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Volumn 184, Issue 2, 2013, Pages 129-135

Electron microscopy analysis of a disaccharide analog complex reveals receptor interactions of adeno-associated virus

Author keywords

Attachment; Difference map; Heparin; Parvovirus; Receptor; Refinement

Indexed keywords

ARGININE; DISACCHARIDE; HEPARIN; PARVOVIRUS VECTOR; SUCROSOFATE;

EID: 84887231402     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2013.09.004     Document Type: Article
Times cited : (17)

References (71)
  • 1
    • 33748945422 scopus 로고    scopus 로고
    • The 37/67-kilodalton laminin receptor is a receptor for adeno-associated virus serotypes 8, 2, 3, and 9
    • Akache B., Grimm D., Pandey K., Yant S.R., Xu H., et al. The 37/67-kilodalton laminin receptor is a receptor for adeno-associated virus serotypes 8, 2, 3, and 9. J. Virol. 2006, 80:9831-9836.
    • (2006) J. Virol. , vol.80 , pp. 9831-9836
    • Akache, B.1    Grimm, D.2    Pandey, K.3    Yant, S.R.4    Xu, H.5
  • 2
    • 33748494015 scopus 로고    scopus 로고
    • Adeno-associated virus type 2 contains an integrin alpha5beta1 binding domain essential for viral cell entry
    • Asokan A., Hamra J.B., Govindasamy L., Agbandje-McKenna M., Samulski R.J. Adeno-associated virus type 2 contains an integrin alpha5beta1 binding domain essential for viral cell entry. J. Virol. 2006, 80:8961-8969.
    • (2006) J. Virol. , vol.80 , pp. 8961-8969
    • Asokan, A.1    Hamra, J.B.2    Govindasamy, L.3    Agbandje-McKenna, M.4    Samulski, R.J.5
  • 3
    • 74049120342 scopus 로고    scopus 로고
    • Reengineering a receptor footprint of adeno-associated virus enables selective and systemic gene transfer to muscle
    • Asokan A., Conway J.C., Phillips J.L., Li C., Hegge J., et al. Reengineering a receptor footprint of adeno-associated virus enables selective and systemic gene transfer to muscle. Nat. Biotechnol. 2010, 28:79-82.
    • (2010) Nat. Biotechnol. , vol.28 , pp. 79-82
    • Asokan, A.1    Conway, J.C.2    Phillips, J.L.3    Li, C.4    Hegge, J.5
  • 4
    • 84859440283 scopus 로고    scopus 로고
    • The AAV vector toolkit: poised at the clinical crossroads
    • Asokan A., Schaffer D.V., Samulski R.J. The AAV vector toolkit: poised at the clinical crossroads. Mol. Ther. 2012, 20:699-708.
    • (2012) Mol. Ther. , vol.20 , pp. 699-708
    • Asokan, A.1    Schaffer, D.V.2    Samulski, R.J.3
  • 5
    • 84878580683 scopus 로고    scopus 로고
    • Ribosome structures to near-atomic resolution from thirty thousand cryo-EM particles
    • Bai X.C., Fernandez I.S., McMullan G., Scheres S.H. Ribosome structures to near-atomic resolution from thirty thousand cryo-EM particles. elife 2013, 2:e00461.
    • (2013) elife , vol.2
    • Bai, X.C.1    Fernandez, I.S.2    McMullan, G.3    Scheres, S.H.4
  • 6
    • 0033998692 scopus 로고    scopus 로고
    • Infectious entry pathway of adeno-associated virus and adeno-associated virus vectors
    • Bartlett J.S., Wilcher R., Samulski R.J. Infectious entry pathway of adeno-associated virus and adeno-associated virus vectors. J. Virol. 2000, 74:2777-2785.
    • (2000) J. Virol. , vol.74 , pp. 2777-2785
    • Bartlett, J.S.1    Wilcher, R.2    Samulski, R.J.3
  • 8
    • 1842409555 scopus 로고    scopus 로고
    • Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy
    • Böttcher B., Wynne S.A., Crowther R.A. Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy. Nature 1997, 386:88-91.
    • (1997) Nature , vol.386 , pp. 88-91
    • Böttcher, B.1    Wynne, S.A.2    Crowther, R.A.3
  • 9
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR system: a new software system for macromolecular structure determination
    • Brünger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., et al. Crystallography and NMR system: a new software system for macromolecular structure determination. Acta Crystallogr. A 1998, D54:905-921.
    • (1998) Acta Crystallogr. A , vol.D54 , pp. 905-921
    • Brünger, A.T.1    Adams, P.D.2    Clore, G.M.3    DeLano, W.L.4    Gros, P.5
  • 11
    • 84875024670 scopus 로고    scopus 로고
    • Atomic modeling of cryo-electron microscopy reconstructions - joint refinement of model and imaging parameters
    • Chapman M.S., Trzynka A., Chapman B.K. Atomic modeling of cryo-electron microscopy reconstructions - joint refinement of model and imaging parameters. J. Struct. Biol. 2013, 182:10-21.
    • (2013) J. Struct. Biol. , vol.182 , pp. 10-21
    • Chapman, M.S.1    Trzynka, A.2    Chapman, B.K.3
  • 12
    • 21244491577 scopus 로고    scopus 로고
    • AAV hybrid serotypes: improved vectors for gene delivery
    • Choi V.W., McCarty D.M., Samulski R.J. AAV hybrid serotypes: improved vectors for gene delivery. Curr. Gene Ther. 2005, 5:299-310.
    • (2005) Curr. Gene Ther. , vol.5 , pp. 299-310
    • Choi, V.W.1    McCarty, D.M.2    Samulski, R.J.3
  • 14
    • 34548250956 scopus 로고    scopus 로고
    • Parvoviral host range and cell entry mechanisms
    • Cotmore S.F., Tattersall P. Parvoviral host range and cell entry mechanisms. Adv. Virus Res. 2007, 70:183-232.
    • (2007) Adv. Virus Res. , vol.70 , pp. 183-232
    • Cotmore, S.F.1    Tattersall, P.2
  • 16
    • 84864003612 scopus 로고    scopus 로고
    • Structural insight into the unique properties of adeno-associated virus serotype 9
    • DiMattia M.A., Nam H.J., Van Vliet K., Mitchell M., Bennett A., et al. Structural insight into the unique properties of adeno-associated virus serotype 9. J. Virol. 2012, 86:6947-6958.
    • (2012) J. Virol. , vol.86 , pp. 6947-6958
    • DiMattia, M.A.1    Nam, H.J.2    Van Vliet, K.3    Mitchell, M.4    Bennett, A.5
  • 17
    • 0031470456 scopus 로고    scopus 로고
    • How do viruses enter cells? The HIV coreceptors teach us a lesson of complexity
    • Dimitrov D.S. How do viruses enter cells? The HIV coreceptors teach us a lesson of complexity. Cell 1997, 91:721-730.
    • (1997) Cell , vol.91 , pp. 721-730
    • Dimitrov, D.S.1
  • 18
    • 77957726816 scopus 로고    scopus 로고
    • Adeno-associated virus for the treatment of muscle diseases: toward clinical trials
    • DiPrimio N., McPhee S.W., Samulski R.J. Adeno-associated virus for the treatment of muscle diseases: toward clinical trials. Curr. Opin. Mol. Ther. 2010, 12:553-560.
    • (2010) Curr. Opin. Mol. Ther. , vol.12 , pp. 553-560
    • DiPrimio, N.1    McPhee, S.W.2    Samulski, R.J.3
  • 20
    • 51549084591 scopus 로고    scopus 로고
    • Sharpening high resolution information in single particle electron cryomicroscopy
    • Fernandez J.J., Luque D., Caston J.R., Carrascosa J.L. Sharpening high resolution information in single particle electron cryomicroscopy. J. Struct. Biol. 2008, 164:170-175.
    • (2008) J. Struct. Biol. , vol.164 , pp. 170-175
    • Fernandez, J.J.1    Luque, D.2    Caston, J.R.3    Carrascosa, J.L.4
  • 21
    • 0033081979 scopus 로고    scopus 로고
    • The structure and function of a foot-and-mouth disease virus-oligosaccharide receptor complex
    • Fry E.E., Lea S.M., Jackson T., Newman J.W., Ellard F.M., et al. The structure and function of a foot-and-mouth disease virus-oligosaccharide receptor complex. EMBO J. 1999, 18:543-554.
    • (1999) EMBO J. , vol.18 , pp. 543-554
    • Fry, E.E.1    Lea, S.M.2    Jackson, T.3    Newman, J.W.4    Ellard, F.M.5
  • 22
    • 0033777020 scopus 로고    scopus 로고
    • Resolution measurement in structures derived from single particles
    • Grigorieff N. Resolution measurement in structures derived from single particles. Acta Crystallogr. D Biol. Crystallogr. 2000, 56:1270-1277.
    • (2000) Acta Crystallogr. D Biol. Crystallogr. , vol.56 , pp. 1270-1277
    • Grigorieff, N.1
  • 23
    • 33845348200 scopus 로고    scopus 로고
    • FREALIGN: high-resolution refinement of single particle structures
    • Grigorieff N. FREALIGN: high-resolution refinement of single particle structures. J. Struct. Biol. 2007, 157:117-125.
    • (2007) J. Struct. Biol. , vol.157 , pp. 117-125
    • Grigorieff, N.1
  • 24
    • 44949131860 scopus 로고    scopus 로고
    • In vitro and in vivo gene therapy vector evolution via multispecies interbreeding and retargeting of adeno-associated viruses
    • Grimm D., Lee J.S., Wang L., Desai T., Akache B., et al. In vitro and in vivo gene therapy vector evolution via multispecies interbreeding and retargeting of adeno-associated viruses. J. Virol. 2008, 82:5887-5911.
    • (2008) J. Virol. , vol.82 , pp. 5887-5911
    • Grimm, D.1    Lee, J.S.2    Wang, L.3    Desai, T.4    Akache, B.5
  • 25
    • 0000313739 scopus 로고
    • Exact filters for general geometry 3-dimensional reconstruction
    • Harauz G., van Heel M. Exact filters for general geometry 3-dimensional reconstruction. Optik 1986, 73:146-156.
    • (1986) Optik , vol.73 , pp. 146-156
    • Harauz, G.1    van Heel, M.2
  • 26
    • 84874191297 scopus 로고    scopus 로고
    • High-resolution cryo-electron microscopy structure of the Trypanosoma brucei ribosome
    • Hashem Y., des Georges A., Fu J., Buss S.N., Jossinet F., et al. High-resolution cryo-electron microscopy structure of the Trypanosoma brucei ribosome. Nature 2013, 494:385-389.
    • (2013) Nature , vol.494 , pp. 385-389
    • Hashem, Y.1    des Georges, A.2    Fu, J.3    Buss, S.N.4    Jossinet, F.5
  • 27
    • 0000895319 scopus 로고
    • The difference fourier technique in protein crystallography: errors and their treatment
    • Henderson R., Moffat J.K. The difference fourier technique in protein crystallography: errors and their treatment. Acta Crystallogr. B 1971, 27:1414-1420.
    • (1971) Acta Crystallogr. B , vol.27 , pp. 1414-1420
    • Henderson, R.1    Moffat, J.K.2
  • 28
    • 0013852450 scopus 로고
    • Structure of some crystalline lysozyme-inhibitor complexes determined by X-ray analysis at 6Å resolution
    • Johnson L.N., Phillips D.C. Structure of some crystalline lysozyme-inhibitor complexes determined by X-ray analysis at 6Å resolution. Nature 1965, 206:761-763.
    • (1965) Nature , vol.206 , pp. 761-763
    • Johnson, L.N.1    Phillips, D.C.2
  • 29
    • 0034957168 scopus 로고    scopus 로고
    • Adeno-associated virus serotype 4 (AAV4) and AAV5 both require sialic acid binding for hemagglutination and efficient transduction but differ in sialic acid linkage specificity
    • Kaludov N., Brown K.E., Walters R.W., Zabner J., Chiorini J.A. Adeno-associated virus serotype 4 (AAV4) and AAV5 both require sialic acid binding for hemagglutination and efficient transduction but differ in sialic acid linkage specificity. J. Virol. 2001, 75:6884-6893.
    • (2001) J. Virol. , vol.75 , pp. 6884-6893
    • Kaludov, N.1    Brown, K.E.2    Walters, R.W.3    Zabner, J.4    Chiorini, J.A.5
  • 30
    • 10644225886 scopus 로고    scopus 로고
    • Hepatocyte growth factor receptor is a coreceptor for adeno-associated virus type 2 infection
    • Kashiwakura Y., Tamayose K., Iwabuchi K., Hirai Y., Shimada T., et al. Hepatocyte growth factor receptor is a coreceptor for adeno-associated virus type 2 infection. J. Virol. 2005, 79:609-614.
    • (2005) J. Virol. , vol.79 , pp. 609-614
    • Kashiwakura, Y.1    Tamayose, K.2    Iwabuchi, K.3    Hirai, Y.4    Shimada, T.5
  • 31
    • 0141454787 scopus 로고    scopus 로고
    • Identification of a heparin-binding motif on adeno-associated virus type 2 capsids
    • Kern A., Schmidt K., Leder C., Muller O.J., Wobus C.E., et al. Identification of a heparin-binding motif on adeno-associated virus type 2 capsids. J. Virol. 2003, 77:11072-11081.
    • (2003) J. Virol. , vol.77 , pp. 11072-11081
    • Kern, A.1    Schmidt, K.2    Leder, C.3    Muller, O.J.4    Wobus, C.E.5
  • 32
    • 60649103238 scopus 로고    scopus 로고
    • Appion: an integrated, database-driven pipeline to facilitate EM image processing
    • Lander G.C., Stagg S.M., Voss N.R., Cheng A., Fellmann D., et al. Appion: an integrated, database-driven pipeline to facilitate EM image processing. J. Struct. Biol. 2009, 166:95-102.
    • (2009) J. Struct. Biol. , vol.166 , pp. 95-102
    • Lander, G.C.1    Stagg, S.M.2    Voss, N.R.3    Cheng, A.4    Fellmann, D.5
  • 33
    • 84855341055 scopus 로고    scopus 로고
    • Identification of the heparin binding site on adeno-associated virus serotype 3B (AAV-3B)
    • Lerch T.F., Chapman M.S. Identification of the heparin binding site on adeno-associated virus serotype 3B (AAV-3B). Virology 2012, 423:6-13.
    • (2012) Virology , vol.423 , pp. 6-13
    • Lerch, T.F.1    Chapman, M.S.2
  • 34
    • 84864829908 scopus 로고    scopus 로고
    • Structure of AAV-DJ, a retargeted gene therapy vector: cryo-electron microscopy at 4.5Å resolution
    • Lerch Thomas F., O'Donnell Jason K., Meyer Nancy L., Xie Q., Taylor Kenneth A., et al. Structure of AAV-DJ, a retargeted gene therapy vector: cryo-electron microscopy at 4.5Å resolution. Structure 2012, 20:1310-1320.
    • (2012) Structure , vol.20 , pp. 1310-1320
    • Lerch, T.F.1    O'Donnell, J.K.2    Meyer, N.L.3    Xie, Q.4    Taylor, K.A.5
  • 35
    • 59149090531 scopus 로고    scopus 로고
    • Heparin binding induces conformational changes in adeno-associated virus serotype 2
    • Levy H.C., Bowman V.D., Govindasamy L., McKenna R., Nash K., et al. Heparin binding induces conformational changes in adeno-associated virus serotype 2. J. Struct. Biol. 2009, 165:146-156.
    • (2009) J. Struct. Biol. , vol.165 , pp. 146-156
    • Levy, H.C.1    Bowman, V.D.2    Govindasamy, L.3    McKenna, R.4    Nash, K.5
  • 36
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: semiautomated software for high-resolution single-particle reconstructions
    • Ludtke S.J., Baldwin P.R., Chiu W. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 1999, 128:82-97.
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 37
    • 40049105503 scopus 로고    scopus 로고
    • De novo backbone trace of GroEL from single particle electron cryomicroscopy
    • Ludtke S.J., Baker M.L., Chen D.H., Song J.L., Chuang D.T., et al. De novo backbone trace of GroEL from single particle electron cryomicroscopy. Structure 2008, 16:441-448.
    • (2008) Structure , vol.16 , pp. 441-448
    • Ludtke, S.J.1    Baker, M.L.2    Chen, D.H.3    Song, J.L.4    Chuang, D.T.5
  • 38
    • 32344438754 scopus 로고    scopus 로고
    • Directed evolution of adeno-associated virus yields enhanced gene delivery vectors
    • Maheshri N., Koerber J.T., Kaspar B.K., Schaffer D.V. Directed evolution of adeno-associated virus yields enhanced gene delivery vectors. Nat. Biotechnol. 2006, 24:198-204.
    • (2006) Nat. Biotechnol. , vol.24 , pp. 198-204
    • Maheshri, N.1    Koerber, J.T.2    Kaspar, B.K.3    Schaffer, D.V.4
  • 40
    • 30344459715 scopus 로고    scopus 로고
    • Low pH-dependent endosomal processing of the incoming parvovirus minute virus of mice virion leads to externalization of the VP1 N-terminal sequence (N-VP1), N-VP2 cleavage, and uncoating of the full-length genome
    • Mani B., Baltzer C., Valle N., Almendral J.M., Kempf C., et al. Low pH-dependent endosomal processing of the incoming parvovirus minute virus of mice virion leads to externalization of the VP1 N-terminal sequence (N-VP1), N-VP2 cleavage, and uncoating of the full-length genome. J. Virol. 2006, 80:1015-1024.
    • (2006) J. Virol. , vol.80 , pp. 1015-1024
    • Mani, B.1    Baltzer, C.2    Valle, N.3    Almendral, J.M.4    Kempf, C.5
  • 41
    • 84862329652 scopus 로고    scopus 로고
    • Structure of adeno-associated virus-2 in complex with neutralizing monoclonal antibody A20
    • McCraw D.M., O'Donnell J.K., Taylor K.A., Stagg S.M., Chapman M.S. Structure of adeno-associated virus-2 in complex with neutralizing monoclonal antibody A20. Virology 2012, 431:40-49.
    • (2012) Virology , vol.431 , pp. 40-49
    • McCraw, D.M.1    O'Donnell, J.K.2    Taylor, K.A.3    Stagg, S.M.4    Chapman, M.S.5
  • 42
    • 84879038703 scopus 로고    scopus 로고
    • De novo modeling of the F420-reducing [NiFe]-hydrogenase from a methanogenic archaeon by cryo-electron microscopy
    • Mills D.J., Vitt S., Strauss M., Shima S., Vonck J. De novo modeling of the F420-reducing [NiFe]-hydrogenase from a methanogenic archaeon by cryo-electron microscopy. elife 2013, 2:e00218.
    • (2013) elife , vol.2
    • Mills, D.J.1    Vitt, S.2    Strauss, M.3    Shima, S.4    Vonck, J.5
  • 43
  • 44
    • 70349597601 scopus 로고    scopus 로고
    • Electronic ligand builder and optimization workbench (eLBOW): a tool for ligand coordinate and restraint generation
    • Moriarty N.W., Grosse-Kunstleve R.W., Adams P.D. Electronic ligand builder and optimization workbench (eLBOW): a tool for ligand coordinate and restraint generation. Acta Crystallogr. D Biol. Crystallogr. 2009, 65:1074-1080.
    • (2009) Acta Crystallogr. D Biol. Crystallogr. , vol.65 , pp. 1074-1080
    • Moriarty, N.W.1    Grosse-Kunstleve, R.W.2    Adams, P.D.3
  • 45
    • 36049020398 scopus 로고    scopus 로고
    • Structure of adeno-associated virus serotype 8, a gene therapy vector
    • Nam H.J., Lane M.D., Padron E., Gurda B., McKenna R., et al. Structure of adeno-associated virus serotype 8, a gene therapy vector. J. Virol. 2007, 81:12260-12271.
    • (2007) J. Virol. , vol.81 , pp. 12260-12271
    • Nam, H.J.1    Lane, M.D.2    Padron, E.3    Gurda, B.4    McKenna, R.5
  • 46
    • 80655142508 scopus 로고    scopus 로고
    • Structural studies of adeno-associated virus serotype 8 capsid transitions associated with endosomal trafficking
    • Nam H.J., Gurda B.L., McKenna R., Potter M., Byrne B., et al. Structural studies of adeno-associated virus serotype 8 capsid transitions associated with endosomal trafficking. J. Virol. 2011, 85:11791-11799.
    • (2011) J. Virol. , vol.85 , pp. 11791-11799
    • Nam, H.J.1    Gurda, B.L.2    McKenna, R.3    Potter, M.4    Byrne, B.5
  • 48
    • 60949103263 scopus 로고    scopus 로고
    • Adeno-associated virus-2 and its primary cellular receptor - cryo-EM structure of a heparin complex
    • O'Donnell J., Taylor K.A., Chapman M.S. Adeno-associated virus-2 and its primary cellular receptor - cryo-EM structure of a heparin complex. Virology 2009, 385:434-443.
    • (2009) Virology , vol.385 , pp. 434-443
    • O'Donnell, J.1    Taylor, K.A.2    Chapman, M.S.3
  • 49
    • 0038618725 scopus 로고    scopus 로고
    • Identification of amino acid residues in the capsid proteins of adeno-associated virus type 2 that contribute to heparan sulfate proteoglycan binding
    • Opie S.R., Warrington K.H., Agbandje-McKenna M., Zolotukhin S., Muzyczka N. Identification of amino acid residues in the capsid proteins of adeno-associated virus type 2 that contribute to heparan sulfate proteoglycan binding. J. Virol. 2003, 77:6995-7006.
    • (2003) J. Virol. , vol.77 , pp. 6995-7006
    • Opie, S.R.1    Warrington, K.H.2    Agbandje-McKenna, M.3    Zolotukhin, S.4    Muzyczka, N.5
  • 51
    • 33745776920 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycan binding properties of adeno-associated virus retargeting mutants and consequences for their in vivo tropism
    • Perabo L., Goldnau D., White K., Endell J., Boucas J., et al. Heparan sulfate proteoglycan binding properties of adeno-associated virus retargeting mutants and consequences for their in vivo tropism. J. Virol. 2006, 80:7265-7269.
    • (2006) J. Virol. , vol.80 , pp. 7265-7269
    • Perabo, L.1    Goldnau, D.2    White, K.3    Endell, J.4    Boucas, J.5
  • 52
    • 0033010884 scopus 로고    scopus 로고
    • Human fibroblast growth factor receptor 1 is a co-receptor for infection by adeno-associated virus 2
    • Qing K., Mah C., Hansen J., Zhou S., Dwarki V., et al. Human fibroblast growth factor receptor 1 is a co-receptor for infection by adeno-associated virus 2. Nat. Med. 1999, 5:71-77.
    • (1999) Nat. Med. , vol.5 , pp. 71-77
    • Qing, K.1    Mah, C.2    Hansen, J.3    Zhou, S.4    Dwarki, V.5
  • 53
    • 0033604366 scopus 로고    scopus 로고
    • Integrin alphaVbeta5 is not involved in adeno-associated virus type 2 (AAV2) infection
    • Qiu J., Brown K.E. Integrin alphaVbeta5 is not involved in adeno-associated virus type 2 (AAV2) infection. Virology 1999, 264:436-440.
    • (1999) Virology , vol.264 , pp. 436-440
    • Qiu, J.1    Brown, K.E.2
  • 54
    • 33845389502 scopus 로고    scopus 로고
    • Conformational changes in the VP1-unique region of native human parvovirus B19 lead to exposure of internal sequences that play a role in virus neutralization and infectivity
    • Ros C., Gerber M., Kempf C. Conformational changes in the VP1-unique region of native human parvovirus B19 lead to exposure of internal sequences that play a role in virus neutralization and infectivity. J. Virol. 2006, 80:12017-12024.
    • (2006) J. Virol. , vol.80 , pp. 12017-12024
    • Ros, C.1    Gerber, M.2    Kempf, C.3
  • 55
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • Rosenthal P.B., Henderson R. Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J. Mol. Biol. 2003, 333:721-745.
    • (2003) J. Mol. Biol. , vol.333 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 56
    • 79953857433 scopus 로고    scopus 로고
    • Terminal N-linked galactose is the primary receptor for adeno-associated virus 9
    • Shen S., Bryant K.D., Brown S.M., Randell S.H., Asokan A. Terminal N-linked galactose is the primary receptor for adeno-associated virus 9. J. Biol. Chem. 2011, 286:13532-13540.
    • (2011) J. Biol. Chem. , vol.286 , pp. 13532-13540
    • Shen, S.1    Bryant, K.D.2    Brown, S.M.3    Randell, S.H.4    Asokan, A.5
  • 57
    • 84869069238 scopus 로고    scopus 로고
    • Glycan binding avidity determines the systemic fate of adeno-associated virus type 9
    • Shen S., Bryant K.D., Sun J., Brown S.M., Troupes A., et al. Glycan binding avidity determines the systemic fate of adeno-associated virus type 9. J. Virol. 2012, 86:10408-10417.
    • (2012) J. Virol. , vol.86 , pp. 10408-10417
    • Shen, S.1    Bryant, K.D.2    Sun, J.3    Brown, S.M.4    Troupes, A.5
  • 58
    • 0013862835 scopus 로고
    • An X-ray diffraction study of inhibited derivatives of alpha-chymotrypsin
    • Sigler P.B., Jeffery B.A., Matthews B.W., Blow D.M. An X-ray diffraction study of inhibited derivatives of alpha-chymotrypsin. J. Mol. Biol. 1966, 15:175-192.
    • (1966) J. Mol. Biol. , vol.15 , pp. 175-192
    • Sigler, P.B.1    Jeffery, B.A.2    Matthews, B.W.3    Blow, D.M.4
  • 59
    • 0022489613 scopus 로고
    • The site of attachment in human rhinovirus 14 for antiviral agents that inhibit uncoating
    • Smith T.J., Kremer M.J., Luo M., Vriend G., Arnold E., et al. The site of attachment in human rhinovirus 14 for antiviral agents that inhibit uncoating. Science 1986, 233:1286-1293.
    • (1986) Science , vol.233 , pp. 1286-1293
    • Smith, T.J.1    Kremer, M.J.2    Luo, M.3    Vriend, G.4    Arnold, E.5
  • 60
    • 33750712806 scopus 로고    scopus 로고
    • Adeno-associated virus type 2 capsids with externalized VP1/VP2 trafficking domains are generated prior to passage through the cytoplasm and are maintained until uncoating occurs in the nucleus
    • Sonntag F., Bleker S., Leuchs B., Fischer R., Kleinschmidt J.A. Adeno-associated virus type 2 capsids with externalized VP1/VP2 trafficking domains are generated prior to passage through the cytoplasm and are maintained until uncoating occurs in the nucleus. J. Virol. 2006, 80:11040-11054.
    • (2006) J. Virol. , vol.80 , pp. 11040-11054
    • Sonntag, F.1    Bleker, S.2    Leuchs, B.3    Fischer, R.4    Kleinschmidt, J.A.5
  • 61
    • 33845291163 scopus 로고    scopus 로고
    • Ab initio resolution measurement for single particle structures
    • Sousa D., Grigorieff N. Ab initio resolution measurement for single particle structures. J. Struct. Biol. 2007, 157:201-210.
    • (2007) J. Struct. Biol. , vol.157 , pp. 201-210
    • Sousa, D.1    Grigorieff, N.2
  • 62
    • 0027184774 scopus 로고
    • Difference imaging of adenovirus: bridging the resolution gap between X-ray crystallography and electron microscopy
    • Stewart P.L., Fuller S.D., Burnett R.M. Difference imaging of adenovirus: bridging the resolution gap between X-ray crystallography and electron microscopy. EMBO J. 1993, 12:2589-2599.
    • (1993) EMBO J. , vol.12 , pp. 2589-2599
    • Stewart, P.L.1    Fuller, S.D.2    Burnett, R.M.3
  • 63
    • 0002400397 scopus 로고
    • The mode of attachment of the azide ion to sperm whale metmyoglobin
    • Stryer L., Kendrew J.C., Watson H.C. The mode of attachment of the azide ion to sperm whale metmyoglobin. J. Mol. Biol. 1964, 8:96-104.
    • (1964) J. Mol. Biol. , vol.8 , pp. 96-104
    • Stryer, L.1    Kendrew, J.C.2    Watson, H.C.3
  • 65
    • 0031906147 scopus 로고    scopus 로고
    • Membrane-associated heparan sulfate proteoglycan is a receptor for adeno-associated virus type 2 virions
    • Summerford C., Samulski R.J. Membrane-associated heparan sulfate proteoglycan is a receptor for adeno-associated virus type 2 virions. J. Virol. 1998, 72:1438-1445.
    • (1998) J. Virol. , vol.72 , pp. 1438-1445
    • Summerford, C.1    Samulski, R.J.2
  • 66
    • 0032589751 scopus 로고    scopus 로고
    • AlphaVbeta5 integrin: a co-receptor for adeno-associated virus type 2 infection
    • Summerford C., Bartlett J.S., Samulski R.J. AlphaVbeta5 integrin: a co-receptor for adeno-associated virus type 2 infection. Nat. Med. 1999, 5:78-82.
    • (1999) Nat. Med. , vol.5 , pp. 78-82
    • Summerford, C.1    Bartlett, J.S.2    Samulski, R.J.3
  • 67
    • 85145109981 scopus 로고    scopus 로고
    • Cell infection processes of autonomous parvoviruses
    • Hodder Arnold Ltd., London, J.R. Kerr (Ed.)
    • Vihinen-Ranta M., Parrish C.R. Cell infection processes of autonomous parvoviruses. Parvoviruses 2006, 157-163. Hodder Arnold Ltd., London. J.R. Kerr (Ed.).
    • (2006) Parvoviruses , pp. 157-163
    • Vihinen-Ranta, M.1    Parrish, C.R.2
  • 68
    • 33645502138 scopus 로고    scopus 로고
    • Vascular bed-targeted in vivo gene delivery using tropism-modified adeno-associated viruses
    • Work L.M., Buning H., Hunt E., Nicklin S.A., Denby L., et al. Vascular bed-targeted in vivo gene delivery using tropism-modified adeno-associated viruses. Mol. Ther. 2006, 13:683-693.
    • (2006) Mol. Ther. , vol.13 , pp. 683-693
    • Work, L.M.1    Buning, H.2    Hunt, E.3    Nicklin, S.A.4    Denby, L.5
  • 69
    • 33750722840 scopus 로고    scopus 로고
    • Single amino acid changes can influence titer, heparin binding, and tissue tropism in different adeno-associated virus (AAV) serotypes
    • Wu Z., Asokan A., Grieger J.C., Govindasamy L., Agbandje-McKenna M., et al. Single amino acid changes can influence titer, heparin binding, and tissue tropism in different adeno-associated virus (AAV) serotypes. J. Virol. 2006, 80:11393-11397.
    • (2006) J. Virol. , vol.80 , pp. 11393-11397
    • Wu, Z.1    Asokan, A.2    Grieger, J.C.3    Govindasamy, L.4    Agbandje-McKenna, M.5
  • 70
    • 0036678455 scopus 로고    scopus 로고
    • The atomic structure of adeno-associated virus (AAV-2), a vector for human gene therapy
    • Xie Q., Bu W., Bhatia S., Hare J., Somasundaram T., et al. The atomic structure of adeno-associated virus (AAV-2), a vector for human gene therapy. Proc. Natl. Acad. Sci. USA 2002, 99:10405-10410.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 10405-10410
    • Xie, Q.1    Bu, W.2    Bhatia, S.3    Hare, J.4    Somasundaram, T.5
  • 71
    • 84884249850 scopus 로고    scopus 로고
    • Characterization of interactions between heparin/glycosaminoglycan and adeno-associated virus
    • Zhang F., Aguilera J., Beaudet J.M., Xie Q., Lerch T.F., et al. Characterization of interactions between heparin/glycosaminoglycan and adeno-associated virus. Biochemistry 2013, 52:6275-6285.
    • (2013) Biochemistry , vol.52 , pp. 6275-6285
    • Zhang, F.1    Aguilera, J.2    Beaudet, J.M.3    Xie, Q.4    Lerch, T.F.5


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