메뉴 건너뛰기




Volumn 370, Issue 1, 2008, Pages 164-168

Development of homogeneous immunoassays based on protein fragment complementation

Author keywords

Enzyme immunoassay; Homogeneous assay; Protein fragment complementation assay; TEM 1 lactamase

Indexed keywords

BETA LACTAMASE; BETA LACTAMASE INHIBITOR; BETA LACTAMASE TEM 1; CLAVULANIC ACID; NITROCEFIN; TAZOBACTAM;

EID: 41849111244     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.03.057     Document Type: Article
Times cited : (10)

References (25)
  • 1
    • 0035957521 scopus 로고    scopus 로고
    • Fast selection of antibodies without antigen purification: adaptation of the protein fragment complementation assay to select antigen-antibody pairs
    • Mossner E., Koch H., and Pluckthun A. Fast selection of antibodies without antigen purification: adaptation of the protein fragment complementation assay to select antigen-antibody pairs. J. Mol. Biol. 308 (2001) 115-122
    • (2001) J. Mol. Biol. , vol.308 , pp. 115-122
    • Mossner, E.1    Koch, H.2    Pluckthun, A.3
  • 2
    • 0035984722 scopus 로고    scopus 로고
    • β-Lactamase protein fragment complementation assays as in vivo and in vitro sensors of protein-protein interactions
    • Galarneau A., Primeau M., Trudeau L.-E., and Michnick S.W. β-Lactamase protein fragment complementation assays as in vivo and in vitro sensors of protein-protein interactions. Nat. Biotechnol. 20 (2002) 619-622
    • (2002) Nat. Biotechnol. , vol.20 , pp. 619-622
    • Galarneau, A.1    Primeau, M.2    Trudeau, L.-E.3    Michnick, S.W.4
  • 3
    • 0037133629 scopus 로고    scopus 로고
    • Protein-protein interactions monitored in mammalian cells via complementation of β-lactamase enzyme fragments
    • Wehrman T., Kleaveland B., Her J.-H., Balint R.F., and Blau H.M. Protein-protein interactions monitored in mammalian cells via complementation of β-lactamase enzyme fragments. Proc. Natl. Acad. Sci. USA 99 (2002) 3469-3474
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 3469-3474
    • Wehrman, T.1    Kleaveland, B.2    Her, J.-H.3    Balint, R.F.4    Blau, H.M.5
  • 4
    • 1642462155 scopus 로고    scopus 로고
    • Homogeneous sandwich immunoassay based on the enzymatic complementation induced by single-chain Fv fragments
    • Komiya N., Ueda H., Ohiro Y., and Nagamune T. Homogeneous sandwich immunoassay based on the enzymatic complementation induced by single-chain Fv fragments. Anal. Biochem. 327 (2004) 241-246
    • (2004) Anal. Biochem. , vol.327 , pp. 241-246
    • Komiya, N.1    Ueda, H.2    Ohiro, Y.3    Nagamune, T.4
  • 5
    • 0142061076 scopus 로고    scopus 로고
    • An optimized homogeneous noncompetitive immunoassay based on the antigen-driven enzymatic complementation
    • Ueda H., Yokozeki T., Arai R., Tsumoto K., Kumagai I., and Nagamune T. An optimized homogeneous noncompetitive immunoassay based on the antigen-driven enzymatic complementation. J. Immunol. Methods 279 (2003) 209-218
    • (2003) J. Immunol. Methods , vol.279 , pp. 209-218
    • Ueda, H.1    Yokozeki, T.2    Arai, R.3    Tsumoto, K.4    Kumagai, I.5    Nagamune, T.6
  • 6
    • 0032514623 scopus 로고    scopus 로고
    • Oligomerization domain-directed reassembly of active dihydrofolate reductase from rationally designed fragments
    • Pelletier J.N., Campbell-Valois F.-X., and Michnick S.W. Oligomerization domain-directed reassembly of active dihydrofolate reductase from rationally designed fragments. Proc. Natl. Acad. Sci. USA 95 (1998) 12141-12146
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12141-12146
    • Pelletier, J.N.1    Campbell-Valois, F.-X.2    Michnick, S.W.3
  • 7
    • 0025123399 scopus 로고
    • Folding and aggregation of beta-lactamase in the periplasmic space of Escherichia coli
    • Bowden G.A., and Georgiou G. Folding and aggregation of beta-lactamase in the periplasmic space of Escherichia coli. J. Biol. Chem. 265 (1990) 16760-16766
    • (1990) J. Biol. Chem. , vol.265 , pp. 16760-16766
    • Bowden, G.A.1    Georgiou, G.2
  • 8
    • 0015327122 scopus 로고
    • Novel Method for detection of β-lactamases by using a chromogenic cephalosporin substrate
    • O'Callaghan C.H., Morris A., Kirby S.M., and Shingler A.H. Novel Method for detection of β-lactamases by using a chromogenic cephalosporin substrate. Antimicrob. Agents Chemother. 1 (1972) 283-288
    • (1972) Antimicrob. Agents Chemother. , vol.1 , pp. 283-288
    • O'Callaghan, C.H.1    Morris, A.2    Kirby, S.M.3    Shingler, A.H.4
  • 9
    • 11144312470 scopus 로고    scopus 로고
    • Fluorescent detection of beta-lactamase activity in living Escherichia coli cells via esterase supplementation
    • Nord O., Gustrin A., and Nygren P.A. Fluorescent detection of beta-lactamase activity in living Escherichia coli cells via esterase supplementation. FEMS Microbiol. Lett. 242 (2005) 73-79
    • (2005) FEMS Microbiol. Lett. , vol.242 , pp. 73-79
    • Nord, O.1    Gustrin, A.2    Nygren, P.A.3
  • 10
    • 34848887128 scopus 로고    scopus 로고
    • A bioluminogenic substrate for in vivo imaging of beta-lactamase activity
    • Yao H., So M.K., and Rao J. A bioluminogenic substrate for in vivo imaging of beta-lactamase activity. Angew. Chem. Int. Ed. Engl. 46 (2007) 7031-7034
    • (2007) Angew. Chem. Int. Ed. Engl. , vol.46 , pp. 7031-7034
    • Yao, H.1    So, M.K.2    Rao, J.3
  • 11
    • 0024363590 scopus 로고
    • The precursor of beta-lactamase: purification, properties and folding kinetics
    • Laminet A.A., and Pluckthun A. The precursor of beta-lactamase: purification, properties and folding kinetics. EMBO J. 8 (1989) 1469-1477
    • (1989) EMBO J. , vol.8 , pp. 1469-1477
    • Laminet, A.A.1    Pluckthun, A.2
  • 12
    • 0028170640 scopus 로고
    • TEM beta-lactamase mutants hydrolysing third-generation cephalosporins. A kinetic and molecular modelling analysis
    • Raquet X., Lamotte-Brasseur J., Fonze E., Goussard S., Courvalin P., and Frere J.M. TEM beta-lactamase mutants hydrolysing third-generation cephalosporins. A kinetic and molecular modelling analysis. J. Mol. Biol. 244 (1994) 625-639
    • (1994) J. Mol. Biol. , vol.244 , pp. 625-639
    • Raquet, X.1    Lamotte-Brasseur, J.2    Fonze, E.3    Goussard, S.4    Courvalin, P.5    Frere, J.M.6
  • 13
    • 33645226595 scopus 로고    scopus 로고
    • Sequence-enabled reassembly of beta-lactamase (SEER-LAC): a sensitive method for the detection of double-stranded DNA
    • Ooi A.T., Stains C.I., Ghosh I., and Segal D.J. Sequence-enabled reassembly of beta-lactamase (SEER-LAC): a sensitive method for the detection of double-stranded DNA. Biochemistry 45 (2006) 3620-3625
    • (2006) Biochemistry , vol.45 , pp. 3620-3625
    • Ooi, A.T.1    Stains, C.I.2    Ghosh, I.3    Segal, D.J.4
  • 14
    • 0030788941 scopus 로고    scopus 로고
    • A natural polymorphism in beta-lactamase is a global suppressor
    • Huang W., and Palzkill T. A natural polymorphism in beta-lactamase is a global suppressor. Proc. Natl. Acad. Sci. USA 94 (1997) 8801-8806
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 8801-8806
    • Huang, W.1    Palzkill, T.2
  • 15
    • 0035793095 scopus 로고    scopus 로고
    • A secondary drug resistance mutation of TEM-1 beta-lactamase that suppresses misfolding and aggregation
    • Sideraki V., Huang W., Palzkill T., and Gilbert H.F. A secondary drug resistance mutation of TEM-1 beta-lactamase that suppresses misfolding and aggregation. Proc. Natl. Acad. Sci. USA 98 (2001) 283-288
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 283-288
    • Sideraki, V.1    Huang, W.2    Palzkill, T.3    Gilbert, H.F.4
  • 16
    • 0035814792 scopus 로고    scopus 로고
    • Fragment complementation studies of protein stabilization by hydrophobic core residues
    • Berggard T., Julenius K., Ogard A., Drakenberg T., and Linse S. Fragment complementation studies of protein stabilization by hydrophobic core residues. Biochemistry 40 (2001) 1257-1264
    • (2001) Biochemistry , vol.40 , pp. 1257-1264
    • Berggard, T.1    Julenius, K.2    Ogard, A.3    Drakenberg, T.4    Linse, S.5
  • 17
    • 0037328859 scopus 로고    scopus 로고
    • Identical pattern of highly variable absorption of clavulanic acid from four different oral formulations of co-amoxiclav in healthy subjects
    • Vree T.B., Dammers E., and Exler P.S. Identical pattern of highly variable absorption of clavulanic acid from four different oral formulations of co-amoxiclav in healthy subjects. J. Antimicrob. Chemother. 51 (2003) 373-378
    • (2003) J. Antimicrob. Chemother. , vol.51 , pp. 373-378
    • Vree, T.B.1    Dammers, E.2    Exler, P.S.3
  • 18
    • 0033002105 scopus 로고    scopus 로고
    • Pharmacokinetics and pharmacodynamics of amoxicillin-sulbactam, a novel aminopenicillin-beta-lactamase inhibitor combination, against Escherichia coli
    • Bantar C., Nicola F., Arenoso H.J., Galas M., Soria L., Dana D., Rossi A., Bianchini H., and Jasovich A. Pharmacokinetics and pharmacodynamics of amoxicillin-sulbactam, a novel aminopenicillin-beta-lactamase inhibitor combination, against Escherichia coli. Antimicrob. Agents Chemother. 43 (1999) 1503-1504
    • (1999) Antimicrob. Agents Chemother. , vol.43 , pp. 1503-1504
    • Bantar, C.1    Nicola, F.2    Arenoso, H.J.3    Galas, M.4    Soria, L.5    Dana, D.6    Rossi, A.7    Bianchini, H.8    Jasovich, A.9
  • 19
    • 0025774926 scopus 로고
    • Pharmacokinetics and tissue penetration of tazobactam administered alone and with piperacillin
    • Wise R., Logan M., Cooper M., and Andrews J.M. Pharmacokinetics and tissue penetration of tazobactam administered alone and with piperacillin. Antimicrob. Agents Chemother. 35 (1991) 1081-1084
    • (1991) Antimicrob. Agents Chemother. , vol.35 , pp. 1081-1084
    • Wise, R.1    Logan, M.2    Cooper, M.3    Andrews, J.M.4
  • 20
    • 0032816956 scopus 로고    scopus 로고
    • Construction and characterization of mutants of the TEM-1 beta-lactamase containing amino acid substitutions associated with both extended-spectrum resistance and resistance to beta-lactamase inhibitors
    • Stapleton P.D., Shannon K.P., and French G.L. Construction and characterization of mutants of the TEM-1 beta-lactamase containing amino acid substitutions associated with both extended-spectrum resistance and resistance to beta-lactamase inhibitors. Antimicrob. Agents Chemother. 43 (1999) 1881-1887
    • (1999) Antimicrob. Agents Chemother. , vol.43 , pp. 1881-1887
    • Stapleton, P.D.1    Shannon, K.P.2    French, G.L.3
  • 21
    • 0343686104 scopus 로고    scopus 로고
    • Inhibitor-resistant TEM beta-lactamases: phenotypic, genetic and biochemical characteristics
    • Chaibi E.B., Sirot D., Paul G., and Labia R. Inhibitor-resistant TEM beta-lactamases: phenotypic, genetic and biochemical characteristics. J. Antimicrob. Chemother. 43 (1999) 447-458
    • (1999) J. Antimicrob. Chemother. , vol.43 , pp. 447-458
    • Chaibi, E.B.1    Sirot, D.2    Paul, G.3    Labia, R.4
  • 22
    • 0036295508 scopus 로고    scopus 로고
    • Evolution of an antibiotic resistance enzyme constrained by stability and activity trade-offs
    • Wang X., Minasov G., and Shoichet B.K. Evolution of an antibiotic resistance enzyme constrained by stability and activity trade-offs. J. Mol. Biol. 320 (2002) 85-95
    • (2002) J. Mol. Biol. , vol.320 , pp. 85-95
    • Wang, X.1    Minasov, G.2    Shoichet, B.K.3
  • 23
    • 34347374044 scopus 로고    scopus 로고
    • Universal strategies in research and drug discovery based on protein-fragment complementation assays
    • Michnick S.W., Ear P.H., Manderson E.N., Remy I., and Stefan E. Universal strategies in research and drug discovery based on protein-fragment complementation assays. Nat. Rev. Drug Discov. 6 (2007) 569-582
    • (2007) Nat. Rev. Drug Discov. , vol.6 , pp. 569-582
    • Michnick, S.W.1    Ear, P.H.2    Manderson, E.N.3    Remy, I.4    Stefan, E.5
  • 24
    • 34548580356 scopus 로고    scopus 로고
    • Split beta-lactamase sensor for the sequence-specific detection of DNA methylation
    • Porter J.R., Stains C.I., Segal D.J., and Ghosh I. Split beta-lactamase sensor for the sequence-specific detection of DNA methylation. Anal. Chem. 79 (2007) 6702-6708
    • (2007) Anal. Chem. , vol.79 , pp. 6702-6708
    • Porter, J.R.1    Stains, C.I.2    Segal, D.J.3    Ghosh, I.4
  • 25
    • 32344440872 scopus 로고    scopus 로고
    • Reconstitution of the enzyme AroA and its glyphosate tolerance by fragment complementation
    • Sun Y.C., Li Y., Zhang H., Yan H.Q., Dowling D.N., and Wang Y.P. Reconstitution of the enzyme AroA and its glyphosate tolerance by fragment complementation. FEBS Lett. 580 (2006) 1521-1527
    • (2006) FEBS Lett. , vol.580 , pp. 1521-1527
    • Sun, Y.C.1    Li, Y.2    Zhang, H.3    Yan, H.Q.4    Dowling, D.N.5    Wang, Y.P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.