메뉴 건너뛰기




Volumn 6, Issue 10, 2011, Pages

Fluorescent labeling of antibody fragments using split GFP

Author keywords

[No Author keywords available]

Indexed keywords

GREEN FLUORESCENT PROTEIN; GREEN FLUORESCENT PROTEIN 11; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY; UNCLASSIFIED DRUG; FLUORESCENT DYE; PEPTIDE FRAGMENT;

EID: 80053591305     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0025727     Document Type: Article
Times cited : (16)

References (47)
  • 1
    • 3142743794 scopus 로고    scopus 로고
    • Antibodies from phage antibody libraries
    • Bradbury AR, Marks JD, (2004) Antibodies from phage antibody libraries. J Immunol Methods 290: 29-49.
    • (2004) J Immunol Methods , vol.290 , pp. 29-49
    • Bradbury, A.R.1    Marks, J.D.2
  • 2
  • 3
    • 0030994634 scopus 로고    scopus 로고
    • Yeast surface display for screening combinatorial polypeptide libraries
    • Boder ET, Wittrup KD, (1997) Yeast surface display for screening combinatorial polypeptide libraries. Nat Biotechnol 15: 553-557.
    • (1997) Nat Biotechnol , vol.15 , pp. 553-557
    • Boder, E.T.1    Wittrup, K.D.2
  • 4
    • 0030974119 scopus 로고    scopus 로고
    • In vitro selection and evolution of functional proteins by using ribosome display
    • Hanes J, Pluckthun A, (1997) In vitro selection and evolution of functional proteins by using ribosome display. Proc Natl Acad Sci U S A 94: 4937-4942.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 4937-4942
    • Hanes, J.1    Pluckthun, A.2
  • 5
    • 0004198722 scopus 로고
    • Protein engineering of antibody binding sites: recovery of specific activity in an anti-digoxin single-chain Fv analogue produced in Escherichia coli
    • Huston JS, Levinson D, Mudgett HM, Tai MS, Novotny J, et al. (1988) Protein engineering of antibody binding sites: recovery of specific activity in an anti-digoxin single-chain Fv analogue produced in Escherichia coli. Proc Natl Acad Sci USA 85: 5879-5883.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 5879-5883
    • Huston, J.S.1    Levinson, D.2    Mudgett, H.M.3    Tai, M.S.4    Novotny, J.5
  • 6
    • 70449276523 scopus 로고
    • The hydrolysis of rabbit y-globulin and antibodies with crystalline papain
    • Porter RR, (1959) The hydrolysis of rabbit y-globulin and antibodies with crystalline papain. Biochem J 73: 119-126.
    • (1959) Biochem J , vol.73 , pp. 119-126
    • Porter, R.R.1
  • 7
    • 0025572492 scopus 로고
    • Properties of FV and Fab fragments of the antibody McPC603 expressed in E. coli
    • Pluckthun A, Glockshuber R, Skerra A, Stadmuller J, (1990) Properties of FV and Fab fragments of the antibody McPC603 expressed in E. coli. Behring Inst Mitt pp. 48-55.
    • (1990) Behring Inst Mitt , pp. 48-55
    • Pluckthun, A.1    Glockshuber, R.2    Skerra, A.3    Stadmuller, J.4
  • 8
    • 0022340978 scopus 로고
    • Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product
    • Evan GI, Lewis GK, Ramsay G, Bishop JM, (1985) Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product. Mol Cell Biol 5: 3610-3616.
    • (1985) Mol Cell Biol , vol.5 , pp. 3610-3616
    • Evan, G.I.1    Lewis, G.K.2    Ramsay, G.3    Bishop, J.M.4
  • 9
    • 0026568735 scopus 로고
    • Construction of solid matrix-antibody-antigen complexes containing simian immunodeficiency virus p27 using tag-specific monoclonal antibody and tag-linked antigen
    • Hanke T, Szawlowski P, Randall RE, (1992) Construction of solid matrix-antibody-antigen complexes containing simian immunodeficiency virus p27 using tag-specific monoclonal antibody and tag-linked antigen. J Gen Virol 73 (Pt 3): 653-660.
    • (1992) J Gen Virol , vol.73 , Issue.Pt 3 , pp. 653-660
    • Hanke, T.1    Szawlowski, P.2    Randall, R.E.3
  • 10
    • 0026603594 scopus 로고
    • Single-step purification of bacterially expressed polypeptides containing an oligo-histidine domain
    • Van Dyke MW, Sirito M, Sawadogo M, (1992) Single-step purification of bacterially expressed polypeptides containing an oligo-histidine domain. Gene 111: 99-104.
    • (1992) Gene , vol.111 , pp. 99-104
    • van Dyke, M.W.1    Sirito, M.2    Sawadogo, M.3
  • 11
    • 0031035521 scopus 로고    scopus 로고
    • Specific detection of his-tagged proteins with recombinant anti-His tag scFv-phosphatase or scFv-phage fusions
    • Lindner P, Bauer K, Krebber A, Nieba L, Kremmer E, et al. (1997) Specific detection of his-tagged proteins with recombinant anti-His tag scFv-phosphatase or scFv-phage fusions. Biotechniques 22: 140-149.
    • (1997) Biotechniques , vol.22 , pp. 140-149
    • Lindner, P.1    Bauer, K.2    Krebber, A.3    Nieba, L.4    Kremmer, E.5
  • 12
    • 0032817913 scopus 로고    scopus 로고
    • Recombinant single-chain Fv antibody fragment-alkaline phosphatase conjugate for one-step immunodetection in molecular hybridization
    • Muller BH, Chevrier D, Boulain JC, Guesdon JL, (1999) Recombinant single-chain Fv antibody fragment-alkaline phosphatase conjugate for one-step immunodetection in molecular hybridization. J Immunol Methods 227: 177-185.
    • (1999) J Immunol Methods , vol.227 , pp. 177-185
    • Muller, B.H.1    Chevrier, D.2    Boulain, J.C.3    Guesdon, J.L.4
  • 13
    • 0033152010 scopus 로고    scopus 로고
    • pSKAP/S: An expression vector for the production of single-chain Fv alkaline phosphatase fusion proteins
    • Griep RA, van Twisk C, Kerschbaumer RJ, Harper K, Torrance L, et al. (1999) pSKAP/S: An expression vector for the production of single-chain Fv alkaline phosphatase fusion proteins. Protein Expr Purif 16: 63-69.
    • (1999) Protein Expr Purif , vol.16 , pp. 63-69
    • Griep, R.A.1    van Twisk, C.2    Kerschbaumer, R.J.3    Harper, K.4    Torrance, L.5
  • 15
    • 0034625458 scopus 로고    scopus 로고
    • Structural dynamics of green fluorescent protein alone and fused with a single chain Fv protein
    • Hink MA, Griep RA, Borst JW, van Hoek A, Eppink MH, et al. (2000) Structural dynamics of green fluorescent protein alone and fused with a single chain Fv protein. J Biol Chem 275: 17556-17560.
    • (2000) J Biol Chem , vol.275 , pp. 17556-17560
    • Hink, M.A.1    Griep, R.A.2    Borst, J.W.3    van Hoek, A.4    Eppink, M.H.5
  • 16
    • 0033922052 scopus 로고    scopus 로고
    • Green fluorescent antibodies: novel in vitro tools
    • Casey JL, Coley AM, Tilley LM, Foley M, (2000) Green fluorescent antibodies: novel in vitro tools. Protein Eng 13: 445-452.
    • (2000) Protein Eng , vol.13 , pp. 445-452
    • Casey, J.L.1    Coley, A.M.2    Tilley, L.M.3    Foley, M.4
  • 17
    • 0036806997 scopus 로고    scopus 로고
    • Fluorophor-linked immunosorbent assay: a time- and cost-saving method for the characterization of antibody fragments using a fusion protein of a single-chain antibody fragment and enhanced green fluorescent protein
    • Oelschlaeger P, Srikant-Iyer S, Lange S, Schmitt J, Schmid RD, (2002) Fluorophor-linked immunosorbent assay: a time- and cost-saving method for the characterization of antibody fragments using a fusion protein of a single-chain antibody fragment and enhanced green fluorescent protein. Anal Biochem 309: 27-34.
    • (2002) Anal Biochem , vol.309 , pp. 27-34
    • Oelschlaeger, P.1    Srikant-Iyer, S.2    Lange, S.3    Schmitt, J.4    Schmid, R.D.5
  • 18
    • 0033917124 scopus 로고    scopus 로고
    • Green fluorescent protein functions as a reporter for protein localization in Escherichia coli
    • Feilmeier BJ, Iseminger G, Schroeder D, Webber H, Phillips GJ, (2000) Green fluorescent protein functions as a reporter for protein localization in Escherichia coli. J Bacteriol 182: 4068-4076.
    • (2000) J Bacteriol , vol.182 , pp. 4068-4076
    • Feilmeier, B.J.1    Iseminger, G.2    Schroeder, D.3    Webber, H.4    Phillips, G.J.5
  • 19
    • 13244296604 scopus 로고    scopus 로고
    • Protein tagging and detection with engineered self-assembling fragments of green fluorescent protein
    • Cabantous S, Terwilliger TC, Waldo GS, (2005) Protein tagging and detection with engineered self-assembling fragments of green fluorescent protein. Nat Biotechnol 23: 102-107.
    • (2005) Nat Biotechnol , vol.23 , pp. 102-107
    • Cabantous, S.1    Terwilliger, T.C.2    Waldo, G.S.3
  • 20
    • 1542375250 scopus 로고    scopus 로고
    • A cDNA library functional screening strategy based on fluorescent protein complementation assays to identify novel components of signaling pathways
    • Remy I, Michnick SW, (2004) A cDNA library functional screening strategy based on fluorescent protein complementation assays to identify novel components of signaling pathways. Methods 32: 381-388.
    • (2004) Methods , vol.32 , pp. 381-388
    • Remy, I.1    Michnick, S.W.2
  • 21
    • 24144454858 scopus 로고    scopus 로고
    • Detecting protein-protein interactions with GFP-fragment reassembly
    • Wilson CG, Magliery TJ, Regan L, (2004) Detecting protein-protein interactions with GFP-fragment reassembly. Nat Methods 1: 255-262.
    • (2004) Nat Methods , vol.1 , pp. 255-262
    • Wilson, C.G.1    Magliery, T.J.2    Regan, L.3
  • 22
    • 0023264706 scopus 로고
    • Fluorescence-linked immunosorbent assay (FLISA) for quantification of antibodies to food antigens
    • Magnusson KE, Bartonek E, Nordkvist E, Sundqvist T, Asbrink E, (1987) Fluorescence-linked immunosorbent assay (FLISA) for quantification of antibodies to food antigens. Immunol Invest 16: 227-240.
    • (1987) Immunol Invest , vol.16 , pp. 227-240
    • Magnusson, K.E.1    Bartonek, E.2    Nordkvist, E.3    Sundqvist, T.4    Asbrink, E.5
  • 24
    • 33947591688 scopus 로고    scopus 로고
    • High-throughput screening of single-chain antibodies using multiplexed flow cytometry
    • Ayriss J, Woods T, Bradbury A, Pavlik P, (2007) High-throughput screening of single-chain antibodies using multiplexed flow cytometry. J Proteome Res 6: 1072-1082.
    • (2007) J Proteome Res , vol.6 , pp. 1072-1082
    • Ayriss, J.1    Woods, T.2    Bradbury, A.3    Pavlik, P.4
  • 25
    • 12244313435 scopus 로고    scopus 로고
    • Real-time monitoring of the interactions of two-stranded de novo designed coiled-coils: effect of chain length on the kinetic and thermodynamic constants of binding
    • De Crescenzo G, Litowski JR, Hodges RS, O'Connor-McCourt MD, (2003) Real-time monitoring of the interactions of two-stranded de novo designed coiled-coils: effect of chain length on the kinetic and thermodynamic constants of binding. Biochemistry 42: 1754-1763.
    • (2003) Biochemistry , vol.42 , pp. 1754-1763
    • de Crescenzo, G.1    Litowski, J.R.2    Hodges, R.S.3    O'Connor-McCourt, M.D.4
  • 26
    • 0037318058 scopus 로고    scopus 로고
    • Flow-cytometric isolation of human antibodies from a nonimmune Saccharomyces cerevisiae surface display library
    • Feldhaus MJ, Siegel RW, Opresko LK, Coleman JR, Feldhaus JM, et al. (2003) Flow-cytometric isolation of human antibodies from a nonimmune Saccharomyces cerevisiae surface display library. Nat Biotechnol.
    • (2003) Nat Biotechnol
    • Feldhaus, M.J.1    Siegel, R.W.2    Opresko, L.K.3    Coleman, J.R.4    Feldhaus, J.M.5
  • 27
    • 0033987925 scopus 로고    scopus 로고
    • Exploiting recombination in single bacteria to make large phage antibody libraries
    • Sblattero D, Bradbury A, (2000) Exploiting recombination in single bacteria to make large phage antibody libraries. Nat Biotechnol 18: 75-80.
    • (2000) Nat Biotechnol , vol.18 , pp. 75-80
    • Sblattero, D.1    Bradbury, A.2
  • 28
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier FW, (2005) Protein production by auto-induction in high density shaking cultures. Protein Expr Purif 41: 207-234.
    • (2005) Protein Expr Purif , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 29
    • 33749005086 scopus 로고    scopus 로고
    • In vivo and in vitro protein solubility assays using split GFP
    • Cabantous S, Waldo GS, (2006) In vivo and in vitro protein solubility assays using split GFP. Nat Methods 3: 845-854.
    • (2006) Nat Methods , vol.3 , pp. 845-854
    • Cabantous, S.1    Waldo, G.S.2
  • 30
    • 60849139060 scopus 로고    scopus 로고
    • Automated, high-throughput platform for protein solubility screening using a split-GFP system
    • Listwan P, Terwilliger TC, Waldo GS, (2009) Automated, high-throughput platform for protein solubility screening using a split-GFP system. J Struct Funct Genomics 10: 47-55.
    • (2009) J Struct Funct Genomics , vol.10 , pp. 47-55
    • Listwan, P.1    Terwilliger, T.C.2    Waldo, G.S.3
  • 31
    • 26444492138 scopus 로고    scopus 로고
    • Recent advances in GFP folding reporter and split-GFP solubility reporter technologies. Application to improving the folding and solubility of recalcitrant proteins from Mycobacterium tuberculosis
    • Cabantous S, Pedelacq JD, Mark BL, Naranjo C, Terwilliger TC, et al. (2005) Recent advances in GFP folding reporter and split-GFP solubility reporter technologies. Application to improving the folding and solubility of recalcitrant proteins from Mycobacterium tuberculosis. J Struct Funct Genomics 6: 113-119.
    • (2005) J Struct Funct Genomics , vol.6 , pp. 113-119
    • Cabantous, S.1    Pedelacq, J.D.2    Mark, B.L.3    Naranjo, C.4    Terwilliger, T.C.5
  • 32
    • 78349239240 scopus 로고    scopus 로고
    • One-step split GFP staining for sensitive protein detection and localization in mammalian cells
    • Kaddoum L, Magdeleine E, Waldo G, Joly E, Cabantous S, (2010) One-step split GFP staining for sensitive protein detection and localization in mammalian cells. Biotechniques 49: 727-736.
    • (2010) Biotechniques , vol.49 , pp. 727-736
    • Kaddoum, L.1    Magdeleine, E.2    Waldo, G.3    Joly, E.4    Cabantous, S.5
  • 33
    • 77951296511 scopus 로고    scopus 로고
    • The optimization of in vitro high-throughput chemical lysis of Escherichia coli. Application to ACP domain of the polyketide synthase ppsC from Mycobacterium tuberculosis
    • Listwan P, Pedelacq JD, Lockard M, Bell C, Terwilliger TC, et al. (2010) The optimization of in vitro high-throughput chemical lysis of Escherichia coli. Application to ACP domain of the polyketide synthase ppsC from Mycobacterium tuberculosis. J Struct Funct Genomics 11: 41-49.
    • (2010) J Struct Funct Genomics , vol.11 , pp. 41-49
    • Listwan, P.1    Pedelacq, J.D.2    Lockard, M.3    Bell, C.4    Terwilliger, T.C.5
  • 34
    • 0032456837 scopus 로고    scopus 로고
    • Thermodynamic characterization of affinity maturation: the D1.3 antibody and a higher-affinity mutant
    • VanAntwerp JJ, Wittrup KD, (1998) Thermodynamic characterization of affinity maturation: the D1.3 antibody and a higher-affinity mutant. Journal of molecular recognition: JMR 11: 10-13.
    • (1998) Journal of Molecular Recognition: JMR , vol.11 , pp. 10-13
    • VanAntwerp, J.J.1    Wittrup, K.D.2
  • 35
    • 0020329336 scopus 로고
    • Fluorescent phycobiliprotein conjugates for analyses of cells and molecules
    • Oi VT, Glazer AN, Stryer L, (1982) Fluorescent phycobiliprotein conjugates for analyses of cells and molecules. The Journal of cell biology 93: 981-986.
    • (1982) The Journal of Cell Biology , vol.93 , pp. 981-986
    • Oi, V.T.1    Glazer, A.N.2    Stryer, L.3
  • 36
    • 0030580059 scopus 로고    scopus 로고
    • Crystal structure of R-phycoerythrin from Polysiphonia urceolata at 2.8 A resolution
    • Chang WR, Jiang T, Wan ZL, Zhang JP, Yang ZX, et al. (1996) Crystal structure of R-phycoerythrin from Polysiphonia urceolata at 2.8 A resolution. Journal of molecular biology 262: 721-731.
    • (1996) Journal of Molecular Biology , vol.262 , pp. 721-731
    • Chang, W.R.1    Jiang, T.2    Wan, Z.L.3    Zhang, J.P.4    Yang, Z.X.5
  • 37
    • 0027768856 scopus 로고
    • The contribution of contact and non-contact residues of antibody in the affinity of binding to antigen. The interaction of mutant D1.3 antibodies with lysozyme
    • Hawkins RE, Russell SJ, Baier M, Winter G, (1993) The contribution of contact and non-contact residues of antibody in the affinity of binding to antigen. The interaction of mutant D1.3 antibodies with lysozyme. J Mol Biol 234: 958-964.
    • (1993) J Mol Biol , vol.234 , pp. 958-964
    • Hawkins, R.E.1    Russell, S.J.2    Baier, M.3    Winter, G.4
  • 38
    • 0028945817 scopus 로고
    • High-affinity antigen binding by chelating recombinant antibodies (CRAbs)
    • Neri D, Momo M, Prospero T, Winter G, (1995) High-affinity antigen binding by chelating recombinant antibodies (CRAbs). J Mol Biol 246: 367-373.
    • (1995) J Mol Biol , vol.246 , pp. 367-373
    • Neri, D.1    Momo, M.2    Prospero, T.3    Winter, G.4
  • 39
    • 0026559783 scopus 로고
    • Antibody framework residues affecting the conformation of the hypervariable loops
    • Foote J, Winter G, (1992) Antibody framework residues affecting the conformation of the hypervariable loops. Journal of molecular biology 224: 487-499.
    • (1992) Journal of Molecular Biology , vol.224 , pp. 487-499
    • Foote, J.1    Winter, G.2
  • 40
    • 0023119101 scopus 로고
    • Antigen specificity and cross-reactivity of monoclonal anti-lysozyme antibodies
    • Harper M, Lema F, Boulot G, Poljak RJ, (1987) Antigen specificity and cross-reactivity of monoclonal anti-lysozyme antibodies. Molecular immunology 24: 97-108.
    • (1987) Molecular Immunology , vol.24 , pp. 97-108
    • Harper, M.1    Lema, F.2    Boulot, G.3    Poljak, R.J.4
  • 41
    • 0033558333 scopus 로고    scopus 로고
    • Functional characterization of the somatic hypermutation process leading to antibody D1.3, a high affinity antibody directed against lysozyme
    • England P, Nageotte R, Renard M, Page AL, Bedouelle H, (1999) Functional characterization of the somatic hypermutation process leading to antibody D1.3, a high affinity antibody directed against lysozyme. Journal of immunology 162: 2129-2136.
    • (1999) Journal of Immunology , vol.162 , pp. 2129-2136
    • England, P.1    Nageotte, R.2    Renard, M.3    Page, A.L.4    Bedouelle, H.5
  • 42
    • 0027999119 scopus 로고
    • Use of human leukocyte-specific monoclonal antibodies for clinically immunophenotyping lymphocytes of rhesus monkeys
    • Reimann KA, Waite BC, Lee-Parritz DE, Lin W, Uchanska-Ziegler B, et al. (1994) Use of human leukocyte-specific monoclonal antibodies for clinically immunophenotyping lymphocytes of rhesus monkeys. Cytometry 17: 102-108.
    • (1994) Cytometry , vol.17 , pp. 102-108
    • Reimann, K.A.1    Waite, B.C.2    Lee-Parritz, D.E.3    Lin, W.4    Uchanska-Ziegler, B.5
  • 43
    • 34748919097 scopus 로고    scopus 로고
    • Design of recombinant antibody microarrays for complex proteome analysis: choice of sample labeling-tag and solid support
    • Wingren C, Ingvarsson J, Dexlin L, Szul D, Borrebaeck CA, (2007) Design of recombinant antibody microarrays for complex proteome analysis: choice of sample labeling-tag and solid support. Proteomics 7: 3055-3065.
    • (2007) Proteomics , vol.7 , pp. 3055-3065
    • Wingren, C.1    Ingvarsson, J.2    Dexlin, L.3    Szul, D.4    Borrebaeck, C.A.5
  • 45
    • 0035514481 scopus 로고    scopus 로고
    • Antibody fusions with fluorescent proteins: a versatile reagent for profiling protein expression
    • Morino K, Katsumi H, Akahori Y, Iba Y, Shinohara M, et al. (2001) Antibody fusions with fluorescent proteins: a versatile reagent for profiling protein expression. J Immunol Methods 257: 175-184.
    • (2001) J Immunol Methods , vol.257 , pp. 175-184
    • Morino, K.1    Katsumi, H.2    Akahori, Y.3    Iba, Y.4    Shinohara, M.5
  • 46
    • 0037993790 scopus 로고    scopus 로고
    • Recombinant antibodies to the small GTPase Rab6 as conformation sensors
    • Nizak C, Monier S, del Nery E, Moutel S, Goud B, et al. (2003) Recombinant antibodies to the small GTPase Rab6 as conformation sensors. Science 300: 984-987.
    • (2003) Science , vol.300 , pp. 984-987
    • Nizak, C.1    Monier, S.2    del Nery, E.3    Moutel, S.4    Goud, B.5
  • 47
    • 67749127839 scopus 로고    scopus 로고
    • Development of GFP-based biosensors possessing the binding properties of antibodies
    • Pavoor TV, Cho YK, Shusta EV, (2009) Development of GFP-based biosensors possessing the binding properties of antibodies. Proc Natl Acad Sci U S A.
    • (2009) Proc Natl Acad Sci U S A
    • Pavoor, T.V.1    Cho, Y.K.2    Shusta, E.V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.