메뉴 건너뛰기




Volumn 85, Issue 23, 2011, Pages 12733-12741

Solution properties of murine leukemia virus gag protein: Differences from HIV-1 Gag

Author keywords

[No Author keywords available]

Indexed keywords

GAG PROTEIN; PROLINE;

EID: 81255163687     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.05889-11     Document Type: Article
Times cited : (24)

References (59)
  • 1
    • 70450164528 scopus 로고    scopus 로고
    • Analysis of human immunodeficiency virus type 1 matrix binding to membranes and nucleic acids
    • Alfadhli, A., A. Still, and E. Barklis. 2009. Analysis of human immunodeficiency virus type 1 matrix binding to membranes and nucleic acids. J. Virol. 83:12196-12203.
    • (2009) J. Virol. , vol.83 , pp. 12196-12203
    • Alfadhli, A.1    Still, A.2    Barklis, E.3
  • 2
    • 67650482702 scopus 로고    scopus 로고
    • Structure and assembly of immature HIV
    • Briggs, J. A., et al. 2009. Structure and assembly of immature HIV. Proc. Natl. Acad. Sci. U. S. A. 106:11090-11095.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 11090-11095
    • Briggs, J.A.1
  • 3
    • 0035845576 scopus 로고    scopus 로고
    • Modulation of HIV-like particle assembly in vitro by inositol phosphates
    • Campbell, S., et al. 2001. Modulation of HIV-like particle assembly in vitro by inositol phosphates. Proc. Natl. Acad. Sci. U. S. A. 98:10875-10879.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 10875-10879
    • Campbell, S.1
  • 4
    • 0033027711 scopus 로고    scopus 로고
    • In vitro assembly properties of human immunodeficiency virus type 1 Gag protein lacking the p6 domain
    • Campbell, S., and A. Rein. 1999. In vitro assembly properties of human immunodeficiency virus type 1 Gag protein lacking the p6 domain. J. Virol. 73:2270-2279.
    • (1999) J. Virol. , vol.73 , pp. 2270-2279
    • Campbell, S.1    Rein, A.2
  • 5
    • 0029103178 scopus 로고
    • Self-assembly in vitro of purified CA-NC proteins from Rous sarcoma virus and human immunodeficiency virus type 1
    • Campbell, S., and V. M. Vogt. 1995. Self-assembly in vitro of purified CA-NC proteins from Rous sarcoma virus and human immunodeficiency virus type 1. J. Virol. 69:6487-6497.
    • (1995) J. Virol. , vol.69 , pp. 6487-6497
    • Campbell, S.1    Vogt, V.M.2
  • 6
    • 0037604494 scopus 로고    scopus 로고
    • Charged assembly helix motif in murine leukemia virus capsid: an important region for virus assembly and particle size determination
    • Cheslock, S. R., et al. 2003. Charged assembly helix motif in murine leukemia virus capsid: an important region for virus assembly and particle size determination. J. Virol. 77:7058-7066.
    • (2003) J. Virol. , vol.77 , pp. 7058-7066
    • Cheslock, S.R.1
  • 7
    • 76549119994 scopus 로고    scopus 로고
    • Opposing mechanisms involving RNA and lipids regulate HIV-1 Gag membrane binding through the highly basic region of the matrix domain
    • Chukkapalli, V., S. J. Oh, and A. Ono. 2010. Opposing mechanisms involving RNA and lipids regulate HIV-1 Gag membrane binding through the highly basic region of the matrix domain. Proc. Natl. Acad. Sci. U. S. A. 107:1600-1605.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 1600-1605
    • Chukkapalli, V.1    Oh, S.J.2    Ono, A.3
  • 8
    • 0032486598 scopus 로고    scopus 로고
    • Retroviral matrix proteins: a structural perspective
    • Conte, M. R., and S. Matthews. 1998. Retroviral matrix proteins: a structural perspective. Virology 246:191-198.
    • (1998) Virology , vol.246 , pp. 191-198
    • Conte, M.R.1    Matthews, S.2
  • 9
    • 33845651410 scopus 로고    scopus 로고
    • Conformation of the HIV-1 Gag protein in solution
    • Datta, S. A., et al. 2007. Conformation of the HIV-1 Gag protein in solution. J. Mol. Biol. 365:812-824.
    • (2007) J. Mol. Biol. , vol.365 , pp. 812-824
    • Datta, S.A.1
  • 10
    • 79251596756 scopus 로고    scopus 로고
    • HIV- 1 Gag extension: conformational changes require simultaneous interaction with membrane and nucleic acid
    • Datta, S. A., et al. 2011. HIV-1 Gag extension: conformational changes require simultaneous interaction with membrane and nucleic acid. J. Mol. Biol. 406:205-214.
    • (2011) J. Mol. Biol. , vol.406 , pp. 205-214
    • Datta, S.A.1
  • 11
    • 60349108481 scopus 로고    scopus 로고
    • Preparation of recombinant HIV-1 gag protein and assembly of virus-like particles in vitro
    • Datta, S. A., and A. Rein. 2009. Preparation of recombinant HIV-1 gag protein and assembly of virus-like particles in vitro. Methods Mol. Biol. 485:197-208.
    • (2009) Methods Mol. Biol. , vol.485 , pp. 197-208
    • Datta, S.A.1    Rein, A.2
  • 12
    • 33845676742 scopus 로고    scopus 로고
    • Interactions between HIV-1 Gag molecules in solution: an inositol phosphate-mediated switch
    • Datta, S. A., et al. 2007. Interactions between HIV-1 Gag molecules in solution: an inositol phosphate-mediated switch. J. Mol. Biol. 365:799-811.
    • (2007) J. Mol. Biol. , vol.365 , pp. 799-811
    • Datta, S.A.1
  • 13
    • 78049516342 scopus 로고    scopus 로고
    • Conserved and variable features of Gag structure and arrangement in immature retrovirus particles
    • de Marco, A., et al. 2010. Conserved and variable features of Gag structure and arrangement in immature retrovirus particles. J. Virol. 84:11729-11736.
    • (2010) J. Virol. , vol.84 , pp. 11729-11736
    • de Marco, A.1
  • 14
    • 0028232502 scopus 로고
    • Functional exchange of an oncoretrovirus and a lentivirus matrix protein
    • Deminie, C. A., and M. Emerman. 1994. Functional exchange of an oncoretrovirus and a lentivirus matrix protein. J. Virol. 68:4442-4449.
    • (1994) J. Virol. , vol.68 , pp. 4442-4449
    • Deminie, C.A.1    Emerman, M.2
  • 15
    • 0027521321 scopus 로고
    • Incorporation of human immunodeficiency virus type 1 Gag proteins into murine leukemia virus virions
    • Deminie, C. A., and M. Emerman. 1993. Incorporation of human immunodeficiency virus type 1 Gag proteins into murine leukemia virus virions. J. Virol. 67:6499-6506.
    • (1993) J. Virol. , vol.67 , pp. 6499-6506
    • Deminie, C.A.1    Emerman, M.2
  • 16
    • 62649139615 scopus 로고    scopus 로고
    • DAMMIF, a program for rapid ab initio shape determination in small-angle scattering
    • Franke, D., and D. I. Svergun. 2009. DAMMIF, a program for rapid ab initio shape determination in small-angle scattering. J. Appl. Crystallogr. 42:342-346.
    • (2009) J. Appl. Crystallogr. , vol.42 , pp. 342-346
    • Franke, D.1    Svergun, D.I.2
  • 17
    • 0031260436 scopus 로고    scopus 로고
    • Cryo-electron microscopy reveals ordered domains in the immature HIV-1 particle
    • Fuller, S. D., T. Wilk, B. E. Gowen, H. G. Krausslich, and V. M. Vogt. 1997. Cryo-electron microscopy reveals ordered domains in the immature HIV-1 particle. Curr. Biol. 7:729-738.
    • (1997) Curr. Biol. , vol.7 , pp. 729-738
    • Fuller, S.D.1    Wilk, T.2    Gowen, B.E.3    Krausslich, H.G.4    Vogt, V.M.5
  • 18
    • 0030448994 scopus 로고    scopus 로고
    • Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid
    • Gamble, T. R., et al. 1996. Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid. Cell 87:1285-1294.
    • (1996) Cell , vol.87 , pp. 1285-1294
    • Gamble, T.R.1
  • 19
    • 0030693391 scopus 로고    scopus 로고
    • Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein
    • Gamble, T. R., et al. 1997. Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein. Science 278:849-853.
    • (1997) Science , vol.278 , pp. 849-853
    • Gamble, T.R.1
  • 20
    • 0038376141 scopus 로고    scopus 로고
    • Threedimensional structure of the M-MuLV CA protein on a lipid monolayer: a general model for retroviral capsid assembly
    • Ganser, B. K., A. Cheng, W. I. Sundquist, and M. Yeager. 2003. Threedimensional structure of the M-MuLV CA protein on a lipid monolayer: a general model for retroviral capsid assembly. EMBO J. 22:2886-2892.
    • (2003) EMBO J , vol.22 , pp. 2886-2892
    • Ganser, B.K.1    Cheng, A.2    Sundquist, W.I.3    Yeager, M.4
  • 21
    • 0036149965 scopus 로고    scopus 로고
    • Structure of equine infectious anemia virus matrix protein
    • Hatanaka, H., et al. 2002. Structure of equine infectious anemia virus matrix protein. J. Virol. 76:1876-1883.
    • (2002) J. Virol. , vol.76 , pp. 1876-1883
    • Hatanaka, H.1
  • 22
    • 0029966361 scopus 로고    scopus 로고
    • Crystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: implications for membrane association and assembly
    • Hill, C. P., D. Worthylake, D. P. Bancroft, A. M. Christensen, and W. I. Sundquist. 1996. Crystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: implications for membrane association and assembly. Proc. Natl. Acad. Sci. U. S. A. 93:3099-3104.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 3099-3104
    • Hill, C.P.1    Worthylake, D.2    Bancroft, D.P.3    Christensen, A.M.4    Sundquist, W.I.5
  • 23
    • 78951492319 scopus 로고    scopus 로고
    • Matrix domain modulates HIV-1 Gag's nucleic acid chaperone activity via inositol phosphate binding
    • Jones, C. P., S. A. Datta, A. Rein, I. Rouzina, and K. Musier-Forsyth. 2011. Matrix domain modulates HIV-1 Gag's nucleic acid chaperone activity via inositol phosphate binding. J. Virol. 85:1594-1603.
    • (2011) J. Virol. , vol.85 , pp. 1594-1603
    • Jones, C.P.1    Datta, S.A.2    Rein, A.3    Rouzina, I.4    Musier-Forsyth, K.5
  • 24
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and low-resolution structural models
    • Kozin, M. B., and D. I. Svergun. 2001. Automated matching of high- and low-resolution structural models. J. Appl. Crystallogr. 34:33-41.
    • (2001) J. Appl. Crystallogr. , vol.34 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2
  • 25
    • 44849091683 scopus 로고    scopus 로고
    • The p12 domain is unstructured in a murine leukemia virus p12-CA(N) Gag construct
    • Kyere, S. K., P. R. Joseph, and M. F. Summers. 2008. The p12 domain is unstructured in a murine leukemia virus p12-CA(N) Gag construct. PLoS One 3:e1902.
    • (2008) PLoS One , vol.3
    • Kyere, S.K.1    Joseph, P.R.2    Summers, M.F.3
  • 26
    • 0002498995 scopus 로고
    • Computer-aided interpretation of analytical sedimentation data for proteins
    • S. Harding, A. Rowe, and J. Horton (ed.), Royal Society of Chemistry, Cambridge, United Kingdom
    • Laue, T. M., B. Shah, T. Ridgeway, and S. Pelletier. 1992. Computer-aided interpretation of analytical sedimentation data for proteins, p. 90-125. In S. Harding, A. Rowe, and J. Horton (ed.), Analytical ultracentrifugation in biochemistry and polymer science. Royal Society of Chemistry, Cambridge, United Kingdom.
    • (1992) Analytical ultracentrifugation in biochemistry and polymer science , pp. 90-125
    • Laue, T.M.1    Shah, B.2    Ridgeway, T.3    Pelletier, S.4
  • 27
    • 0036707991 scopus 로고    scopus 로고
    • Modern analytical ultracentrifugation in protein science: a tutorial review
    • Lebowitz, J., M. S. Lewis, and P. Schuck. 2002. Modern analytical ultracentrifugation in protein science: a tutorial review. Protein Sci. 11:2067-2079.
    • (2002) Protein Sci , vol.11 , pp. 2067-2079
    • Lebowitz, J.1    Lewis, M.S.2    Schuck, P.3
  • 29
    • 33646797426 scopus 로고    scopus 로고
    • Interaction of Moloney murine leukemia virus matrix protein with IQGAP
    • Leung, J., et al. 2006. Interaction of Moloney murine leukemia virus matrix protein with IQGAP. EMBO J. 25:2155-2166.
    • (2006) EMBO J , vol.25 , pp. 2155-2166
    • Leung, J.1
  • 30
    • 0034699383 scopus 로고    scopus 로고
    • Image reconstructions of helical assemblies of the HIV-1 CA protein
    • Li, S., C. P. Hill, W. I. Sundquist, and J. T. Finch. 2000. Image reconstructions of helical assemblies of the HIV-1 CA protein. Nature 407:409-413.
    • (2000) Nature , vol.407 , pp. 409-413
    • Li, S.1    Hill, C.P.2    Sundquist, W.I.3    Finch, J.T.4
  • 31
    • 0030805546 scopus 로고    scopus 로고
    • In vitro selection of RNAs that bind to the human immunodeficiency virus type 1 Gag polyprotein
    • Lochrie, M. A., et al. 1997. In vitro selection of RNAs that bind to the human immunodeficiency virus type 1 Gag polyprotein. Nucleic Acids Res. 25:2902-2910.
    • (1997) Nucleic Acids Res , vol.25 , pp. 2902-2910
    • Lochrie, M.A.1
  • 32
    • 0027987979 scopus 로고
    • Three-dimensional structure of the human immunodeficiency virus type 1 matrix protein
    • Massiah, M. A., et al. 1994. Three-dimensional structure of the human immunodeficiency virus type 1 matrix protein. J. Mol. Biol. 244:198-223.
    • (1994) J. Mol. Biol. , vol.244 , pp. 198-223
    • Massiah, M.A.1
  • 33
    • 0023723196 scopus 로고
    • Oligopeptide biases in protein sequences and their use in predicting protein coding regions in nucleotide sequences
    • McCaldon, P., and P. Argos. 1988. Oligopeptide biases in protein sequences and their use in predicting protein coding regions in nucleotide sequences. Proteins 4:99-122.
    • (1988) Proteins , vol.4 , pp. 99-122
    • McCaldon, P.1    Argos, P.2
  • 34
    • 13144249234 scopus 로고    scopus 로고
    • Solution structure and dynamics of the bioactive retroviral M domain from Rous sarcoma virus
    • McDonnell, J. M., et al. 1998. Solution structure and dynamics of the bioactive retroviral M domain from Rous sarcoma virus. J. Mol. Biol. 279:921-928.
    • (1998) J. Mol. Biol. , vol.279 , pp. 921-928
    • McDonnell, J.M.1
  • 35
    • 4644301808 scopus 로고    scopus 로고
    • High-resolution structure of a retroviral capsid hexameric amino-terminal domain
    • Mortuza, G. B., et al. 2004. High-resolution structure of a retroviral capsid hexameric amino-terminal domain. Nature 431:481-485.
    • (2004) Nature , vol.431 , pp. 481-485
    • Mortuza, G.B.1
  • 36
    • 7644240076 scopus 로고    scopus 로고
    • Role of murine leukemia virus nucleocapsid protein in virus assembly
    • Muriaux, D., et al. 2004. Role of murine leukemia virus nucleocapsid protein in virus assembly. J. Virol. 78:12378-12385.
    • (2004) J. Virol. , vol.78 , pp. 12378-12385
    • Muriaux, D.1
  • 39
    • 0038710633 scopus 로고    scopus 로고
    • Elimination of protease activity restores efficient virion production to a human immunodeficiency virus type 1 nucleocapsid deletion mutant
    • Ott, D. E., et al. 2003. Elimination of protease activity restores efficient virion production to a human immunodeficiency virus type 1 nucleocapsid deletion mutant. J. Virol. 77:5547-5556.
    • (2003) J. Virol. , vol.77 , pp. 5547-5556
    • Ott, D.E.1
  • 40
    • 27644469860 scopus 로고    scopus 로고
    • Redundant roles for nucleocapsid and matrix RNA-binding sequences in human immunodeficiency virus type 1 assembly
    • Ott, D. E., L. V. Coren, and T. D. Gagliardi. 2005. Redundant roles for nucleocapsid and matrix RNA-binding sequences in human immunodeficiency virus type 1 assembly. J. Virol. 79:13839-13847.
    • (2005) J. Virol. , vol.79 , pp. 13839-13847
    • Ott, D.E.1    Coren, L.V.2    Gagliardi, T.D.3
  • 41
    • 34248359067 scopus 로고    scopus 로고
    • ATSAS 2.1: towards automated and web-supported small-angle scattering data analysis
    • Petoukhov, M. V., P. V. Konarev, A. G. Kikhney, and D. I. Svergun. 2007. ATSAS 2.1: towards automated and web-supported small-angle scattering data analysis. J. Appl. Crystallogr. 40:s223-s228.
    • (2007) J. Appl. Crystallogr. , vol.40
    • Petoukhov, M.V.1    Konarev, P.V.2    Kikhney, A.G.3    Svergun, D.I.4
  • 42
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera-a visualization system for exploratory research and analysis
    • Pettersen, E. F., et al. 2004. UCSF Chimera-a visualization system for exploratory research and analysis. J. Comput. Chem. 25:1605-1612.
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1
  • 43
    • 0033621117 scopus 로고    scopus 로고
    • Compactness of the denatured state of a fast-folding protein measured by submillisecond small-angle x-ray scattering
    • Pollack, L., et al. 1999. Compactness of the denatured state of a fast-folding protein measured by submillisecond small-angle x-ray scattering. Proc. Natl. Acad. Sci. 96:10115-10117.
    • (1999) Proc. Natl. Acad. Sci. , vol.96 , pp. 10115-10117
    • Pollack, L.1
  • 44
    • 0035003983 scopus 로고    scopus 로고
    • Sequencespecific interaction between HIV-1 matrix protein and viral genomic RNA revealed by in vitro genetic selection
    • Purohit, P., S. Dupont, M. Stevenson, and M. R. Green. 2001. Sequencespecific interaction between HIV-1 matrix protein and viral genomic RNA revealed by in vitro genetic selection. RNA 7:576-584.
    • (2001) RNA , vol.7 , pp. 576-584
    • Purohit, P.1    Dupont, S.2    Stevenson, M.3    Green, M.R.4
  • 45
    • 1842859044 scopus 로고    scopus 로고
    • Atomic resolution structure of Moloney murine leukemia virus matrix protein and its relationship to other retroviral matrix proteins
    • Riffel, N., et al. 2002. Atomic resolution structure of Moloney murine leukemia virus matrix protein and its relationship to other retroviral matrix proteins. Structure (Cambridge) 10:1627-1636.
    • (2002) Structure (Cambridge) , vol.10 , pp. 1627-1636
    • Riffel, N.1
  • 46
    • 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
  • 47
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • Schuck, P. 2000. Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling. Biophys. J. 78:1606-1619.
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 48
    • 0014007813 scopus 로고
    • Determination of molecular weights and frictional ratios of proteins in impure systems by use of gel filtration and density gradient centrifugation: application to crude preparations of sulfite and hydroxylamine reductases
    • Siegel, L. M., and K. J. Monty. 1966. Determination of molecular weights and frictional ratios of proteins in impure systems by use of gel filtration and density gradient centrifugation: application to crude preparations of sulfite and hydroxylamine reductases. Biochim. Biophys. Acta 112:346-362.
    • (1966) Biochim. Biophys. Acta , vol.112 , pp. 346-362
    • Siegel, L.M.1    Monty, K.J.2
  • 49
    • 0032980562 scopus 로고    scopus 로고
    • A survey of left-handed polyproline II helices
    • Stapley, B. J., and T. P. Creamer. 1999. A survey of left-handed polyproline II helices. Protein Sci. 8:587-595.
    • (1999) Protein Sci , vol.8 , pp. 587-595
    • Stapley, B.J.1    Creamer, T.P.2
  • 50
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun, D. I. 1992. Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J. Appl. Crystallogr. 25: 492-503.
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 492-503
    • Svergun, D.I.1
  • 51
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun, D. I. 1999. Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys. J. 76:2879-2886.
    • (1999) Biophys. J. , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 52
    • 0001118596 scopus 로고    scopus 로고
    • Synthesis, assembly, and processing of viral proteins
    • J. M. Coffin, S. H. Hughes, and H. E. Varmus (ed.), Cold Spring Harbor Laboratory Press, Plainview, NY
    • Swanstrom, R., and J. W. Wills. 1997. Synthesis, assembly, and processing of viral proteins, p. 263-334. In J. M. Coffin, S. H. Hughes, and H. E. Varmus (ed.), Retroviruses. Cold Spring Harbor Laboratory Press, Plainview, NY.
    • (1997) Retroviruses , pp. 263-334
    • Swanstrom, R.1    Wills, J.W.2
  • 53
    • 0036294666 scopus 로고    scopus 로고
    • Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein
    • Tang, C., Y. Ndassa, and M. F. Summers. 2002. Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein. Nat. Struct. Biol. 9:537-543.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 537-543
    • Tang, C.1    Ndassa, Y.2    Summers, M.F.3
  • 54
    • 0037404501 scopus 로고    scopus 로고
    • Functional surfaces of the human immunodeficiency virus type 1 capsid protein
    • von Schwedler, U. K., K. M. Stray, J. E. Garrus, and W. I. Sundquist. 2003. Functional surfaces of the human immunodeficiency virus type 1 capsid protein. J. Virol. 77:5439-5450.
    • (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
  • 55
    • 0032925240 scopus 로고    scopus 로고
    • Structures of the HIV-1 capsid protein dimerization domain at 2. 6 Å resolution. Acta Crystallogr
    • Worthylake, D. K., H. Wang, S. Yoo, W. I. Sundquist, and C. P. Hill. 1999. Structures of the HIV-1 capsid protein dimerization domain at 2.6 Å resolution. Acta Crystallogr. D Biol. Crystallogr. 55(Pt. 1):85-92.
    • (1999) D Biol. Crystallogr. , vol.55 , Issue.PART 1 , pp. 85-92
    • Worthylake, D.K.1    Wang, H.2    Yoo, S.3    Sundquist, W.I.4    Hill, C.P.5
  • 56
    • 0035209087 scopus 로고    scopus 로고
    • Using Situs for the registration of protein structures with low-resolution bead models from X-ray solution scattering
    • Wriggers, W., and P. Chacon. 2001. Using Situs for the registration of protein structures with low-resolution bead models from X-ray solution scattering. J. Appl. Crystallogr. 34:773-776.
    • (2001) J. Appl. Crystallogr. , vol.34 , pp. 773-776
    • Wriggers, W.1    Chacon, P.2
  • 57
    • 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., et al. 2007. Electron cryotomography of immature HIV-1 virions reveals the structure of the CA and SP1 Gag shells. EMBO J. 26:2218-2226.
    • (2007) EMBO J , vol.26 , pp. 2218-2226
    • Wright, E.R.1
  • 58
    • 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., E. M. Wilson-Kubalek, S. G. Weiner, P. O. Brown, and A. Rein. 1998. Supramolecular organization of immature and mature murine leukemia virus revealed by electron cryo-microscopy: implications for retroviral assembly mechanisms. Proc. Natl. Acad. Sci. U. S. A. 95:7299-7304.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 7299-7304
    • Yeager, M.1    Wilson-Kubalek, E.M.2    Weiner, S.G.3    Brown, P.O.4    Rein, A.5
  • 59
    • 0344035661 scopus 로고    scopus 로고
    • Mutations altering the Moloney murine leukemia virus p12 Gag protein affect virion production and early events of the virus life cycle
    • Yuan, B., X. Li, and S. P. Goff. 1999. Mutations altering the Moloney murine leukemia virus p12 Gag protein affect virion production and early events of the virus life cycle. EMBO J. 18:4700-4710.
    • (1999) EMBO J , vol.18 , pp. 4700-4710
    • Yuan, B.1    Li, X.2    Goff, S.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.