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Volumn 40, Issue 4, 2006, Pages 433-440

One-step high-throughput assay for quantitative detection of β-galactosidase activity in intact Gram-negative bacteria, yeast and mammalian cells

Author keywords

[No Author keywords available]

Indexed keywords

BETA GALACTOSIDASE; FLUORESCENT DYE; HYBRID PROTEIN;

EID: 33646854383     PISSN: 07366205     EISSN: None     Source Type: Journal    
DOI: 10.2144/000112145     Document Type: Review
Times cited : (45)

References (22)
  • 1
    • 0036270928 scopus 로고    scopus 로고
    • LacZ assays in yeast
    • Rupp, S. 2002. LacZ assays in yeast. Methods Enzymol. 350:112-131.
    • (2002) Methods Enzymol , vol.350 , pp. 112-131
    • Rupp, S.1
  • 2
    • 2442564717 scopus 로고    scopus 로고
    • Quantitative β-galactosidase assay suitable for high-throughput applications in the yeast two-hybrid system
    • Mockli, N. and D. Auerbach. 2004. Quantitative β-galactosidase assay suitable for high-throughput applications in the yeast two-hybrid system. BioTechniques 36:872-876.
    • (2004) BioTechniques , vol.36 , pp. 872-876
    • Mockli, N.1    Auerbach, D.2
  • 4
    • 1542346163 scopus 로고    scopus 로고
    • High-throughput β-galactosidase assay for bacterial cell-based reporter systems
    • Thibodeau, S.A., R. Fang, and J.K. Joung. 2004. High-throughput β-galactosidase assay for bacterial cell-based reporter systems. BioTechniques 36:410-415.
    • (2004) BioTechniques , vol.36 , pp. 410-415
    • Thibodeau, S.A.1    Fang, R.2    Joung, J.K.3
  • 5
    • 0034307355 scopus 로고    scopus 로고
    • Uses of lacZ to study gene function: Evaluation of β-galactosidase assays employed in the yeast two-hybrid system
    • Serebriiskii, I.G. and E.A. Golemis. 2000. Uses of lacZ to study gene function: evaluation of β-galactosidase assays employed in the yeast two-hybrid system. Anal. Biochem. 285:1-15.
    • (2000) Anal. Biochem , vol.285 , pp. 1-15
    • Serebriiskii, I.G.1    Golemis, E.A.2
  • 7
    • 0038623777 scopus 로고    scopus 로고
    • β-galactosidase enzyme fragment complementation as a novel technology for high throughput screening
    • Eglen, R.M. and R. Singh. 2003. β-galactosidase enzyme fragment complementation as a novel technology for high throughput screening. Comb. Chem. High Throughput Screen. 6:381-387.
    • (2003) Comb. Chem. High Throughput Screen , vol.6 , pp. 381-387
    • Eglen, R.M.1    Singh, R.2
  • 8
    • 0042237026 scopus 로고    scopus 로고
    • Use of yeast two-hybrid system for detection of Bacillus subtilis FtsZ protein partners
    • Prepiak, P., Z. Chromikova, and I. Barak. 2001. Use of yeast two-hybrid system for detection of Bacillus subtilis FtsZ protein partners. Folia Microbiol. (Praha) 46:292-296.
    • (2001) Folia Microbiol. (Praha) , vol.46 , pp. 292-296
    • Prepiak, P.1    Chromikova, Z.2    Barak, I.3
  • 10
    • 0029063837 scopus 로고
    • Activation of the transcriptional regulator XylR of Pseudomonas putida by release of repression between functional domains
    • Fernández, S., V. de Lorenzo, and J. Pérez- Martín. 1995. Activation of the transcriptional regulator XylR of Pseudomonas putida by release of repression between functional domains. Mol. Microbiol. 16:205-213.
    • (1995) Mol. Microbiol , vol.16 , pp. 205-213
    • Fernández, S.1    de Lorenzo, V.2    Pérez- Martín, J.3
  • 11
    • 0025797356 scopus 로고
    • An upstream Xy1R-and IHF-induced nucleoprotein complex regulates the sigma 54-dependent Pu promoter of TOL plasmid
    • de Lorenzo, V., M. Herrero, M. Metzke, and K.N. Timmis. 1991. An upstream Xy1R-and IHF-induced nucleoprotein complex regulates the sigma 54-dependent Pu promoter of TOL plasmid. EMBO J. 10:1159-1167.
    • (1991) EMBO J , vol.10 , pp. 1159-1167
    • de Lorenzo, V.1    Herrero, M.2    Metzke, M.3    Timmis, K.N.4
  • 12
    • 0034981053 scopus 로고    scopus 로고
    • Arenghi, F.L., P. Barbieri, G. Bertoni, and V. de Lorenzo. 2001. New insights into the activation of o-xylene biodegradation in Pseudomonas stutzeri OX1 by pathway substrates. EMBO Rep. 2:409-414.
    • Arenghi, F.L., P. Barbieri, G. Bertoni, and V. de Lorenzo. 2001. New insights into the activation of o-xylene biodegradation in Pseudomonas stutzeri OX1 by pathway substrates. EMBO Rep. 2:409-414.
  • 13
    • 0034548711 scopus 로고    scopus 로고
    • Pentapeptide scanning mutagenesis: Encouraging old proteins to execute unusual tricks
    • Hayes, F. and B. Hallet. 2000. Pentapeptide scanning mutagenesis: encouraging old proteins to execute unusual tricks. Trends Microbiol. 8:571-577.
    • (2000) Trends Microbiol , vol.8 , pp. 571-577
    • Hayes, F.1    Hallet, B.2
  • 14
    • 0028358260 scopus 로고
    • Analysis and construction of stable phenotypes in gram-negative bacteria with Tn5-and Tn10-derived minitransposons
    • de Lorenzo, V. and K.N. Timmis. 1994. Analysis and construction of stable phenotypes in gram-negative bacteria with Tn5-and Tn10-derived minitransposons. Methods Enzymol. 235:386-405.
    • (1994) Methods Enzymol , vol.235 , pp. 386-405
    • de Lorenzo, V.1    Timmis, K.N.2
  • 15
    • 1542320702 scopus 로고    scopus 로고
    • Physical and functional interactions between nucleotide excision repair and DNA damage checkpoint
    • Giannattasio, M., F. Lazzaro, M.P. Longhese, P. Plevani, and M. Muzi-Falconi. 2004. Physical and functional interactions between nucleotide excision repair and DNA damage checkpoint. EMBO J. 25:429-438.
    • (2004) EMBO J , vol.25 , pp. 429-438
    • Giannattasio, M.1    Lazzaro, F.2    Longhese, M.P.3    Plevani, P.4    Muzi-Falconi, M.5
  • 16
    • 33644616440 scopus 로고    scopus 로고
    • The 9-1-1 checkpoint clamp physically interacts with Polzeta and is partially required for spontaneous Polzeta-dependent mutagenesis in Saccharomyces cerevisiae
    • Sabbioneda, S., B.K. Minesinger, M. Giannattasio, P. Plevani, M. Muzi-Falconi, and S. Jinks-Robertson. 2005. The 9-1-1 checkpoint clamp physically interacts with Polzeta and is partially required for spontaneous Polzeta-dependent mutagenesis in Saccharomyces cerevisiae. J. Biol. Chem. 280:38657-38665.
    • (2005) J. Biol. Chem , vol.280 , pp. 38657-38665
    • Sabbioneda, S.1    Minesinger, B.K.2    Giannattasio, M.3    Plevani, P.4    Muzi-Falconi, M.5    Jinks-Robertson, S.6
  • 17
    • 0000632797 scopus 로고
    • TnphoA: A transposon probe for protein export signals
    • Manoil, C. and J. Beckwith. 1985. TnphoA: a transposon probe for protein export signals. Proc. Natl. Acad. Sci. USA 82:8129-8133.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 8129-8133
    • Manoil, C.1    Beckwith, J.2
  • 18
    • 0017807890 scopus 로고
    • Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the Pl5A cryptic miniplasmid
    • Chang, A.C. and S.N. Cohen. 1978. Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the Pl5A cryptic miniplasmid. J.Bacteriol. 134:1141-1156.
    • (1978) J.Bacteriol , vol.134 , pp. 1141-1156
    • Chang, A.C.1    Cohen, S.N.2
  • 19
    • 0023777735 scopus 로고
    • Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli
    • Amann, E., B. Ochs, and K.J. Abel. 1988. Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli. Gene 69:301-315.
    • (1988) Gene , vol.69 , pp. 301-315
    • Amann, E.1    Ochs, B.2    Abel, K.J.3
  • 20
    • 0030825248 scopus 로고    scopus 로고
    • Pentapeptide scanning mutagenesis: Random insertion of a variable five amino acid cassette in a target protein
    • Hallet, B., D.J. Sherratt, and F. Hayes. 1997. Pentapeptide scanning mutagenesis: random insertion of a variable five amino acid cassette in a target protein. Nucleic Acids Res. 25:1866-1867.
    • (1997) Nucleic Acids Res , vol.25 , pp. 1866-1867
    • Hallet, B.1    Sherratt, D.J.2    Hayes, F.3
  • 21
    • 0027437850 scopus 로고
    • Cdil, a human G1 and S phase protein phosphatase that associates with Cdk2
    • Gyuris, J., E. Golemis, H. Chertkov, and R. Brent. 1993. Cdil, a human G1 and S phase protein phosphatase that associates with Cdk2. Cell 75:791-803.
    • (1993) Cell , vol.75 , pp. 791-803
    • Gyuris, J.1    Golemis, E.2    Chertkov, H.3    Brent, R.4
  • 22
    • 0029092610 scopus 로고
    • Correlation of two-hybrid affinity data with in vitro measurements
    • Estojak, J., R. Brent, and E.A. Golemis. 1995. Correlation of two-hybrid affinity data with in vitro measurements. Mol. Cell. Biol. 15:5820-5829.
    • (1995) Mol. Cell. Biol , vol.15 , pp. 5820-5829
    • Estojak, J.1    Brent, R.2    Golemis, E.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.