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Volumn 1130, Issue , 2008, Pages 44-51

Investigating transcriptional regulation by fluorescence spectroscopy, from traditional methods to state-of-the-art single-molecule approaches

Author keywords

Biomolecular interactions; Fluorescence anisotropy; Fluorescence correlation and cross correlation spectroscopy; Transcriptional regulation

Indexed keywords

REGULATOR PROTEIN;

EID: 47249103805     PISSN: 00778923     EISSN: 17496632     Source Type: Book Series    
DOI: 10.1196/annals.1430.023     Document Type: Conference Paper
Times cited : (4)

References (20)
  • 1
    • 0034910795 scopus 로고    scopus 로고
    • Transcription of glycolytic genes and operons in Bacillus subtilis: Evidence for the presence of multiple levels of control of the gapA operon
    • Ludwig, H., G. Homuth, M. Schmalisch, et al. 2001. Transcription of glycolytic genes and operons in Bacillus subtilis: evidence for the presence of multiple levels of control of the gapA operon. Mol. Microbiol. 41 : 409 422.
    • (2001) Mol. Microbiol. , vol.41 , pp. 409-422
    • Ludwig, H.1    Homuth, G.2    Schmalisch, M.3
  • 2
    • 0037009447 scopus 로고    scopus 로고
    • A cell-cell signaling peptide activates the PlcR virulence regulon in bacteria of the Bacillus cereus group
    • &
    • Slamti, L. & D. Lereclus. 2002. A cell-cell signaling peptide activates the PlcR virulence regulon in bacteria of the Bacillus cereus group. EMBO J. 21 : 4550 4559.
    • (2002) EMBO J. , vol.21 , pp. 4550-4559
    • Slamti, L.1    Lereclus, D.2
  • 3
    • 15744369973 scopus 로고    scopus 로고
    • Nuclear receptors as targets for drug development: Molecular mechanisms for regulation of obesity and insulin resistance by peroxisome proliferator-activated receptor gamma, CREB-binding protein, and adiponectin
    • &
    • Tsuchida, A., T. Yamauchi & T. Kadowaki. 2005. Nuclear receptors as targets for drug development: molecular mechanisms for regulation of obesity and insulin resistance by peroxisome proliferator-activated receptor gamma, CREB-binding protein, and adiponectin. J. Pharmacol. Sci. 97 : 164 170.
    • (2005) J. Pharmacol. Sci. , vol.97 , pp. 164-170
    • Tsuchida, A.1    Yamauchi, T.2    Kadowaki, T.3
  • 4
    • 0037344870 scopus 로고    scopus 로고
    • Regulation of the central glycolytic genes in Bacillus subtilis: Binding of the repressor CggR to its single DNA target sequence is modulated by fructose-1,6-bisphosphate
    • &
    • Doan, T. & S. Aymerich. 2003. Regulation of the central glycolytic genes in Bacillus subtilis: binding of the repressor CggR to its single DNA target sequence is modulated by fructose-1,6-bisphosphate. Mol. Microbiol. 47 : 1709 1721.
    • (2003) Mol. Microbiol. , vol.47 , pp. 1709-1721
    • Doan, T.1    Aymerich, S.2
  • 5
    • 14844295003 scopus 로고    scopus 로고
    • CcpN (YqzB), a novel regulator for CcpA-independent catabolite repression of Bacillus subtilis gluconeogenic genes
    • &
    • Servant, P., D. Le Coq & S. Aymerich. 2005. CcpN (YqzB), a novel regulator for CcpA-independent catabolite repression of Bacillus subtilis gluconeogenic genes. Mol. Microbiol. 55 : 1435 1451.
    • (2005) Mol. Microbiol. , vol.55 , pp. 1435-1451
    • Servant, P.1    Le Coq, D.2    Aymerich, S.3
  • 6
    • 34247646036 scopus 로고    scopus 로고
    • Inducer-modulated cooperative binding of the tetrameric CggR repressor to operator DNA
    • Zorrilla, S., T. Doan, C. Alfonso, et al. 2007. Inducer-modulated cooperative binding of the tetrameric CggR repressor to operator DNA. Biophys. J. 92 : 3215 3227.
    • (2007) Biophys. J. , vol.92 , pp. 3215-3227
    • Zorrilla, S.1    Doan, T.2    Alfonso, C.3
  • 7
    • 37349094934 scopus 로고    scopus 로고
    • Fructose-1,6-bisphosphate acts both as an inducer and as a structural cofactor of the central glycolytic genes repressor (CggR)
    • Zorrilla, S., D. Chaix, A. Ortega, 2007. Fructose-1,6-bisphosphate acts both as an inducer and as a structural cofactor of the central glycolytic genes repressor (CggR). Biochemistry 46 : 14996 15008.
    • (2007) Biochemistry , vol.46 , pp. 14996-15008
    • Zorrilla, S.1    Chaix, D.2    Ortega, A.3
  • 8
    • 0028934572 scopus 로고
    • Fluorescence anisotropy applied to biomolecular interactions
    • &
    • Jameson, D.M. & W.H. Sawyer. 1995. Fluorescence anisotropy applied to biomolecular interactions. Methods Enzymol. 246 : 283 300.
    • (1995) Methods Enzymol. , vol.246 , pp. 283-300
    • Jameson, D.M.1    Sawyer, W.H.2
  • 9
    • 0031015166 scopus 로고    scopus 로고
    • Fluorescence spectroscopy as a tool to investigate protein interactions
    • &
    • Brown, M.P. & C. Royer. 1997. Fluorescence spectroscopy as a tool to investigate protein interactions. Curr. Opin. Biotechnol. 8 : 45 49.
    • (1997) Curr. Opin. Biotechnol. , vol.8 , pp. 45-49
    • Brown, M.P.1    Royer, C.2
  • 11
    • 0001301977 scopus 로고
    • The polarisation of fluorescence light. Average life of molecules in their excited state
    • Perrin, F. 1926. The polarisation of fluorescence light. Average life of molecules in their excited state. J. De Physique Et Le Radium. 7 : 390 401.
    • (1926) J. de Physique et Le Radium. , vol.7 , pp. 390-401
    • Perrin, F.1
  • 12
    • 4544387972 scopus 로고    scopus 로고
    • Fluorescence anisotropy as a probe to study tracer proteins in crowded solutions
    • &
    • Zorrilla, S., G. Rivas & M.P. Lillo. 2004. Fluorescence anisotropy as a probe to study tracer proteins in crowded solutions. J. Mol. Recognit. 17 : 408 416.
    • (2004) J. Mol. Recognit. , vol.17 , pp. 408-416
    • Zorrilla, S.1    Rivas, G.2    Lillo, M.P.3
  • 13
    • 0037124326 scopus 로고    scopus 로고
    • Plasticity in protein-DNA recognition: Lac repressor interacts with its natural operator 01 through alternative conformations of its DNA-binding domain
    • Kalodimos, C.G., A. Bonvin, R.K. Salinas, et al. 2002. Plasticity in protein-DNA recognition: lac repressor interacts with its natural operator 01 through alternative conformations of its DNA-binding domain. EMBO J. 21 : 2866 2876.
    • (2002) EMBO J. , vol.21 , pp. 2866-2876
    • Kalodimos, C.G.1    Bonvin, A.2    Salinas, R.K.3
  • 14
    • 33646950257 scopus 로고    scopus 로고
    • New perspectives of fluorescence correlation spectroscopy
    • &
    • Visser, A. & M.A. Hink. 1999. New perspectives of fluorescence correlation spectroscopy. J. Fluoresc. 9 : 81 87.
    • (1999) J. Fluoresc. , vol.9 , pp. 81-87
    • Visser, A.1    Hink, M.A.2
  • 15
    • 47249150661 scopus 로고    scopus 로고
    • The characterization of biomolecular interactions using fluorescence fluctuation techniques
    • & In. Vol. P. Schuck, Ed. Springer-Verlag. New York.
    • Margeat, E., H. Boukari & C.A. Royer. 2007. The characterization of biomolecular interactions using fluorescence fluctuation techniques. In Protein Interactions, Vol. 5. P. Schuck, Ed 1 38. Springer-Verlag. New York.
    • (2007) Protein Interactions , vol.5 , pp. 1-38
    • Margeat, E.1    Boukari, H.2    Royer, C.A.3
  • 16
    • 22244464837 scopus 로고    scopus 로고
    • Two-photon cross-correlation analysis of intracellular reactions with variable stoichiometry
    • Kim, S.A., K.G. Heinze, K. Bacia, et al. 2005. Two-photon cross-correlation analysis of intracellular reactions with variable stoichiometry. Biophys. J. 88 : 4319 4336.
    • (2005) Biophys. J. , vol.88 , pp. 4319-4336
    • Kim, S.A.1    Heinze, K.G.2    Bacia, K.3
  • 17
    • 24144444670 scopus 로고    scopus 로고
    • Observation volumes and gamma-factors in two-photon fluorescence fluctuation spectroscopy
    • &
    • Nagy, A., J.R. Wu & K.M. Berland. 2005. Observation volumes and gamma-factors in two-photon fluorescence fluctuation spectroscopy. Biophys. J. 89 : 2077 2090.
    • (2005) Biophys. J. , vol.89 , pp. 2077-2090
    • Nagy, A.1    Wu, J.R.2    Berland, K.M.3
  • 18
    • 0037057630 scopus 로고    scopus 로고
    • Initiation and re-initiation of DNA unwinding by the Escherichia coli rep helicase
    • Ha, T., I. Rasnik, W. Cheng, et al. 2002. Initiation and re-initiation of DNA unwinding by the Escherichia coli rep helicase. Nature 419 : 638 641.
    • (2002) Nature , vol.419 , pp. 638-641
    • Ha, T.1    Rasnik, I.2    Cheng, W.3
  • 19
    • 0033021689 scopus 로고    scopus 로고
    • Resolution of fluorescence correlation measurements
    • Meseth, U., T. Wohland, R. Rigler, et al. 1999. Resolution of fluorescence correlation measurements. Biophys. J. 76 : 1619 1631.
    • (1999) Biophys. J. , vol.76 , pp. 1619-1631
    • Meseth, U.1    Wohland, T.2    Rigler, R.3
  • 20
    • 33645754536 scopus 로고    scopus 로고
    • A two-photon excitation fluorescence cross-correlation assay for a model ligand-receptor binding system using quantum dots
    • &
    • Swift, J.L., R. Heuff & D.T. Cramb. 2006. A two-photon excitation fluorescence cross-correlation assay for a model ligand-receptor binding system using quantum dots. Biophys. J. 90 : 1396 1410.
    • (2006) Biophys. J. , vol.90 , pp. 1396-1410
    • Swift, J.L.1    Heuff, R.2    Cramb, D.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.