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Volumn 414, Issue 4, 2011, Pages 499-510

The scope of phage display for membrane proteins

Author keywords

membrane proteins; mutagenesis; phage display; protein engineering; barrel membrane proteins

Indexed keywords

CAVEOLIN 1; EMERIN; F ACTIN; HEMOPROTEIN; MATRIPTASE; MEMBRANE PROTEIN; NEUROMODULIN; OUTER MEMBRANE PROTEIN; PROTEIN NOGO;

EID: 82555168245     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.10.021     Document Type: Article
Times cited : (13)

References (46)
  • 1
    • 0034213573 scopus 로고    scopus 로고
    • Do more complex organisms have a greater proportion of membrane proteins in their genomes?
    • DOI 10.1002/(SICI)1097-0134(20000601)39:4<417::AID-PROT140>3.0. CO;2-Y
    • Stevens T.J., and Arkin I.T. Do more complex organisms have a greater proportion of membrane proteins in their genomes? Proteins 39 2000 417 420 (Pubitemid 30414179)
    • (2000) Proteins: Structure, Function and Genetics , vol.39 , Issue.4 , pp. 417-420
    • Stevens, T.J.1    Arkin, I.T.2
  • 2
    • 0033767941 scopus 로고    scopus 로고
    • New roles for structure in biology and drug discovery
    • Russell R.B., and Eggleston D.S. New roles for structure in biology and drug discovery Nat. Struct. Biol. 7 2000 928 930
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 928-930
    • Russell, R.B.1    Eggleston, D.S.2
  • 3
    • 3042621274 scopus 로고    scopus 로고
    • The progress of membrane protein structure determination
    • DOI 10.1110/ps.04712004
    • White S.H. The progress of membrane protein structure determination Protein Sci. 13 2004 1948 1949 (Pubitemid 38822136)
    • (2004) Protein Science , vol.13 , Issue.7 , pp. 1948-1949
    • White, S.H.1
  • 4
    • 77953627340 scopus 로고    scopus 로고
    • Amphipols, nanodiscs, and fluorinated surfactants: Three nonconventional approaches to studying membrane proteins in aqueous solutions
    • Popot J.L. Amphipols, nanodiscs, and fluorinated surfactants: three nonconventional approaches to studying membrane proteins in aqueous solutions Annu. Rev. Biochem. 79 2010 737 775
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 737-775
    • Popot, J.L.1
  • 10
    • 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 228 1985 1315 1317 (Pubitemid 15000355)
    • (1985) Science , vol.228 , Issue.4705 , pp. 1315-1317
    • Smith, G.P.1
  • 11
    • 0000627452 scopus 로고
    • Rapid evolution of peptide and protein binding properties in vitro
    • Wells J.A., and Lowman H.B. Rapid evolution of peptide and protein binding properties in vitro Curr. Opin. Struct. Biol. 2 1992 597 604
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 597-604
    • Wells, J.A.1    Lowman, H.B.2
  • 12
    • 28444488346 scopus 로고    scopus 로고
    • Filamentous phage display in the new millennium
    • DOI 10.1021/cr000261r
    • Kehoe J.W., and Kay B.K. Filamentous phage display in the new millennium Chem. Rev. 105 2005 4056 4072 (Pubitemid 41724069)
    • (2005) Chemical Reviews , vol.105 , Issue.11 , pp. 4056-4072
    • Kehoe, J.W.1    Kay, B.K.2
  • 14
    • 55249122654 scopus 로고    scopus 로고
    • Phage display of functional, full-length human and viral membrane proteins
    • Majumdar S., Hajduczki A., Mendez A.S., and Weiss G.A. Phage display of functional, full-length human and viral membrane proteins Bioorg. Med. Chem. Lett. 18 2008 5937 5940
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , pp. 5937-5940
    • Majumdar, S.1    Hajduczki, A.2    Mendez, A.S.3    Weiss, G.A.4
  • 15
    • 0028223378 scopus 로고
    • In vitro selection from protein and peptide libraries
    • DOI 10.1016/0167-7799(94)90079-5
    • Clackson T., and Wells J.A. In vitro selection from protein and peptide libraries Trends Biotechnol. 12 1994 173 184 (Pubitemid 24160424)
    • (1994) Trends in Biotechnology , vol.12 , Issue.5 , pp. 173-184
    • Clackson, T.1    Wells, J.A.2
  • 16
    • 0031876195 scopus 로고    scopus 로고
    • Phage display: Applications, innovations, and issues in phage and host biology
    • Wilson D.R., and Finlay B.B. Phage display: applications, innovations, and issues in phage and host biology Can. J. Microbiol. 44 1998 313 329
    • (1998) Can. J. Microbiol. , vol.44 , pp. 313-329
    • Wilson, D.R.1    Finlay, B.B.2
  • 17
    • 0037333841 scopus 로고    scopus 로고
    • mRNA display: Ligand discovery, interaction analysis and beyond
    • DOI 10.1016/S0968-0004(03)00036-7
    • Takahashi T.T., Austin R.J., and Roberts R.W. mRNA display: ligand discovery, interaction analysis and beyond Trends Biochem. Sci. 28 2003 159 165 (Pubitemid 36293854)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.3 , pp. 159-165
    • Takahashi, T.T.1    Austin, R.J.2    Roberts, R.W.3
  • 18
    • 17044426359 scopus 로고    scopus 로고
    • A twin-arginine translocation (Tat)-mediated phage display system
    • Paschke M., and Hohne W. A twin-arginine translocation (Tat)-mediated phage display system Gene 350 2005 79 88
    • (2005) Gene , vol.350 , pp. 79-88
    • Paschke, M.1    Hohne, W.2
  • 19
    • 0034093301 scopus 로고    scopus 로고
    • Mutational analysis of the major coat protein of M13 identifies residues that control protein display
    • Weiss G.A., Wells J.A., and Sidhu S.S. Mutational analysis of the major coat protein of M13 identifies residues that control protein display Protein Sci. 9 2000 647 654 (Pubitemid 30217613)
    • (2000) Protein Science , vol.9 , Issue.4 , pp. 647-654
    • Weiss, G.A.1    Wells, J.A.2    Sidhu, S.S.3
  • 20
    • 2642652226 scopus 로고    scopus 로고
    • Selection for a periplasmic factor improving phage display and functional periplasmic expression
    • DOI 10.1038/nbt0498-376
    • Bothmann H., and Pluckthun A. Selection for a periplasmic factor improving phage display and functional periplasmic expression Nat. Biotechnol. 16 1998 376 380 (Pubitemid 28164659)
    • (1998) Nature Biotechnology , vol.16 , Issue.4 , pp. 376-380
    • Bothmann, H.1    Pluckthun, A.2
  • 21
    • 33746161571 scopus 로고    scopus 로고
    • Signal sequences directing cotranslational translocation expand the range of proteins amenable to phage display
    • DOI 10.1038/nbt1218, PII NBT1218
    • Steiner D., Forrer P., Stumpp M.T., and Pluckthun A. Signal sequences directing cotranslational translocation expand the range of proteins amenable to phage display Nat. Biotechnol. 24 2006 823 831 (Pubitemid 44086624)
    • (2006) Nature Biotechnology , vol.24 , Issue.7 , pp. 823-831
    • Steiner, D.1    Forrer, P.2    Stumpp, M.T.3    Pluckthun, A.4
  • 22
    • 0015514472 scopus 로고
    • The fluid mosaic model of the structure of cell membranes
    • Singer S.J., and Nicolson G.L. The fluid mosaic model of the structure of cell membranes Science 175 1972 720 731
    • (1972) Science , vol.175 , pp. 720-731
    • Singer, S.J.1    Nicolson, G.L.2
  • 23
    • 0032875098 scopus 로고    scopus 로고
    • Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins
    • DOI 10.1016/S0167-4889(99)00075-0, PII S0167488999000750
    • Resh M.D. Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins Biochim. Biophys. Acta 1451 1999 1 16 (Pubitemid 29364242)
    • (1999) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1451 , Issue.1 , pp. 1-16
    • Resh, M.D.1
  • 25
    • 0023944337 scopus 로고
    • Cell-surface anchoring of proteins via glycosyl-phosphatidylinositol structures
    • Ferguson M.A., and Williams A.F. Cell-surface anchoring of proteins via glycosyl-phosphatidylinositol structures Annu. Rev. Biochem. 57 1988 285 320
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 285-320
    • Ferguson, M.A.1    Williams, A.F.2
  • 26
    • 0037031868 scopus 로고    scopus 로고
    • Mass spectrometric analysis of GAP-43/neuromodulin reveals the presence of a variety of fatty acylated species
    • DOI 10.1074/jbc.M204607200
    • Liang X., Lu Y., Neubert T.A., and Resh M.D. Mass spectrometric analysis of GAP-43/neuromodulin reveals the presence of a variety of fatty acylated species J. Biol. Chem. 277 2002 33032 33040 (Pubitemid 34984818)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.36 , pp. 33032-33040
    • Liang, X.1    Lu, Y.2    Neubert, T.A.3    Resh, M.D.4
  • 27
    • 0031009292 scopus 로고    scopus 로고
    • Modulation of actin filament behavior by GAP-43 (neuromodulin) is dependent on the phosphorylation status of serine 41, the protein kinase C site
    • He Q., Dent E.W., and Meiri K.F. Modulation of actin filament behavior by GAP-43 (neuromodulin) is dependent on the phosphorylation status of serine 41, the protein kinase C site J. Neurosci. 17 1997 3515 3524 (Pubitemid 27200580)
    • (1997) Journal of Neuroscience , vol.17 , Issue.10 , pp. 3515-3524
    • He, Q.1    Dent, E.W.2    Meiri, K.F.3
  • 28
    • 0025965848 scopus 로고
    • Characterization of the calmodulin binding domain of neuromodulin: Functional significance of serine 41 and phenylalanine 42
    • Chapman E.R., Au D., Alexander K.A., Nicolson T.A., and Storm D.R. Characterization of the calmodulin binding domain of neuromodulin. Functional significance of serine 41 and phenylalanine 42 J. Biol. Chem. 266 1991 207 213 (Pubitemid 21906110)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.1 , pp. 207-213
    • Chapman, E.R.1    Au, D.2    Alexander, K.A.3    Nicolson, T.A.4    Storm, D.R.5
  • 29
    • 0037931791 scopus 로고    scopus 로고
    • A phage display-based method for determination of relative affinities of mutants. Application to the actin-binding motifs in thymosin β4 and the villin headpiece
    • DOI 10.1074/jbc.M208311200
    • Rossenu S., Leyman S., Dewitte D., Peelaers D., Jonckheere V., and Van Troys M. A phage display-based method for determination of relative affinities of mutants. Application to the actin-binding motifs in thymosin beta 4 and the villin headpiece J. Biol. Chem. 278 2003 16642 16650 (Pubitemid 36799527)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.19 , pp. 16642-16650
    • Rossenu, S.1    Leyman, S.2    Dewitte, D.3    Peelaers, D.4    Jonckheere, V.5    Van Troys, M.6    Vandekerckhove, J.7    Ampe, C.8
  • 30
    • 0018987976 scopus 로고
    • Intracellular protein topogenesis
    • Blobel G. Intracellular protein topogenesis Proc. Natl Acad. Sci. USA 77 1980 1496 1500
    • (1980) Proc. Natl Acad. Sci. USA , vol.77 , pp. 1496-1500
    • Blobel, G.1
  • 31
    • 33144486308 scopus 로고    scopus 로고
    • NMR structure and molecular dynamics of the in-plane membrane anchor of nonstructural protein 5A from bovine viral diarrhea virus
    • DOI 10.1021/bi0517685
    • Sapay N., Montserret R., Chipot C., Brass V., Moradpour D., Deleage G., and Penin F. NMR structure and molecular dynamics of the in-plane membrane anchor of nonstructural protein 5A from bovine viral diarrhea virus Biochemistry 45 2006 2221 2233 (Pubitemid 43271321)
    • (2006) Biochemistry , vol.45 , Issue.7 , pp. 2221-2233
    • Sapay, N.1    Montserret, R.2    Chipot, C.3    Brass, V.4    Moradpour, D.5    Deleage, G.6    Penin, F.7
  • 32
    • 64349113647 scopus 로고    scopus 로고
    • Interaction of monotopic membrane enzymes with a lipid bilayer: A coarse-grained MD simulation study
    • Balali-Mood K., Bond P.J., and Sansom M.S. Interaction of monotopic membrane enzymes with a lipid bilayer: a coarse-grained MD simulation study Biochemistry 48 2009 2135 2145
    • (2009) Biochemistry , vol.48 , pp. 2135-2145
    • Balali-Mood, K.1    Bond, P.J.2    Sansom, M.S.3
  • 33
    • 77951066645 scopus 로고    scopus 로고
    • Protein folding at the membrane interface, the structure of Nogo-66 requires interactions with a phosphocholine surface
    • Vasudevan S.V., Schulz J., Zhou C., and Cocco M.J. Protein folding at the membrane interface, the structure of Nogo-66 requires interactions with a phosphocholine surface Proc. Natl Acad. Sci. USA 107 2010 6847 6851
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 6847-6851
    • Vasudevan, S.V.1    Schulz, J.2    Zhou, C.3    Cocco, M.J.4
  • 35
    • 0021152462 scopus 로고
    • Three-dimensional structure of membrane and surface proteins
    • Eisenberg D. Three-dimensional structure of membrane and surface proteins Annu. Rev. Biochem. 53 1984 595 623
    • (1984) Annu. Rev. Biochem. , vol.53 , pp. 595-623
    • Eisenberg, D.1
  • 36
  • 37
    • 34447508443 scopus 로고    scopus 로고
    • Characterization of the outer membrane receptor ShuA from the heme uptake system of Shigella dysenteriae: Substrate specificity and identification of the heme protein ligands
    • DOI 10.1074/jbc.M611121200
    • Burkhard K.A., and Wilks A. Characterization of the outer membrane receptor ShuA from the heme uptake system of Shigella dysenteriae. Substrate specificity and identification of the heme protein ligands J. Biol. Chem. 282 2007 15126 15136 (Pubitemid 47093339)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.20 , pp. 15126-15136
    • Burkhard, K.A.1    Wilks, A.2
  • 38
    • 77449152698 scopus 로고    scopus 로고
    • Structure of the heme/hemoglobin outer membrane receptor ShuA from Shigella dysenteriae: Heme binding by an induced fit mechanism
    • Cobessi D., Meksem A., and Brillet K. Structure of the heme/hemoglobin outer membrane receptor ShuA from Shigella dysenteriae: heme binding by an induced fit mechanism Proteins 78 2010 286 294
    • (2010) Proteins , vol.78 , pp. 286-294
    • Cobessi, D.1    Meksem, A.2    Brillet, K.3
  • 40
    • 12544255082 scopus 로고    scopus 로고
    • Receptor-selective mutants of apoptosis-inducing ligand 2/tumor necrosis factor-related apoptosis-inducing ligand reveal a greater contribution of death receptor (DR) 5 than DR4 to apoptosis signaling
    • Kelley R.F., Totpal K., Lindstrom S.H., Mathieu M., Billeci K., and Deforge L. Receptor-selective mutants of apoptosis-inducing ligand 2/tumor necrosis factor-related apoptosis-inducing ligand reveal a greater contribution of death receptor (DR) 5 than DR4 to apoptosis signaling J. Biol. Chem. 280 2005 2205 2212
    • (2005) J. Biol. Chem. , vol.280 , pp. 2205-2212
    • Kelley, R.F.1    Totpal, K.2    Lindstrom, S.H.3    Mathieu, M.4    Billeci, K.5    Deforge, L.6
  • 41
    • 0037984384 scopus 로고    scopus 로고
    • Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide
    • DOI 10.1074/jbc.M211177200
    • Bulieris P.V., Behrens S., Holst O., and Kleinschmidt J.H. Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide J. Biol. Chem. 278 2003 9092 9099 (Pubitemid 36800389)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.11 , pp. 9092-9099
    • Bulieris, P.V.1    Behrens, S.2    Holst, O.3    Kleinschmidt, J.H.4
  • 42
    • 0029918686 scopus 로고    scopus 로고
    • SurA assists the folding of Escherichia coli outer membrane proteins
    • Lazar S.W., and Kolter R. SurA assists the folding of Escherichia coli outer membrane proteins J. Bacteriol. 178 1996 1770 1773 (Pubitemid 26085629)
    • (1996) Journal of Bacteriology , vol.178 , Issue.6 , pp. 1770-1773
    • Lazar, S.W.1    Kolter, R.2
  • 43
    • 0037325329 scopus 로고    scopus 로고
    • EF-Tu binding peptides identified, dissected, and affinity optimized by phage display
    • DOI 10.1016/S1074-5521(03)00025-5
    • Murase K., Morrison K.L., Tam P.Y., Stafford R.L., Jurnak F., and Weiss G.A. EF-Tu binding peptides identified, dissected, and affinity optimized by phage display Chem. Biol. 10 2003 161 168 (Pubitemid 36250974)
    • (2003) Chemistry and Biology , vol.10 , Issue.2 , pp. 161-168
    • Murase, K.1    Morrison, K.L.2    Tam, P.Y.3    Stafford, R.L.4    Jurnak, F.5    Weiss, G.A.6
  • 44
    • 0034681299 scopus 로고    scopus 로고
    • High copy display of large proteins on phage for functional selections
    • Sidhu S.S., Weiss G.A., and Wells J.A. High copy display of large proteins on phage for functional selections J. Mol. Biol. 296 2000 487 495
    • (2000) J. Mol. Biol. , vol.296 , pp. 487-495
    • Sidhu, S.S.1    Weiss, G.A.2    Wells, J.A.3
  • 45
    • 0347634533 scopus 로고    scopus 로고
    • Bivalent antibody phage display mimics natural immunoglobulin
    • DOI 10.1016/j.jim.2003.11.001
    • Lee C.V., Sidhu S.S., and Fuh G. Bivalent antibody phage display mimics natural immunoglobulin J. Immunol. Methods 284 2004 119 132 (Pubitemid 38084919)
    • (2004) Journal of Immunological Methods , vol.284 , Issue.1-2 , pp. 119-132
    • Lee, C.V.1    Sidhu, S.S.2    Fuh, G.3


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