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Volumn 375, Issue 3, 2008, Pages 351-355

Intrinsic fluorescence as an analytical probe of virus-like particle assembly and maturation

Author keywords

Intrinsic fluorescence; Maturation; Papillomavirus; Self assembly; Tryptophan fluorescence; Virus like particle

Indexed keywords

GLUTATHIONE;

EID: 50849126046     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.08.019     Document Type: Article
Times cited : (18)

References (20)
  • 2
    • 0030610813 scopus 로고    scopus 로고
    • L-1(a) and L-1(b) transitions of tryptophan: applications of theory and experimental observations to fluorescence of proteins
    • Callis P.R. L-1(a) and L-1(b) transitions of tryptophan: applications of theory and experimental observations to fluorescence of proteins. Methods Enzymol. 278 (1997) 113-150
    • (1997) Methods Enzymol. , vol.278 , pp. 113-150
    • Callis, P.R.1
  • 3
    • 0016287129 scopus 로고
    • Intramolecular distances determined by energy-transfer-dependence on orientational freedom of donor and acceptor
    • Dale R.E., and Eisinger J. Intramolecular distances determined by energy-transfer-dependence on orientational freedom of donor and acceptor. Biopolymers 13 (1974) 1573-1605
    • (1974) Biopolymers , vol.13 , pp. 1573-1605
    • Dale, R.E.1    Eisinger, J.2
  • 4
    • 0032516433 scopus 로고    scopus 로고
    • Toward understanding tryptophan fluorescence in proteins
    • Chen Y., and Barkley M.D. Toward understanding tryptophan fluorescence in proteins. Biochemistry 37 (1998) 9976-9982
    • (1998) Biochemistry , vol.37 , pp. 9976-9982
    • Chen, Y.1    Barkley, M.D.2
  • 5
    • 0028053187 scopus 로고
    • Understanding how proteins fold-the lysozyme story so far
    • Dobson C.M., Evans P.A., and Radford S.E. Understanding how proteins fold-the lysozyme story so far. Trends Biochem. Sci. 19 (1994) 31-37
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 31-37
    • Dobson, C.M.1    Evans, P.A.2    Radford, S.E.3
  • 6
    • 0031937871 scopus 로고    scopus 로고
    • Stability and folding properties of a model beta-sheet protein, Escherichia coli CspA
    • Reid K.L., Rodriguez H.M., J Hillier B., and Gregoret L.M. Stability and folding properties of a model beta-sheet protein, Escherichia coli CspA. Protein Sci. 7 (1998) 470-479
    • (1998) Protein Sci. , vol.7 , pp. 470-479
    • Reid, K.L.1    Rodriguez, H.M.2    J Hillier, B.3    Gregoret, L.M.4
  • 7
    • 0042035633 scopus 로고    scopus 로고
    • Folding of phage P22 coat protein monomers: kinetic and thermodynamic properties
    • Anderson E., and Teschke C.M. Folding of phage P22 coat protein monomers: kinetic and thermodynamic properties. Virology 313 (2003) 184-197
    • (2003) Virology , vol.313 , pp. 184-197
    • Anderson, E.1    Teschke, C.M.2
  • 8
    • 33745820802 scopus 로고    scopus 로고
    • Conformational stability and disassembly of Norwalk virus-like particles-effect of pH and temperature
    • Ausar S.F., Foubert T.R., Hudson M.H., Vedvick T.S., and Middaugh C.R. Conformational stability and disassembly of Norwalk virus-like particles-effect of pH and temperature. J. Biol. Chem. 281 (2006) 19478-19488
    • (2006) J. Biol. Chem. , vol.281 , pp. 19478-19488
    • Ausar, S.F.1    Foubert, T.R.2    Hudson, M.H.3    Vedvick, T.S.4    Middaugh, C.R.5
  • 9
    • 0037705348 scopus 로고    scopus 로고
    • Observed hysteresis of virus capsid disassembly is implicit in kinetic models of assembly
    • Singh S., and Zlotnick A. Observed hysteresis of virus capsid disassembly is implicit in kinetic models of assembly. J. Biol. Chem. 278 (2003) 18249-18255
    • (2003) J. Biol. Chem. , vol.278 , pp. 18249-18255
    • Singh, S.1    Zlotnick, A.2
  • 10
    • 2942720746 scopus 로고    scopus 로고
    • Evidence that a local refolding event triggers maturation of HK97 bacteriophage capsid
    • Lee K.K., Gan L., Tsuruta H., Hendrix R.W., Duda R.L., and Johnson J.E. Evidence that a local refolding event triggers maturation of HK97 bacteriophage capsid. J. Mol. Biol. 340 (2004) 419-433
    • (2004) J. Mol. Biol. , vol.340 , pp. 419-433
    • Lee, K.K.1    Gan, L.2    Tsuruta, H.3    Hendrix, R.W.4    Duda, R.L.5    Johnson, J.E.6
  • 11
    • 0030983747 scopus 로고    scopus 로고
    • Expression of the human papillomavirus type 11 L1 capsid protein in Escherichia coli: characterization of protein domains involved in DNA binding and capsid assembly
    • Li M.L., Cripe T.P., Estes P.A., Lyon M.K., Rose R.C., and Garcea R.L. Expression of the human papillomavirus type 11 L1 capsid protein in Escherichia coli: characterization of protein domains involved in DNA binding and capsid assembly. J. Virol. 71 (1997) 2988-2995
    • (1997) J. Virol. , vol.71 , pp. 2988-2995
    • Li, M.L.1    Cripe, T.P.2    Estes, P.A.3    Lyon, M.K.4    Rose, R.C.5    Garcea, R.L.6
  • 12
    • 0031777693 scopus 로고    scopus 로고
    • Papillomavirus assembly requires trimerization of the major capsid protein by disulfides between two highly conserved cysteines
    • Sapp M., Fligge C., Petzak I., Harris J.R., and Streeck R.E. Papillomavirus assembly requires trimerization of the major capsid protein by disulfides between two highly conserved cysteines. J. Virol. 72 (1998) 6186-6189
    • (1998) J. Virol. , vol.72 , pp. 6186-6189
    • Sapp, M.1    Fligge, C.2    Petzak, I.3    Harris, J.R.4    Streeck, R.E.5
  • 13
    • 0026329210 scopus 로고
    • Structures of Bovine and Human Papillomaviruses-analysis by cryoelectron microscopy and 3-dimensional image-reconstruction
    • Baker T.S., Newcomb W.W., Olson N.H., Cowsert L.M., Olson C., and Brown J.C. Structures of Bovine and Human Papillomaviruses-analysis by cryoelectron microscopy and 3-dimensional image-reconstruction. Biophys. J. 60 (1991) 445-1456
    • (1991) Biophys. J. , vol.60 , pp. 445-1456
    • Baker, T.S.1    Newcomb, W.W.2    Olson, N.H.3    Cowsert, L.M.4    Olson, C.5    Brown, J.C.6
  • 14
    • 0037119997 scopus 로고    scopus 로고
    • Atomic model of the papillomavirus capsid
    • Modis Y., Trus B.L., and Harrison S.C. Atomic model of the papillomavirus capsid. EMBO J. 21 (2002) 4754-4762
    • (2002) EMBO J. , vol.21 , pp. 4754-4762
    • Modis, Y.1    Trus, B.L.2    Harrison, S.C.3
  • 15
    • 3142634785 scopus 로고    scopus 로고
    • In vitro papillomavirus capsid assembly analyzed by light scattering
    • Casini G.L., Graham D., Heine D., Garcea R.L., and Wu D.T. In vitro papillomavirus capsid assembly analyzed by light scattering. Virology 325 (2004) 320-327
    • (2004) Virology , vol.325 , pp. 320-327
    • Casini, G.L.1    Graham, D.2    Heine, D.3    Garcea, R.L.4    Wu, D.T.5
  • 17
    • 0035896012 scopus 로고    scopus 로고
    • Papillomavirus capsid protein expression in Escherichia coli: purification and assembly of HPV11 and HPV16 L1
    • Chen X.J.S., Casini G., Harrison S.C., and Garcea R.L. Papillomavirus capsid protein expression in Escherichia coli: purification and assembly of HPV11 and HPV16 L1. J. Mol. Biol. 307 (2001) 173-182
    • (2001) J. Mol. Biol. , vol.307 , pp. 173-182
    • Chen, X.J.S.1    Casini, G.2    Harrison, S.C.3    Garcea, R.L.4
  • 18
    • 0034866669 scopus 로고    scopus 로고
    • Decomposition of protein tryptophan fluorescence spectra into log-normal components. II: The statistical proof of discreteness of tryptophan classes in proteins
    • Reshetnyak Y.K., and Burstein E.A. Decomposition of protein tryptophan fluorescence spectra into log-normal components. II: The statistical proof of discreteness of tryptophan classes in proteins. Biophys. J. 81 (2001) 1710-1734
    • (2001) Biophys. J. , vol.81 , pp. 1710-1734
    • Reshetnyak, Y.K.1    Burstein, E.A.2
  • 19
    • 33646065318 scopus 로고    scopus 로고
    • Assembly of human papillomavirus type-16 virus-like particles: multifactorial study of assembly and competing aggregation
    • Hanslip S.J., Zaccai N.R., Middelberg A.P.J., and Falconer R.J. Assembly of human papillomavirus type-16 virus-like particles: multifactorial study of assembly and competing aggregation. Biotechnol. Prog. 22 (2006) 554-560
    • (2006) Biotechnol. Prog. , vol.22 , pp. 554-560
    • Hanslip, S.J.1    Zaccai, N.R.2    Middelberg, A.P.J.3    Falconer, R.J.4
  • 20
    • 34347265820 scopus 로고    scopus 로고
    • In vitro screening for molecules that affect virus capsid assembly (and other protein association reactions)
    • Zlotnick A., Lee A., Bourne C.R., Johnson J.M., Domanico P.L., and Stray S.J. In vitro screening for molecules that affect virus capsid assembly (and other protein association reactions). Nat. Protoc. 2 (2007) 490-498
    • (2007) Nat. Protoc. , vol.2 , pp. 490-498
    • Zlotnick, A.1    Lee, A.2    Bourne, C.R.3    Johnson, J.M.4    Domanico, P.L.5    Stray, S.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.