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Volumn 49, Issue 45, 2010, Pages 9830-9838

Self-association of the adenoviral L4-22K protein

Author keywords

[No Author keywords available]

Indexed keywords

ASSEMBLY PROCESS; CORE PROTEINS; DNA-PACKAGING; DOUBLE STRANDED DNA; EQUILIBRIUM ASSOCIATION CONSTANT; FREE CONCENTRATION; GASTROINTESTINAL TRACT; HIGHER-ORDER STRUCTURE; HUMAN ADENOVIRUS; ISODESMIC; RESPIRATORY TRACT; SELF-ASSOCIATIONS; SPECIFIC BINDING; TRANSCRIPTIONAL ACTIVATORS; URINARY TRACT; VIRAL GENOME; VIRAL PROTEINS;

EID: 78149456074     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi101144q     Document Type: Article
Times cited : (5)

References (31)
  • 1
    • 4544261298 scopus 로고    scopus 로고
    • Treatment of adenovirus infections in the immunocompromised host
    • Ljungman, P. (2004) Treatment of adenovirus infections in the immunocompromised host Eur. J. Clin. Microbiol. Infect. Dis. 23, 583-588
    • (2004) Eur. J. Clin. Microbiol. Infect. Dis. , vol.23 , pp. 583-588
    • Ljungman, P.1
  • 2
    • 9244257887 scopus 로고    scopus 로고
    • Biology of adenovirus and its use as a vector for gene therapy
    • McConnell, M. J. and Imperiale, M. J. (2004) Biology of adenovirus and its use as a vector for gene therapy Hum. Gene Ther. 15, 1022-1033
    • (2004) Hum. Gene Ther. , vol.15 , pp. 1022-1033
    • McConnell, M.J.1    Imperiale, M.J.2
  • 3
    • 26444561955 scopus 로고    scopus 로고
    • Control of adenovirus packaging
    • Ostapchuk, P. and Hearing, P. (2005) Control of adenovirus packaging J. Cell. Biochem. 96, 25-35
    • (2005) J. Cell. Biochem. , vol.96 , pp. 25-35
    • Ostapchuk, P.1    Hearing, P.2
  • 4
    • 36048969242 scopus 로고    scopus 로고
    • Ternary complex formation on the adenovirus packaging sequence by the IVa2 and L4 22-kilodalton proteins
    • Ewing, S. G., Byrd, S. A., Christensen, J. B., Tyler, R. E., and Imperiale, M. J. (2007) Ternary complex formation on the adenovirus packaging sequence by the IVa2 and L4 22-kilodalton proteins J. Virol. 81, 12450-12457
    • (2007) J. Virol. , vol.81 , pp. 12450-12457
    • Ewing, S.G.1    Byrd, S.A.2    Christensen, J.B.3    Tyler, R.E.4    Imperiale, M.J.5
  • 5
    • 33745780727 scopus 로고    scopus 로고
    • The L4 22-kilodalton protein plays a role in packaging of the adenovirus genome
    • Ostapchuk, P., Anderson, M. E., Chandrasekhar, S., and Hearing, P. (2006) The L4 22-kilodalton protein plays a role in packaging of the adenovirus genome J. Virol. 80, 6973-6981
    • (2006) J. Virol. , vol.80 , pp. 6973-6981
    • Ostapchuk, P.1    Anderson, M.E.2    Chandrasekhar, S.3    Hearing, P.4
  • 6
    • 33947427084 scopus 로고    scopus 로고
    • Formation of a multiple protein complex on the adenovirus packaging sequence by the IVa2 protein
    • Tyler, R. E., Ewing, S. G., and Imperiale, M. J. (2007) Formation of a multiple protein complex on the adenovirus packaging sequence by the IVa2 protein J. Virol. 81, 3447-3454
    • (2007) J. Virol. , vol.81 , pp. 3447-3454
    • Tyler, R.E.1    Ewing, S.G.2    Imperiale, M.J.3
  • 7
    • 0037334484 scopus 로고    scopus 로고
    • Requirement of the adenovirus IVa2 protein for virus assembly
    • Zhang, W. and Imperiale, M. J. (2003) Requirement of the adenovirus IVa2 protein for virus assembly J. Virol. 77, 3586-3594
    • (2003) J. Virol. , vol.77 , pp. 3586-3594
    • Zhang, W.1    Imperiale, M.J.2
  • 8
    • 0025265591 scopus 로고
    • Adenovirus type 5 packaging domain is composed of a repeated element that is functionally redundant
    • Grable, M. and Hearing, P. (1990) Adenovirus type 5 packaging domain is composed of a repeated element that is functionally redundant J. Virol. 64, 2047-2056
    • (1990) J. Virol. , vol.64 , pp. 2047-2056
    • Grable, M.1    Hearing, P.2
  • 9
    • 0030894765 scopus 로고    scopus 로고
    • Bipartite structure and functional independence of adenovirus type 5 packaging elements
    • Schmid, S. I. and Hearing, P. (1997) Bipartite structure and functional independence of adenovirus type 5 packaging elements J. Virol. 71, 3375-3384
    • (1997) J. Virol. , vol.71 , pp. 3375-3384
    • Schmid, S.I.1    Hearing, P.2
  • 10
    • 33846472402 scopus 로고    scopus 로고
    • The adenovirus L4 33-kilodalton protein binds to intragenic sequences of the major late promoter required for late phase-specific stimulation of transcription
    • Ali, H., LeRoy, G., Bridge, G., and Flint, S. J. (2007) The adenovirus L4 33-kilodalton protein binds to intragenic sequences of the major late promoter required for late phase-specific stimulation of transcription J. Virol. 81, 1327-1338
    • (2007) J. Virol. , vol.81 , pp. 1327-1338
    • Ali, H.1    Leroy, G.2    Bridge, G.3    Flint, S.J.4
  • 11
    • 0030025840 scopus 로고    scopus 로고
    • Properties of the adenovirus IVa2 gene product, an effector of late-phase-dependent activation of the major late promoter
    • Lutz, P. and Kedinger, C. (1996) Properties of the adenovirus IVa2 gene product, an effector of late-phase-dependent activation of the major late promoter J. Virol. 70, 1396-1405
    • (1996) J. Virol. , vol.70 , pp. 1396-1405
    • Lutz, P.1    Kedinger, C.2
  • 12
    • 0028227606 scopus 로고
    • The product of the adenovirus intermediate gene IVa2 is a transcriptional activator of the major late promoter
    • Tribouley, C., Lutz, P., Staub, A., and Kedinger, C. (1994) The product of the adenovirus intermediate gene IVa2 is a transcriptional activator of the major late promoter J. Virol. 68, 4450-4457
    • (1994) J. Virol. , vol.68 , pp. 4450-4457
    • Tribouley, C.1    Lutz, P.2    Staub, A.3    Kedinger, C.4
  • 13
    • 0042855798 scopus 로고    scopus 로고
    • On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation
    • Schuck, P. (2003) On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation Anal. Biochem. 320, 104-124
    • (2003) Anal. Biochem. , vol.320 , pp. 104-124
    • Schuck, P.1
  • 14
    • 1642309516 scopus 로고    scopus 로고
    • Global analysis of non-specific protein-nucleic interactions by sedimentation equilibrium
    • Ucci, J. W. and Cole, J. L. (2004) Global analysis of non-specific protein-nucleic interactions by sedimentation equilibrium Biophys. Chem. 108, 127-140
    • (2004) Biophys. Chem. , vol.108 , pp. 127-140
    • Ucci, J.W.1    Cole, J.L.2
  • 15
    • 7744243144 scopus 로고    scopus 로고
    • Comparisons of Indefinite Self-Association Models
    • Martin, R. B. (1996) Comparisons of Indefinite Self-Association Models Chem. Rev. 96, 3043-3064
    • (1996) Chem. Rev. , vol.96 , pp. 3043-3064
    • Martin, R.B.1
  • 16
    • 0018928849 scopus 로고
    • Stoichiometry of the vinblastine-induced self-association of calf brain tubulin
    • Na, G. C. and Timasheff, S. N. (1980) Stoichiometry of the vinblastine-induced self-association of calf brain tubulin Biochemistry 19, 1347-1354
    • (1980) Biochemistry , vol.19 , pp. 1347-1354
    • Na, G.C.1    Timasheff, S.N.2
  • 17
    • 33947613349 scopus 로고
    • A theory of linear and helical aggregations of macromolecules
    • Oosawa, F. and Kasai, M. (1962) A theory of linear and helical aggregations of macromolecules J. Mol. Biol. 4, 10-21
    • (1962) J. Mol. Biol. , vol.4 , pp. 10-21
    • Oosawa, F.1    Kasai, M.2
  • 18
    • 1642298085 scopus 로고    scopus 로고
    • A comparison of weight average and direct boundary fitting of sedimentation velocity data for indefinite polymerizing systems
    • Sontag, C. A., Stafford, W. F., and Correia, J. J. (2004) A comparison of weight average and direct boundary fitting of sedimentation velocity data for indefinite polymerizing systems Biophys. Chem. 108, 215-230
    • (2004) Biophys. Chem. , vol.108 , pp. 215-230
    • Sontag, C.A.1    Stafford, W.F.2    Correia, J.J.3
  • 21
    • 58549102104 scopus 로고    scopus 로고
    • Interaction of the adenoviral IVa2 protein with a truncated viral DNA packaging sequence
    • Yang, T. C., Yang, Q., and Maluf, N. K. (2009) Interaction of the adenoviral IVa2 protein with a truncated viral DNA packaging sequence Biophys. Chem. 140, 78-90
    • (2009) Biophys. Chem. , vol.140 , pp. 78-90
    • Yang, T.C.1    Yang, Q.2    Maluf, N.K.3
  • 22
    • 0015241654 scopus 로고
    • Hydration of macromolecules. IV. Polypeptide conformation in frozen solutions
    • Kuntz, I. D. (1971) Hydration of macromolecules. IV. Polypeptide conformation in frozen solutions J. Am. Chem. Soc. 93, 516-518
    • (1971) J. Am. Chem. Soc. , vol.93 , pp. 516-518
    • Kuntz, I.D.1
  • 23
    • 0036153571 scopus 로고    scopus 로고
    • What does it mean to be natively unfolded?
    • Uversky, V. N. (2002) What does it mean to be natively unfolded? Eur. J. Biochem. 269, 2-12
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2-12
    • Uversky, V.N.1
  • 24
    • 0003060984 scopus 로고
    • Comments on the analysis of sedimentation equilibrium experiments
    • Birkhauser, Boston
    • Johnson, M. L. and Straume, M. (1994) Comments on the analysis of sedimentation equilibrium experiments. In Modern Analytical Ultracentrifugation, pp 37 - 65, Birkhauser, Boston.
    • (1994) Modern Analytical Ultracentrifugation , pp. 37-65
    • Johnson, M.L.1    Straume, M.2
  • 25
    • 0034668130 scopus 로고    scopus 로고
    • Determination of the sedimentation coefficient distribution by least-squares boundary modeling
    • Schuck, P. and Rossmanith, P. (2000) Determination of the sedimentation coefficient distribution by least-squares boundary modeling Biopolymers 54, 328-341
    • (2000) Biopolymers , vol.54 , pp. 328-341
    • Schuck, P.1    Rossmanith, P.2
  • 26
    • 0028672523 scopus 로고
    • Boundary analysis in sedimentation velocity experiments
    • Stafford, W. F., III (1994) Boundary analysis in sedimentation velocity experiments Methods Enzymol. 240, 478-501
    • (1994) Methods Enzymol. , vol.240 , pp. 478-501
    • Stafford III, W.F.1
  • 27
    • 0029118618 scopus 로고
    • Sedimentation equilibrium as thermodynamic tool
    • Laue, T. M. (1995) Sedimentation equilibrium as thermodynamic tool Methods Enzymol. 259, 427-452
    • (1995) Methods Enzymol. , vol.259 , pp. 427-452
    • Laue, T.M.1
  • 28
    • 0024418550 scopus 로고
    • A thermodynamic model for the self-association of human spectrin
    • Morris, M. and Ralston, G. B. (1989) A thermodynamic model for the self-association of human spectrin Biochemistry 28, 8561-8567
    • (1989) Biochemistry , vol.28 , pp. 8561-8567
    • Morris, M.1    Ralston, G.B.2
  • 29
    • 0026351773 scopus 로고
    • Thermodynamic methods for model-independent determination of equilibrium binding isotherms for protein-DNA interactions: Spectroscopic approaches to monitor binding
    • Lohman, T. M. and Bujalowski, W. (1991) Thermodynamic methods for model-independent determination of equilibrium binding isotherms for protein-DNA interactions: Spectroscopic approaches to monitor binding Methods Enzymol. 208, 258-290
    • (1991) Methods Enzymol. , vol.208 , pp. 258-290
    • Lohman, T.M.1    Bujalowski, W.2
  • 30
    • 0343659146 scopus 로고
    • Ligand-linked phase changes in a biological system: Applications to sickle cell hemoglobin
    • Wyman, J. and Gill, S. J. (1980) Ligand-linked phase changes in a biological system: Applications to sickle cell hemoglobin Proc. Natl. Acad. Sci. U.S.A. 77, 5239-5242
    • (1980) Proc. Natl. Acad. Sci. U.S.A. , vol.77 , pp. 5239-5242
    • Wyman, J.1    Gill, S.J.2


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