메뉴 건너뛰기




Volumn 407, Issue 1, 2011, Pages 230-235

Probing the structural determinants of yellow fluorescence of a protein from Phialidium sp

Author keywords

Autocatalysis; Chromophore; Fluorescence; Posttranslational modification

Indexed keywords

GREEN FLUORESCENT PROTEIN; YELLOW FLUORESCENT PROTEIN;

EID: 79953161803     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.03.004     Document Type: Article
Times cited : (14)

References (32)
  • 1
    • 70349328443 scopus 로고    scopus 로고
    • GFP: from jellyfish to the Nobel prize and beyond
    • Zimmer M. GFP: from jellyfish to the Nobel prize and beyond. Chem. Soc. Rev. 2009, 38:2823-2832.
    • (2009) Chem. Soc. Rev. , vol.38 , pp. 2823-2832
    • Zimmer, M.1
  • 2
    • 77955640606 scopus 로고    scopus 로고
    • Fluorescent proteins and their applications in imaging living cells and tissues
    • Chudakov D.M., Matz M.V., Lukyanov S., Lukyanov K.A. Fluorescent proteins and their applications in imaging living cells and tissues. Physiol. Rev. 2010, 90:1103-1163.
    • (2010) Physiol. Rev. , vol.90 , pp. 1103-1163
    • Chudakov, D.M.1    Matz, M.V.2    Lukyanov, S.3    Lukyanov, K.A.4
  • 3
    • 49449115068 scopus 로고    scopus 로고
    • GFP family: structural insights into spectral tuning
    • Pakhomov A.A., Martynov V.I. GFP family: structural insights into spectral tuning. Chem. Biol. 2008, 15:755-764.
    • (2008) Chem. Biol. , vol.15 , pp. 755-764
    • Pakhomov, A.A.1    Martynov, V.I.2
  • 4
    • 33947416691 scopus 로고    scopus 로고
    • Chromogenic cross-link formation in green fluorescent protein
    • Wachter R.M. Chromogenic cross-link formation in green fluorescent protein. Acc. Chem. Res. 2007, 40:120-127.
    • (2007) Acc. Chem. Res. , vol.40 , pp. 120-127
    • Wachter, R.M.1
  • 5
    • 0142027791 scopus 로고    scopus 로고
    • Mechanism and energetics of green fluorescent protein chromophore synthesis revealed by trapped intermediate structures
    • Barondeau D.P., Putnam C.D., Kassmann C.J., Tainer J.A., Getzoff E.D. Mechanism and energetics of green fluorescent protein chromophore synthesis revealed by trapped intermediate structures. Proc. Natl. Acad. Sci. USA 2003, 100:12111-12116.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12111-12116
    • Barondeau, D.P.1    Putnam, C.D.2    Kassmann, C.J.3    Tainer, J.A.4    Getzoff, E.D.5
  • 7
    • 55249109968 scopus 로고    scopus 로고
    • Structural characterization of a thiazoline-containing chromophore in an orange fluorescent protein monomeric Kusabira Orange
    • Kikuchi A., Fukumura E., Karasawa S., Mizuno H., Miyawaki A., Shiro Y. Structural characterization of a thiazoline-containing chromophore in an orange fluorescent protein monomeric Kusabira Orange. Biochemistry 2008, 47:11573-11580.
    • (2008) Biochemistry , vol.47 , pp. 11573-11580
    • Kikuchi, A.1    Fukumura, E.2    Karasawa, S.3    Mizuno, H.4    Miyawaki, A.5    Shiro, Y.6
  • 10
    • 77956152936 scopus 로고    scopus 로고
    • Mechanistic diversity of red fluorescence acquisition by GFP-like proteins
    • Wachter R.M., Watkins J.L., Kim H. Mechanistic diversity of red fluorescence acquisition by GFP-like proteins. Biochemistry 2010, 49:7417-7427.
    • (2010) Biochemistry , vol.49 , pp. 7417-7427
    • Wachter, R.M.1    Watkins, J.L.2    Kim, H.3
  • 12
    • 33745044208 scopus 로고    scopus 로고
    • Structure and reactivity of the chromophore of a GFP-like chromoprotein from Condylactis gigantea
    • Pakhomov A.A., Pletneva N.V., Balashova T.A., Martynov V.I. Structure and reactivity of the chromophore of a GFP-like chromoprotein from Condylactis gigantea. Biochemistry 2006, 45:7256-7264.
    • (2006) Biochemistry , vol.45 , pp. 7256-7264
    • Pakhomov, A.A.1    Pletneva, N.V.2    Balashova, T.A.3    Martynov, V.I.4
  • 14
    • 77649110107 scopus 로고    scopus 로고
    • Posttranslational reactions that shift spectra of asFP595 a protein from Anemonia sulcata towards the long-wavelength region
    • Pakhomov A.A., Tretyakova Y.A., Martynov V.I. Posttranslational reactions that shift spectra of asFP595 a protein from Anemonia sulcata towards the long-wavelength region. Russ. J. Bioorg. Chem. 2010, 36:109-113.
    • (2010) Russ. J. Bioorg. Chem. , vol.36 , pp. 109-113
    • Pakhomov, A.A.1    Tretyakova, Y.A.2    Martynov, V.I.3
  • 15
    • 34347259176 scopus 로고    scopus 로고
    • Chromophore structure of the kindling fluorescent protein asFP595 from Anemonia sulcata
    • Tretyakova Y.A., Pakhomov A.A., Martynov V.I. Chromophore structure of the kindling fluorescent protein asFP595 from Anemonia sulcata. J. Am. Chem. Soc. 2007, 129:7748-7749.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 7748-7749
    • Tretyakova, Y.A.1    Pakhomov, A.A.2    Martynov, V.I.3
  • 17
    • 0032532156 scopus 로고    scopus 로고
    • Structural basis of spectral shifts in the yellow-emission variants of green fluorescent protein
    • Wachter R.M., Elsliger M.A., Kallio K., Hanson G.T., Remington S.J. Structural basis of spectral shifts in the yellow-emission variants of green fluorescent protein. Structure 1998, 6:1267-1277.
    • (1998) Structure , vol.6 , pp. 1267-1277
    • Wachter, R.M.1    Elsliger, M.A.2    Kallio, K.3    Hanson, G.T.4    Remington, S.J.5
  • 19
    • 19744378582 scopus 로고    scopus 로고
    • Maturation efficiency trypsin sensitivity optical properties of Arg96 Glu222 and Gly67 variants of green fluorescent protein
    • Sniegowski J.A., Phail M.E., Wachter R.M. Maturation efficiency trypsin sensitivity optical properties of Arg96 Glu222 and Gly67 variants of green fluorescent protein. Biochem. Biophys. Res. Commun. 2005, 332:657-663.
    • (2005) Biochem. Biophys. Res. Commun. , vol.332 , pp. 657-663
    • Sniegowski, J.A.1    Phail, M.E.2    Wachter, R.M.3
  • 21
    • 0027136282 scopus 로고
    • Comparative protein modeling by satisfaction of spatial restraints
    • Sali A., Blundell T.L. Comparative protein modeling by satisfaction of spatial restraints. J. Mol. Biol. 1993, 234:779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 23
    • 22544460277 scopus 로고    scopus 로고
    • Base catalysis of chromophore formation in Arg96 and Glu222 variants of green fluorescent protein
    • Sniegowski J.A., Lappe J.W., Patel H.N., Huffman H.A., Wachter R.M. Base catalysis of chromophore formation in Arg96 and Glu222 variants of green fluorescent protein. J. Biol. Chem. 2005, 280:26248-26255.
    • (2005) J. Biol. Chem. , vol.280 , pp. 26248-26255
    • Sniegowski, J.A.1    Lappe, J.W.2    Patel, H.N.3    Huffman, H.A.4    Wachter, R.M.5
  • 24
    • 0036138908 scopus 로고    scopus 로고
    • A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications
    • Nagai T., Ibata K., Park E.S., Kubota M., Mikoshiba K., Miyawaki A. A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications. Nat. Biotechnol. 2002, 20:87-90.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 87-90
    • Nagai, T.1    Ibata, K.2    Park, E.S.3    Kubota, M.4    Mikoshiba, K.5    Miyawaki, A.6
  • 25
  • 27
    • 0029757121 scopus 로고    scopus 로고
    • Ultra-fast excited state dynamics in green fluorescent prote multiple states and proton transfer
    • Chattoraj M., King B.A., Bublitz G.U., Boxer S.G. Ultra-fast excited state dynamics in green fluorescent prote multiple states and proton transfer. Proc. Natl. Acad. Sci. USA 1996, 93:8362-8367.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8362-8367
    • Chattoraj, M.1    King, B.A.2    Bublitz, G.U.3    Boxer, S.G.4
  • 28
    • 0001350436 scopus 로고    scopus 로고
    • Effects of threonine 203 replacements on excited-state dynamics and fluorescence properties of the green fluorescent protein (GFP)
    • Kummer A.D., Wiehler J., Rehaber H., Kompa C., Steipe B., Michel-Beyerle M.E. Effects of threonine 203 replacements on excited-state dynamics and fluorescence properties of the green fluorescent protein (GFP). J. Phys. Chem. B 2000, 104:4791-4798.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 4791-4798
    • Kummer, A.D.1    Wiehler, J.2    Rehaber, H.3    Kompa, C.4    Steipe, B.5    Michel-Beyerle, M.E.6
  • 29
    • 19744365121 scopus 로고    scopus 로고
    • The photophysics of green fluorescent prote influence of the key amino acids at positions 65, 203, and 222
    • Jung G., Wiehler J., Zumbusch A. The photophysics of green fluorescent prote influence of the key amino acids at positions 65, 203, and 222. Biophys. J. 2005, 88:1932-1947.
    • (2005) Biophys. J. , vol.88 , pp. 1932-1947
    • Jung, G.1    Wiehler, J.2    Zumbusch, A.3
  • 30
    • 1642542523 scopus 로고    scopus 로고
    • Solution pKa values of the green fluorescent protein chromophore from hybrid quantum-classical calculations
    • Scharnagl C., Raupp-Kossmann R.A. Solution pKa values of the green fluorescent protein chromophore from hybrid quantum-classical calculations. J. Phys. Chem. 2004, 108:477-489.
    • (2004) J. Phys. Chem. , vol.108 , pp. 477-489
    • Scharnagl, C.1    Raupp-Kossmann, R.A.2
  • 31
    • 0033609034 scopus 로고    scopus 로고
    • Structural and spectral response of green fluorescent protein variants to changes in pH
    • Elsliger M.A., Wachter R.M., Hanson G.T., Kallio K., Remington S.J. Structural and spectral response of green fluorescent protein variants to changes in pH. Biochemistry 1999, 38:5296-5301.
    • (1999) Biochemistry , vol.38 , pp. 5296-5301
    • Elsliger, M.A.1    Wachter, R.M.2    Hanson, G.T.3    Kallio, K.4    Remington, S.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.