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Volumn 17, Issue 5, 2009, Pages 737-748

Proton-Linked Dimerization of a Retroviral Capsid Protein Initiates Capsid Assembly

Author keywords

MICROBIO; PROTEINS

Indexed keywords

ASPARTIC ACID; CAPSID PROTEIN; DIMER; PROTON;

EID: 65149095269     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2009.03.010     Document Type: Article
Times cited : (31)

References (79)
  • 2
    • 57649116079 scopus 로고    scopus 로고
    • Residues in the HIV-1 capsid assembly inhibitor binding site are essential for maintaining the assembly-competent quaternary structure of the capsid protein
    • Bartonova V., Igonet S., Sticht J., Glass B., Habermann A., Vaney M.C., Sehr P., Lewis J., Rey F.A., and Kraüsslich H.G. Residues in the HIV-1 capsid assembly inhibitor binding site are essential for maintaining the assembly-competent quaternary structure of the capsid protein. J. Biol. Chem. 283 (2008) 32024-32033
    • (2008) J. Biol. Chem. , vol.283 , pp. 32024-32033
    • Bartonova, V.1    Igonet, S.2    Sticht, J.3    Glass, B.4    Habermann, A.5    Vaney, M.C.6    Sehr, P.7    Lewis, J.8    Rey, F.A.9    Kraüsslich, H.G.10
  • 5
    • 0034954578 scopus 로고    scopus 로고
    • Second-site suppressors of Rous sarcoma virus CA mutations: evidence for interdomain interactions
    • Bowzard J.B., Wills J.W., and Craven R.C. Second-site suppressors of Rous sarcoma virus CA mutations: evidence for interdomain interactions. J. Virol. 75 (2001) 6850-6856
    • (2001) J. Virol. , vol.75 , pp. 6850-6856
    • Bowzard, J.B.1    Wills, J.W.2    Craven, R.C.3
  • 6
    • 0037388765 scopus 로고    scopus 로고
    • Structural organization of authentic, mature HIV-1 virions and cores
    • Briggs J.A., Wilk T., Welker R., Kräusslich H.G., and Fuller S.D. Structural organization of authentic, mature HIV-1 virions and cores. EMBO J. 22 (2003) 1707-1715
    • (2003) EMBO J. , vol.22 , pp. 1707-1715
    • Briggs, J.A.1    Wilk, T.2    Welker, R.3    Kräusslich, H.G.4    Fuller, S.D.5
  • 8
    • 1242274447 scopus 로고    scopus 로고
    • Cryoelectron microscopy of mouse mammary tumor virus
    • Briggs J.A., Watson B.E., Gowen B.E., and Fuller S.D. Cryoelectron microscopy of mouse mammary tumor virus. J. Virol. 78 (2004) 2606-2608
    • (2004) J. Virol. , vol.78 , pp. 2606-2608
    • Briggs, J.A.1    Watson, B.E.2    Gowen, B.E.3    Fuller, S.D.4
  • 9
    • 33644806492 scopus 로고    scopus 로고
    • The mechanism of HIV-1 core assembly: insights from three-dimensional reconstructions of authentic virions
    • Briggs J.A., Grünewald K., Glass B., Förster F., Kräusslich H.G., and Fuller S.D. The mechanism of HIV-1 core assembly: insights from three-dimensional reconstructions of authentic virions. Structure 14 (2006) 15-20
    • (2006) Structure , vol.14 , pp. 15-20
    • Briggs, J.A.1    Grünewald, K.2    Glass, B.3    Förster, F.4    Kräusslich, H.G.5    Fuller, S.D.6
  • 10
    • 84881194271 scopus 로고    scopus 로고
    • Cryo-electron microscopy reveals conserved and divergent features of Gag packing in immature particles of Rous sarcoma virus and human immunodeficiency virus
    • Briggs J.A., Johnson M.C., Simon M.N., Fuller S.D., and Vogt V.M. Cryo-electron microscopy reveals conserved and divergent features of Gag packing in immature particles of Rous sarcoma virus and human immunodeficiency virus. J. Mol. Biol. 355 (2006) 157-168
    • (2006) J. Mol. Biol. , vol.355 , pp. 157-168
    • Briggs, J.A.1    Johnson, M.C.2    Simon, M.N.3    Fuller, S.D.4    Vogt, V.M.5
  • 11
    • 39049108146 scopus 로고    scopus 로고
    • RSV capsid polymorphism correlates with polymerization efficiency and envelope glycoprotein content: implications that nucleation controls morphogenesis
    • Butan C., Winkler D.C., Heymann J.B., Craven R.C., and Steven A.C. RSV capsid polymorphism correlates with polymerization efficiency and envelope glycoprotein content: implications that nucleation controls morphogenesis. J. Mol. Biol. 376 (2008) 1168-1181
    • (2008) J. Mol. Biol. , vol.376 , pp. 1168-1181
    • Butan, C.1    Winkler, D.C.2    Heymann, J.B.3    Craven, R.C.4    Steven, A.C.5
  • 12
    • 0034681298 scopus 로고    scopus 로고
    • Solution structure and dynamics of the Rous sarcoma virus capsid protein and comparison with capsid proteins of other retroviruses
    • Campos-Olivas R., Newman J.L., and Summers M.F. Solution structure and dynamics of the Rous sarcoma virus capsid protein and comparison with capsid proteins of other retroviruses. J. Mol. Biol. 296 (2000) 633-649
    • (2000) J. Mol. Biol. , vol.296 , pp. 633-649
    • Campos-Olivas, R.1    Newman, J.L.2    Summers, M.F.3
  • 13
    • 59649084913 scopus 로고    scopus 로고
    • Visualization of a missing link in retrovirus capsid assembly
    • Cardone G., Purdy J., Cheng N., Craven R., and Steven A. Visualization of a missing link in retrovirus capsid assembly. Nature 457 (2009) 694-698
    • (2009) Nature , vol.457 , pp. 694-698
    • Cardone, G.1    Purdy, J.2    Cheng, N.3    Craven, R.4    Steven, A.5
  • 14
    • 16244392086 scopus 로고    scopus 로고
    • When X-rays modify the protein structure: radiation damage at work
    • Carugo O., and Djinović Carugo K. When X-rays modify the protein structure: radiation damage at work. Trends Biochem. Sci. 30 (2005) 213-219
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 213-219
    • Carugo, O.1    Djinović Carugo, K.2
  • 15
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • CCP4 (Collaborative Computational Project, Number 4)
    • CCP4 (Collaborative Computational Project, Number 4). The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50 (1994) 760-763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 17
    • 0034687127 scopus 로고    scopus 로고
    • Coupled energetics of λ cro repressor self-assembly and site-specific DNA operator binding I: analysis of cro dimerization from nanomolar to micromolar concentrations
    • Darling P.J., Holt J.M., and Ackers G.K. Coupled energetics of λ cro repressor self-assembly and site-specific DNA operator binding I: analysis of cro dimerization from nanomolar to micromolar concentrations. Biochemistry 39 (2000) 11500-11507
    • (2000) Biochemistry , vol.39 , pp. 11500-11507
    • Darling, P.J.1    Holt, J.M.2    Ackers, G.K.3
  • 18
    • 27644552564 scopus 로고    scopus 로고
    • Effect of macromolecular crowding agents on human immunodeficiency virus type 1 capsid protein assembly in vitro
    • del Alamo M., Rivas G., and Mateu M.G. Effect of macromolecular crowding agents on human immunodeficiency virus type 1 capsid protein assembly in vitro. J. Virol. 79 (2005) 14271-14281
    • (2005) J. Virol. , vol.79 , pp. 14271-14281
    • del Alamo, M.1    Rivas, G.2    Mateu, M.G.3
  • 19
    • 0036892612 scopus 로고    scopus 로고
    • Endocytosis is a critical step in entry of subgroup B avian leukosis viruses
    • Diaz-Griffero F., Hoschander S.A., and Brojatsch J. Endocytosis is a critical step in entry of subgroup B avian leukosis viruses. J. Virol. 76 (2002) 12866-12876
    • (2002) J. Virol. , vol.76 , pp. 12866-12876
    • Diaz-Griffero, F.1    Hoschander, S.A.2    Brojatsch, J.3
  • 20
    • 33645793789 scopus 로고    scopus 로고
    • Evidence for a functional link between uncoating of the human immunodeficiency virus type 1 core and nuclear import of the viral preintegration complex
    • Dismuke D.J., and Aiken C. Evidence for a functional link between uncoating of the human immunodeficiency virus type 1 core and nuclear import of the viral preintegration complex. J. Virol. 80 (2006) 3712-3720
    • (2006) J. Virol. , vol.80 , pp. 3712-3720
    • Dismuke, D.J.1    Aiken, C.2
  • 22
    • 0036094824 scopus 로고    scopus 로고
    • Formation of a human immunodeficiency virus type 1 core of optimal stability is crucial for viral replication
    • Forshey B.M., von Schwedler U., Sundquist W.I., and Aiken C. Formation of a human immunodeficiency virus type 1 core of optimal stability is crucial for viral replication. J. Virol. 76 (2002) 5667-5677
    • (2002) J. Virol. , vol.76 , pp. 5667-5677
    • Forshey, B.M.1    von Schwedler, U.2    Sundquist, W.I.3    Aiken, C.4
  • 23
    • 0031260436 scopus 로고    scopus 로고
    • Cryo-electron microscopy reveals ordered domains in the immature HIV-1 particle
    • Fuller S.D., Wilk T., Gowen B.E., Kräusslich H.G., and Vogt V.M. Cryo-electron microscopy reveals ordered domains in the immature HIV-1 particle. Curr. Biol. 7 (1997) 729-738
    • (1997) Curr. Biol. , vol.7 , pp. 729-738
    • Fuller, S.D.1    Wilk, T.2    Gowen, B.E.3    Kräusslich, H.G.4    Vogt, V.M.5
  • 26
    • 34848866243 scopus 로고    scopus 로고
    • Structure of full-length HIV-1 CA: a model for the mature capsid lattice
    • Ganser-Pornillos B.K., Cheng A., and Yeager M. Structure of full-length HIV-1 CA: a model for the mature capsid lattice. Cell 131 (2007) 70-79
    • (2007) Cell , vol.131 , pp. 70-79
    • Ganser-Pornillos, B.K.1    Cheng, A.2    Yeager, M.3
  • 28
    • 0031954466 scopus 로고    scopus 로고
    • N-terminal extension of human immunodeficiency virus capsid protein converts the in vitro assembly phenotype from tubular to spherical particles
    • Gross I., Hohenberg H., Huckhagel C., and Kräusslich H.G. N-terminal extension of human immunodeficiency virus capsid protein converts the in vitro assembly phenotype from tubular to spherical particles. J. Virol. 72 (1998) 4798-4810
    • (1998) J. Virol. , vol.72 , pp. 4798-4810
    • Gross, I.1    Hohenberg, H.2    Huckhagel, C.3    Kräusslich, H.G.4
  • 29
    • 0030039296 scopus 로고    scopus 로고
    • PROMOTIF-a program to identify and analyze structural motifs in proteins
    • Hutchinson E.G., and Thornton J.M. PROMOTIF-a program to identify and analyze structural motifs in proteins. Protein Sci. 5 (1996) 212-220
    • (1996) Protein Sci. , vol.5 , pp. 212-220
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 30
    • 0036827828 scopus 로고    scopus 로고
    • Nucleic acid-independent retrovirus assembly can be driven by dimerization
    • Johnson M.C., Scobie H.M., Ma Y.M., and Vogt V.M. Nucleic acid-independent retrovirus assembly can be driven by dimerization. J. Virol. 76 (2002) 11177-11185
    • (2002) J. Virol. , vol.76 , pp. 11177-11185
    • Johnson, M.C.1    Scobie, H.M.2    Ma, Y.M.3    Vogt, V.M.4
  • 31
    • 0032781006 scopus 로고    scopus 로고
    • Solution structure of the capsid protein from the human T-cell leukemia virus type-I
    • Khorasanizadeh S., Campos-Olivas R., and Summers M.F. Solution structure of the capsid protein from the human T-cell leukemia virus type-I. J. Mol. Biol. 291 (1999) 491-505
    • (1999) J. Mol. Biol. , vol.291 , pp. 491-505
    • Khorasanizadeh, S.1    Campos-Olivas, R.2    Summers, M.F.3
  • 34
    • 0035782860 scopus 로고    scopus 로고
    • The organization of mature Rous sarcoma virus as studied by cryoelectron microscopy
    • Kingston R.L., Olson N.H., and Vogt V.M. The organization of mature Rous sarcoma virus as studied by cryoelectron microscopy. J. Struct. Biol. 136 (2001) 67-80
    • (2001) J. Struct. Biol. , vol.136 , pp. 67-80
    • Kingston, R.L.1    Olson, N.H.2    Vogt, V.M.3
  • 35
    • 0024293096 scopus 로고
    • Structure of light-harvesting chlorophyll a/b protein complex from plant photosynthetic membranes at 7 Å resolution in projection
    • Kühlbrandt W. Structure of light-harvesting chlorophyll a/b protein complex from plant photosynthetic membranes at 7 Å resolution in projection. J. Mol. Biol. 202 (1988) 849-864
    • (1988) J. Mol. Biol. , vol.202 , pp. 849-864
    • Kühlbrandt, W.1
  • 36
    • 0036634466 scopus 로고    scopus 로고
    • Kinetic analysis of the role of intersubunit interactions in human immunodeficiency virus type 1 capsid protein assembly in vitro
    • Lanman J., Sexton J., Sakalian M., and Prevelige P.E. Kinetic analysis of the role of intersubunit interactions in human immunodeficiency virus type 1 capsid protein assembly in vitro. J. Virol. 76 (2002) 6900-6908
    • (2002) J. Virol. , vol.76 , pp. 6900-6908
    • Lanman, J.1    Sexton, J.2    Sakalian, M.3    Prevelige, P.E.4
  • 37
    • 0037462921 scopus 로고    scopus 로고
    • Identification of novel interactions in HIV-1 capsid protein assembly by high-resolution mass spectrometry
    • Lanman J., Lam T.T., Barnes S., Sakalian M., Emmett M.R., Marshall A.G., and Prevelige P.E. Identification of novel interactions in HIV-1 capsid protein assembly by high-resolution mass spectrometry. J. Mol. Biol. 325 (2003) 759-772
    • (2003) J. Mol. Biol. , vol.325 , pp. 759-772
    • Lanman, J.1    Lam, T.T.2    Barnes, S.3    Sakalian, M.4    Emmett, M.R.5    Marshall, A.G.6    Prevelige, P.E.7
  • 39
    • 0034699383 scopus 로고    scopus 로고
    • Image reconstructions of helical assemblies of the HIV-1 CA protein
    • Li S., Hill C.P., Sundquist W.I., and Finch J.T. Image reconstructions of helical assemblies of the HIV-1 CA protein. Nature 407 (2000) 409-413
    • (2000) Nature , vol.407 , pp. 409-413
    • Li, S.1    Hill, C.P.2    Sundquist, W.I.3    Finch, J.T.4
  • 40
    • 33846610519 scopus 로고    scopus 로고
    • Cyclophilin A, TRIM5, and resistance to human immunodeficiency virus type 1 infection
    • Luban J. Cyclophilin A, TRIM5, and resistance to human immunodeficiency virus type 1 infection. J. Virol. 81 (2006) 1054-1061
    • (2006) J. Virol. , vol.81 , pp. 1054-1061
    • Luban, J.1
  • 41
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: semiautomated software for high-resolution single-particle reconstructions
    • Ludtke S.J., Baldwin P.R., and Chiu W. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128 (1999) 82-97
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 42
    • 0036091735 scopus 로고    scopus 로고
    • Rous sarcoma virus Gag protein-oligonucleotide interaction suggests a critical role for protein dimer formation in assembly
    • Ma Y.M., and Vogt V.M. Rous sarcoma virus Gag protein-oligonucleotide interaction suggests a critical role for protein dimer formation in assembly. J. Virol. 76 (2002) 5452-5462
    • (2002) J. Virol. , vol.76 , pp. 5452-5462
    • Ma, Y.M.1    Vogt, V.M.2
  • 43
    • 0344610289 scopus 로고    scopus 로고
    • Nucleic acid binding-induced Gag dimerization in the assembly of Rous sarcoma virus particles in vitro
    • Ma Y.M., and Vogt V.M. Nucleic acid binding-induced Gag dimerization in the assembly of Rous sarcoma virus particles in vitro. J. Virol. 78 (2004) 52-60
    • (2004) J. Virol. , vol.78 , pp. 52-60
    • Ma, Y.M.1    Vogt, V.M.2
  • 45
    • 1842509971 scopus 로고    scopus 로고
    • Low pH is required for avian sarcoma and leukosis virus Env-induced hemifusion and fusion pore formation but not for pore growth
    • Melikyan G.B., Barnard R.J., Markosyan R.M., Young J.A., and Cohen F.S. Low pH is required for avian sarcoma and leukosis virus Env-induced hemifusion and fusion pore formation but not for pore growth. J. Virol. 78 (2004) 3753-3762
    • (2004) J. Virol. , vol.78 , pp. 3753-3762
    • Melikyan, G.B.1    Barnard, R.J.2    Markosyan, R.M.3    Young, J.A.4    Cohen, F.S.5
  • 46
    • 4644301808 scopus 로고    scopus 로고
    • High-resolution structure of a retroviral capsid hexameric amino-terminal domain
    • Mortuza G.B., Haire L.F., Stevens A., Smerdon S.J., Stoye J.P., and Taylor I.A. High-resolution structure of a retroviral capsid hexameric amino-terminal domain. Nature 431 (2004) 481-485
    • (2004) Nature , vol.431 , pp. 481-485
    • Mortuza, G.B.1    Haire, L.F.2    Stevens, A.3    Smerdon, S.J.4    Stoye, J.P.5    Taylor, I.A.6
  • 47
    • 39149136512 scopus 로고    scopus 로고
    • Structure of B-MLV capsid amino-terminal domain reveals key features of viral tropism, Gag assembly and core formation
    • Mortuza G.B., Dodding M.P., Goldstone D.C., Haire L.F., Stoye J.P., and Taylor I.A. Structure of B-MLV capsid amino-terminal domain reveals key features of viral tropism, Gag assembly and core formation. J. Mol. Biol. 376 (2008) 1493-1508
    • (2008) J. Mol. Biol. , vol.376 , pp. 1493-1508
    • Mortuza, G.B.1    Dodding, M.P.2    Goldstone, D.C.3    Haire, L.F.4    Stoye, J.P.5    Taylor, I.A.6
  • 49
    • 0033697734 scopus 로고    scopus 로고
    • Retroviral entry mediated by receptor priming and low pH triggering of an envelope glycoprotein
    • Mothes W., Boerger A.L., Narayan S., Cunningham J.M., and Young J.A. Retroviral entry mediated by receptor priming and low pH triggering of an envelope glycoprotein. Cell 103 (2000) 679-689
    • (2000) Cell , vol.103 , pp. 679-689
    • Mothes, W.1    Boerger, A.L.2    Narayan, S.3    Cunningham, J.M.4    Young, J.A.5
  • 51
    • 0037303326 scopus 로고    scopus 로고
    • Two retroviral entry pathways distinguished by lipid raft association of the viral receptor and differences in viral infectivity
    • Narayan S., Barnard R.J., and Young J.A. Two retroviral entry pathways distinguished by lipid raft association of the viral receptor and differences in viral infectivity. J. Virol. 77 (2003) 1977-1983
    • (2003) J. Virol. , vol.77 , pp. 1977-1983
    • Narayan, S.1    Barnard, R.J.2    Young, J.A.3
  • 52
    • 0028116662 scopus 로고
    • Reduced-scale large-zone analytical gel filtration chromatography for measurement of protein association equilibria
    • Nenortas E., and Beckett D. Reduced-scale large-zone analytical gel filtration chromatography for measurement of protein association equilibria. Anal. Biochem. 222 (1994) 366-373
    • (1994) Anal. Biochem. , vol.222 , pp. 366-373
    • Nenortas, E.1    Beckett, D.2
  • 53
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 54
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace C.N., Vajdos F., Fee L., Grimsley G., and Gray T. How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4 (1995) 2411-2423
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 55
    • 43749097090 scopus 로고    scopus 로고
    • Critical role of conserved hydrophobic residues within the major homology region in mature retroviral capsid assembly
    • Purdy J.G., Flanagan J.M., Ropson I.J., Rennoll-Bankert K.E., and Craven R.C. Critical role of conserved hydrophobic residues within the major homology region in mature retroviral capsid assembly. J. Virol. 82 (2008) 5951-5961
    • (2008) J. Virol. , vol.82 , pp. 5951-5961
    • Purdy, J.G.1    Flanagan, J.M.2    Ropson, I.J.3    Rennoll-Bankert, K.E.4    Craven, R.C.5
  • 56
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • Read R.J. Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr. A. 42 (1986) 140-149
    • (1986) Acta Crystallogr. A. , vol.42 , pp. 140-149
    • Read, R.J.1
  • 57
    • 34347226647 scopus 로고    scopus 로고
    • On the nature of hydrogen bonds: an overview on computational studies and a word about patterns
    • Rozas I. On the nature of hydrogen bonds: an overview on computational studies and a word about patterns. Phys. Chem. Chem. Phys. 9 (2007) 2782-2790
    • (2007) Phys. Chem. Chem. Phys. , vol.9 , pp. 2782-2790
    • Rozas, I.1
  • 58
    • 37549039510 scopus 로고    scopus 로고
    • A short history of SHELX
    • Sheldrick G.M. A short history of SHELX. Acta Crystallogr. A. 64 (2008) 112-122
    • (2008) Acta Crystallogr. A. , vol.64 , pp. 112-122
    • Sheldrick, G.M.1
  • 60
    • 0024818499 scopus 로고
    • Stereochemical modeling of disulfide bridges. Criteria for introduction into proteins by site-directed mutagenesis
    • Sowdhamini R., Srinivasan N., Shoichet B., Santi D.V., Ramakrishnan C., and Balaram P. Stereochemical modeling of disulfide bridges. Criteria for introduction into proteins by site-directed mutagenesis. Protein Eng. 3 (1989) 95-103
    • (1989) Protein Eng. , vol.3 , pp. 95-103
    • Sowdhamini, R.1    Srinivasan, N.2    Shoichet, B.3    Santi, D.V.4    Ramakrishnan, C.5    Balaram, P.6
  • 63
    • 34447317534 scopus 로고    scopus 로고
    • The control of viral infection by tripartite motif proteins and cyclophilin A
    • Towers G.J. The control of viral infection by tripartite motif proteins and cyclophilin A. Retrovirology 4 (2007) 40
    • (2007) Retrovirology , vol.4 , pp. 40
    • Towers, G.J.1
  • 64
    • 0018369485 scopus 로고
    • Study of protein subunit association equilibria by elution gel chromatography
    • Valdes R., and Ackers G.K. Study of protein subunit association equilibria by elution gel chromatography. Methods Enzymol. 61 (1979) 125-142
    • (1979) Methods Enzymol. , vol.61 , pp. 125-142
    • Valdes, R.1    Ackers, G.K.2
  • 65
    • 3242726206 scopus 로고    scopus 로고
    • Characterization of protein-protein interactions by isothermal titration calorimetry
    • Velazquez-Campoy A., Leavitt S.A., and Freire E. Characterization of protein-protein interactions by isothermal titration calorimetry. Methods Mol. Biol. 261 (2004) 35-54
    • (2004) Methods Mol. Biol. , vol.261 , pp. 35-54
    • Velazquez-Campoy, A.1    Leavitt, S.A.2    Freire, E.3
  • 66
    • 0032795497 scopus 로고    scopus 로고
    • Mass determination of Rous sarcoma virus virions by scanning transmission electron microscopy
    • Vogt V.M., and Simon M.N. Mass determination of Rous sarcoma virus virions by scanning transmission electron microscopy. J. Virol. 73 (1999) 7050-7055
    • (1999) J. Virol. , vol.73 , pp. 7050-7055
    • Vogt, V.M.1    Simon, M.N.2
  • 68
    • 0037404501 scopus 로고    scopus 로고
    • Functional surfaces of the human immunodeficiency virus type 1 capsid protein
    • von Schwedler U.K., Stray K.M., Garrus J.E., and Sundquist W.I. Functional surfaces of the human immunodeficiency virus type 1 capsid protein. J. Virol. 77 (2003) 5439-5450
    • (2003) J. Virol. , vol.77 , pp. 5439-5450
    • von Schwedler, U.K.1    Stray, K.M.2    Garrus, J.E.3    Sundquist, W.I.4
  • 69
    • 0030793507 scopus 로고    scopus 로고
    • SIMS: computation of a smooth invariant molecular surface
    • Vorobjev Y.N., and Hermans J. SIMS: computation of a smooth invariant molecular surface. Biophys. J. 73 (1997) 722-732
    • (1997) Biophys. J. , vol.73 , pp. 722-732
    • Vorobjev, Y.N.1    Hermans, J.2
  • 70
    • 0033958427 scopus 로고    scopus 로고
    • Biochemical and structural analysis of isolated mature cores of human immunodeficiency virus type 1
    • Welker R., Hohenberg H., Tessmer U., Huckhagel C., and Kräusslich H.G. Biochemical and structural analysis of isolated mature cores of human immunodeficiency virus type 1. J. Virol. 74 (2000) 1168-1177
    • (2000) J. Virol. , vol.74 , pp. 1168-1177
    • Welker, R.1    Hohenberg, H.2    Tessmer, U.3    Huckhagel, C.4    Kräusslich, H.G.5
  • 72
    • 0037756781 scopus 로고    scopus 로고
    • Analytical exclusion chromatography
    • Winzor D.J. Analytical exclusion chromatography. J. Biochem. Biophys. Methods 56 (2003) 15-52
    • (2003) J. Biochem. Biophys. Methods , vol.56 , pp. 15-52
    • Winzor, D.J.1
  • 73
    • 34250157541 scopus 로고
    • Cooperativity of ligand binding as a function of monomer-dimer equilibrium parameters and acceptor concentration
    • Wolfer G., Neil J., and Rippon W. Cooperativity of ligand binding as a function of monomer-dimer equilibrium parameters and acceptor concentration. J. Protein Chem. 6 (1987) 441-454
    • (1987) J. Protein Chem. , vol.6 , pp. 441-454
    • Wolfer, G.1    Neil, J.2    Rippon, W.3
  • 75
    • 34247185183 scopus 로고    scopus 로고
    • Electron cryotomography of immature HIV-1 virions reveals the structure of the CA and SP1 Gag shells
    • Wright E.R., Schooler J.B., Ding H.J., Kieffer C., Fillmore C., Sundquist W.I., and Jensen G.J. Electron cryotomography of immature HIV-1 virions reveals the structure of the CA and SP1 Gag shells. EMBO J. 26 (2007) 2218-2226
    • (2007) EMBO J. , vol.26 , pp. 2218-2226
    • Wright, E.R.1    Schooler, J.B.2    Ding, H.J.3    Kieffer, C.4    Fillmore, C.5    Sundquist, W.I.6    Jensen, G.J.7
  • 77
    • 0032560502 scopus 로고    scopus 로고
    • Supramolecular organization of immature and mature murine leukemia virus revealed by electron cryo-microscopy: implications for retroviral assembly mechanisms
    • Yeager M., Wilson-Kubalek E.M., Weiner S.G., Brown P.O., and Rein A. Supramolecular organization of immature and mature murine leukemia virus revealed by electron cryo-microscopy: implications for retroviral assembly mechanisms. Proc. Natl. Acad. Sci. USA 95 (1998) 7299-7304
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7299-7304
    • Yeager, M.1    Wilson-Kubalek, E.M.2    Weiner, S.G.3    Brown, P.O.4    Rein, A.5
  • 78
    • 0035123571 scopus 로고    scopus 로고
    • Characterization of Rous sarcoma virus Gag particles assembled in vitro
    • Yu F., Joshi S.M., Ma Y.M., Kingston R.L., Simon M.N., and Vogt V.M. Characterization of Rous sarcoma virus Gag particles assembled in vitro. J. Virol. 75 (2001) 2753-2764
    • (2001) J. Virol. , vol.75 , pp. 2753-2764
    • Yu, F.1    Joshi, S.M.2    Ma, Y.M.3    Kingston, R.L.4    Simon, M.N.5    Vogt, V.M.6
  • 79
    • 27744467626 scopus 로고    scopus 로고
    • Theoretical aspects of virus capsid assembly
    • Zlotnick A. Theoretical aspects of virus capsid assembly. J. Mol. Recognit. 18 (2005) 479-490
    • (2005) J. Mol. Recognit. , vol.18 , pp. 479-490
    • Zlotnick, A.1


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