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Volumn 370, Issue 1, 2008, Pages 57-61

Mechanism of copper induced fluorescence quenching of red fluorescent protein, DsRed

Author keywords

Copper binding; DsRed; DsRed Express; DsRed Monomer; Fluorescence quenching; Static quenching

Indexed keywords

COPPER; CYSTEINE; HISTIDINE; PROTEIN DSRED; RED FLUORESCENT PROTEIN; UNCLASSIFIED DRUG;

EID: 41849084431     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.03.034     Document Type: Article
Times cited : (65)

References (30)
  • 1
    • 0034710920 scopus 로고    scopus 로고
    • Biochemistry, mutagenesis, and oligomerization of DsRed, a red fluorescent protein from coral
    • Baird G.S., Zacharias D.A., and Tsien R.Y. Biochemistry, mutagenesis, and oligomerization of DsRed, a red fluorescent protein from coral. Proc. Natl. Acad. Sci. USA 97 (2000) 11984-11989
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 11984-11989
    • Baird, G.S.1    Zacharias, D.A.2    Tsien, R.Y.3
  • 2
    • 1542336956 scopus 로고    scopus 로고
    • The molecular properties and applications of Anthozoa fluorescent proteins and chromoproteins
    • Verkhusha V.V., and Lukyanov K.A. The molecular properties and applications of Anthozoa fluorescent proteins and chromoproteins. Nat. Biotechnol. 22 (2004) 289-296
    • (2004) Nat. Biotechnol. , vol.22 , pp. 289-296
    • Verkhusha, V.V.1    Lukyanov, K.A.2
  • 3
  • 4
    • 0037564929 scopus 로고    scopus 로고
    • DsRed as a potential FRET partner with CFP and GFP
    • Erickson M.G., Moon D.L., and Yue D.T. DsRed as a potential FRET partner with CFP and GFP. Biophys. J. 85 (2003) 599-611
    • (2003) Biophys. J. , vol.85 , pp. 599-611
    • Erickson, M.G.1    Moon, D.L.2    Yue, D.T.3
  • 6
    • 33749075329 scopus 로고    scopus 로고
    • Anthozoa red fluorescent protein in biosensing
    • Shrestha S., and Deo S.K. Anthozoa red fluorescent protein in biosensing. Anal. Bioanal. Chem. 386 (2006) 515-524
    • (2006) Anal. Bioanal. Chem. , vol.386 , pp. 515-524
    • Shrestha, S.1    Deo, S.K.2
  • 7
    • 33646140570 scopus 로고    scopus 로고
    • Development of a novel GFP-based ratiometric excitation and emission pH indicator for intracellular studies
    • Bizzarri R., Arcangeli C., Arosio D., Ricci F., Faraci P., Cardarelli F., and Beltram F. Development of a novel GFP-based ratiometric excitation and emission pH indicator for intracellular studies. Biophys. J. 90 (2006) 3300-3314
    • (2006) Biophys. J. , vol.90 , pp. 3300-3314
    • Bizzarri, R.1    Arcangeli, C.2    Arosio, D.3    Ricci, F.4    Faraci, P.5    Cardarelli, F.6    Beltram, F.7
  • 8
    • 0035933577 scopus 로고    scopus 로고
    • Green fluorescent protein-based halide indicators with improved chloride and iodide affinities
    • Galietta L.J., Haggie P.M., and Verkman A.S. Green fluorescent protein-based halide indicators with improved chloride and iodide affinities. FEBS Lett. 499 (2001) 220-224
    • (2001) FEBS Lett. , vol.499 , pp. 220-224
    • Galietta, L.J.1    Haggie, P.M.2    Verkman, A.S.3
  • 9
    • 0033613235 scopus 로고    scopus 로고
    • Circular permutation and receptor insertion within green fluorescent proteins
    • Baird G.S., Zacharias D.A., and Tsien R.Y. Circular permutation and receptor insertion within green fluorescent proteins. Proc. Natl. Acad. Sci. USA 96 (1999) 11241-11246
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11241-11246
    • Baird, G.S.1    Zacharias, D.A.2    Tsien, R.Y.3
  • 11
    • 0034052719 scopus 로고    scopus 로고
    • Mechanism and cellular applications of a green fluorescent protein-based halide sensor
    • Jayaraman S., Haggie P., Wachter R.M., Remington S.J., and Verkman A.S. Mechanism and cellular applications of a green fluorescent protein-based halide sensor. J. Biol. Chem. 275 (2000) 6047-6050
    • (2000) J. Biol. Chem. , vol.275 , pp. 6047-6050
    • Jayaraman, S.1    Haggie, P.2    Wachter, R.M.3    Remington, S.J.4    Verkman, A.S.5
  • 12
    • 0034604399 scopus 로고    scopus 로고
    • Crystallographic and energetic analysis of binding of selected anions to the yellow variants of green fluorescent protein
    • Wachter R.M., Yarbrough D., Kallio K., and Remington S.J. Crystallographic and energetic analysis of binding of selected anions to the yellow variants of green fluorescent protein. J. Mol. Biol. 301 (2000) 157-171
    • (2000) J. Mol. Biol. , vol.301 , pp. 157-171
    • Wachter, R.M.1    Yarbrough, D.2    Kallio, K.3    Remington, S.J.4
  • 13
    • 33749318823 scopus 로고    scopus 로고
    • Variants of DsRed fluorescent protein: development of a copper sensor
    • Eli P., and Chakrabartty A. Variants of DsRed fluorescent protein: development of a copper sensor. Protein Sci. 15 (2006) 2442-2447
    • (2006) Protein Sci. , vol.15 , pp. 2442-2447
    • Eli, P.1    Chakrabartty, A.2
  • 15
    • 34247644884 scopus 로고    scopus 로고
    • Metal affinity-based purification of a red fluorescent protein
    • Rahimi Y. Metal affinity-based purification of a red fluorescent protein. Chromatographia 65 (2007) 429-433
    • (2007) Chromatographia , vol.65 , pp. 429-433
    • Rahimi, Y.1
  • 17
    • 41849113842 scopus 로고    scopus 로고
    • Y. Rahimi, S. Shrestha, S.K. Deo, Study of metal binding to monomeric red fluorescent protein, DsRed-Monomer, in: L.J. Kricka, Stanley, P.E. (Eds.), Proceedings of the 14th International Symposium on Bioluminescence and Chemiluminescence, San Diego, CA, Part 5, 2006, pp. 235-238.
    • Y. Rahimi, S. Shrestha, S.K. Deo, Study of metal binding to monomeric red fluorescent protein, DsRed-Monomer, in: L.J. Kricka, Stanley, P.E. (Eds.), Proceedings of the 14th International Symposium on Bioluminescence and Chemiluminescence, San Diego, CA, Part 5, 2006, pp. 235-238.
  • 19
    • 41849124575 scopus 로고    scopus 로고
    • Copper transport and Alzheimer's disease
    • Macreadie I.G. Copper transport and Alzheimer's disease. Eur. Biophys. J. (2007)
    • (2007) Eur. Biophys. J.
    • Macreadie, I.G.1
  • 20
    • 33847759062 scopus 로고    scopus 로고
    • Differential regulation of the Menkes and Wilson disease copper transporters by hormones: an integrated model of metal transport in the placenta
    • Richardson D.R., and Suryo Rahmanto Y. Differential regulation of the Menkes and Wilson disease copper transporters by hormones: an integrated model of metal transport in the placenta. Biochem. J. 402 (2007) e1-e3
    • (2007) Biochem. J. , vol.402
    • Richardson, D.R.1    Suryo Rahmanto, Y.2
  • 22
    • 41849133995 scopus 로고    scopus 로고
    • Living ColorsTM DsRed Monomer Fluorescent Protein, CLONTECHniques, 2005.
    • Living ColorsTM DsRed Monomer Fluorescent Protein, CLONTECHniques, 2005.
  • 24
    • 34247644884 scopus 로고    scopus 로고
    • Metal affinity-based purification of a red fluorescent protein
    • Rahimi Y., Surestha S., and Deo S.K. Metal affinity-based purification of a red fluorescent protein. Chromatographia 65 (2007) 429-433
    • (2007) Chromatographia , vol.65 , pp. 429-433
    • Rahimi, Y.1    Surestha, S.2    Deo, S.K.3
  • 25
    • 33751108289 scopus 로고    scopus 로고
    • The affinity of copper binding to the prion protein octarepeat domain: evidence for negative cooperativity
    • Walter E.D., Chattopadhyay M., and Millhauser G.L. The affinity of copper binding to the prion protein octarepeat domain: evidence for negative cooperativity. Biochemistry 45 (2006) 13083-13092
    • (2006) Biochemistry , vol.45 , pp. 13083-13092
    • Walter, E.D.1    Chattopadhyay, M.2    Millhauser, G.L.3
  • 26
    • 0027289198 scopus 로고
    • The design of metal-binding sites in proteins
    • Regan L. The design of metal-binding sites in proteins. Annu. Rev. Biophys. Biomol. Struct. 22 (1993) 257-287
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 257-287
    • Regan, L.1
  • 28
    • 0037531291 scopus 로고    scopus 로고
    • Single-molecule fluorescence lifetime and anisotropy measurements of the red fluorescent protein, DsRed, in solution
    • Bowen B., and Woodbury N. Single-molecule fluorescence lifetime and anisotropy measurements of the red fluorescent protein, DsRed, in solution. Photochem. Photobiol. 77 (2003) 362-369
    • (2003) Photochem. Photobiol. , vol.77 , pp. 362-369
    • Bowen, B.1    Woodbury, N.2
  • 29
    • 1842686905 scopus 로고    scopus 로고
    • Study of the interactions between tetracycline analogues and lysozyme
    • Jiang C.Q., and Wang T. Study of the interactions between tetracycline analogues and lysozyme. Bioorg. Med. Chem. 12 (2004) 2043-2047
    • (2004) Bioorg. Med. Chem. , vol.12 , pp. 2043-2047
    • Jiang, C.Q.1    Wang, T.2
  • 30
    • 0027190754 scopus 로고
    • Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network
    • Andrade M.A., Chacon P., Merelo J.J., and Moran F. Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network. Protein Eng. 6 (1993) 383-390
    • (1993) Protein Eng. , vol.6 , pp. 383-390
    • Andrade, M.A.1    Chacon, P.2    Merelo, J.J.3    Moran, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.