integration of theory and experiment
    • Elson E.L., Fried E., Dolbow J.E., Genin G.M. Phase separation in biological membranes: integration of theory and experiment. Annu. Rev. Biophys. 2010, 39:207-226.
    • (2010) Annu. Rev. Biophys. , vol.39 , pp. 207-226
    • Elson, E.L.1    Fried, E.2    Dolbow, J.E.3    Genin, G.M.4
  • 99
    • 0029087064 scopus 로고
    • Location of filamentous phage minor coat proteins in phage and in infected cells
    • Endemann H., Model P. Location of filamentous phage minor coat proteins in phage and in infected cells. J.Mol. Biol. 1995, 250:496-506.
    • (1995) J.Mol. Biol. , vol.250 , pp. 496-506
    • Endemann, H.1    Model, P.2
  • 100
    • 0018197443 scopus 로고
    • Molecular weight determination by scanning transmission electron microscopy
    • Engel A. Molecular weight determination by scanning transmission electron microscopy. Ultramicroscopy 1978, 3:273-281.
    • (1978) Ultramicroscopy , vol.3 , pp. 273-281
    • Engel, A.1
  • 101
    • 34948877554 scopus 로고    scopus 로고
    • Bacterial lipid composition and the antimicrobial efficacy of cationic steroid compounds (Ceragenins)
    • Epand R.F., Savage P.B., Epand R.M. Bacterial lipid composition and the antimicrobial efficacy of cationic steroid compounds (Ceragenins). Biochim. Biophys. Acta 2007, 1768:2500-2509.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 2500-2509
    • Epand, R.F.1    Savage, P.B.2    Epand, R.M.3
  • 103
    • 0023196196 scopus 로고
    • Protein redistribution in model membranes: clearing of M13 coat protein from calcium-induced gel-phase regions in phosphatidylserine/phosphatidylcholine multilamellar vesicles
    • Florine K.I., Feigenson G.W. Protein redistribution in model membranes: clearing of M13 coat protein from calcium-induced gel-phase regions in phosphatidylserine/phosphatidylcholine multilamellar vesicles. Biochemistry 1987, 26:2978-2983.
    • (1987) Biochemistry , vol.26 , pp. 2978-2983
    • Florine, K.I.1    Feigenson, G.W.2
  • 104
    • 0028216128 scopus 로고
    • The solution structure of the Tyr41→His mutant of the single-stranded DNA binding protein encoded by gene V of the filamentous bacteriophage M13
    • Folkers P.J., Nilges M., Folmer R.H., Konings R.N., Hilbers C.W. The solution structure of the Tyr41→His mutant of the single-stranded DNA binding protein encoded by gene V of the filamentous bacteriophage M13. J.Mol. Biol. 1994, 236:229-246.
    • (1994) J.Mol. Biol. , vol.236 , pp. 229-246
    • Folkers, P.J.1    Nilges, M.2    Folmer, R.H.3    Konings, R.N.4    Hilbers, C.W.5
  • 105
    • 0028066921 scopus 로고
    • Amodel of the complex between single-stranded DNA and the single-stranded DNA binding protein encoded by gene V of filamentous bacteriophage M13
    • Folmer R.H.A., Nilges M., Folkers P.J.M., Konings R.N.H., Hilbers C.W. Amodel of the complex between single-stranded DNA and the single-stranded DNA binding protein encoded by gene V of filamentous bacteriophage M13. J.Mol. Biol. 1994, 240:341-357.
    • (1994) J.Mol. Biol. , vol.240 , pp. 341-357
    • Folmer, R.H.A.1    Nilges, M.2    Folkers, P.J.M.3    Konings, R.N.H.4    Hilbers, C.W.5
  • 106
    • 0030872558 scopus 로고    scopus 로고
    • Refined structure, DNA binding studies, and dynamics of the bacteriophage Pf3 encoded single-stranded DNA binding protein
    • Folmer R.H.A., Nilges M., Papavoine C.H.M., Harmsen B.J.M., Konings R.N.H., Hilbers C.W. Refined structure, DNA binding studies, and dynamics of the bacteriophage Pf3 encoded single-stranded DNA binding protein. Biochemistry 1997, 36:9120-9135.
    • (1997) Biochemistry , vol.36 , pp. 9120-9135
    • Folmer, R.H.A.1    Nilges, M.2    Papavoine, C.H.M.3    Harmsen, B.J.M.4    Konings, R.N.H.5    Hilbers, C.W.6
  • 107
    • 80052782538 scopus 로고    scopus 로고
    • Membrane localization of small proteins in Escherichia coli
    • Fontaine F., Fuchs R.T., Storz G. Membrane localization of small proteins in Escherichia coli. J.Biol. Chem. 2011, 286:32464-32474.
    • (2011) J.Biol. Chem. , vol.286 , pp. 32464-32474
    • Fontaine, F.1    Fuchs, R.T.2    Storz, G.3
  • 108
    • 84867780142 scopus 로고    scopus 로고
    • Crystal structures of a CTXφ pIII domain unbound and in complex with a Vibrio cholerae TolA domain reveal novel interaction interfaces
    • Ford C.G., Kolappan S., Phan H.T.H., Waldor M.K., Winther-Larsen H.C., Craig L. Crystal structures of a CTXφ pIII domain unbound and in complex with a Vibrio cholerae TolA domain reveal novel interaction interfaces. J.Biol. Chem. 2012, 287:36258-36272.
    • (2012) J.Biol. Chem. , vol.287 , pp. 36258-36272
    • Ford, C.G.1    Kolappan, S.2    Phan, H.T.H.3    Waldor, M.K.4    Winther-Larsen, H.C.5    Craig, L.6
  • 109
    • 0032704889 scopus 로고    scopus 로고
    • Conformational studies of the C-terminal domain of bacteriophage Pf1 gene 5 protein
    • Fox D.G., Cary P.D., Kneale G.G. Conformational studies of the C-terminal domain of bacteriophage Pf1 gene 5 protein. Biochim. Biophys. Acta 1999, 1435:138-146.
    • (1999) Biochim. Biophys. Acta , vol.1435 , pp. 138-146
    • Fox, D.G.1    Cary, P.D.2    Kneale, G.G.3
  • 110
    • 34447135010 scopus 로고    scopus 로고
    • Structural similarity of a membrane protein in micelles and membranes
    • Franzin C.M., Teriete P., Marassi F.M. Structural similarity of a membrane protein in micelles and membranes. J.Am. Chem. Soc. 2007, 129:8078-8079.
    • (2007) J.Am. Chem. Soc. , vol.129 , pp. 8078-8079
    • Franzin, C.M.1    Teriete, P.2    Marassi, F.M.3
  • 111
    • 33745942732 scopus 로고
    • Infra-red dichroism and protein structure
    • Fraser R.D.B., Price W.C. Infra-red dichroism and protein structure. Nature 1952, 170:490-491.
    • (1952) Nature , vol.170 , pp. 490-491
    • Fraser, R.D.B.1    Price, W.C.2
  • 112
    • 0037117459 scopus 로고    scopus 로고
    • Filamentous phage as vector-mediated antibodydelivery to the brain
    • Frenkel D., Solomon B. Filamentous phage as vector-mediated antibodydelivery to the brain. Proc. Natl. Acad. Sci. U.S.A. 2002, 99:5675-5679.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 5675-5679
    • Frenkel, D.1    Solomon, B.2
  • 113
    • 51049118119 scopus 로고    scopus 로고
    • Architectures and biogenesis of non-flagellar protein appendages in Gram-negative bacteria
    • Fronzes R., Remaut H., Waksman G. Architectures and biogenesis of non-flagellar protein appendages in Gram-negative bacteria. EMBO J. 2008, 27:2271-2280.
    • (2008) EMBO J. , vol.27 , pp. 2271-2280
    • Fronzes, R.1    Remaut, H.2    Waksman, G.3
  • 114
    • 0001367853 scopus 로고
    • Conjugative pill and pilus-specific phages
    • Plenum Press, New York, D.B. Clewell (Ed.)
    • Frost L.S. Conjugative pill and pilus-specific phages. Bacterial Conjugation 1993, 189-221. Plenum Press, New York. D.B. Clewell (Ed.).
    • (1993) Bacterial Conjugation , pp. 189-221
    • Frost, L.S.1
  • 115
    • 0034284537 scopus 로고    scopus 로고
    • Efficient phage display of polypeptides fused to the carboxy-terminus of the M13 gene-3 minor coat protein
    • Fuh G., Sidhu S.S. Efficient phage display of polypeptides fused to the carboxy-terminus of the M13 gene-3 minor coat protein. FEBS Lett. 2000, 480:231-234.
    • (2000) FEBS Lett. , vol.480 , pp. 231-234
    • Fuh, G.1    Sidhu, S.S.2
  • 116
    • 0028217913 scopus 로고
    • The adsorption protein of bacteriophage fd and its neighbour minor coat protein build a structural entity
    • Gailus V., Rasched I. The adsorption protein of bacteriophage fd and its neighbour minor coat protein build a structural entity. Eur. J. Biochem 1994, 222:927-931.
    • (1994) Eur. J. Biochem , vol.222 , pp. 927-931
    • Gailus, V.1    Rasched, I.2
  • 118
    • 0026638315 scopus 로고
    • Three dimensional structure of a cloning vector. X-ray diffraction studies of filamentous bacteriophage M13 at 7Å resolution
    • Glucksman M.J., Bhattacharjee S., Makowski L. Three dimensional structure of a cloning vector. X-ray diffraction studies of filamentous bacteriophage M13 at 7Å resolution. J.Mol. Biol. 1992, 226:455-470.
    • (1992) J.Mol. Biol. , vol.226 , pp. 455-470
    • Glucksman, M.J.1    Bhattacharjee, S.2    Makowski, L.3
  • 119
    • 33847628307 scopus 로고    scopus 로고
    • Filamentous phage studied by magic-angle spinning NMR: resonance assignment and secondary structure of the coat protein in Pf1
    • Goldbourt A., Gross B.J., Day L.A., McDermott A.E. Filamentous phage studied by magic-angle spinning NMR: resonance assignment and secondary structure of the coat protein in Pf1. J.Am. Chem. Soc. 2007, 129:2338-2344.
    • (2007) J.Am. Chem. Soc. , vol.129 , pp. 2338-2344
    • Goldbourt, A.1    Gross, B.J.2    Day, L.A.3    McDermott, A.E.4
  • 120
    • 78449261977 scopus 로고    scopus 로고
    • Intersubunit hydrophobic interactions in Pf1 filamentous phage
    • Goldbourt A., Day L.A., McDermott A.E. Intersubunit hydrophobic interactions in Pf1 filamentous phage. J.Biol. Chem. 2010, 285:37051-37059.
    • (2010) J.Biol. Chem. , vol.285 , pp. 37051-37059
    • Goldbourt, A.1    Day, L.A.2    McDermott, A.E.3
  • 121
    • 34547146401 scopus 로고    scopus 로고
    • The mechanism of Hsp70 chaperones: (entropic) pulling the models together
    • Goloubinoff P., De Los Rios P. The mechanism of Hsp70 chaperones: (entropic) pulling the models together. Trends Biochem. Sci. 2007, 32:372-380.
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 372-380
    • Goloubinoff, P.1    De Los Rios, P.2
  • 122
    • 84899074016 scopus 로고
    • Fibre diffraction studies on filamentous viruses
    • Clarendon Press, Oxford, B. Chance (Ed.)
    • Gonzalez A., Nave C., Marvin D.A. Fibre diffraction studies on filamentous viruses. Synchrotron Radiation in the Biosciences 1994, 530-535. Clarendon Press, Oxford. B. Chance (Ed.).
    • (1994) Synchrotron Radiation in the Biosciences , pp. 530-535
    • Gonzalez, A.1    Nave, C.2    Marvin, D.A.3
  • 123
    • 0000568172 scopus 로고
    • Pf1 filamentous bacteriophage: refinement of a molecular model by simulated annealing using 3.3Å resolution X-ray fibre diffraction data
    • Gonzalez A., Nave C., Marvin D.A. Pf1 filamentous bacteriophage: refinement of a molecular model by simulated annealing using 3.3Å resolution X-ray fibre diffraction data. Acta Crystallogr. Sect. D. 1995, 51:792-804.
    • (1995) Acta Crystallogr. Sect. D. , vol.51 , pp. 792-804
    • Gonzalez, A.1    Nave, C.2    Marvin, D.A.3
  • 124
    • 0024328846 scopus 로고
    • Three-dimensional structure of complexes of single-stranded DNA-binding proteins with DNA. IKe and fd gene 5 proteins form left-handed helices with single-stranded DNA
    • Gray C.W. Three-dimensional structure of complexes of single-stranded DNA-binding proteins with DNA. IKe and fd gene 5 proteins form left-handed helices with single-stranded DNA. J.Mol. Biol. 1989, 208:57-64.
    • (1989) J.Mol. Biol. , vol.208 , pp. 57-64
    • Gray, C.W.1
  • 125
    • 0019461994 scopus 로고
    • Adsorption complex of filamentous fd virus
    • Gray C.W., Brown R.S., Marvin D.A. Adsorption complex of filamentous fd virus. J.Mol. Biol. 1981, 146:621-627.
    • (1981) J.Mol. Biol. , vol.146 , pp. 621-627
    • Gray, C.W.1    Brown, R.S.2    Marvin, D.A.3
  • 126
    • 0020077958 scopus 로고
    • Anucleoprotein complex in bacteria infected with Pf1 filamentous virus: identification and electron microscopic analysis
    • Gray C.W., Kneale G.G., Leonard K.R., Siegrist H., Marvin D.A. Anucleoprotein complex in bacteria infected with Pf1 filamentous virus: identification and electron microscopic analysis. Virology 1982, 116:40-52.
    • (1982) Virology , vol.116 , pp. 40-52
    • Gray, C.W.1    Kneale, G.G.2    Leonard, K.R.3    Siegrist, H.4    Marvin, D.A.5
  • 127
    • 0019902758 scopus 로고
    • Neutron scattering data on reconstituted complexes of fd deoxyribonucleic acid and gene 5 protein show that the deoxyribonucleic acid is near the center
    • Gray D.M., Gray C.W., Carlson R.D. Neutron scattering data on reconstituted complexes of fd deoxyribonucleic acid and gene 5 protein show that the deoxyribonucleic acid is near the center. Biochemistry 1982, 21:2702-2713.
    • (1982) Biochemistry , vol.21 , pp. 2702-2713
    • Gray, D.M.1    Gray, C.W.2    Carlson, R.D.3
  • 128
    • 39749116244 scopus 로고    scopus 로고
    • Measured and calculated CD spectra of G-quartets stacked with the same or opposite polarities
    • Gray D.M., Wen J.-D., Gray C.W., Repges R., Repges C., Raabe G., Fleischhauer J. Measured and calculated CD spectra of G-quartets stacked with the same or opposite polarities. Chirality 2008, 20:431-440.
    • (2008) Chirality , vol.20 , pp. 431-440
    • Gray, D.M.1    Wen, J.-D.2    Gray, C.W.3    Repges, R.4    Repges, C.5    Raabe, G.6    Fleischhauer, J.7
  • 129
    • 0033302353 scopus 로고    scopus 로고
    • Expression of pattern in plants: combining molecular and calculus-based biophysical paradigms
    • Green P.B. Expression of pattern in plants: combining molecular and calculus-based biophysical paradigms. Am. J. Bot. 1999, 86:1059-1076.
    • (1999) Am. J. Bot. , vol.86 , pp. 1059-1076
    • Green, P.B.1
  • 130
    • 0026073776 scopus 로고
    • Regulation of filamentous bacteriophage length by modification of electrostatic interactions between coat protein and DNA
    • Greenwood J., Hunter G.J., Perham R.N. Regulation of filamentous bacteriophage length by modification of electrostatic interactions between coat protein and DNA. J.Mol. Biol. 1991, 217:223-227.
    • (1991) J.Mol. Biol. , vol.217 , pp. 223-227
    • Greenwood, J.1    Hunter, G.J.2    Perham, R.N.3
  • 131
    • 0024309086 scopus 로고
    • Dual importance of positive charge in the C-terminal region of filamentous bacteriophage coat protein for membrane insertion and DNA-protein interaction in virus assembly
    • Greenwood J., Perham R.N. Dual importance of positive charge in the C-terminal region of filamentous bacteriophage coat protein for membrane insertion and DNA-protein interaction in virus assembly. Virology 1989, 444-452.
    • (1989) Virology , pp. 444-452
    • Greenwood, J.1    Perham, R.N.2
  • 132
    • 0019474849 scopus 로고
    • Filamentous bacteriophage contract into hollow spherical particles upon exposure to a chloroform-water interface
    • Griffith J., Manning M., Dunn K. Filamentous bacteriophage contract into hollow spherical particles upon exposure to a chloroform-water interface. Cell 1981, 23:747-753.
    • (1981) Cell , vol.23 , pp. 747-753
    • Griffith, J.1    Manning, M.2    Dunn, K.3
  • 133
    • 0028334576 scopus 로고
    • Crystal structures of Y41H and Y41F mutants of gene V protein from Ff phage suggest possible protein-protein interactions in the GVP-ssDNA complex
    • Guan Y., Zhang H., Konings R.N.H., Hilbers C.W., Terwilliger T.C., Wang A.H.-J. Crystal structures of Y41H and Y41F mutants of gene V protein from Ff phage suggest possible protein-protein interactions in the GVP-ssDNA complex. Biochemistry 1994, 33:7768-7778.
    • (1994) Biochemistry , vol.33 , pp. 7768-7778
    • Guan, Y.1    Zhang, H.2    Konings, R.N.H.3    Hilbers, C.W.4    Terwilliger, T.C.5    Wang, A.H.-J.6
  • 134
    • 0028942225 scopus 로고
    • Electrostatic potential distribution of the gene V protein from Ff phage facilitates cooperative DNA binding: a model of the GVP-ssDNA complex
    • Guan Y., Zhang H., Wang A.H.-J. Electrostatic potential distribution of the gene V protein from Ff phage facilitates cooperative DNA binding: a model of the GVP-ssDNA complex. Prot. Sci. 1995, 4:187-197.
    • (1995) Prot. Sci. , vol.4 , pp. 187-197
    • Guan, Y.1    Zhang, H.2    Wang, A.H.-J.3
  • 135
    • 0026723972 scopus 로고
    • Membrane localization and topology of a viral assembly protein
    • Guy-Caffey J.K., Rapoza M.P., Jolley K.A., Webster R.E. Membrane localization and topology of a viral assembly protein. J.Bacteriol. 1992, 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
  • 136
    • 33746038138 scopus 로고    scopus 로고
    • Detection of a phage genome carrying a zonula occludens like toxin gene (zot) in clinical isolates of Stenotrophomonas maltophilia
    • Hagemann M., Hasse D., Berg G. Detection of a phage genome carrying a zonula occludens like toxin gene (zot) in clinical isolates of Stenotrophomonas maltophilia. Arch. Microbiol. 2006, 185:449-458.
    • (2006) Arch. Microbiol. , vol.185 , pp. 449-458
    • Hagemann, M.1    Hasse, D.2    Berg, G.3
  • 137
    • 0018072054 scopus 로고
    • Fluorotyrosine M13 coat protein: fluorine-19 nuclear magnetic resonance study of the motional properties of an integral membrane protein in phospholipid vesicles
    • Hagen D.S., Weiner J.H., Sykes B.D. Fluorotyrosine M13 coat protein: fluorine-19 nuclear magnetic resonance study of the motional properties of an integral membrane protein in phospholipid vesicles. Biochemistry 1978, 17:3860-3866.
    • (1978) Biochemistry , vol.17 , pp. 3860-3866
    • Hagen, D.S.1    Weiner, J.H.2    Sykes, B.D.3
  • 138
    • 0018791397 scopus 로고
    • Investigation of solvent accessibility of the fluorotyrosyl residues of M13 coat protein in deoxycholate micelles and phospholipid vesicles
    • Hagen D.S., Weiner J.H., Sykes B.D. Investigation of solvent accessibility of the fluorotyrosyl residues of M13 coat protein in deoxycholate micelles and phospholipid vesicles. Biochemistry 1979, 18:2007-2012.
    • (1979) Biochemistry , vol.18 , pp. 2007-2012
    • Hagen, D.S.1    Weiner, J.H.2    Sykes, B.D.3
  • 139
    • 0032577317 scopus 로고    scopus 로고
    • The major coat protein of filamentous bacteriophage f1 specifically pairs in the bacterial cytoplasmic membrane
    • Haigh N.G., Webster R.E. The major coat protein of filamentous bacteriophage f1 specifically pairs in the bacterial cytoplasmic membrane. J.Mol. Biol. 1998, 279:19-29.
    • (1998) J.Mol. Biol. , vol.279 , pp. 19-29
    • Haigh, N.G.1    Webster, R.E.2
  • 140
    • 0031760503 scopus 로고    scopus 로고
    • Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions
    • Hansen M.R., Mueller L., Pardi A. Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions. Nat. Struct. Biol. 1998, 5:1065-1074.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 1065-1074
    • Hansen, M.R.1    Mueller, L.2    Pardi, A.3
  • 141
    • 0037289729 scopus 로고    scopus 로고
    • CTX, a predicted CTXφminor coat protein, can expand the host range of coliphage fd to include Vibrio cholerae
    • CTX, a predicted CTXφminor coat protein, can expand the host range of coliphage fd to include Vibrio cholerae. J.Bacteriol. 2003, 185:1037-1044.
    • (2003) J.Bacteriol. , vol.185 , pp. 1037-1044
    • Heilpern, A.J.1    Waldor, M.K.2
  • 142
    • 84864805946 scopus 로고    scopus 로고
    • Physical properties of biological membranes
    • Wiley-VCH, H.G. Bohr (Ed.)
    • Heimburg T. Physical properties of biological membranes. Handbook of Molecular Biophysics 2009, 593-616. Wiley-VCH. H.G. Bohr (Ed.).
    • (2009) Handbook of Molecular Biophysics , pp. 593-616
    • Heimburg, T.1
  • 143
    • 56749151013 scopus 로고    scopus 로고
    • Small membrane proteins found by comparative genomics and ribosome binding site models
    • Hemm M.R., Paul B.J., Schneider T.D., Storz G., Rudd K.E. Small membrane proteins found by comparative genomics and ribosome binding site models. Mol. Microbiol. 2008, 70:1487-1501.
    • (2008) Mol. Microbiol. , vol.70 , pp. 1487-1501
    • Hemm, M.R.1    Paul, B.J.2    Schneider, T.D.3    Storz, G.4    Rudd, K.E.5
  • 145
    • 0025127567 scopus 로고
    • Structure and dynamics of detergent-solubilized M13 coat protein (an integral membrane protein) determined by 13C and 15N nuclear magnetic resonance spectroscopy
    • Henry G.D., Sykes B.D. Structure and dynamics of detergent-solubilized M13 coat protein (an integral membrane protein) determined by 13C and 15N nuclear magnetic resonance spectroscopy. Biochem. Cell Biol. 1990, 68:318-329.
    • (1990) Biochem. Cell Biol. , vol.68 , pp. 318-329
    • Henry, G.D.1    Sykes, B.D.2
  • 147
    • 0018834130 scopus 로고
    • Conversion of bacteriophage fd into an efficient single-stranded DNA vector system
    • Herrmann R., Neugebauer K., Pirkl E., Zentgraf H., Schaller H. Conversion of bacteriophage fd into an efficient single-stranded DNA vector system. Mol. Gen. Genet. 1980, 177:231-242.
    • (1980) Mol. Gen. Genet. , vol.177 , pp. 231-242
    • Herrmann, R.1    Neugebauer, K.2    Pirkl, E.3    Zentgraf, H.4    Schaller, H.5
  • 148
    • 0017819299 scopus 로고
    • Transposition of a DNA sequence determining kanamycin resistance into the single-stranded genome of bacteriophage fd
    • Herrmann R., Neugebauer K., Zentgraf H., Schaller H. Transposition of a DNA sequence determining kanamycin resistance into the single-stranded genome of bacteriophage fd. Mol. Gen. Genet. 1978, 159:171-178.
    • (1978) Mol. Gen. Genet. , vol.159 , pp. 171-178
    • Herrmann, R.1    Neugebauer, K.2    Zentgraf, H.3    Schaller, H.4
  • 149
    • 62449174500 scopus 로고    scopus 로고
    • General M13 phage display: M13 phage display in identification and characterization of protein-protein interactions
    • Hertveldt K., Beliën T., Volckaert G. General M13 phage display: M13 phage display in identification and characterization of protein-protein interactions. Methods Mol. Biol. 2009, 502:321-339.
    • (2009) Methods Mol. Biol. , vol.502 , pp. 321-339
    • Hertveldt, K.1    Beliën, T.2    Volckaert, G.3
  • 152
    • 0019170720 scopus 로고
    • Calorimetric, density and circular dichroism studies of the reversible structural transition in Pf1 filamentous bacterial virus
    • Hinz H.-J., Greulich K.O., Ludwig H., Marvin D.A. Calorimetric, density and circular dichroism studies of the reversible structural transition in Pf1 filamentous bacterial virus. J.Mol. Biol. 1980, 144:281-289.
    • (1980) J.Mol. Biol. , vol.144 , pp. 281-289
    • Hinz, H.-J.1    Greulich, K.O.2    Ludwig, H.3    Marvin, D.A.4
  • 153
    • 78651122018 scopus 로고
    • Ein fädiger DNS-Phage (fd) und ein sphärischer RNS-Phage (fr) wirtsspezifisch fur männliche Stämme von E.coli. III. Biologisches Verhalten von fd und fr
    • Hoffmann-Berling H., Dürwald H., Beulke I. Ein fädiger DNS-Phage (fd) und ein sphärischer RNS-Phage (fr) wirtsspezifisch fur männliche Stämme von E.coli. III. Biologisches Verhalten von fd und fr. Zeit. Naturforsch. B 1963, 18:893-898.
    • (1963) Zeit. Naturforsch. B , vol.18 , pp. 893-898
    • Hoffmann-Berling, H.1    Dürwald, H.2    Beulke, I.3
  • 154
    • 0001278901 scopus 로고
    • Release of male-specific bacteriophages from surviving host bacteria
    • Hoffmann-Berling H., Mazé R. Release of male-specific bacteriophages from surviving host bacteria. Virology 1964, 22:305-313.
    • (1964) Virology , vol.22 , pp. 305-313
    • Hoffmann-Berling, H.1    Mazé, R.2
  • 156
    • 84941612047 scopus 로고
    • Untersuchungen über "kleine" E.coli K12 Bacteriophagen
    • Hofschneider P.H. Untersuchungen über "kleine" E.coli K12 Bacteriophagen. Zeit. Naturforsch. B 1963, 18:203-205.
    • (1963) Zeit. Naturforsch. B , vol.18 , pp. 203-205
    • Hofschneider, P.H.1
  • 157
    • 31944445169 scopus 로고    scopus 로고
    • Identification and specificity of pilus adsorption proteins of filamentous bacteriophages infecting Pseudomonas aeruginosa
    • Holland S.J., Sanz C., Perham R.N. Identification and specificity of pilus adsorption proteins of filamentous bacteriophages infecting Pseudomonas aeruginosa. Virology 2006, 345:540-548.
    • (2006) Virology , vol.345 , pp. 540-548
    • Holland, S.J.1    Sanz, C.2    Perham, R.N.3
  • 158
    • 0031568809 scopus 로고    scopus 로고
    • Aconserved infection pathway for filamentous bacteriophages is suggested by the structure of the membrane penetration domain of the minor coat protein gp3 from phage fd
    • Holliger P., Riechmann L. Aconserved infection pathway for filamentous bacteriophages is suggested by the structure of the membrane penetration domain of the minor coat protein gp3 from phage fd. Structure 1997, 5:265-275.
    • (1997) Structure , vol.5 , pp. 265-275
    • Holliger, P.1    Riechmann, L.2
  • 159
    • 0033010511 scopus 로고    scopus 로고
    • Crystal structure of the two N-terminal domains of g3p from filamentous phage fd at 1.9Å. Evidence for conformational lability
    • Holliger P., Riechmann L., Williams R.L. Crystal structure of the two N-terminal domains of g3p from filamentous phage fd at 1.9Å. Evidence for conformational lability. J.Mol. Biol. 1999, 288:649-657.
    • (1999) J.Mol. Biol. , vol.288 , pp. 649-657
    • Holliger, P.1    Riechmann, L.2    Williams, R.L.3
  • 160
    • 77952093470 scopus 로고    scopus 로고
    • Orientation and dynamics of transmembrane peptides: the power of simple models
    • Holt A., Killian J.A. Orientation and dynamics of transmembrane peptides: the power of simple models. Eur. Biophys. J. 2010, 39:609-621.
    • (2010) Eur. Biophys. J. , vol.39 , pp. 609-621
    • Holt, A.1    Killian, J.A.2
  • 161
    • 0033515432 scopus 로고    scopus 로고
    • Functionally important correlated motions in the single-stranded DNA-binding protein encoded by filamentous phage Pf3
    • Horstink L.M., Abseher R., Nilges M., Hilbers C.W. Functionally important correlated motions in the single-stranded DNA-binding protein encoded by filamentous phage Pf3. J.Mol. Biol. 1999, 287:569-577.
    • (1999) J.Mol. Biol. , vol.287 , pp. 569-577
    • Horstink, L.M.1    Abseher, R.2    Nilges, M.3    Hilbers, C.W.4
  • 162
    • 11144349743 scopus 로고    scopus 로고
    • Protein-lipid interactions of bacteriophage M13 gene 9 minor coat protein
    • Houbiers M.C., Hemminga M.A. Protein-lipid interactions of bacteriophage M13 gene 9 minor coat protein. Mol. Membr. Biol. 2004, 21:351-359.
    • (2004) Mol. Membr. Biol. , vol.21 , pp. 351-359
    • Houbiers, M.C.1    Hemminga, M.A.2
  • 164
  • 165
    • 0023661694 scopus 로고
    • Interactions between DNA and coat protein in the structure and assembly of filamentous bacteriophage fd
    • Hunter G.J., Rowitch D.H., Perham R.N. Interactions between DNA and coat protein in the structure and assembly of filamentous bacteriophage fd. Nature 1987, 327:252-254.
    • (1987) Nature , vol.327 , pp. 252-254
    • Hunter, G.J.1    Rowitch, D.H.2    Perham, R.N.3
  • 166
    • 79952149017 scopus 로고    scopus 로고
    • The evolution of the phage shock protein response system: interplay between protein function, genomic organization, and system function
    • Huvet M., Toni T., Sheng X., Thorne T., Jovanovic G., Engl C., Buck M., Pinney J.W., Stumpf M.P.H. The evolution of the phage shock protein response system: interplay between protein function, genomic organization, and system function. Mol. Biol. Evol. 2011, 28:1141-1155.
    • (2011) Mol. Biol. Evol. , vol.28 , pp. 1141-1155
    • Huvet, M.1    Toni, T.2    Sheng, X.3    Thorne, T.4    Jovanovic, G.5    Engl, C.6    Buck, M.7    Pinney, J.W.8    Stumpf, M.P.H.9
  • 167
    • 79953899813 scopus 로고    scopus 로고
    • Substrate-dependent conformational dynamics of the Escherichia coli membrane insertaseYidC
    • Imhof N., Kuhn A., Gerken U. Substrate-dependent conformational dynamics of the Escherichia coli membrane insertaseYidC. Biochemistry 2011, 50:3229-3239.
    • (2011) Biochemistry , vol.50 , pp. 3229-3239
    • Imhof, N.1    Kuhn, A.2    Gerken, U.3
  • 168
    • 0015414934 scopus 로고
    • Role of the F-pili in the penetration of bacteriophage f1
    • Jacobson A. Role of the F-pili in the penetration of bacteriophage f1. J.Virol. 1972, 10:835-843.
    • (1972) J.Virol. , vol.10 , pp. 835-843
    • Jacobson, A.1
  • 171
    • 0015545389 scopus 로고
    • Acoat protein of the bacteriophage M13 virion participates in membrane-oriented synthesis of DNA
    • Jazwinski S.M., Marco R., Kornberg A. Acoat protein of the bacteriophage M13 virion participates in membrane-oriented synthesis of DNA. Proc. Nat. Acad. Sci. U.S.A. 1973, 70:205-209.
    • (1973) Proc. Nat. Acad. Sci. U.S.A. , vol.70 , pp. 205-209
    • Jazwinski, S.M.1    Marco, R.2    Kornberg, A.3
  • 172
    • 0029021730 scopus 로고
    • Phyllotaxis: the status of the field
    • Jean R.V. Phyllotaxis: the status of the field. Math. Biosci 1995, 127:181-206.
    • (1995) Math. Biosci , vol.127 , pp. 181-206
    • Jean, R.V.1
  • 173
    • 77957882515 scopus 로고    scopus 로고
    • Properties of the phage-shock-protein (Psp) regulatory complex that govern signal transductionand induction of the Psp response in Escherichia coli
    • Jovanovic G., Engl C., Mayhew A.J., Burrows P.C., Buck M. Properties of the phage-shock-protein (Psp) regulatory complex that govern signal transductionand induction of the Psp response in Escherichia coli. Microbiology 2010, 156:2920-2932.
    • (2010) Microbiology , vol.156 , pp. 2920-2932
    • Jovanovic, G.1    Engl, C.2    Mayhew, A.J.3    Burrows, P.C.4    Buck, M.5
  • 175
    • 34547767054 scopus 로고    scopus 로고
    • Genomic characterization of the filamentous integrative bacteriophages φRSS1 and φRSM1, which infect Ralstonia solanacearum
    • Kawasaki T., Nagata S., Fujiwara A., Satsuma H., Fujie M., Usami S., Yamada T. Genomic characterization of the filamentous integrative bacteriophages φRSS1 and φRSM1, which infect Ralstonia solanacearum. J.Bacteriol. 2007, 189:5792-5802.
    • (2007) J.Bacteriol. , vol.189 , pp. 5792-5802
    • Kawasaki, T.1    Nagata, S.2    Fujiwara, A.3    Satsuma, H.4    Fujie, M.5    Usami, S.6    Yamada, T.7
  • 176
    • 28444488346 scopus 로고    scopus 로고
    • Filamentous phage display in the new millennium
    • Kehoe J.W., Kay B.K. Filamentous phage display in the new millennium. Chem. Rev. 2005, 105:4056-4072.
    • (2005) Chem. Rev. , vol.105 , pp. 4056-4072
    • Kehoe, J.W.1    Kay, B.K.2
  • 178
    • 0028980923 scopus 로고
    • Accessibility and dynamics of cys residues in bacteriophage IKe and M13 major coat protein mutants
    • Khan A.R., Williams K.A., Boggs J.M., Deber C.M. Accessibility and dynamics of cys residues in bacteriophage IKe and M13 major coat protein mutants. Biochemistry 1995, 34:12388-12397.
    • (1995) Biochemistry , vol.34 , pp. 12388-12397
    • Khan, A.R.1    Williams, K.A.2    Boggs, J.M.3    Deber, C.M.4
  • 179
    • 0033571246 scopus 로고    scopus 로고
    • Hydrophobic forces drive spontaneous membrane insertion of the bacteriophage Pf3 coat protein without topological control
    • Kiefer D., Kuhn A. Hydrophobic forces drive spontaneous membrane insertion of the bacteriophage Pf3 coat protein without topological control. EMBO J. 1999, 18:6299-6306.
    • (1999) EMBO J. , vol.18 , pp. 6299-6306
    • Kiefer, D.1    Kuhn, A.2
  • 180
    • 0036787577 scopus 로고    scopus 로고
    • Uniformity, ideality and hydrogen bonds in transmembrane α-helices
    • Kim S., Cross T.A. Uniformity, ideality and hydrogen bonds in transmembrane α-helices. Biophys. J. 2002, 83:2084-2095.
    • (2002) Biophys. J. , vol.83 , pp. 2084-2095
    • Kim, S.1    Cross, T.A.2
  • 181
    • 0037076540 scopus 로고    scopus 로고
    • GXXXG and AXXXA: common α-helical interaction motifs in proteins, particularly in extremophiles
    • Kleiger G., Grothe R., Mallick P., Eisenberg D. GXXXG and AXXXA: common α-helical interaction motifs in proteins, particularly in extremophiles. Biochemistry 2002, 41:5990-5997.
    • (2002) Biochemistry , vol.41 , pp. 5990-5997
    • Kleiger, G.1    Grothe, R.2    Mallick, P.3    Eisenberg, D.4
  • 182
    • 56649088137 scopus 로고    scopus 로고
    • The Pf3 coat protein contacts TM1 and TM3 of YidC during membrane biogenesis
    • Klenner C., Yuan J., Dalbey R.E., Kuhn A. The Pf3 coat protein contacts TM1 and TM3 of YidC during membrane biogenesis. FEBS Lett. 2008, 582:3967-3972.
    • (2008) FEBS Lett. , vol.582 , pp. 3967-3972
    • Klenner, C.1    Yuan, J.2    Dalbey, R.E.3    Kuhn, A.4
  • 184
    • 0020074873 scopus 로고
    • Pf1 bacteriophage replication-assembly complex. X-ray fibre diffraction and scanning transmission electron microscopy
    • Kneale G.G., Freeman R., Marvin D.A. Pf1 bacteriophage replication-assembly complex. X-ray fibre diffraction and scanning transmission electron microscopy. J.Mol. Biol. 1982, 156:279-292.
    • (1982) J.Mol. Biol. , vol.156 , pp. 279-292
    • Kneale, G.G.1    Freeman, R.2    Marvin, D.A.3
  • 185
    • 0021095915 scopus 로고
    • Pf1 bacteriophage replication-assembly complex. X-ray fibre diffraction of the high humidity form
    • Kneale G.G., Marvin D.A. Pf1 bacteriophage replication-assembly complex. X-ray fibre diffraction of the high humidity form. J.Mol. Biol. 1983, 171:229-232.
    • (1983) J.Mol. Biol. , vol.171 , pp. 229-232
    • Kneale, G.G.1    Marvin, D.A.2
  • 186
    • 0025955259 scopus 로고
    • Structural parameters of the Pf1gene 5 protein-DNA complex in solution by neutron scattering
    • Kneale G.G., Plyte S.E., Timmins P. Structural parameters of the Pf1gene 5 protein-DNA complex in solution by neutron scattering. J.Mol. Biol. 1991, 221:755-759.
    • (1991) J.Mol. Biol. , vol.221 , pp. 755-759
    • Kneale, G.G.1    Plyte, S.E.2    Timmins, P.3
  • 187
    • 71849084758 scopus 로고    scopus 로고
    • Electrostatics and optimal arrangement of ionic triangular lattices confined to cylindrical fibers
    • Kohlstedt K.L., Vernizzi G., Olvera de la Cruz M. Electrostatics and optimal arrangement of ionic triangular lattices confined to cylindrical fibers. Phys. Rev. E 2009, 80:051503.
    • (2009) Phys. Rev. E , vol.80 , pp. 051503
    • Kohlstedt, K.L.1    Vernizzi, G.2    Olvera de la Cruz, M.3
  • 188
    • 57649119791 scopus 로고    scopus 로고
    • Mechanisms of YidC-mediated insertion and assembly of multimeric membrane protein complexes
    • Kol S., Nouwen N., Driessen A.J. Mechanisms of YidC-mediated insertion and assembly of multimeric membrane protein complexes. J.Biol. Chem. 2008, 283:31269-31273.
    • (2008) J.Biol. Chem. , vol.283 , pp. 31269-31273
    • Kol, S.1    Nouwen, N.2    Driessen, A.J.3
  • 189
    • 33847272113 scopus 로고    scopus 로고
    • Molecular motors: a theorist's perspective
    • Kolomeisky A.B., Fisher M. Molecular motors: a theorist's perspective. Annu. Rev. Phys. Chem. 2007, 58:675-695.
    • (2007) Annu. Rev. Phys. Chem. , vol.58 , pp. 675-695
    • Kolomeisky, A.B.1    Fisher, M.2
  • 190
    • 0029164949 scopus 로고
    • Three-dimensional structure of the single-stranded DNA-binding protein encoded by gene V of the filamentous bacteriophage M13 and a model of its complex with single-stranded DNA
    • Konings R.N.H., Folmer R.H.A., Folkers P.J.M., Nilges M., Hilbers C.W. Three-dimensional structure of the single-stranded DNA-binding protein encoded by gene V of the filamentous bacteriophage M13 and a model of its complex with single-stranded DNA. FEMS Microbiol. Rev. 1995, 17:57-72.
    • (1995) FEMS Microbiol. Rev. , vol.17 , pp. 57-72
    • Konings, R.N.H.1    Folmer, R.H.A.2    Folkers, P.J.M.3    Nilges, M.4    Hilbers, C.W.5
  • 191
    • 0028213921 scopus 로고
    • Ultraviolet absorbance and circular dichroism of Pf1 virus: nucleotide/subunit ratio of unity, hyperchromic tyrosines and DNA bases, and high helicity in the subunits
    • Kostrikis L.G., Liu D.J., Day L.A. Ultraviolet absorbance and circular dichroism of Pf1 virus: nucleotide/subunit ratio of unity, hyperchromic tyrosines and DNA bases, and high helicity in the subunits. Biochemistry 1994, 33:1694-1703.
    • (1994) Biochemistry , vol.33 , pp. 1694-1703
    • Kostrikis, L.G.1    Liu, D.J.2    Day, L.A.3
  • 192
    • 0028138294 scopus 로고
    • The adsorption protein of filamentous phage fd: assignment of its disulfide bridges and identification of the domain incorporated in the coat
    • Kremser A., Rasched I. The adsorption protein of filamentous phage fd: assignment of its disulfide bridges and identification of the domain incorporated in the coat. Biochemistry 1994, 33:13954-13958.
    • (1994) Biochemistry , vol.33 , pp. 13954-13958
    • Kremser, A.1    Rasched, I.2
  • 193
    • 0023280757 scopus 로고
    • Integration of the DNA of filamentous bacteriophage Cf1t into the chromosomal DNA of its host
    • Kuo T.T., Chao Y.S., Lin Y.H., Lin B.Y., Liu L.F., Feng T.Y. Integration of the DNA of filamentous bacteriophage Cf1t into the chromosomal DNA of its host. J.Virol. 1987, 61:60-65.
    • (1987) J.Virol. , vol.61 , pp. 60-65
    • Kuo, T.T.1    Chao, Y.S.2    Lin, Y.H.3    Lin, B.Y.4    Liu, L.F.5    Feng, T.Y.6
  • 194
    • 0023141115 scopus 로고
    • The lysogenic cycle of the filamentous phage Cf1t from Xanthomonas campestris pv.citri
    • Kuo T.T., Lin Y.H., Huang C.M., Chang S.F., Dai H., Feng T.Y. The lysogenic cycle of the filamentous phage Cf1t from Xanthomonas campestris pv.citri. Virology 1987, 156:305-312.
    • (1987) Virology , vol.156 , pp. 305-312
    • Kuo, T.T.1    Lin, Y.H.2    Huang, C.M.3    Chang, S.F.4    Dai, H.5    Feng, T.Y.6
  • 195
    • 0025782871 scopus 로고
    • Complete nucleotide sequence of filamentous phage Cf1c from Xanthomonas campestris pv. citri
    • Kuo T.T., Tan M.S., Su M.T., Yang M.K. Complete nucleotide sequence of filamentous phage Cf1c from Xanthomonas campestris pv. citri. Nuclear Acids Res. 1991, 19:2498.
    • (1991) Nuclear Acids Res. , vol.19 , pp. 2498
    • Kuo, T.T.1    Tan, M.S.2    Su, M.T.3    Yang, M.K.4
  • 196
    • 0029151113 scopus 로고
    • Colicin import and pore formation: a system for studying protein transport across membranes?
    • Lazdunski C.J. Colicin import and pore formation: a system for studying protein transport across membranes?. Mol. Microbiol. 1995, 16:1059-1066.
    • (1995) Mol. Microbiol. , vol.16 , pp. 1059-1066
    • Lazdunski, C.J.1
  • 198
    • 0032906548 scopus 로고    scopus 로고
    • The adsorption protein genes of Xanthomonas campestris filamentous phages determining host specificity
    • Lin N.-T., Liu T.-J., Lee T.-C., You B.-Y., Yang M.-H., Wen F.-S., Tseng Y.-H. The adsorption protein genes of Xanthomonas campestris filamentous phages determining host specificity. J.Bacteriol. 1999, 181:2465-2471.
    • (1999) J.Bacteriol. , vol.181 , pp. 2465-2471
    • Lin, N.-T.1    Liu, T.-J.2    Lee, T.-C.3    You, B.-Y.4    Yang, M.-H.5    Wen, F.-S.6    Tseng, Y.-H.7
  • 199
    • 0029875905 scopus 로고    scopus 로고
    • Essential role of a sodium dodecyl sulfate-resistant protein IV multimer in assembly-export of filamentous phage
    • Linderoth N.A., Model P., Russel M. Essential role of a sodium dodecyl sulfate-resistant protein IV multimer in assembly-export of filamentous phage. J.Bacteriol. 1996, 178:1962-1970.
    • (1996) J.Bacteriol. , vol.178 , pp. 1962-1970
    • Linderoth, N.A.1    Model, P.2    Russel, M.3
  • 200
    • 0028108799 scopus 로고
    • Pf1 virus structure: helical coat protein and DNA with paraxial phosphates
    • Liu D.J., Day L.A. Pf1 virus structure: helical coat protein and DNA with paraxial phosphates. Science 1994, 265:671-674.
    • (1994) Science , vol.265 , pp. 671-674
    • Liu, D.J.1    Day, L.A.2
  • 203
    • 33744490360 scopus 로고    scopus 로고
    • Positioning of proteins in membranes: a computational approach
    • Lomize A.L., Pogozheva I.D., Lomize M.A., Mosberg H.I. Positioning of proteins in membranes: a computational approach. Protein Sci. 2006, 15:1318-1333.
    • (2006) Protein Sci. , vol.15 , pp. 1318-1333
    • Lomize, A.L.1    Pogozheva, I.D.2    Lomize, M.A.3    Mosberg, H.I.4
  • 204
    • 79955409906 scopus 로고    scopus 로고
    • Anisotropic solvent model of the lipid bilayer. 2. Energetics of insertion of small molecules, peptides, and proteins in membranes
    • Lomize A.L., Pogozheva I.D., Mosberg H.I. Anisotropic solvent model of the lipid bilayer. 2. Energetics of insertion of small molecules, peptides, and proteins in membranes. J.Chem. Inf. Model 2011, 51:930-946.
    • (2011) J.Chem. Inf. Model , vol.51 , pp. 930-946
    • Lomize, A.L.1    Pogozheva, I.D.2    Mosberg, H.I.3
  • 205
    • 84861060898 scopus 로고    scopus 로고
    • OPM database and PPM web server: resources for positioning of proteins in membranes
    • Lomize M.A., Pogozheva I.D., Joo H., Mosberg H.I., Lomize A.L. OPM database and PPM web server: resources for positioning of proteins in membranes. Nucleic Acids Res. 2012, 40(Database issue):D370-D376.
    • (2012) Nucleic Acids Res. , vol.40 , Issue.DATABASE ISSUE
    • Lomize, M.A.1    Pogozheva, I.D.2    Joo, H.3    Mosberg, H.I.4    Lomize, A.L.5
  • 206
    • 0020075898 scopus 로고
    • Minor coat protein composition and location of the A protein in bacteriophage spheroids and I-forms
    • Lopez J., Webster R.E. Minor coat protein composition and location of the A protein in bacteriophage spheroids and I-forms. J.Virol. 1982, 42:1099-1107.
    • (1982) J.Virol. , vol.42 , pp. 1099-1107
    • Lopez, J.1    Webster, R.E.2
  • 207
    • 0020619299 scopus 로고
    • Morphogenesis of filamentous bacteriophage f1: orientation of extrusion and production of polyphage
    • Lopez J., Webster R.E. Morphogenesis of filamentous bacteriophage f1: orientation of extrusion and production of polyphage. Virology 1983, 127:177-193.
    • (1983) Virology , vol.127 , pp. 177-193
    • Lopez, J.1    Webster, R.E.2
  • 208
    • 0022362701 scopus 로고
    • Assembly site of bacteriophage f1 corresponds to adhesion zones between the inner and outer membranes of the host cell
    • Lopez J., Webster R.E. Assembly site of bacteriophage f1 corresponds to adhesion zones between the inner and outer membranes of the host cell. J.Bacteriol. 1985, 163:1270-1274.
    • (1985) J.Bacteriol. , vol.163 , pp. 1270-1274
    • Lopez, J.1    Webster, R.E.2
  • 209
    • 79251596373 scopus 로고    scopus 로고
    • The filamentous phages fd and If1 use different mechanisms to infect Escherichia coli
    • Lorenz S.H., Jakob R.P., Weininger U., Balbach J., Dobbek H., Schmid F.X. The filamentous phages fd and If1 use different mechanisms to infect Escherichia coli. J.Mol. Biol. 2011, 405:989-1003.
    • (2011) J.Mol. Biol. , vol.405 , pp. 989-1003
    • Lorenz, S.H.1    Jakob, R.P.2    Weininger, U.3    Balbach, J.4    Dobbek, H.5    Schmid, F.X.6
  • 210
    • 79955012080 scopus 로고    scopus 로고
    • Reprogramming the infection mechanism of a filamentous phage
    • Lorenz S.H., Schmid F.X. Reprogramming the infection mechanism of a filamentous phage. Mol. Microbiol. 2011, 80:827-834.
    • (2011) Mol. Microbiol. , vol.80 , pp. 827-834
    • Lorenz, S.H.1    Schmid, F.X.2
  • 211
    • 48749091080 scopus 로고    scopus 로고
    • Conformational dynamics of an intact virus: order parameters for the coat protein of Pf1 bacteriophage
    • Lorieau J.L., Day L.A., McDermott A.E. Conformational dynamics of an intact virus: order parameters for the coat protein of Pf1 bacteriophage. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:10366-10371.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 10366-10371
    • Lorieau, J.L.1    Day, L.A.2    McDermott, A.E.3
  • 212
    • 84868355864 scopus 로고    scopus 로고
    • Next generation phage display by use of pVII and pIX as display scaffolds
    • Løset G.A., Sandlie I. Next generation phage display by use of pVII and pIX as display scaffolds. Methods 2012, 58:40-46.
    • (2012) Methods , vol.58 , pp. 40-46
    • Løset, G.A.1    Sandlie, I.2
  • 213
    • 0031911439 scopus 로고    scopus 로고
    • The structural basis of phage display elucidated by the crystal structure of the N-terminal domains of g3p
    • Lubkowski J., Hennecke F., Plückthun A., Wlodawer A. The structural basis of phage display elucidated by the crystal structure of the N-terminal domains of g3p. Nat. Struct. Biol. 1998, 5:140-147.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 140-147
    • Lubkowski, J.1    Hennecke, F.2    Plückthun, A.3    Wlodawer, A.4
  • 214
    • 30444449377 scopus 로고    scopus 로고
    • Diffraction by DNA, carbon nanotubes and other hefical nanostructures
    • Lucas A.A., Lambin P. Diffraction by DNA, carbon nanotubes and other hefical nanostructures. Rep. Prog. Phys. 2005, 68:1181-1249.
    • (2005) Rep. Prog. Phys. , vol.68 , pp. 1181-1249
    • Lucas, A.A.1    Lambin, P.2
  • 215
    • 0022383671 scopus 로고
    • Nucleotide sequence of the genome of Pf3, an IncP-1 plasmid-specific filamentous bacteriophage of Pseudomonas aeruginosa
    • Luiten R.G.M., Putterman D.G., Schoenmakers J.G.G., Konings R.N.H., Day L.A. Nucleotide sequence of the genome of Pf3, an IncP-1 plasmid-specific filamentous bacteriophage of Pseudomonas aeruginosa. J.Virol. 1985, 56:268-276.
    • (1985) J.Virol. , vol.56 , pp. 268-276
    • Luiten, R.G.M.1    Putterman, D.G.2    Schoenmakers, J.G.G.3    Konings, R.N.H.4    Day, L.A.5
  • 216
    • 1642424934 scopus 로고
    • Recherches sur un Bacillus mégatherium lysogène
    • Lwoff A., Gutmann A. Recherches sur un Bacillus mégatherium lysogène. Ann. Inst. Pasteur. 1950, 78:711-724.
    • (1950) Ann. Inst. Pasteur. , vol.78 , pp. 711-724
    • Lwoff, A.1    Gutmann, A.2
  • 217
    • 0015371464 scopus 로고
    • The genetic map of the filamentous bacteriophage f1
    • Lyons L.B., Zinder N.D. The genetic map of the filamentous bacteriophage f1. Virology 1972, 49:45-60.
    • (1972) Virology , vol.49 , pp. 45-60
    • Lyons, L.B.1    Zinder, N.D.2
  • 218
    • 31144476153 scopus 로고    scopus 로고
    • The role of aperiodic order in science and technology
    • Maciá E. The role of aperiodic order in science and technology. Rep. Prog. Phys. 2006, 69:397-441.
    • (2006) Rep. Prog. Phys. , vol.69 , pp. 397-441
    • Maciá, E.1
  • 219
    • 0019201172 scopus 로고
    • Filamentous bacteriophage structure determined at 7Å resolution by refinement of models for the α-helical subunit
    • Makowski L., Caspar D.L.D., Marvin D.A. Filamentous bacteriophage structure determined at 7Å resolution by refinement of models for the α-helical subunit. J.Mol. Biol. 1980, 140:149-181.
    • (1980) J.Mol. Biol. , vol.140 , pp. 149-181
    • Makowski, L.1    Caspar, D.L.D.2    Marvin, D.A.3
  • 220
    • 0027080165 scopus 로고
    • Terminating a macromolecular helix: structural model for the minor proteins of bacteriophage M13
    • Makowski L. Terminating a macromolecular helix: structural model for the minor proteins of bacteriophage M13. J.Mol. Biol. 1992, 228:885-892.
    • (1992) J.Mol. Biol. , vol.228 , pp. 885-892
    • Makowski, L.1
  • 221
    • 0031592934 scopus 로고    scopus 로고
    • Selective phage infection mediated by epitope expression on F pilus
    • Malmborg A.-C., Soderlind E., Frost L., Borrebaeck C.A.D. Selective phage infection mediated by epitope expression on F pilus. J.Mol. Biol. 1997, 273:544-551.
    • (1997) J.Mol. Biol. , vol.273 , pp. 544-551
    • Malmborg, A.-C.1    Soderlind, E.2    Frost, L.3    Borrebaeck, C.A.D.4
  • 222
    • 0019802390 scopus 로고
    • Mechanism of coliphageM13 contraction: intermediate structures trapped at low temperatures
    • Manning M., Chrysogelos S., Griffith J. Mechanism of coliphageM13 contraction: intermediate structures trapped at low temperatures. J.Virol. 1981, 40:912-919.
    • (1981) J.Virol. , vol.40 , pp. 912-919
    • Manning, M.1    Chrysogelos, S.2    Griffith, J.3
  • 223
    • 0021973691 scopus 로고
    • Association of M13 I-forms and spheroids with lipid vesicles
    • Manning M., Griffith J. Association of M13 I-forms and spheroids with lipid vesicles. Arch. Biochem. Biophys. 1985, 236:297-303.
    • (1985) Arch. Biochem. Biophys. , vol.236 , pp. 297-303
    • Manning, M.1    Griffith, J.2
  • 225
    • 0034186215 scopus 로고    scopus 로고
    • Asolid-state NMR index of helical membrane protein structure and topology
    • Marassi F.M., Opella S.J. Asolid-state NMR index of helical membrane protein structure and topology. J.Magn. Reson. 2000, 144:150-155.
    • (2000) J.Magn. Reson. , vol.144 , pp. 150-155
    • Marassi, F.M.1    Opella, S.J.2
  • 226
    • 0037372352 scopus 로고    scopus 로고
    • Simultaneous assignment and structure determination of a membrane protein from NMR orientational restraints
    • Marassi F.M., Opella S.J. Simultaneous assignment and structure determination of a membrane protein from NMR orientational restraints. Protein Sci. 2003, 12:403-411.
    • (2003) Protein Sci. , vol.12 , pp. 403-411
    • Marassi, F.M.1    Opella, S.J.2
  • 228
    • 0001133188 scopus 로고
    • Recent biophysical studies in high magnetic fields
    • Maret G. Recent biophysical studies in high magnetic fields. Phys. B 1990, 164:205-212.
    • (1990) Phys. B , vol.164 , pp. 205-212
    • Maret, G.1
  • 229
    • 0001192682 scopus 로고
    • Biomolecules and polymers in high steady magnetic fields
    • Springer, Berlin
    • Maret G., Dransfeld K. Biomolecules and polymers in high steady magnetic fields. Topics in Applied Physics 1985, vol. 57:143-204. Springer, Berlin.
    • (1985) Topics in Applied Physics , vol.57 , pp. 143-204
    • Maret, G.1    Dransfeld, K.2
  • 231
    • 0028840548 scopus 로고
    • Circular dichroism spectroscopy of three tyrosine-to-phenylalanine substitutions of fd gene 5 protein
    • Mark B.L., Terwilliger T.C., Vaughan M.R., Gray D.M. Circular dichroism spectroscopy of three tyrosine-to-phenylalanine substitutions of fd gene 5 protein. Biochemistry 1995, 34:12854-12865.
    • (1995) Biochemistry , vol.34 , pp. 12854-12865
    • Mark, B.L.1    Terwilliger, T.C.2    Vaughan, M.R.3    Gray, D.M.4
  • 232
    • 0013870932 scopus 로고
    • X-ray diffraction and electron microscope studies on the structure of the small filamentous bacteriophage fd
    • Marvin D.A. X-ray diffraction and electron microscope studies on the structure of the small filamentous bacteriophage fd. J.Mol. Biol. 1966, 15:8-17.
    • (1966) J.Mol. Biol. , vol.15 , pp. 8-17
    • Marvin, D.A.1
  • 233
    • 0006082902 scopus 로고
    • Structure of the filamentous phage virion
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, D.T. Denhardt, D. Dressler, D.S. Ray (Eds.)
    • Marvin D.A. Structure of the filamentous phage virion. The Single-stranded DNA Phages 1978, 583-603. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. D.T. Denhardt, D. Dressler, D.S. Ray (Eds.).
    • (1978) The Single-stranded DNA Phages , pp. 583-603
    • Marvin, D.A.1
  • 234
    • 0021115522 scopus 로고
    • Proton currents and protein motion in membranes
    • Marvin D.A. Proton currents and protein motion in membranes. FEBS Lett. 1983, 156:1-5.
    • (1983) FEBS Lett. , vol.156 , pp. 1-5
    • Marvin, D.A.1
  • 235
    • 0024685772 scopus 로고
    • Dynamics of telescoping Inovirus: a mechanism for assembly at membrane adhesions
    • Marvin D.A. Dynamics of telescoping Inovirus: a mechanism for assembly at membrane adhesions. Int. J. Biol. Macromol. 1989, 11:159-164.
    • (1989) Int. J. Biol. Macromol. , vol.11 , pp. 159-164
    • Marvin, D.A.1
  • 236
    • 0025036161 scopus 로고
    • Model-building studies of Inovirus: genetic variations on a geometric theme
    • (Erratum in: Int. J. Biol. Macromol. 12, 335)
    • Marvin D.A. Model-building studies of Inovirus: genetic variations on a geometric theme. Int. J. Biol. Macromol. 1990, 12:125-138. (Erratum in: Int. J. Biol. Macromol. 12, 335).
    • (1990) Int. J. Biol. Macromol. , vol.12 , pp. 125-138
    • Marvin, D.A.1
  • 237
    • 0032054113 scopus 로고    scopus 로고
    • Filamentous phage structure, infection and assembly
    • Marvin D.A. Filamentous phage structure, infection and assembly. Curr. Opin. Struct. Biol. 1998, 8:150-158.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 150-158
    • Marvin, D.A.1
  • 238
    • 0001434048 scopus 로고
    • Physical and chemical properties of two new small bacteriophages
    • Marvin D.A., Hoffmann-Berling H. Physical and chemical properties of two new small bacteriophages. Nature 1963, 197:517-518.
    • (1963) Nature , vol.197 , pp. 517-518
    • Marvin, D.A.1    Hoffmann-Berling, H.2
  • 239
    • 78651129653 scopus 로고
    • Afibrous DNA phage (fd) and a spherical RNA phage (fr) specific for male strains of E.coli. II. Physical characteristics
    • Marvin D.A., Hoffmann-Berling H. Afibrous DNA phage (fd) and a spherical RNA phage (fr) specific for male strains of E.coli. II. Physical characteristics. Z.Naturforsch. B 1963, 18:884-893.
    • (1963) Z.Naturforsch. B , vol.18 , pp. 884-893
    • Marvin, D.A.1    Hoffmann-Berling, H.2
  • 240
    • 0014530863 scopus 로고
    • Filamentous bacterial viruses
    • (now published as Microbiol. Mol. Biol. Rev.)
    • Marvin D.A., Hohn B. Filamentous bacterial viruses. Bacteriol. Rev. 1969, 33:172-209. (now published as Microbiol. Mol. Biol. Rev.).
    • (1969) Bacteriol. Rev. , vol.33 , pp. 172-209
    • Marvin, D.A.1    Hohn, B.2
  • 241
    • 0013870811 scopus 로고
    • The topology of DNA from the small filamentous bacteriophage fd
    • Marvin D.A., Schaller H. The topology of DNA from the small filamentous bacteriophage fd. J.Mol. Biol. 1966, 15:1-7.
    • (1966) J.Mol. Biol. , vol.15 , pp. 1-7
    • Marvin, D.A.1    Schaller, H.2
  • 242
    • 0016606071 scopus 로고
    • Structure and assembly of filamentous bacterial viruses
    • Marvin D.A., Wachtel E.J. Structure and assembly of filamentous bacterial viruses. Nature (London) 1975, 253:19-23.
    • (1975) Nature (London) , vol.253 , pp. 19-23
    • Marvin, D.A.1    Wachtel, E.J.2
  • 243
    • 0017319019 scopus 로고
    • Structure and assembly of filamentous bacterial viruses
    • Marvin D.A., Wachtel E.J. Structure and assembly of filamentous bacterial viruses. Phil. Trans. Roy. Soc. Ser. B 1976, 276:81-98.
    • (1976) Phil. Trans. Roy. Soc. Ser. B , vol.276 , pp. 81-98
    • Marvin, D.A.1    Wachtel, E.J.2
  • 244
    • 0023123048 scopus 로고
    • Pf1 Inovirus Electron density distribution calculated by a maximum entropy algorithm from native fibre diffraction data to 3Å resolution and single isomorphous replacement data to 5Å resolution
    • Marvin D.A., Bryan R.K., Nave C. Pf1 Inovirus Electron density distribution calculated by a maximum entropy algorithm from native fibre diffraction data to 3Å resolution and single isomorphous replacement data to 5Å resolution. J.Mol. Biol. 1987, 193:315-343.
    • (1987) J.Mol. Biol. , vol.193 , pp. 315-343
    • Marvin, D.A.1    Bryan, R.K.2    Nave, C.3
  • 245
    • 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., Helmer-Citterich M. Molecular models and structural comparisons of native and mutant Class I filamentous bacteriophages Ff (fd, f1, M13), If1 and IKe. J.Mol. Biol. 1994, 235:260-286.
    • (1994) J.Mol. Biol. , vol.235 , pp. 260-286
    • Marvin, D.A.1    Hale, R.D.2    Nave, C.3    Helmer-Citterich, M.4
  • 246
    • 4444272766 scopus 로고    scopus 로고
    • Type-4 bacterial pili: molecular models and their simulated diffraction patterns
    • Marvin D.A., Nadassy K., Welsh L.C., Forest K.T. Type-4 bacterial pili: molecular models and their simulated diffraction patterns. Fibre Diffract. Rev. 2003, 11:87-94.
    • (2003) Fibre Diffract. Rev. , vol.11 , pp. 87-94
    • Marvin, D.A.1    Nadassy, K.2    Welsh, L.C.3    Forest, K.T.4
  • 247
    • 84963178787 scopus 로고
    • Two forms of Pf1 Inovirus: X-ray diffraction studies on a structural phase transition and a calculated libration normal mode of the asymmetric unit
    • Marvin D.A., Nave C., Bansal M., Hale R.D., Salje E.K.H. Two forms of Pf1 Inovirus: X-ray diffraction studies on a structural phase transition and a calculated libration normal mode of the asymmetric unit. Phase Transit. 1992, 39:45-80.
    • (1992) Phase Transit. , vol.39 , pp. 45-80
    • Marvin, D.A.1    Nave, C.2    Bansal, M.3    Hale, R.D.4    Salje, E.K.H.5
  • 249
    • 0016276266 scopus 로고
    • Filamentous bacterial viruses XII. Molecular architecture of the Class I (fd, If1, Ike) virion
    • Marvin D.A., Pigram W.J., Wiseman R.L., Wachtel E.J., Marvin F.J. Filamentous bacterial viruses XII. Molecular architecture of the Class I (fd, If1, Ike) virion. J.Mol. Biol. 1974, 88:581-600.
    • (1974) J.Mol. Biol. , vol.88 , pp. 581-600
    • Marvin, D.A.1    Pigram, W.J.2    Wiseman, R.L.3    Wachtel, E.J.4    Marvin, F.J.5
  • 250
    • 0015955088 scopus 로고
    • Filamentous bacterial viruses XI.Molecular architecture of the Class II (Pf1, Xf) virion
    • Marvin D.A., Wiseman R.L., Wachtel E.J. Filamentous bacterial viruses XI.Molecular architecture of the Class II (Pf1, Xf) virion. J.Mol. Biol. 1974, 82:121-138.
    • (1974) J.Mol. Biol. , vol.82 , pp. 121-138
    • Marvin, D.A.1    Wiseman, R.L.2    Wachtel, E.J.3
  • 251
    • 28844441971 scopus 로고    scopus 로고
    • Molecular structure of fd (f1, M13) filamentous bacteriophage refined with respect to X-ray fibre diffraction and solid-state NMR data supports specific models of phage assembly at the bacterial membrane
    • Marvin D.A., Welsh L.C., Symmons M.F., Scott W.R.P., Straus S.K. Molecular structure of fd (f1, M13) filamentous bacteriophage refined with respect to X-ray fibre diffraction and solid-state NMR data supports specific models of phage assembly at the bacterial membrane. J.Mol. Biol. 2006, 355:294-309.
    • (2006) J.Mol. Biol. , vol.355 , pp. 294-309
    • Marvin, D.A.1    Welsh, L.C.2    Symmons, M.F.3    Scott, W.R.P.4    Straus, S.K.5
  • 252
    • 0031031766 scopus 로고    scopus 로고
    • Extending filamentous phage host range by the grafting of a heterologous receptor binding domain
    • Marzari R., Sblattero D., Righi M., Bradbury A. Extending filamentous phage host range by the grafting of a heterologous receptor binding domain. Gene 1997, 197:27-33.
    • (1997) Gene , vol.197 , pp. 27-33
    • Marzari, R.1    Sblattero, D.2    Righi, M.3    Bradbury, A.4
  • 253
    • 70350448700 scopus 로고    scopus 로고
    • Modeling the functional consequences of single residue replacements in bacteriophage f1 gene V protein
    • Masso M., Mathe E., Parvez N., Hijazi K., Vaisman I.I. Modeling the functional consequences of single residue replacements in bacteriophage f1 gene V protein. Protein Eng. Des. Sel. 2009, 22:665-671.
    • (2009) Protein Eng. Des. Sel. , vol.22 , pp. 665-671
    • Masso, M.1    Mathe, E.2    Parvez, N.3    Hijazi, K.4    Vaisman, I.I.5
  • 254
    • 0027438626 scopus 로고
    • Fd coat protein structure in membrane environments
    • McDonnell P.A., Shon K., Kim Y., Opella S.J. fd coat protein structure in membrane environments. J.Mol. Biol. 1993, 233:447-463.
    • (1993) J.Mol. Biol. , vol.233 , pp. 447-463
    • McDonnell, P.A.1    Shon, K.2    Kim, Y.3    Opella, S.J.4
  • 255
    • 0018727421 scopus 로고
    • Structure at 2.3Å resolution of the gene 5 product of bacteriophage fd: a DNA unwinding protein
    • McPherson A., Jurnak F.A., Wang A.H., Molineux I., Rich A. Structure at 2.3Å resolution of the gene 5 product of bacteriophage fd: a DNA unwinding protein. J.Mol. Biol. 1979, 134:379-400.
    • (1979) J.Mol. Biol. , vol.134 , pp. 379-400
    • McPherson, A.1    Jurnak, F.A.2    Wang, A.H.3    Molineux, I.4    Rich, A.5
  • 256
    • 0030907620 scopus 로고    scopus 로고
    • The Escherichia coli phage-shock-protein (psp) operon
    • Model P., Jovanovic G., Dworkin J. The Escherichia coli phage-shock-protein (psp) operon. Mol. Microbiol. 1997, 24:255-261.
    • (1997) Mol. Microbiol. , vol.24 , pp. 255-261
    • Model, P.1    Jovanovic, G.2    Dworkin, J.3
  • 257
    • 46049088691 scopus 로고    scopus 로고
    • Protein-protein interactions in themembrane: sequence, structural, and biological motifs
    • Moore D.T., Berger B.W., DeGrado W.F. Protein-protein interactions in themembrane: sequence, structural, and biological motifs. Structure 2008, 16:991-1001.
    • (2008) Structure , vol.16 , pp. 991-1001
    • Moore, D.T.1    Berger, B.W.2    DeGrado, W.F.3
  • 259
    • 0347481158 scopus 로고    scopus 로고
    • Binding and reversible denaturation of double-stranded DNA by Ff gene 5 protein
    • Mou T.-C., Shen M.C., Terwilliger T.C., Gray D.M. Binding and reversible denaturation of double-stranded DNA by Ff gene 5 protein. Biopolymers 2003, 70:637-648.
    • (2003) Biopolymers , vol.70 , pp. 637-648
    • Mou, T.-C.1    Shen, M.C.2    Terwilliger, T.C.3    Gray, D.M.4
  • 261
    • 0035239217 scopus 로고    scopus 로고
    • Structure and mass analysis by scanning transmission electron microscopy
    • Müller S.A., Engel A. Structure and mass analysis by scanning transmission electron microscopy. Micron 2001, 32:21-31.
    • (2001) Micron , vol.32 , pp. 21-31
    • Müller, S.A.1    Engel, A.2
  • 262
    • 84878718307 scopus 로고    scopus 로고
    • Virus-based photo-responsive nanowires formed by linking site-directed mutagenesis and chemical reaction
    • Murugesan M., Abbineni G., Nimmo S.L., Cao B., Mao C.B. Virus-based photo-responsive nanowires formed by linking site-directed mutagenesis and chemical reaction. Sci. Rep. 2013, 3:1820.
    • (2013) Sci. Rep. , vol.3 , pp. 1820
    • Murugesan, M.1    Abbineni, G.2    Nimmo, S.L.3    Cao, B.4    Mao, C.B.5
  • 263
    • 0027479161 scopus 로고
    • OB(oligonucleotide/oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences
    • Murzin A.G. OB(oligonucleotide/oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences. EMBO J. 1993, 12:861-867.
    • (1993) EMBO J. , vol.12 , pp. 861-867
    • Murzin, A.G.1
  • 264
    • 34147182082 scopus 로고    scopus 로고
    • Cysteine residues in the transmembrane regions of M13 procoat protein suggest that oligomeric coat proteins assemble onto phage progeny
    • Nagler C., Nagler G., Kuhn A. Cysteine residues in the transmembrane regions of M13 procoat protein suggest that oligomeric coat proteins assemble onto phage progeny. J.Bacteriol. 2007, 189:2897-2905.
    • (2007) J.Bacteriol. , vol.189 , pp. 2897-2905
    • Nagler, C.1    Nagler, G.2    Kuhn, A.3
  • 265
    • 0018964070 scopus 로고
    • Chemical modification and molecular orientation of the B protein in the filamentous bacterial virus Pf1
    • Nakashima Y., Konigsberg W.H. Chemical modification and molecular orientation of the B protein in the filamentous bacterial virus Pf1. J.Mol. Biol. 1980, 138:493-501.
    • (1980) J.Mol. Biol. , vol.138 , pp. 493-501
    • Nakashima, Y.1    Konigsberg, W.H.2
  • 266
    • 0016614442 scopus 로고
    • Primary structure and sidechain interactions of Pf1 filamentous bacterial virus coat protein
    • Nakashima Y., Wiseman R.L., Konigsberg W., Marvin D.A. Primary structure and sidechain interactions of Pf1 filamentous bacterial virus coat protein. Nature 1975, 253:68-71.
    • (1975) Nature , vol.253 , pp. 68-71
    • Nakashima, Y.1    Wiseman, R.L.2    Konigsberg, W.3    Marvin, D.A.4
  • 267
    • 0026434570 scopus 로고
    • Membrane-mediated assembly of filamentous bacteriophage Pf1 coat protein
    • Nambudripad R., Stark W., Opella S.J., Makowski L. Membrane-mediated assembly of filamentous bacteriophage Pf1 coat protein. Science 1991, 252:1305-1308.
    • (1991) Science , vol.252 , pp. 1305-1308
    • Nambudripad, R.1    Stark, W.2    Opella, S.J.3    Makowski, L.4
  • 269
  • 270
    • 33846847707 scopus 로고    scopus 로고
    • FRET study of membrane proteins: determination of the tilt and orientation of the N-terminal domain of M13 major coat protein
    • Nazarov P.V., Koehorst R.B.M., Vos W.L., Apanasovich V.V., Hemminga M.A. FRET study of membrane proteins: determination of the tilt and orientation of the N-terminal domain of M13 major coat protein. Biophys. J. 2007, 92:1296-1305.
    • (2007) Biophys. J. , vol.92 , pp. 1296-1305
    • Nazarov, P.V.1    Koehorst, R.B.M.2    Vos, W.L.3    Apanasovich, V.V.4    Hemminga, M.A.5
  • 271
    • 84855794241 scopus 로고    scopus 로고
    • Heliostat field optimization: a new computationally efficient model and biomimetic layout
    • Noone C.J., Torrilhon M., Mitsos A. Heliostat field optimization: a new computationally efficient model and biomimetic layout. Sol. Energy 2012, 86:792-803.
    • (2012) Sol. Energy , vol.86 , pp. 792-803
    • Noone, C.J.1    Torrilhon, M.2    Mitsos, A.3
  • 273
    • 84887647338 scopus 로고    scopus 로고
    • Biologically enhanced cathode design for improved capacity and cycle life for lithium-oxygen batteries
    • Oh D., Qi J., Lu Y.C., Zhang Y., Shao-Horn Y., Belcher A.M. Biologically enhanced cathode design for improved capacity and cycle life for lithium-oxygen batteries. Nat. Commun. 2013, 4:2756.
    • (2013) Nat. Commun. , vol.4 , pp. 2756
    • Oh, D.1    Qi, J.2    Lu, Y.C.3    Zhang, Y.4    Shao-Horn, Y.5    Belcher, A.M.6
  • 274
    • 0029017513 scopus 로고
    • Structures of fd gene 5 protein-nucleic acid complexes: a combined solution scattering and electron microscopy study
    • Olah G.A., Gray D.M., Gray C.W., Kergil D.L., Sosnick T.R., Mark B.L., Vaughan M.R., Trewhella J. Structures of fd gene 5 protein-nucleic acid complexes: a combined solution scattering and electron microscopy study. J.Mol. Biol. 1995, 249:576-594.
    • (1995) J.Mol. Biol. , vol.249 , pp. 576-594
    • Olah, G.A.1    Gray, D.M.2    Gray, C.W.3    Kergil, D.L.4    Sosnick, T.R.5    Mark, B.L.6    Vaughan, M.R.7    Trewhella, J.8
  • 276
    • 0019073186 scopus 로고
    • Nuclear magnetic resonance of the filamentous bacteriophagefd
    • Opella S.J., Cross T.A., DiVerdi J.A., Sturm C.F. Nuclear magnetic resonance of the filamentous bacteriophagefd. Biophys. J. 1980, 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
  • 277
    • 4344704702 scopus 로고    scopus 로고
    • Structure determination of membrane proteins by NMR spectroscopy
    • Opella S.J., Marassi F.M. Structure determination of membrane proteins by NMR spectroscopy. Chem. Rev. 2004, 104:3587-3606.
    • (2004) Chem. Rev. , vol.104 , pp. 3587-3606
    • Opella, S.J.1    Marassi, F.M.2
  • 279
    • 44149106414 scopus 로고    scopus 로고
    • Structure, dynamics, and assembly of filamentous bacteriophages by nuclear magnetic resonance spectroscopy
    • Opella S.J., Zeri A.C., Park S.H. Structure, dynamics, and assembly of filamentous bacteriophages by nuclear magnetic resonance spectroscopy. Annu. Rev. Phys. Chem. 2008, 59:635-657.
    • (2008) Annu. Rev. Phys. Chem. , vol.59 , pp. 635-657
    • Opella, S.J.1    Zeri, A.C.2    Park, S.H.3
  • 280
    • 0020690937 scopus 로고
    • Outer and inner membrane preparations of extreme thermophile and their physico-chemical properties
    • Oshima M., Osawa Y. Outer and inner membrane preparations of extreme thermophile and their physico-chemical properties. J.Biochem. 1983, 93:225-234.
    • (1983) J.Biochem. , vol.93 , pp. 225-234
    • Oshima, M.1    Osawa, Y.2
  • 281
    • 14344262928 scopus 로고    scopus 로고
    • Structural characterization of the filamentous bacteriophage PH75 from Thermus thermophilus by Raman and UV-resonance Raman spectroscopy
    • Overman S.A., Bondre P., Maiti N.C., Thomas G.J. Structural characterization of the filamentous bacteriophage PH75 from Thermus thermophilus by Raman and UV-resonance Raman spectroscopy. Biochemistry 2005, 44:3091-3100.
    • (2005) Biochemistry , vol.44 , pp. 3091-3100
    • Overman, S.A.1    Bondre, P.2    Maiti, N.C.3    Thomas, G.J.4
  • 282
    • 0028999261 scopus 로고
    • Raman spectroscopy of the filamentous virus Ff (fd, fl, M13): structural interpretation for coat protein aromatics
    • Overman S.A., Thomas G.J. Raman spectroscopy of the filamentous virus Ff (fd, fl, M13): structural interpretation for coat protein aromatics. Biochemistry 1995, 34:5440-5451.
    • (1995) Biochemistry , vol.34 , pp. 5440-5451
    • Overman, S.A.1    Thomas, G.J.2
  • 283
    • 38849158529 scopus 로고    scopus 로고
    • Lipid bilayers: an essential environment for the understanding of membrane proteins
    • Page R.C., Li C., Hu J., Gao F.P., Cross T.A. Lipid bilayers: an essential environment for the understanding of membrane proteins. Magn. Reson. Chem 2007, 45:S2-S11.
    • (2007) Magn. Reson. Chem , vol.45
    • Page, R.C.1    Li, C.2    Hu, J.3    Gao, F.P.4    Cross, T.A.5
  • 284
    • 34147135478 scopus 로고    scopus 로고
    • Characterization of the structure and membrane interaction of the antimicrobial peptides aurein 2.2 and 2.3 from Australian southern bell frogs
    • Pan Y.L., Cheng J.T., Hale J., Pan J., Hancock R.E., Straus S.K. Characterization of the structure and membrane interaction of the antimicrobial peptides aurein 2.2 and 2.3 from Australian southern bell frogs. Biophys. J. 2007, 92:2854-2864.
    • (2007) Biophys. J. , vol.92 , pp. 2854-2864
    • Pan, Y.L.1    Cheng, J.T.2    Hale, J.3    Pan, J.4    Hancock, R.E.5    Straus, S.K.6
  • 285
    • 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., Hilbers C.W. 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. 1998, 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
  • 286
    • 77956582409 scopus 로고    scopus 로고
    • Structure and dynamics of the membrane-bound form of Pf1 coat protein: implications of structural rearrangement for virus assembly
    • Park S.H., Marassi F.M., Black D., Opella S.J. Structure and dynamics of the membrane-bound form of Pf1 coat protein: implications of structural rearrangement for virus assembly. Biophys. J. 2010, 99:1465-1474.
    • (2010) Biophys. J. , vol.99 , pp. 1465-1474
    • Park, S.H.1    Marassi, F.M.2    Black, D.3    Opella, S.J.4
  • 289
    • 0037466515 scopus 로고    scopus 로고
    • The role of aqueous interfaces in the cell
    • Pollack G.H. The role of aqueous interfaces in the cell. Adv. Colloid Interf. Sci. 2003, 103:173-196.
    • (2003) Adv. Colloid Interf. Sci. , vol.103 , pp. 173-196
    • Pollack, G.H.1
  • 290
    • 0029004769 scopus 로고
    • Role of Tyr-22 in the binding of Pf3 ssDNA binding protein to nucleic acids
    • Powell M.D., Gray D.M. Role of Tyr-22 in the binding of Pf3 ssDNA binding protein to nucleic acids. Biochemistry 1995, 34:5635-5643.
    • (1995) Biochemistry , vol.34 , pp. 5635-5643
    • Powell, M.D.1    Gray, D.M.2
  • 291
    • 0015982404 scopus 로고
    • Complex of bacteriophage M13 single-stranded DNA and gene 5 protein
    • Pratt D., Laws P., Griffith J. Complex of bacteriophage M13 single-stranded DNA and gene 5 protein. J.Mol. Biol. 1974, 82:425-439.
    • (1974) J.Mol. Biol. , vol.82 , pp. 425-439
    • Pratt, D.1    Laws, P.2    Griffith, J.3
  • 292
    • 0014575324 scopus 로고
    • Conditional lethal mutants of the small filamentous phage M13. II. Two genes for coat proteins
    • Pratt D., Tzagoloff H., Beaudoin J. Conditional lethal mutants of the small filamentous phage M13. II. Two genes for coat proteins. Virology 1969, 39:42-53.
    • (1969) Virology , vol.39 , pp. 42-53
    • Pratt, D.1    Tzagoloff, H.2    Beaudoin, J.3
  • 293
    • 0013967520 scopus 로고
    • Conditional lethal mutants of the small filamentous coliphage M13. I. Isolation, complementation, cell killing, time of cistron action
    • Pratt D., Tzagoloff H., Erdahl W.S. Conditional lethal mutants of the small filamentous coliphage M13. I. Isolation, complementation, cell killing, time of cistron action. Virology 1966, 30:397-410.
    • (1966) Virology , vol.30 , pp. 397-410
    • Pratt, D.1    Tzagoloff, H.2    Erdahl, W.S.3
  • 294
    • 33746045690 scopus 로고    scopus 로고
    • Current applications of bicelles in NMR studies of membrane-associated amphiphiles and proteins
    • Prosser R.S., Evanics F., Kitevski J.L., Al-Abdul-Wahid M.S. Current applications of bicelles in NMR studies of membrane-associated amphiphiles and proteins. Biochemistry 2006, 45:8453-8465.
    • (2006) Biochemistry , vol.45 , pp. 8453-8465
    • Prosser, R.S.1    Evanics, F.2    Kitevski, J.L.3    Al-Abdul-Wahid, M.S.4
  • 295
    • 0035578761 scopus 로고    scopus 로고
    • Lanthanide ion assisted magnetic alignment of model membranes and macromolecules
    • Prosser R.S., Shiyanovskaya I.V. Lanthanide ion assisted magnetic alignment of model membranes and macromolecules. Concept Magn. Reson. 2001, 13:19-31.
    • (2001) Concept Magn. Reson. , vol.13 , pp. 19-31
    • Prosser, R.S.1    Shiyanovskaya, I.V.2
  • 296
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn O.B. Molten globule and protein folding. Adv. Protein Chem. 1995, 47:83-229.
    • (1995) Adv. Protein Chem. , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 298
    • 0033603625 scopus 로고    scopus 로고
    • Filamentous phage are released from the bacterial membrane by a two- step mechanism involving a short C-terminal fragment of pIII
    • Rakonjac J., Feng J.N., Model P. Filamentous phage are released from the bacterial membrane by a two- step mechanism involving a short C-terminal fragment of pIII. J.Mol. Biol. 1999, 289:1253-1265.
    • (1999) J.Mol. Biol. , vol.289 , pp. 1253-1265
    • Rakonjac, J.1    Feng, J.N.2    Model, P.3
  • 299
    • 0027399020 scopus 로고
    • The filamentous bacteriophage assembly proteins require the bacterial SecA protein for correct localization to the membrane
    • Rapoza M.P., Webster R.E. The filamentous bacteriophage assembly proteins require the bacterial SecA protein for correct localization to the membrane. J.Bacteriol. 1993, 175:1856-1859.
    • (1993) J.Bacteriol. , vol.175 , pp. 1856-1859
    • Rapoza, M.P.1    Webster, R.E.2
  • 300
    • 0029041283 scopus 로고
    • The products of gene I and the overlapping in-frame gene XI are required for filamentous phage assembly
    • Rapoza M.P., Webster R.E. The products of gene I and the overlapping in-frame gene XI are required for filamentous phage assembly. J.Mol. Biol. 1995, 248:627-638.
    • (1995) J.Mol. Biol. , vol.248 , pp. 627-638
    • Rapoza, M.P.1    Webster, R.E.2
  • 301
    • 0343057246 scopus 로고
    • Leaf arrangement. Geometry, morphogenesis, and classification
    • Richter P.H., Schranner R. Leaf arrangement. Geometry, morphogenesis, and classification. Naturwissenschaften 1978, 65:319-327.
    • (1978) Naturwissenschaften , vol.65 , pp. 319-327
    • Richter, P.H.1    Schranner, R.2
  • 302
    • 0030797114 scopus 로고    scopus 로고
    • The C-terminal domain of TolA is the coreceptor for filamentous phage infection of E. coli
    • Riechmann L., Holliger P. The C-terminal domain of TolA is the coreceptor for filamentous phage infection of E. coli. Cell 1997, 90:351-360.
    • (1997) Cell , vol.90 , pp. 351-360
    • Riechmann, L.1    Holliger, P.2
  • 303
    • 0027373676 scopus 로고
    • Structural changes accompanying chloroform-induced contraction of the filamentous phage fd
    • Roberts L.M., Dunker A.K. Structural changes accompanying chloroform-induced contraction of the filamentous phage fd. Biochemistry 1993, 32:10479-10488.
    • (1993) Biochemistry , vol.32 , pp. 10479-10488
    • Roberts, L.M.1    Dunker, A.K.2
  • 304
    • 0036385947 scopus 로고    scopus 로고
    • Aminimized M13 coat protein defines the requirements for assembly into the bacteriophage particle
    • Roth T.A., Weiss G.A., Eigenbrot C., Sidhu S.S. Aminimized M13 coat protein defines the requirements for assembly into the bacteriophage particle. J.Mol. Biol. 2002, 322:357-367.
    • (2002) J.Mol. Biol. , vol.322 , pp. 357-367
    • Roth, T.A.1    Weiss, G.A.2    Eigenbrot, C.3    Sidhu, S.S.4
  • 305
    • 33645028600 scopus 로고    scopus 로고
    • Folding DNA to create nano-scale shapes and patterns
    • Rothemund P.W. Folding DNA to create nano-scale shapes and patterns. Nature 2006, 440:297-302.
    • (2006) Nature , vol.440 , pp. 297-302
    • Rothemund, P.W.1
  • 306
    • 0025734125 scopus 로고
    • Filamentous phage assembly
    • Russel M. Filamentous phage assembly. Mol. Microbiol. 1991, 5:1607-1613.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1607-1613
    • Russel, M.1
  • 307
    • 0032511192 scopus 로고    scopus 로고
    • Macromolecular assembly and secretion across the bacterial cell envelope: type II protein secretion systems
    • Russel M. Macromolecular assembly and secretion across the bacterial cell envelope: type II protein secretion systems. J.Mol. Biol. 1998, 279:485-499.
    • (1998) J.Mol. Biol. , vol.279 , pp. 485-499
    • Russel, M.1
  • 308
    • 0030983210 scopus 로고    scopus 로고
    • Filamentous phage assembly: variation on a protein export theme
    • Russel M., Linderoth N.A., Šali A. Filamentous phage assembly: variation on a protein export theme. Gene 1997, 192:23-32.
    • (1997) Gene , vol.192 , pp. 23-32
    • Russel, M.1    Linderoth, N.A.2    Šali, A.3
  • 309
    • 41049097811 scopus 로고    scopus 로고
    • Filamentous phage
    • Oxford University Press, R. Calendar (Ed.)
    • Russel M., Model P. Filamentous phage. The Bacteriophages 2006, 146-160. Oxford University Press. second ed. R. Calendar (Ed.).
    • (2006) The Bacteriophages , pp. 146-160
    • Russel, M.1    Model, P.2
  • 311
    • 12244258510 scopus 로고    scopus 로고
    • Experimental evolution of conflict mediation between genomes
    • Sachs J.L., Bull J.J. Experimental evolution of conflict mediation between genomes. Proc. Natl. Acad. Sci. U.S.A. 2005, 102:390-395.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 390-395
    • Sachs, J.L.1    Bull, J.J.2
  • 312
    • 77954086206 scopus 로고    scopus 로고
    • Chemical shift tensor - the heart of NMR: Insights into biological aspects of proteins
    • SaitÔ H., Ando I., Ramamoorthy A. Chemical shift tensor - the heart of NMR: Insights into biological aspects of proteins. Prog. NMR Spectrosc. 2010, 57:181-228.
    • (2010) Prog. NMR Spectrosc. , vol.57 , pp. 181-228
    • SaitÔ, H.1    Ando, I.2    Ramamoorthy, A.3
  • 313
    • 0015223516 scopus 로고
    • Role of coliphage M13 gene 5 in single-stranded DNA production
    • Salstrom J.S., Pratt D. Role of coliphage M13 gene 5 in single-stranded DNA production. J.Mol. Biol. 1971, 61:489-501.
    • (1971) J.Mol. Biol. , vol.61 , pp. 489-501
    • Salstrom, J.S.1    Pratt, D.2
  • 315
    • 0035860693 scopus 로고    scopus 로고
    • Function of YidC for the insertion of M13 procoat protein in E. coli: translocation of mutants that show differences in their membrane potential dependence and Sec requirement
    • Samuelson J.C., Jiang F., Yi L., Chen M., de Gier J.W., Kuhn A., Dalbey R.E. Function of YidC for the insertion of M13 procoat protein in E. coli: translocation of mutants that show differences in their membrane potential dependence and Sec requirement. J.Biol. Chem. 2001, 276:34847-34852.
    • (2001) J.Biol. Chem. , vol.276 , pp. 34847-34852
    • Samuelson, J.C.1    Jiang, F.2    Yi, L.3    Chen, M.4    de Gier, J.W.5    Kuhn, A.6    Dalbey, R.E.7
  • 316
    • 84985727720 scopus 로고
    • Distorted α-helix for poly(γ-benzylL-glutamate) in the nematic solid state
    • Samulski E.T., Tobolsky A.V. Distorted α-helix for poly(γ-benzylL-glutamate) in the nematic solid state. Biopolymers 1971, 10:1013-1019.
    • (1971) Biopolymers , vol.10 , pp. 1013-1019
    • Samulski, E.T.1    Tobolsky, A.V.2
  • 317
    • 0016678133 scopus 로고
    • Nucleotide sequences in DNA
    • Sanger F. Nucleotide sequences in DNA. Proc. R. Soc. Lond. B. 1975, 191:317-333.
    • (1975) Proc. R. Soc. Lond. B. , vol.191 , pp. 317-333
    • Sanger, F.1
  • 318
    • 84864557301 scopus 로고    scopus 로고
    • Rheology and DWS microrheology of concentrated suspensions of the semiflexible filamentous fd virus
    • Sarmiento-Gomez E., Montalvan-Sorrosa D., Garza C., Mas-Oliva J., Castillo R. Rheology and DWS microrheology of concentrated suspensions of the semiflexible filamentous fd virus. Eur. Phys. J. E 2012, 35:12035-12038.
    • (2012) Eur. Phys. J. E , vol.35 , pp. 12035-12038
    • Sarmiento-Gomez, E.1    Montalvan-Sorrosa, D.2    Garza, C.3    Mas-Oliva, J.4    Castillo, R.5
  • 319
    • 0023296975 scopus 로고
    • Dynamic light-scattering study on changes in flexibility of filamentous bacteriophage Pf1 with temperature
    • Sasaki S., Fujime S. Dynamic light-scattering study on changes in flexibility of filamentous bacteriophage Pf1 with temperature. Biophys. J. 1987, 51:503-507.
    • (1987) Biophys. J. , vol.51 , pp. 503-507
    • Sasaki, S.1    Fujime, S.2
  • 320
    • 0018348776 scopus 로고
    • The intergenic region and the origins for filamentous phage DNA replication
    • Schaller H. The intergenic region and the origins for filamentous phage DNA replication. Cold Spring Harbor Symp. Quant. Biol. 1979, 43:401-408.
    • (1979) Cold Spring Harbor Symp. Quant. Biol. , vol.43 , pp. 401-408
    • Schaller, H.1
  • 321
    • 0014694146 scopus 로고
    • Structure of the DNA of bacteriophage fd. II. Isolation and characterization of a DNA fraction with double strand-like properties
    • Schaller H., Voss H., Gucker S. Structure of the DNA of bacteriophage fd. II. Isolation and characterization of a DNA fraction with double strand-like properties. J.Mol. Biol. 1969, 44:445-458.
    • (1969) J.Mol. Biol. , vol.44 , pp. 445-458
    • Schaller, H.1    Voss, H.2    Gucker, S.3
  • 322
    • 84858222518 scopus 로고    scopus 로고
    • Protein secretion and surface display in Gram-positive bacteria
    • Schneewind O., Missiakas D.M. Protein secretion and surface display in Gram-positive bacteria. Phil. Trans. R. Soc. B 2012, 367:1123-1139.
    • (2012) Phil. Trans. R. Soc. B , vol.367 , pp. 1123-1139
    • Schneewind, O.1    Missiakas, D.M.2
  • 326
    • 83755162549 scopus 로고    scopus 로고
    • Chemical shifts for the unusual DNA structure in Pf1 bacteriophage from dynamic-nuclear-polarization-enhanced solid-state NMR spectroscopy
    • Sergeyev I.V., Day L.A., Goldbourt A., McDermott A.E. Chemical shifts for the unusual DNA structure in Pf1 bacteriophage from dynamic-nuclear-polarization-enhanced solid-state NMR spectroscopy. J.Am. Chem. Soc. 2011, 133:20208-20217.
    • (2011) J.Am. Chem. Soc. , vol.133 , pp. 20208-20217
    • Sergeyev, I.V.1    Day, L.A.2    Goldbourt, A.3    McDermott, A.E.4
  • 327
    • 79960790667 scopus 로고    scopus 로고
    • Proposed ancestors of phage nucleic acid packaging motors (and cells)
    • Serwer P. Proposed ancestors of phage nucleic acid packaging motors (and cells). Viruses 2011, 3:1249-1280.
    • (2011) Viruses , vol.3 , pp. 1249-1280
    • Serwer, P.1
  • 328
    • 0018373419 scopus 로고
    • Aspecific DNA orientation in the filamentous bacteriophage fd as probed by psoralen crosslinking and electron microscopy
    • Shen C.-K.J., Ikoku A., Hearst J.E. Aspecific DNA orientation in the filamentous bacteriophage fd as probed by psoralen crosslinking and electron microscopy. J.Mol. Biol. 1979, 127:163-175.
    • (1979) J.Mol. Biol. , vol.127 , pp. 163-175
    • Shen, C.-K.J.1    Ikoku, A.2    Hearst, J.E.3
  • 329
    • 0026434565 scopus 로고
    • NMR studies of the structure and dynamics of membrane-bound bacteriophage Pf1 coat protein
    • Shon K.-J., Kim Y., Colnago L.A., Opella S.J. NMR studies of the structure and dynamics of membrane-bound bacteriophage Pf1 coat protein. Science 1991, 252:1303-1305.
    • (1991) Science , vol.252 , pp. 1303-1305
    • Shon, K.-J.1    Kim, Y.2    Colnago, L.A.3    Opella, S.J.4
  • 330
    • 84899075210 scopus 로고
    • φX: Multum in Parvo
    • Cold Spring Harbor Laboratory, New York, J. Cairns, G.S. Stent, J.D. Watson (Eds.)
    • Sinsheimer R.L. φX: Multum in Parvo. Phage and the Origins of Molecular Biology 1966, 258-264. Cold Spring Harbor Laboratory, New York. J. Cairns, G.S. Stent, J.D. Watson (Eds.).
    • (1966) Phage and the Origins of Molecular Biology , pp. 258-264
    • Sinsheimer, R.L.1
  • 331
    • 0035810950 scopus 로고    scopus 로고
    • Direct observation of extension and retraction of type IV pili
    • Skerker J.M., Berg H.C. Direct observation of extension and retraction of type IV pili. Proc. Natl. Acad. Sci. U.S.A. 2001, 98:6901-6904.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 6901-6904
    • Skerker, J.M.1    Berg, H.C.2
  • 333
    • 0021818675 scopus 로고
    • Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface
    • Smith G.P. Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface. Science 1985, 228:1315-1317.
    • (1985) Science , vol.228 , pp. 1315-1317
    • Smith, G.P.1
  • 334
    • 33947596205 scopus 로고    scopus 로고
    • Active immunization against Alzheimer's β-amyloid peptide using phage display technology
    • Solomon B. Active immunization against Alzheimer's β-amyloid peptide using phage display technology. Vaccine 2007, 25:3053-3056.
    • (2007) Vaccine , vol.25 , pp. 3053-3056
    • Solomon, B.1
  • 335
    • 70349884311 scopus 로고    scopus 로고
    • Exploring conformational modes of macromolecular assemblies by multiparticle cryo-EM
    • Spahn C.M.T., Penczek P.A. Exploring conformational modes of macromolecular assemblies by multiparticle cryo-EM. Curr. Opin. Struct. Biol. 2009, 19:623-631.
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 623-631
    • Spahn, C.M.T.1    Penczek, P.A.2
  • 336
    • 0023394528 scopus 로고
    • Structural responsiveness of filamentous bacteriophage Pf1: comparison of virion structure in fibers and solution
    • Specthrie L., Greenberg J., Glucksman M.J., Diaz J., Makowski L. Structural responsiveness of filamentous bacteriophage Pf1: comparison of virion structure in fibers and solution. Biophys. J. 1987, 52:199-214.
    • (1987) Biophys. J. , vol.52 , pp. 199-214
    • Specthrie, L.1    Greenberg, J.2    Glucksman, M.J.3    Diaz, J.4    Makowski, L.5
  • 337
    • 82155168216 scopus 로고    scopus 로고
    • Sortase enzymes in Gram-positive bacteria
    • Spirig T., Weiner E.M., Clubb R.Y. Sortase enzymes in Gram-positive bacteria. Mol. Microbiol. 2011, 82:1044-1059.
    • (2011) Mol. Microbiol. , vol.82 , pp. 1044-1059
    • Spirig, T.1    Weiner, E.M.2    Clubb, R.Y.3
  • 338
    • 0024468872 scopus 로고
    • Aggregation-related conformational change of the membrane-associated coat protein of bacteriophage M13
    • Spruijt R.B., Wolfs C.J., Hemminga M.A. Aggregation-related conformational change of the membrane-associated coat protein of bacteriophage M13. Biochemistry 1989, 28:9158-9165.
    • (1989) Biochemistry , vol.28 , pp. 9158-9165
    • Spruijt, R.B.1    Wolfs, C.J.2    Hemminga, M.A.3
  • 339
    • 0020039567 scopus 로고
    • Codon preference and its use in identifying protein coding regions in long DNA sequences
    • Staden R., McLachlan A.D. Codon preference and its use in identifying protein coding regions in long DNA sequences. Nucleic Acids Res. 1982, 10:141-156.
    • (1982) Nucleic Acids Res. , vol.10 , pp. 141-156
    • Staden, R.1    McLachlan, A.D.2
  • 340
    • 0028885272 scopus 로고
    • Single-stranded DNA binding protein encoded by the filamentous bacteriophage M13: structural and functional characteristics
    • Stassen A.P.M., Folmer R.H.A., Hilbers C.W., Konings R.N.H. Single-stranded DNA binding protein encoded by the filamentous bacteriophage M13: structural and functional characteristics. Mol. Biol. Rep. 1995, 20:109-127.
    • (1995) Mol. Biol. Rep. , vol.20 , pp. 109-127
    • Stassen, A.P.M.1    Folmer, R.H.A.2    Hilbers, C.W.3    Konings, R.N.H.4
  • 341
    • 0026724180 scopus 로고
    • Nucleotide sequence of the genome of the filamentous bacteriophage I2-2:Module evolution of the filamentous phage genome
    • Stassen A.P.M., Schoenmakers E.F.P.M., Yu M., Schoenmakers J.G.G., Konings R.N.H. Nucleotide sequence of the genome of the filamentous bacteriophage I2-2:Module evolution of the filamentous phage genome. J.Mol. Evol. 1992, 34:141-152.
    • (1992) J.Mol. Evol. , vol.34 , pp. 141-152
    • Stassen, A.P.M.1    Schoenmakers, E.F.P.M.2    Yu, M.3    Schoenmakers, J.G.G.4    Konings, R.N.H.5
  • 342
    • 0025273561 scopus 로고
    • Dissection of functional domains in phage fd adsorption protein. Discrimination between attachment and penetration sites
    • Stengele I., Bross P., Garces X., Giray J., Rasched I. Dissection of functional domains in phage fd adsorption protein. Discrimination between attachment and penetration sites. J.Mol. Biol. 1990, 212:143-149.
    • (1990) J.Mol. Biol. , vol.212 , pp. 143-149
    • Stengele, I.1    Bross, P.2    Garces, X.3    Giray, J.4    Rasched, I.5
  • 343
    • 79551687349 scopus 로고    scopus 로고
    • M13 procoat protein insertion into YidC and SecYEG proteoliposomes and liposomes
    • Stiegler N., Dalbey R.E., Kuhn A. M13 procoat protein insertion into YidC and SecYEG proteoliposomes and liposomes. J.Mol. Biol. 2011, 406:362-370.
    • (2011) J.Mol. Biol. , vol.406 , pp. 362-370
    • Stiegler, N.1    Dalbey, R.E.2    Kuhn, A.3
  • 344
    • 33646560648 scopus 로고    scopus 로고
    • Anchoring mechanisms of membrane-associated M13 major coat protein
    • Stopar D., Spruijt R.B., Hemminga M.A. Anchoring mechanisms of membrane-associated M13 major coat protein. Chem. Phys. Lipids 2006, 141:83-93.
    • (2006) Chem. Phys. Lipids , vol.141 , pp. 83-93
    • Stopar, D.1    Spruijt, R.B.2    Hemminga, M.A.3
  • 345
    • 0032516430 scopus 로고    scopus 로고
    • Mimicking initial interactions of bacteriophage M13 coat protein disassembly in model membrane systems
    • Stopar D., Spruijt R.B., Wolfs C.J.A.M., Hemminga M.A. Mimicking initial interactions of bacteriophage M13 coat protein disassembly in model membrane systems. Biochemistry 1998, 37:10181-10187.
    • (1998) Biochemistry , vol.37 , pp. 10181-10187
    • Stopar, D.1    Spruijt, R.B.2    Wolfs, C.J.A.M.3    Hemminga, M.A.4
  • 347
    • 2942702123 scopus 로고    scopus 로고
    • Recent developments in solid-state magic-angle spinning, nuclear magnetic resonance of fully and significantly isotopically labelled peptides and proteins
    • Straus S.K. Recent developments in solid-state magic-angle spinning, nuclear magnetic resonance of fully and significantly isotopically labelled peptides and proteins. Phil. Trans. R. Soc. Lond. B 2004, 359:997-1008.
    • (2004) Phil. Trans. R. Soc. Lond. B , vol.359 , pp. 997-1008
    • Straus, S.K.1
  • 348
    • 45849151693 scopus 로고    scopus 로고
    • The hand of the filamentous bacteriophage helix
    • Straus S.K., Scott W.R.P., Marvin D.A. The hand of the filamentous bacteriophage helix. Eur. Biophys. J. 2008, 37:1077-1082.
    • (2008) Eur. Biophys. J. , vol.37 , pp. 1077-1082
    • Straus, S.K.1    Scott, W.R.P.2    Marvin, D.A.3
  • 349
  • 350
    • 79958703146 scopus 로고    scopus 로고
    • Consensus structure of Pf1 filamentous bacteriophage from X-ray fibre diffraction and solid-state NMR
    • Straus S.K., Scott W.R.P., Schwieters C.D., Marvin D.A. Consensus structure of Pf1 filamentous bacteriophage from X-ray fibre diffraction and solid-state NMR. Eur. Biophys. J. 2011, 40:221-234.
    • (2011) Eur. Biophys. J. , vol.40 , pp. 221-234
    • Straus, S.K.1    Scott, W.R.P.2    Schwieters, C.D.3    Marvin, D.A.4
  • 351
    • 0030938552 scopus 로고    scopus 로고
    • Analyses of the stability and functions of three surface mutants (R82C, K69H, and L32R) of the gene V protein from Ff phage by X-ray crystallography
    • Su S., Gao Y.-G., Zhang H., Terwilliger T.C., Wang A.H.-J. Analyses of the stability and functions of three surface mutants (R82C, K69H, and L32R) of the gene V protein from Ff phage by X-ray crystallography. Protein Sci. 1997, 6:771-780.
    • (1997) Protein Sci. , vol.6 , pp. 771-780
    • Su, S.1    Gao, Y.-G.2    Zhang, H.3    Terwilliger, T.C.4    Wang, A.H.-J.5
  • 352
    • 0028894101 scopus 로고
    • Matching electrostatic charge between DNA and coat protein in filamentous bacteriophage. Fibre diffraction of charge-deletion mutants
    • Symmons M.F., Welsh L.C., Nave C., Marvin D.A., Perham R.N. Matching electrostatic charge between DNA and coat protein in filamentous bacteriophage. Fibre diffraction of charge-deletion mutants. J.Mol. Biol. 1995, 245:86-91.
    • (1995) J.Mol. Biol. , vol.245 , pp. 86-91
    • Symmons, M.F.1    Welsh, L.C.2    Nave, C.3    Marvin, D.A.4    Perham, R.N.5
  • 353
    • 0033605076 scopus 로고    scopus 로고
    • Effects of temperature and Y21Mmutation on conformational heterogeneity of the major coat protein (pVIII) of filamentous bacteriophage fd
    • Tan W.M., Jelinek R., Opella S.J., Malik P., Terry T.D., Perham R.N. Effects of temperature and Y21Mmutation on conformational heterogeneity of the major coat protein (pVIII) of filamentous bacteriophage fd. J.Mol. Biol. 1999, 286:787-796.
    • (1999) J.Mol. Biol. , vol.286 , pp. 787-796
    • Tan, W.M.1    Jelinek, R.2    Opella, S.J.3    Malik, P.4    Terry, T.D.5    Perham, R.N.6
  • 355
    • 27744562914 scopus 로고    scopus 로고
    • Divergent evolution within protein superfolds inferred from profile-based phylogenetics
    • Theobald D.L., Wuttke D.S. Divergent evolution within protein superfolds inferred from profile-based phylogenetics. J.Mol. Biol. 2005, 354:722-737.
    • (2005) J.Mol. Biol. , vol.354 , pp. 722-737
    • Theobald, D.L.1    Wuttke, D.S.2
  • 356
    • 15244356304 scopus 로고    scopus 로고
    • Structural basis of the temperature transition of Pf1 bacteriophage
    • Thiriot D.S., Nevzorov A.A., Opella S.J. Structural basis of the temperature transition of Pf1 bacteriophage. Protein Sci. 2005, 14:1064-1070.
    • (2005) Protein Sci. , vol.14 , pp. 1064-1070
    • Thiriot, D.S.1    Nevzorov, A.A.2    Opella, S.J.3
  • 357
    • 4344702276 scopus 로고    scopus 로고
    • Structure of the coat protein in Pf1 bacteriophage determined by solid state NMR spectroscopy
    • Thiriot D.S., Nevzorov A.A., Zagyanskiy L., Wu C.H., Opella S.J. Structure of the coat protein in Pf1 bacteriophage determined by solid state NMR spectroscopy. J.Mol. Biol. 2004, 341:869-879.
    • (2004) J.Mol. Biol. , vol.341 , pp. 869-879
    • Thiriot, D.S.1    Nevzorov, A.A.2    Zagyanskiy, L.3    Wu, C.H.4    Opella, S.J.5
  • 358
    • 0016796210 scopus 로고
    • Structure of coat proteins in Pf1 and fd virions by laser Raman spectroscopy
    • Thomas G.J., Murphy P. Structure of coat proteins in Pf1 and fd virions by laser Raman spectroscopy. Science 1975, 188:1205-1207.
    • (1975) Science , vol.188 , pp. 1205-1207
    • Thomas, G.J.1    Murphy, P.2
  • 359
    • 79955836545 scopus 로고    scopus 로고
    • From qualitative data to quantitative models: analysis of the phage shock protein stressresponse in Escherichia coli
    • Toni T., Jovanovic G., Huvet M., Buck M., Stumpf M.P.H. From qualitative data to quantitative models: analysis of the phage shock protein stressresponse in Escherichia coli. BMC Syst. Biol. 2011, 5:69.
    • (2011) BMC Syst. Biol. , vol.5 , pp. 69
    • Toni, T.1    Jovanovic, G.2    Huvet, M.3    Buck, M.4    Stumpf, M.P.H.5
  • 360
    • 0019472555 scopus 로고
    • Structure of the fd DNA-gene 5 protein complex in solution. A neutron small-angle scattering study
    • Torbet J., Gray D.M., Gray C.W., Marvin D.A., Siegrist H. Structure of the fd DNA-gene 5 protein complex in solution. A neutron small-angle scattering study. J.Mol. Biol. 1981, 146:305-320.
    • (1981) J.Mol. Biol. , vol.146 , pp. 305-320
    • Torbet, J.1    Gray, D.M.2    Gray, C.W.3    Marvin, D.A.4    Siegrist, H.5
  • 361
    • 0018640809 scopus 로고
    • Fibres of highly oriented Pf1 bacteriophage produced in a strong magnetic field
    • Torbet J., Maret G. Fibres of highly oriented Pf1 bacteriophage produced in a strong magnetic field. J.Mol. Biol. 1979, 134:843-845.
    • (1979) J.Mol. Biol. , vol.134 , pp. 843-845
    • Torbet, J.1    Maret, G.2
  • 362
    • 0019804324 scopus 로고
    • High-Field magnetic birefringence study of the structure of rodlike phages Pf1 and fd in solution
    • Torbet J., Maret G. High-Field magnetic birefringence study of the structure of rodlike phages Pf1 and fd in solution. Biopolymers 1981, 20:2657-2660.
    • (1981) Biopolymers , vol.20 , pp. 2657-2660
    • Torbet, J.1    Maret, G.2
  • 363
    • 0037333304 scopus 로고    scopus 로고
    • Membrane proteins: the 'Wild West' of structural biology
    • Torres J., Stevens T.J., Samsó M. Membrane proteins: the 'Wild West' of structural biology. Trends Biochem. Sci. 2003, 28:137-144.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 137-144
    • Torres, J.1    Stevens, T.J.2    Samsó, M.3
  • 364
    • 0346422375 scopus 로고    scopus 로고
    • Lipid bilayers: thermodynamics, structure, fluctuations, and interactions
    • Tristram-Nagle S., Nagle J.F. Lipid bilayers: thermodynamics, structure, fluctuations, and interactions. Chem. Phys. Lipids 2004, 127:3-14.
    • (2004) Chem. Phys. Lipids , vol.127 , pp. 3-14
    • Tristram-Nagle, S.1    Nagle, J.F.2
  • 365
    • 0036629499 scopus 로고    scopus 로고
    • Raman scattering anisotropy of biological systems
    • Tsuboi M. Raman scattering anisotropy of biological systems. J.Biomed. Opt. 2002, 7:435-441.
    • (2002) J.Biomed. Opt. , vol.7 , pp. 435-441
    • Tsuboi, M.1
  • 366
    • 0037417751 scopus 로고    scopus 로고
    • Protein andDNAresidue orientations in the filamentous virus Pf1 determined by polarized Raman and polarized FTIR spectroscopy
    • Tsuboi M., Kubo Y., Ikeda T., Overman S.A., Osman O., Thomas G.J. Protein andDNAresidue orientations in the filamentous virus Pf1 determined by polarized Raman and polarized FTIR spectroscopy. Biochemistry 2003, 42:940-950.
    • (2003) Biochemistry , vol.42 , pp. 940-950
    • Tsuboi, M.1    Kubo, Y.2    Ikeda, T.3    Overman, S.A.4    Osman, O.5    Thomas, G.J.6
  • 367
    • 0029824276 scopus 로고    scopus 로고
    • Orientation of tryptophan-26 in coat protein subunits of the filamentous virus Ff by polarized Raman microspectroscopy
    • Tsuboi M., Overman S.A., Thomas G.J. Orientation of tryptophan-26 in coat protein subunits of the filamentous virus Ff by polarized Raman microspectroscopy. Biochemistry 1996, 35:10403-10410.
    • (1996) Biochemistry , vol.35 , pp. 10403-10410
    • Tsuboi, M.1    Overman, S.A.2    Thomas, G.J.3
  • 368
    • 77749265086 scopus 로고    scopus 로고
    • Astructural model for the single-stranded DNA genome of filamentous bacteriophage Pf1
    • Tsuboi M., Tsunoda M., Overman S.A., Benevides J.M., Thomas G.J. Astructural model for the single-stranded DNA genome of filamentous bacteriophage Pf1. Biochemistry 2010, 49:1737-1743.
    • (2010) Biochemistry , vol.49 , pp. 1737-1743
    • Tsuboi, M.1    Tsunoda, M.2    Overman, S.A.3    Benevides, J.M.4    Thomas, G.J.5
  • 369
    • 0035814753 scopus 로고    scopus 로고
    • Orientations of Tyr 21 and Tyr 24 in the capsid of filamentous virus Ff determined by polarized Raman spectroscopy
    • Tsuboi M., Ushizawa K., Nakamura K., Benevides J.M., Overman S.A., Thomas G.J. Orientations of Tyr 21 and Tyr 24 in the capsid of filamentous virus Ff determined by polarized Raman spectroscopy. Biochemistry 2001, 40:1238-1247.
    • (2001) Biochemistry , vol.40 , pp. 1238-1247
    • Tsuboi, M.1    Ushizawa, K.2    Nakamura, K.3    Benevides, J.M.4    Overman, S.A.5    Thomas, G.J.6
  • 370
    • 77954217602 scopus 로고    scopus 로고
    • The protein kingdom extended: ordered and intrinsically disordered proteins, their folding, supramolecular complex formation, and aggregation
    • Turoverov K.K., Kuznetsova I.M., Uversky V.N. The protein kingdom extended: ordered and intrinsically disordered proteins, their folding, supramolecular complex formation, and aggregation. Prog. Biophys. Mol. Biol. 2010, 102:73-84.
    • (2010) Prog. Biophys. Mol. Biol. , vol.102 , pp. 73-84
    • Turoverov, K.K.1    Kuznetsova, I.M.2    Uversky, V.N.3
  • 371
    • 0027337305 scopus 로고
    • Assignment of proton, nitrogen-15, and backbone carbon-13 resonances in detergent-solubilized M13 coat protein via multinuclear multidimensional NMR: a model for the coat protein monomer
    • Van de Ven F.J.M., Van Os J.W.M., Aelen J.M.A., Wymenga S.S., Remerowski M.L., Konings R.N.H., Hilbers C.W. Assignment of proton, nitrogen-15, and backbone carbon-13 resonances in detergent-solubilized M13 coat protein via multinuclear multidimensional NMR: a model for the coat protein monomer. Biochemistry 1993, 32:8322-8328.
    • (1993) Biochemistry , vol.32 , pp. 8322-8328
    • Van de Ven, F.J.M.1    Van Os, J.W.M.2    Aelen, J.M.A.3    Wymenga, S.S.4    Remerowski, M.L.5    Konings, R.N.H.6    Hilbers, C.W.7
  • 373
    • 36549080549 scopus 로고    scopus 로고
    • Structure of membrane-embedded M13 major coat protein is insensitive to hydrophobic stress
    • Vos W.L., Schor M., Nazarov P.V., Koehorst R.B.M., Spruijt R.B., Hemminga M.A. Structure of membrane-embedded M13 major coat protein is insensitive to hydrophobic stress. Biophys. J. 2007, 93:3541-3547.
    • (2007) Biophys. J. , vol.93 , pp. 3541-3547
    • Vos, W.L.1    Schor, M.2    Nazarov, P.V.3    Koehorst, R.B.M.4    Spruijt, R.B.5    Hemminga, M.A.6
  • 374
    • 0017299573 scopus 로고
    • Structural transition in a filamentous protein
    • (Erratum: J Mol. Biol. 111, 95)
    • Wachtel E.J., Marvin F.J., Marvin D.A. Structural transition in a filamentous protein. J.Mol. Biol. 1976, 107:379-383. (Erratum: J Mol. Biol. 111, 95).
    • (1976) J.Mol. Biol. , vol.107 , pp. 379-383
    • Wachtel, E.J.1    Marvin, F.J.2    Marvin, D.A.3
  • 375
    • 0016296832 scopus 로고
    • Filamentous bacterial viruses XIII.Molecular structure of the virion in projection
    • Wachtel E.J., Wiseman R.L., Pigram W.J., Marvin D.A., Manuelidis L. Filamentous bacterial viruses XIII.Molecular structure of the virion in projection. J.Mol. Biol. 1974, 88:601-618.
    • (1974) J.Mol. Biol. , vol.88 , pp. 601-618
    • Wachtel, E.J.1    Wiseman, R.L.2    Pigram, W.J.3    Marvin, D.A.4    Manuelidis, L.5
  • 376
    • 70350211420 scopus 로고    scopus 로고
    • Structural biology of the chaperone-usher pathway of pilus biogenesis
    • Waksman G., Hultgren S.J. Structural biology of the chaperone-usher pathway of pilus biogenesis. Nat. Rev. Microbiol. 2009, 7:765-774.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 765-774
    • Waksman, G.1    Hultgren, S.J.2
  • 377
    • 0027589340 scopus 로고
    • Molecular dynamics in refinement against fiber diffraction data
    • Wang H., Stubbs G. Molecular dynamics in refinement against fiber diffraction data. Acta Crystallog. 1993, A49:504-513.
    • (1993) Acta Crystallog. , vol.49 , pp. 504-513
    • Wang, H.1    Stubbs, G.2
  • 378
    • 0033541375 scopus 로고    scopus 로고
    • Transcription of the genome of the filamentous bacteriophage cf from both plus and minus DNA strands
    • Wang H.-J., Cheng C.-M., Wang C.-N., Kuo T.-T. Transcription of the genome of the filamentous bacteriophage cf from both plus and minus DNA strands. Virology 1999, 256:228-232.
    • (1999) Virology , vol.256 , pp. 228-232
    • Wang, H.-J.1    Cheng, C.-M.2    Wang, C.-N.3    Kuo, T.-T.4
  • 381
    • 0025897173 scopus 로고
    • The tol gene products and the import of macromoleculesinto Escherichia coli
    • Webster R.E. The tol gene products and the import of macromoleculesinto Escherichia coli. Mol. Microbiol. 1991, 5:1005-1010.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1005-1010
    • Webster, R.E.1
  • 382
    • 0002013346 scopus 로고    scopus 로고
    • Filamentous phage biology
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, C.F. Barbas, D.R. Burton, J.K. Scott, G.J. Silverman (Eds.)
    • Webster R.E. Filamentous phage biology. Phage Display: A Laboratory Manual 2001, 1.1-1.37. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York. C.F. Barbas, D.R. Burton, J.K. Scott, G.J. Silverman (Eds.).
    • (2001) Phage Display: A Laboratory Manual
    • Webster, R.E.1
  • 383
    • 0015805199 scopus 로고
    • Abortive infection of Escherichia coli with the bacteriophage f1: cytoplasmic membrane proteins and the f1 DNA-gene 5 protein complex
    • Webster R.E., Cashman J.S. Abortive infection of Escherichia coli with the bacteriophage f1: cytoplasmic membrane proteins and the f1 DNA-gene 5 protein complex. Virology 1973, 55:20-38.
    • (1973) Virology , vol.55 , pp. 20-38
    • Webster, R.E.1    Cashman, J.S.2
  • 384
    • 0032545177 scopus 로고    scopus 로고
    • Analysis of X-ray diffraction from fibres of Pf1 Inovirus (filamentous bacteriophage) shows that the DNA in the virion is not highly ordered
    • Welsh L.C., Marvin D.A., Perham R.N. Analysis of X-ray diffraction from fibres of Pf1 Inovirus (filamentous bacteriophage) shows that the DNA in the virion is not highly ordered. J.Mol. Biol. 1998, 284:1265-1271.
    • (1998) J.Mol. Biol. , vol.284 , pp. 1265-1271
    • Welsh, L.C.1    Marvin, D.A.2    Perham, R.N.3
  • 385
    • 0032538349 scopus 로고    scopus 로고
    • Structure of the capsid of Pf3 filamentous phage determined from X-ray fibre diffraction data at 3.1Å resolution
    • Welsh L.C., Symmons M.F., Sturtevant J.M., Marvin D.A., Perham R.N. Structure of the capsid of Pf3 filamentous phage determined from X-ray fibre diffraction data at 3.1Å resolution. J.Mol. Biol. 1998, 283:155-177.
    • (1998) J.Mol. Biol. , vol.283 , pp. 155-177
    • Welsh, L.C.1    Symmons, M.F.2    Sturtevant, J.M.3    Marvin, D.A.4    Perham, R.N.5
  • 386
    • 0034142068 scopus 로고    scopus 로고
    • The molecular structure and structural transition of the α-helical capsid in filamentous bacteriophage Pf1
    • Welsh L.C., Symmons M.F., Marvin D.A. The molecular structure and structural transition of the α-helical capsid in filamentous bacteriophage Pf1. Acta Crystallogr. 2000, D56:137-150.
    • (2000) Acta Crystallogr. , vol.56 , pp. 137-150
    • Welsh, L.C.1    Symmons, M.F.2    Marvin, D.A.3
  • 387
    • 1542297707 scopus 로고    scopus 로고
    • Ff gene 5 single-stranded DNA-binding protein assembles on nucleotides constrained by a DNA hairpin
    • Wen J.-D., Gray D.M. Ff gene 5 single-stranded DNA-binding protein assembles on nucleotides constrained by a DNA hairpin. Biochemistry 2004, 43:2622-2634.
    • (2004) Biochemistry , vol.43 , pp. 2622-2634
    • Wen, J.-D.1    Gray, D.M.2
  • 388
    • 0001425321 scopus 로고    scopus 로고
    • Structure and interactions of the single-stranded DNA genome of filamentous virus fd: investigation by ultraviolet resonance Raman spectroscopy
    • Wen Z.Q., Overman S.A., Thomas G.J. Structure and interactions of the single-stranded DNA genome of filamentous virus fd: investigation by ultraviolet resonance Raman spectroscopy. Biochemistry 1997, 36:7810-7820.
    • (1997) Biochemistry , vol.36 , pp. 7810-7820
    • Wen, Z.Q.1    Overman, S.A.2    Thomas, G.J.3
  • 389
    • 0024295024 scopus 로고
    • Mechanisms of membrane assembly: general lessons from the study of M13 coat protein and Escherichia coli leader peptidase
    • Wickner W. Mechanisms of membrane assembly: general lessons from the study of M13 coat protein and Escherichia coli leader peptidase. Biochemistry 1988, 27:1081-1086.
    • (1988) Biochemistry , vol.27 , pp. 1081-1086
    • Wickner, W.1
  • 390
    • 0029819873 scopus 로고    scopus 로고
    • Biophysical characterization of wild-type and mutant bacteriophage IKe major coat protein in the virion and in detergent micelles
    • Williams K.A., Deber C.M. Biophysical characterization of wild-type and mutant bacteriophage IKe major coat protein in the virion and in detergent micelles. Biochemistry 1996, 35:10472-10483.
    • (1996) Biochemistry , vol.35 , pp. 10472-10483
    • Williams, K.A.1    Deber, C.M.2
  • 391
    • 0029164701 scopus 로고
    • Packing of coat protein amphipathic and transmembrane helices in filamentous bacteriophage M13: role of small residues in protein oligomerization
    • Williams K.A., Glibowicka M., Li Z., Li H., Khan A.R., Chen Y.M., Wang J., Marvin D.A., Deber C.M. Packing of coat protein amphipathic and transmembrane helices in filamentous bacteriophage M13: role of small residues in protein oligomerization. J.Mol. Biol. 1995, 252:6-14.
    • (1995) J.Mol. Biol. , vol.252 , pp. 6-14
    • Williams, K.A.1    Glibowicka, M.2    Li, Z.3    Li, H.4    Khan, A.R.5    Chen, Y.M.6    Wang, J.7    Marvin, D.A.8    Deber, C.M.9
  • 392
    • 67650489237 scopus 로고    scopus 로고
    • Substrate-induced conformational change of the Escherichia coli membrane insertase YidC
    • Winterfeld S., Imhof N., Roos T., Bar G., Kuhn A., Gerken U. Substrate-induced conformational change of the Escherichia coli membrane insertase YidC. Biochemistry 2009, 48:6684-6691.
    • (2009) Biochemistry , vol.48 , pp. 6684-6691
    • Winterfeld, S.1    Imhof, N.2    Roos, T.3    Bar, G.4    Kuhn, A.5    Gerken, U.6
  • 393
    • 0017236783 scopus 로고
    • Different arrangements of protein subunits and single-stranded circular DNA in the filamentous bacterial viruses fd and Pf1
    • Wiseman R.L., Berkowitz S.A., Day L.A. Different arrangements of protein subunits and single-stranded circular DNA in the filamentous bacterial viruses fd and Pf1. J.Mol. Biol. 1976, 102:549-561.
    • (1976) J.Mol. Biol. , vol.102 , pp. 549-561
    • Wiseman, R.L.1    Berkowitz, S.A.2    Day, L.A.3
  • 394
    • 0037102135 scopus 로고    scopus 로고
    • Structure of the periplasmic domain of Pseudomonas aeruginosa TolA: evidence for an evolutionary relationship with the TonB transporter protein
    • Witty M., Sanz C., Shah A., Grossmann J.G., Mizuguchi K., Perham R.N., Luisi B. Structure of the periplasmic domain of Pseudomonas aeruginosa TolA: evidence for an evolutionary relationship with the TonB transporter protein. EMBO J. 2002, 21:4207-4218.
    • (2002) EMBO J. , vol.21 , pp. 4207-4218
    • Witty, M.1    Sanz, C.2    Shah, A.3    Grossmann, J.G.4    Mizuguchi, K.5    Perham, R.N.6    Luisi, B.7
  • 396
    • 0016378976 scopus 로고
    • F1 coat protein synthesis and altered phospholipid metabolism in f1 infected Escherichia coli
    • Woolford J.L., Cashman J.S., Webster R.E. f1 coat protein synthesis and altered phospholipid metabolism in f1 infected Escherichia coli. Virology 1974, 58:544-560.
    • (1974) Virology , vol.58 , pp. 544-560
    • Woolford, J.L.1    Cashman, J.S.2    Webster, R.E.3
  • 397
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm
    • Wright P.E., Dyson H.J. Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J.Mol. Biol. 1999, 293:321-331.
    • (1999) J.Mol. Biol. , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 398
    • 39149133696 scopus 로고    scopus 로고
    • Inserting proteins into the bacterial cytoplasmic membrane using the Sec and YidC translocases
    • Xie K., Dalbey R.E. Inserting proteins into the bacterial cytoplasmic membrane using the Sec and YidC translocases. Nat. Rev. Microbiol. 2008, 6:234-244.
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 234-244
    • Xie, K.1    Dalbey, R.E.2
  • 399
    • 0030984348 scopus 로고    scopus 로고
    • The A protein of the filamentous bacteriophage Cf of Xanthomonas campestrispv. citri
    • Yang M.K., Yang Y.C. The A protein of the filamentous bacteriophage Cf of Xanthomonas campestrispv. citri. J.Bacteriol. 1997, 179:2840-2844.
    • (1997) J.Bacteriol. , vol.179 , pp. 2840-2844
    • Yang, M.K.1    Yang, Y.C.2
  • 400
    • 33645019226 scopus 로고    scopus 로고
    • Isolation and characterization of Thermus bacteriophages
    • Yu M.X., Slater M.R., Ackermann H.-W. Isolation and characterization of Thermus bacteriophages. Arch. Virol. 2006, 151:663-679.
    • (2006) Arch. Virol. , vol.151 , pp. 663-679
    • Yu, M.X.1    Slater, M.R.2    Ackermann, H.-W.3
  • 401
    • 67650745346 scopus 로고    scopus 로고
    • Using dynamics-based comparisons to predict nucleic acid binding sites in proteins: an application to OB-fold domains
    • Zen A., de Chiara C., Pastore A., Micheletti C. Using dynamics-based comparisons to predict nucleic acid binding sites in proteins: an application to OB-fold domains. Bioinformatics 2009, 25:1876-1883.
    • (2009) Bioinformatics , vol.25 , pp. 1876-1883
    • Zen, A.1    de Chiara, C.2    Pastore, A.3    Micheletti, C.4
  • 402
    • 0038652081 scopus 로고    scopus 로고
    • Structure of the coat protein in fd filamentous bacteriophage particles determined by solid-state NMR spectroscopy
    • Zeri A.C., Mesleh M.F., Nevzorov A.A., Opella S.J. Structure of the coat protein in fd filamentous bacteriophage particles determined by solid-state NMR spectroscopy. Proc. Natl. Acad. Sci. U.S.A. 2003, 100:6458-6463.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 6458-6463
    • Zeri, A.C.1    Mesleh, M.F.2    Nevzorov, A.A.3    Opella, S.J.4
  • 403
    • 84871753290 scopus 로고    scopus 로고
    • Tuning chirality in the self-assembly of rod-like viruses by chemical surface modifications
    • Zhang Z.K., Grelet E. Tuning chirality in the self-assembly of rod-like viruses by chemical surface modifications. Soft Matter 2013, 9:1015-1024.
    • (2013) Soft Matter , vol.9 , pp. 1015-1024
    • Zhang, Z.K.1    Grelet, E.2
  • 404
    • 84877773919 scopus 로고    scopus 로고
    • Influences of membrane mimetic environments on membrane protein structures
    • Zhou H.X., Cross T.A. Influences of membrane mimetic environments on membrane protein structures. Annu. Rev. Biophys. 2013, 42:361-392.
    • (2013) Annu. Rev. Biophys. , vol.42 , pp. 361-392
    • Zhou, H.X.1    Cross, T.A.2
  • 405
    • 0022765760 scopus 로고
    • Single-stranded DNA-containing bacteriophages
    • Zinder N.D. Single-stranded DNA-containing bacteriophages. BioEssays 1986, 5:84-87.
    • (1986) BioEssays , vol.5 , pp. 84-87
    • Zinder, N.D.1
  • 406
    • 0009713525 scopus 로고
    • F1, A rod-shaped male-specific bacteriophage that contains DNA
    • Zinder N.D., Valentine R.C., Roger M., Stoeckenius W. F1, A rod-shaped male-specific bacteriophage that contains DNA. Virology 1963, 20:638-640.
    • (1963) Virology , vol.20 , pp. 638-640
    • Zinder, N.D.1    Valentine, R.C.2    Roger, M.3    Stoeckenius, W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.