메뉴 건너뛰기




Volumn 118, Issue 8, 2014, Pages 1984-1989

Electrophoretic mobilities of a viral capsid, its capsid protein, and their relation to viral assembly

Author keywords

[No Author keywords available]

Indexed keywords

IONIC STRENGTH; PHASE DIAGRAMS; PROTEINS; VIRUSES;

EID: 84897607823     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp407379t     Document Type: Article
Times cited : (36)

References (35)
  • 1
    • 0014905804 scopus 로고
    • The Self-Assembly of Spherical Plant Viruses
    • Bancroft, J. B. The Self-Assembly of Spherical Plant Viruses Adv. Virus Res. 1970, 116, 99
    • (1970) Adv. Virus Res. , vol.116 , pp. 99
    • Bancroft, J.B.1
  • 2
    • 84894026358 scopus 로고    scopus 로고
    • The Assembly Pathway of an Icosahedral Single-Stranded RNA Virus Depends on the Strength of Inter-Subunit Attractions
    • in press
    • Garmann, R. F.; Comas-Garcia, M.; Gopal, A.; Knobler, C. M.; Gelbart, W. M. The Assembly Pathway of an Icosahedral Single-Stranded RNA Virus Depends on the Strength of Inter-Subunit Attractions. J. Mol. Biol. 2014, in press
    • (2014) J. Mol. Biol.
    • Garmann, R.F.1    Comas-Garcia, M.2    Gopal, A.3    Knobler, C.M.4    Gelbart, W.M.5
  • 6
    • 65249178527 scopus 로고
    • A Titrimetric and Electrophoretic Study of Cowpea Chlorotic Mottle Virus and its Protein
    • Johnson, M. W.; Wagner, G. W.; Bancroft, J. B. A Titrimetric and Electrophoretic Study of Cowpea Chlorotic Mottle Virus and its Protein J. Gen. Virol. 1973, 19, 263
    • (1973) J. Gen. Virol. , vol.19 , pp. 263
    • Johnson, M.W.1    Wagner, G.W.2    Bancroft, J.B.3
  • 7
    • 0014060143 scopus 로고
    • Biochemical and Biophysical Properties of Cucumber Mosaic Virus
    • Van Regenmortel, M. H. V. Biochemical and Biophysical Properties of Cucumber Mosaic Virus Virology 1967, 31, 391
    • (1967) Virology , vol.31 , pp. 391
    • Van Regenmortel, M.H.V.1
  • 8
    • 0012857086 scopus 로고
    • The Electrokinetic Properties of Reovirus Type 3: Electrophoretic Mobility and Zeta Potential in Dilute Electrolytes
    • Taylor, D. H.; Bosmann, H. B. The Electrokinetic Properties of Reovirus Type 3: Electrophoretic Mobility and Zeta Potential in Dilute Electrolytes J. Colloid Interface Sci. 1981, 83, 153
    • (1981) J. Colloid Interface Sci. , vol.83 , pp. 153
    • Taylor, D.H.1    Bosmann, H.B.2
  • 10
    • 43049125220 scopus 로고    scopus 로고
    • Impact of Chemical and Structural Anisotropy on the Electrophoretic Mobility of Spherical Soft Multilayer Particles: The Case of Bacteriophage MS2
    • Langlet, J.; Gaboriaud, F.; Gantzer, C.; Duval, J. F.L. Impact of Chemical and Structural Anisotropy on the Electrophoretic Mobility of Spherical Soft Multilayer Particles: The Case of Bacteriophage MS2 Biophys. J. 2008, 94, 3293
    • (2008) Biophys. J. , vol.94 , pp. 3293
    • Langlet, J.1    Gaboriaud, F.2    Gantzer, C.3    Duval, J.F.L.4
  • 11
    • 79961060279 scopus 로고    scopus 로고
    • Impact of Internal RNA on Aggregation and Electrokinetics of Viruses: Comparison between MS2 Phage and Corresponding Virus-Like Particles
    • Dika, C.; Duval, J. F. L.; Ly-Chatain, H. M.; Merlin, C.; Gantzer, C. Impact of Internal RNA on Aggregation and Electrokinetics of Viruses: Comparison between MS2 Phage and Corresponding Virus-Like Particles Appl. Environ. Microbiol. 2011, 77, 4939
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 4939
    • Dika, C.1    Duval, J.F.L.2    Ly-Chatain, H.M.3    Merlin, C.4    Gantzer, C.5
  • 12
  • 13
  • 14
    • 33646338607 scopus 로고    scopus 로고
    • Electrophoresis of Diffuse Soft Particles
    • Duval, J. F. L.; Ohshima, H. Electrophoresis of Diffuse Soft Particles Langmuir 2006, 22, 3533
    • (2006) Langmuir , vol.22 , pp. 3533
    • Duval, J.F.L.1    Ohshima, H.2
  • 17
    • 0014975080 scopus 로고
    • Limited hydrolysis of cowpea chlorotic mottle virus by trypsin and chymotrypsin
    • Chidlow, J.; Tremaine, J. H. Limited hydrolysis of cowpea chlorotic mottle virus by trypsin and chymotrypsin Virology 1971, 43, 267
    • (1971) Virology , vol.43 , pp. 267
    • Chidlow, J.1    Tremaine, J.H.2
  • 18
    • 0014251162 scopus 로고
    • Properties of Cowpea Chlorotic Mottle Virus, Its Protein and Nucleic Acid
    • Bancroft, J. B.; Hiebert, E.; Rees, M. W.; Markham, R. Properties of Cowpea Chlorotic Mottle Virus, Its Protein and Nucleic Acid Virology 1968, 34, 224
    • (1968) Virology , vol.34 , pp. 224
    • Bancroft, J.B.1    Hiebert, E.2    Rees, M.W.3    Markham, R.4
  • 19
    • 0016286094 scopus 로고
    • Studies on the Assembly of a Spherical Plant Virus I. States of Aggregation of the Isolated Protein
    • Adolph, K. W.; Butler, P. J. G. Studies on the Assembly of a Spherical Plant Virus I. States of Aggregation of the Isolated Protein J. Mol. Biol. 1974, 88, 327
    • (1974) J. Mol. Biol. , vol.88 , pp. 327
    • Adolph, K.W.1    Butler, P.J.G.2
  • 21
    • 84857959507 scopus 로고    scopus 로고
    • Self-Assembly of Viral Capsid Protein and RNA Molecules of Different Sizes: Requirement for a Specific High Protein/RNA Mass Ratio
    • Cadena-Nava, R.; Comas-Garcia, M.; Garmann, R. F.; Rao, A. L. N.; Knobler, C. M.; Gelbart, W. M. Self-Assembly of Viral Capsid Protein and RNA Molecules of Different Sizes: Requirement for a Specific High Protein/RNA Mass Ratio J. Virol. 2012, 86, 3318
    • (2012) J. Virol. , vol.86 , pp. 3318
    • Cadena-Nava, R.1    Comas-Garcia, M.2    Garmann, R.F.3    Rao, A.L.N.4    Knobler, C.M.5    Gelbart, W.M.6
  • 22
    • 38949124465 scopus 로고    scopus 로고
    • Packaging of a Polymer by a Viral Capsid: The Interplay between Polymer Length and Capsid Size
    • Hu, Y.; Zandi, R.; Anavitarte, A.; Knobler, C. M.; Gelbart, W. M. Packaging of a Polymer by a Viral Capsid: The Interplay Between Polymer Length and Capsid Size Biophys. J. 2008, 94, 1428
    • (2008) Biophys. J. , vol.94 , pp. 1428
    • Hu, Y.1    Zandi, R.2    Anavitarte, A.3    Knobler, C.M.4    Gelbart, W.M.5
  • 23
    • 79551478383 scopus 로고    scopus 로고
    • Encapsulation of a Polymer by an Icosahedral Virus
    • 045003
    • Elrad, O. M.; Hagan, M. F. Encapsulation of a Polymer by an Icosahedral Virus Phys. Biol. 2010, 7 045003
    • (2010) Phys. Biol. , vol.7
    • Elrad, O.M.1    Hagan, M.F.2
  • 24
    • 33644995225 scopus 로고    scopus 로고
    • The role of subunit hinges and molecular "switches" in the control of viral capsid polymorphism
    • Tang, J.; Johnson, J. M.; Dryden, K. A.; Young, M. J.; Zlotnick, A.; Johnson, J. E. The role of subunit hinges and molecular "switches" in the control of viral capsid polymorphism J. Struct. Biol. 2006, 154, 59
    • (2006) J. Struct. Biol. , vol.154 , pp. 59
    • Tang, J.1    Johnson, J.M.2    Dryden, K.A.3    Young, M.J.4    Zlotnick, A.5    Johnson, J.E.6
  • 25
    • 33751421851 scopus 로고    scopus 로고
    • Electrostatically Driven Protein Aggregation: β-Lactoglobulin at Low Ionic Strength
    • See, e.g.
    • See, e.g.: Majhi, P. R.; Ganta, R. R.; Vanam, R. P.; Seyrek, E.; Giger, K.; Dubin, P. L. Electrostatically Driven Protein Aggregation: β-Lactoglobulin at Low Ionic Strength Langmuir 2006, 22, 9150
    • (2006) Langmuir , vol.22 , pp. 9150
    • Majhi, P.R.1    Ganta, R.R.2    Vanam, R.P.3    Seyrek, E.4    Giger, K.5    Dubin, P.L.6
  • 26
    • 0030891437 scopus 로고    scopus 로고
    • Electrostatics of lipid bilayer bending
    • Chou, T.; Jaric, M. V.; Siggia, E. D. Electrostatics of lipid bilayer bending Biophys. J. 1997, 72, 2042
    • (1997) Biophys. J. , vol.72 , pp. 2042
    • Chou, T.1    Jaric, M.V.2    Siggia, E.D.3
  • 27
    • 0016224494 scopus 로고
    • Aggregation States of Brome Mosaic Virus Protein
    • Pfeiffer, P.; Hirth, L. Aggregation States of Brome Mosaic Virus Protein Virology 1974, 61, 160
    • (1974) Virology , vol.61 , pp. 160
    • Pfeiffer, P.1    Hirth, L.2
  • 28
    • 84914647423 scopus 로고
    • The Molecular Weight and Other Biophysical Properties of Bromegrass Mosaic Virus
    • Bockstahler, L. E.; Kaesberg, P. The Molecular Weight and Other Biophysical Properties of Bromegrass Mosaic Virus Biophys. J. 1962, 2, 1
    • (1962) Biophys. J. , vol.2 , pp. 1
    • Bockstahler, L.E.1    Kaesberg, P.2
  • 29
    • 0029643791 scopus 로고
    • Structures of the native and swollen forms of cowpea chlorotic mottle virus determined by X-ray crystallography and cryo-electron microscopy
    • Speir, J. A.; Munshi, S.; Wang, G.; Baker, T. S.; Johnson, J. E. Structures of the native and swollen forms of cowpea chlorotic mottle virus determined by X-ray crystallography and cryo-electron microscopy Structure 1995, 3, 63
    • (1995) Structure , vol.3 , pp. 63
    • Speir, J.A.1    Munshi, S.2    Wang, G.3    Baker, T.S.4    Johnson, J.E.5
  • 30
    • 0029390766 scopus 로고
    • Electrophoretic mobility of soft particles
    • Ohshima, H. Electrophoretic mobility of soft particles Colloids Surf., A 1995, 103, 249
    • (1995) Colloids Surf., A , vol.103 , pp. 249
    • Ohshima, H.1
  • 31
    • 0001575623 scopus 로고
    • The cataphoresis of suspended particles. Part I. The equation of cataphoresis
    • Henry, D. C. The cataphoresis of suspended particles. Part I. The equation of cataphoresis Proc. R. Soc. London, Ser. A 1931, 133, 106
    • (1931) Proc. R. Soc. London, Ser. A , vol.133 , pp. 106
    • Henry, D.C.1
  • 33
    • 77955883109 scopus 로고    scopus 로고
    • Multiscale analytic continuation approach to nanosystem simulation: Applications to virus electrostatics
    • Singharoy, A.; Yesnik, A. M.; Ortoleva, P. Multiscale analytic continuation approach to nanosystem simulation: Applications to virus electrostatics J. Chem. Phys. 2010, 132, 174112
    • (2010) J. Chem. Phys. , vol.132 , pp. 174112
    • Singharoy, A.1    Yesnik, A.M.2    Ortoleva, P.3
  • 34
    • 0141456081 scopus 로고    scopus 로고
    • Metal binding to cowpea chlorotic mottle virus using terbium(III) fluorescence
    • Basu, G.; Allen, M.; Willits, D.; Young, M.; Douglas, T. Metal binding to cowpea chlorotic mottle virus using terbium(III) fluorescence J. Biol. Inorg. Chem 2003, 8, 721
    • (2003) J. Biol. Inorg. Chem , vol.8 , pp. 721
    • Basu, G.1    Allen, M.2    Willits, D.3    Young, M.4    Douglas, T.5
  • 35
    • 0036786867 scopus 로고    scopus 로고
    • Weak-protein interactions are sufficient to drive assembly of hepatitis B virus capsid
    • Ceres, P.; Zlotnick, A. Weak-protein interactions are sufficient to drive assembly of hepatitis B virus capsid Biochemistry 2002, 41, 11525
    • (2002) Biochemistry , vol.41 , pp. 11525
    • Ceres, P.1    Zlotnick, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.