메뉴 건너뛰기




Volumn 8, Issue , 2011, Pages

Site directed biotinylation of filamentous phage structural proteins

Author keywords

biotinylation; combinatorial libraries; filamentous bacteriophage; phage display

Indexed keywords

DNA POLYMERASE; ISOPROPYL THIOGALACTOSIDE; OLIGONUCLEOTIDE; RECOMBINANT PROTEIN; STRUCTURAL PROTEIN; VIRUS PROTEIN;

EID: 80055031685     PISSN: None     EISSN: 1743422X     Source Type: Journal    
DOI: 10.1186/1743-422X-8-495     Document Type: Article
Times cited : (12)

References (44)
  • 1
    • 0025293361 scopus 로고
    • Biotination of proteins in vivo. A post-translational modification to label, purify, and study proteins
    • 2113052
    • Biotination of proteins in vivo. A post-translational modification to label, purify, and study proteins. Cronan JE Jr, J Biol Chem 1990 265 18 10327 10333 2113052
    • (1990) J Biol Chem , vol.265 , Issue.18 , pp. 10327-10333
    • Cronan, J.E.1    Jr2
  • 2
    • 0015091997 scopus 로고
    • Acetyl CoA carboxylase: Isolation and characterization of native biotin carboxyl carrier protein
    • 10.1073/pnas.68.7.1512 4934522
    • Acetyl CoA carboxylase: isolation and characterization of native biotin carboxyl carrier protein. Fall RR, Nervi AM, Alberts AW, Vagelos PR, Proc Natl Acad Sci USA 1971 68 7 1512 1515 10.1073/pnas.68.7.1512 4934522
    • (1971) Proc Natl Acad Sci USA , vol.68 , Issue.7 , pp. 1512-1515
    • Fall, R.R.1    Nervi, A.M.2    Alberts, A.W.3    Vagelos, P.R.4
  • 5
    • 0023876319 scopus 로고
    • The avidin-biotin complex in bioanalytical applications
    • 10.1016/0003-2697(88)90120-0 3044183
    • The avidin-biotin complex in bioanalytical applications. Wilchek M, Bayer EA, Anal Biochem 1988 171 1 1 32 10.1016/0003-2697(88)90120-0 3044183
    • (1988) Anal Biochem , vol.171 , Issue.1 , pp. 1-32
    • Wilchek, M.1    Bayer, E.A.2
  • 6
    • 31544481163 scopus 로고    scopus 로고
    • Essentials of biorecognition: The (strept)avidin-biotin system as a model for protein-protein and protein-ligand interaction
    • DOI 10.1016/j.imlet.2005.10.022, PII S016524780500338X, Catalytic Antibodies
    • Essentials of biorecognition: the (strept)avidin-biotin system as a model for protein-protein and protein-ligand interaction. Wilchek M, Bayer EA, Livnah O, Immunol Lett 2006 103 1 27 32 10.1016/j.imlet.2005.10.022 16325268 (Pubitemid 43162942)
    • (2006) Immunology Letters , vol.103 , Issue.1 , pp. 27-32
    • Wilchek, M.1    Bayer, E.A.2    Livnah, O.3
  • 7
    • 0026502763 scopus 로고
    • The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase
    • 1370469
    • The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase. Li SJ, Cronan JE Jr, J Biol Chem 1992 267 2 855 863 1370469
    • (1992) J Biol Chem , vol.267 , Issue.2 , pp. 855-863
    • Li, S.J.1    Jr E., C.J.2
  • 8
    • 0032007565 scopus 로고    scopus 로고
    • Selectivity of post-translational modification in biotinylated proteins: The carboxy carrier protein of the acetyl-CoA carboxylase of Escherichia coli
    • Selectivity of post-translational modification in biotinylated proteins: the carboxy carrier protein of the acetyl-CoA carboxylase of Escherichia coli. Reche P, Li YL, Fuller C, Eichhorn K, Perham RN, Biochem J 1998 329 Pt 3 589 596 9445386 (Pubitemid 28055181)
    • (1998) Biochemical Journal , vol.329 , Issue.3 , pp. 589-596
    • Reche, P.1    Li, Y.-L.2    Fuller, C.3    Eichhorn, K.4    Perham, R.N.5
  • 9
    • 0019482402 scopus 로고
    • The birA gene of Escherichia coli encodes a biotin holoenzyme synthetase
    • DOI 10.1016/0022-2836(81)90042-5
    • The birA gene of Escherichia coli encodes a biotin holoenzyme synthetase. Barker DF, Campbell AM, J Mol Biol 1981 146 4 451 467 10.1016/0022-2836(81) 90042-5 7024555 (Pubitemid 11100437)
    • (1981) Journal of Molecular Biology , vol.146 , Issue.4 , pp. 451-467
    • Barker, D.F.1    Campbell, A.M.2
  • 10
    • 0033621510 scopus 로고    scopus 로고
    • In vivo enzymatic protein biotinylation
    • DOI 10.1016/S1050-3862(99)00046-7, PII S1050386299000467
    • In vivo enzymatic protein biotinylation. Chapman-Smith A, Cronan JE Jr, Biomol Eng 1999 16 1-4 119 125 10.1016/S1050-3862(99)00046-7 10796994 (Pubitemid 30184848)
    • (1999) Biomolecular Engineering , vol.16 , Issue.1-4 , pp. 119-125
    • Chapman-Smith, A.1    Cronan Jr., J.E.2
  • 11
    • 0033819032 scopus 로고    scopus 로고
    • Biotinylation of proteins in vivo: A useful posttranslational modification for protein analysis
    • 11036657
    • Biotinylation of proteins in vivo: a useful posttranslational modification for protein analysis. Cronan JE Jr, Reed KE, Methods Enzymol 2000 326 440 458 11036657
    • (2000) Methods Enzymol , vol.326 , pp. 440-458
    • Cronan Jr., J.E.1    Reed, K.E.2
  • 12
    • 0032573515 scopus 로고    scopus 로고
    • Bacteriophage lambda surface display of a bacterial biotin acceptor domain reveals the minimal peptide size required for biotinylation
    • DOI 10.1016/S0014-5793(98)01454-9, PII S0014579398014549
    • Bacteriophage lambda surface display of a bacterial biotin acceptor domain reveals the minimal peptide size required for biotinylation. Stolz J, Ludwig A, Sauer N, FEBS Lett 1998 440 1-2 213 217 10.1016/S0014-5793(98)01454-9 9862457 (Pubitemid 28558767)
    • (1998) FEBS Letters , vol.440 , Issue.1-2 , pp. 213-217
    • Stolz, J.1    Ludwig, A.2    Sauer, N.3
  • 13
    • 0039310043 scopus 로고
    • Use of peptide libraries to map the substrate specificity of a peptide- modifying enzyme: A 13 residue consensus peptide specifies biotinylation in Escherichia coli
    • Use of peptide libraries to map the substrate specificity of a peptide-modifying enzyme: a 13 residue consensus peptide specifies biotinylation in Escherichia coli. Schatz PJ, Biotechnology (N Y) 1993 11 10 1138 1143 10.1038/nbt1093-1138 (Pubitemid 23307458)
    • (1993) Bio/Technology , vol.11 , Issue.10 , pp. 1138-1143
    • Schatz, P.J.1
  • 14
    • 0035874389 scopus 로고    scopus 로고
    • The rational design of a 'type 88' genetically stable peptide display vector in the filamentous bacteriophage fd
    • 10.1093/nar/29.10.e50 11353095
    • The rational design of a 'type 88' genetically stable peptide display vector in the filamentous bacteriophage fd. Enshell-Seijffers D, Smelyanski L, Gershoni JM, Nucleic Acids Res 2001 29 10 50 50 10.1093/nar/29.10.e50 11353095
    • (2001) Nucleic Acids Res , vol.29 , Issue.10 , pp. 550-50
    • Enshell-Seijffers, D.1    Smelyanski, L.2    Gershoni, J.M.3
  • 15
    • 68949164705 scopus 로고    scopus 로고
    • Phage display selection, analysis, and prediction of B cell epitopes
    • 19653209
    • Phage display selection, analysis, and prediction of B cell epitopes. Freund NT, Enshell-Seijffers D, Gershoni JM, Curr Protoc Immunol 2009 Chapter 9 Unit 9 8 19653209
    • (2009) Curr Protoc Immunol , vol.9 , Issue.UNIT 9 , pp. 8
    • Freund, N.T.1    Enshell-Seijffers, D.2    Gershoni, J.M.3
  • 17
    • 0034810895 scopus 로고    scopus 로고
    • Dissection of the humoral immune response toward an immunodominant epitope of HIV: A model for the analysis of antibody diversity in HIV+ individuals
    • DOI 10.1096/fj.00-0898com
    • Dissection of the humoral immune response toward an immunodominant epitope of HIV: a model for the analysis of antibody diversity in HIV+ individuals. Enshell-Seijffers D, Smelyanski L, Vardinon N, Yust I, Gershoni JM, FASEB J 2001 15 12 2112 2120 10.1096/fj.00-0898com 11641237 (Pubitemid 32927928)
    • (2001) FASEB Journal , vol.15 , Issue.12 , pp. 2112-2120
    • Enshell-Seijffers, D.1    Smelyanski, L.2    Vardinon, N.3    Yust, I.4    Gershoni, J.M.5
  • 18
    • 0029793463 scopus 로고    scopus 로고
    • A library of organic landscapes on filamentous phage
    • A library of organic landscapes on filamentous phage. Petrenko VA, Smith GP, Gong X, Quinn T, Protein Eng 1996 9 9 797 801 10.1093/protein/9.9.797 8888146 (Pubitemid 26308528)
    • (1996) Protein Engineering , vol.9 , Issue.9 , pp. 797-801
    • Petrenko, V.A.1    Smith, G.P.2    Gong, X.3    Quinn, T.4
  • 19
    • 0025112794 scopus 로고
    • Searching for peptide ligands with an epitope library
    • 10.1126/science.1696028 1696028
    • Searching for peptide ligands with an epitope library. Scott JK, Smith GP, Science 1990 249 4967 386 390 10.1126/science.1696028 1696028
    • (1990) Science , vol.249 , Issue.4967 , pp. 386-390
    • Scott, J.K.1    Smith, G.P.2
  • 21
    • 0027962758 scopus 로고
    • Making antibodies by phage display technology
    • 10.1146/annurev.iy.12.040194.002245 8011287
    • Making antibodies by phage display technology. Winter G, Griffiths AD, Hawkins RE, Hoogenboom HR, Annu Rev Immunol 1994 12 433 455 10.1146/annurev.iy. 12.040194.002245 8011287
    • (1994) Annu Rev Immunol , vol.12 , pp. 433-455
    • Winter, G.1    Griffiths, A.D.2    Hawkins, R.E.3    Hoogenboom, H.R.4
  • 22
    • 0034887457 scopus 로고    scopus 로고
    • Engineering M13 for phage display
    • DOI 10.1016/S1389-0344(01)00087-9, PII S1389034401000879
    • Engineering M13 for phage display. Sidhu SS, Biomol Eng 2001 18 2 57 63 10.1016/S1389-0344(01)00087-9 11535417 (Pubitemid 32776595)
    • (2001) Biomolecular Engineering , vol.18 , Issue.2 , pp. 57-63
    • Sidhu, S.S.1
  • 23
    • 0032054113 scopus 로고    scopus 로고
    • Filamentous phage structure, infection and assembly
    • DOI 10.1016/S0959-440X(98)80032-8
    • Filamentous phage structure, infection and assembly. Marvin DA, Curr Opin Struct Biol 1998 8 2 150 158 10.1016/S0959-440X(98)80032-8 9631287 (Pubitemid 28221045)
    • (1998) Current Opinion in Structural Biology , vol.8 , Issue.2 , pp. 150-158
    • Marvin, D.1
  • 25
    • 0023661694 scopus 로고
    • Interactions between DNA and coat protein in the structure and assembly of filamentous bacteriophage fd
    • Interactions between DNA and coat protein in the structure and assembly of filamentous bacteriophage fd. Hunter GJ, Rowitch DH, Perham RN, Nature 1987 327 6119 252 254 10.1038/327252a0 3106834 (Pubitemid 17071058)
    • (1987) Nature , vol.326 , Issue.6119 , pp. 252-254
    • Hunter, G.J.1    Rowitch, D.H.2    Perham, R.N.3
  • 26
    • 0025899542 scopus 로고
    • Multiple display of foreign peptides on a filamentous bacteriophage. Peptides from Plasmodium falciparum circumsporozoite protein as antigens
    • 10.1016/0022-2836(91)90354-9 1880799
    • Multiple display of foreign peptides on a filamentous bacteriophage. Peptides from Plasmodium falciparum circumsporozoite protein as antigens. Greenwood J, Willis AE, Perham RN, J Mol Biol 1991 220 4 821 827 10.1016/0022-2836(91)90354-9 1880799
    • (1991) J Mol Biol , vol.220 , Issue.4 , pp. 821-827
    • Greenwood, J.1    Willis, A.E.2    Perham, R.N.3
  • 27
    • 0027298951 scopus 로고
    • Preface. Surface display and peptide libraries
    • DOI 10.1016/0378-1119(93)90145-S
    • Surface Display and Peptide Libraries. Smith GP, Gene 1993 128 1 2 10.1016/0378-1119(93)90145-S 8508950 (Pubitemid 23179202)
    • (1993) Gene , vol.128 , Issue.1 , pp. 1-2
    • Smith, G.P.1
  • 29
    • 0024384323 scopus 로고
    • Genetic analysis of the filamentous bacteriophage packaging signal and of the proteins that interact with it
    • Genetic analysis of the filamentous bacteriophage packaging signal and of the proteins that interact with it. Russel M, Model P, J Virol 1989 63 8 3284 3295 2746731 (Pubitemid 19181385)
    • (1989) Journal of Virology , vol.63 , Issue.8 , pp. 3284-3295
    • Russel, M.1    Model, P.2
  • 30
    • 0029087064 scopus 로고
    • Location of filamentous phage minor coat proteins in phage and in infected cells
    • 10.1006/jmbi.1995.0393 7616570
    • Location of filamentous phage minor coat proteins in phage and in infected cells. Endemann H, Model P, J Mol Biol 1995 250 4 496 506 10.1006/jmbi.1995.0393 7616570
    • (1995) J Mol Biol , vol.250 , Issue.4 , pp. 496-506
    • Endemann, H.1    Model, P.2
  • 32
    • 0037432155 scopus 로고    scopus 로고
    • A morphologic study of filamentous phage infection of Escherichia coli using biotinylated phages
    • DOI 10.1016/S0014-5793(03)00050-4
    • A morphologic study of filamentous phage infection of Escherichia coli using biotinylated phages. Nakamura M, Tsumoto K, Kumagai I, Ishimura K, FEBS Lett 2003 536 1-3 167 172 10.1016/S0014-5793(03)00050-4 12586358 (Pubitemid 36206426)
    • (2003) FEBS Letters , vol.536 , Issue.1-3 , pp. 167-172
    • Nakamura, M.1    Tsumoto, K.2    Kumagai, I.3    Ishimura, K.4
  • 33
    • 0035433673 scopus 로고    scopus 로고
    • Use of bioluminescent Salmonella for assessing the efficiency of constructed phage-based biosorbent
    • DOI 10.1038/sj.jim.7000198
    • Use of bioluminescent Salmonella for assessing the efficiency of constructed phage-based biosorbent. Sun W, Brovko L, Griffiths M, J Ind Microbiol Biotechnol 2001 27 2 126 128 10.1038/sj.jim.7000198 11641771 (Pubitemid 33702313)
    • (2001) Journal of Industrial Microbiology and Biotechnology , vol.27 , Issue.2 , pp. 126-128
    • Sun, W.1    Brovko, L.2    Griffiths, M.3
  • 34
    • 9644307228 scopus 로고    scopus 로고
    • Biotin-tagged cDNA expression libraries displayed on lambda phage: A new tool for the selection of natural protein ligands
    • 10.1093/nar/gnf077 12140340
    • Biotin-tagged cDNA expression libraries displayed on lambda phage: a new tool for the selection of natural protein ligands. Ansuini H, Cicchini C, Nicosia A, Tripodi M, Cortese R, Luzzago A, Nucleic Acids Res 2002 30 15 78 10.1093/nar/gnf077 12140340
    • (2002) Nucleic Acids Res , vol.30 , Issue.15 , pp. 578
    • Ansuini, H.1    Cicchini, C.2    Nicosia, A.3    Tripodi, M.4    Cortese, R.5    Luzzago, A.6
  • 35
    • 0028999019 scopus 로고
    • Moving through the membrane with filamentous phages
    • 10.1016/S0966-842X(00)88929-5 7648030
    • Moving through the membrane with filamentous phages. Russel M, Trends Microbiol 1995 3 6 223 228 10.1016/S0966-842X(00)88929-5 7648030
    • (1995) Trends Microbiol , vol.3 , Issue.6 , pp. 223-228
    • Russel, M.1
  • 36
    • 0030983210 scopus 로고    scopus 로고
    • Filamentous phage assembly: Variation on a protein export theme
    • DOI 10.1016/S0378-1119(96)00801-3, PII S0378111996008013
    • Filamentous phage assembly: variation on a protein export theme. Russel M, Linderoth NA, Sali A, Gene 1997 192 1 23 32 10.1016/S0378-1119(96)00801-3 9224870 (Pubitemid 27267475)
    • (1997) Gene , vol.192 , Issue.1 , pp. 23-32
    • Russel, M.1    Linderoth, N.A.2    Sali, A.3
  • 37
    • 0030570513 scopus 로고    scopus 로고
    • Role of capsid structure and membrane protein processing in determining the size and copy number of peptides displayed on the major coat protein of filamentous bacteriophage
    • DOI 10.1006/jmbi.1996.0378
    • Role of capsid structure and membrane protein processing in determining the size and copy number of peptides displayed on the major coat protein of filamentous bacteriophage. Malik P, Terry TD, Gowda LR, Langara A, Petukhov SA, Symmons MF, Welsh LC, Marvin DA, Perham RN, J Mol Biol 1996 260 1 9 21 10.1006/jmbi.1996.0378 8676395 (Pubitemid 26241387)
    • (1996) Journal of Molecular Biology , vol.260 , Issue.1 , pp. 9-21
    • Malik, P.1    Terry, T.D.2    Gowda, L.R.3    Langara, A.4    Petukhov, S.A.5    Symmons, M.F.6    Welsh, L.C.7    Marvin, D.A.8    Perham, R.N.9
  • 38
    • 0032508578 scopus 로고    scopus 로고
    • Roles of pIII in filamentous phage assembly
    • DOI 10.1006/jmbi.1998.2006
    • Roles of pIII in filamentous phage assembly. Rakonjac J, Model P, J Mol Biol 1998 282 1 25 41 10.1006/jmbi.1998.2006 9733639 (Pubitemid 28418658)
    • (1998) Journal of Molecular Biology , vol.282 , Issue.1 , pp. 25-41
    • Rakonjac, J.1    Model, P.2
  • 39
    • 0030014628 scopus 로고    scopus 로고
    • Biotinylation in vivo as a sensitive indicator of protein secretion and membrane protein insertion
    • Biotinylation in vivo as a sensitive indicator of protein secretion and membrane protein insertion. Jander G, Cronan JE Jr, Beckwith J, J Bacteriol 1996 178 11 3049 3058 8655479 (Pubitemid 26170021)
    • (1996) Journal of Bacteriology , vol.178 , Issue.11 , pp. 3049-3058
    • Jander, G.1    Cronan Jr., J.E.2    Beckwith, J.3
  • 40
    • 0026001727 scopus 로고
    • Escherichia coli exports previously folded biotinated protein domains
    • Escherichia coli exports previously folded and biotinated protein domains. Reed KE, Cronan JE Jr, J Biol Chem 1991 266 18 11425 11428 2050659 (Pubitemid 21906966)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.18 , pp. 11425-11428
    • Reed, K.E.1    Cronan Jr., J.E.2
  • 42
    • 27144463438 scopus 로고    scopus 로고
    • Biogenesis of inner membrane proteins in Escherichia coli
    • DOI 10.1146/annurev.micro.59.030804.121246
    • Biogenesis of inner membrane proteins in Escherichia coli. Luirink J, von Heijne G, Houben E, de Gier JW, Annu Rev Microbiol 2005 59 329 355 10.1146/annurev.micro.59.030804.121246 16153172 (Pubitemid 41507435)
    • (2005) Annual Review of Microbiology , vol.59 , pp. 329-355
    • Luirink, J.1    Von Heijne, G.2    Houben, E.3    De Gier, J.-W.4
  • 43
    • 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
    • Signal sequences directing cotranslational translocation expand the range of proteins amenable to phage display. Steiner D, Forrer P, Stumpp MT, Pluckthun A, Nat Biotechnol 2006 24 7 823 831 10.1038/nbt1218 16823375 (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
  • 44
    • 33646797435 scopus 로고    scopus 로고
    • Mapping protease substrates by using a biotinylated phage substrate library
    • DOI 10.1002/cbic.200500427
    • Mapping protease substrates by using a biotinylated phage substrate library. Scholle MD, Kriplani U, Pabon A, Sishtla K, Glucksman MJ, Kay BK, Chembiochem 2006 7 5 834 838 10.1002/cbic.200500427 16628754 (Pubitemid 43764194)
    • (2006) ChemBioChem , vol.7 , Issue.5 , pp. 834-838
    • Scholle, M.D.1    Kriplani, U.2    Pabon, A.3    Sishtla, K.4    Glucksman, M.J.5    Kay, B.K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.