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Volumn 2, Issue 1, 2011, Pages

Binding of herpes simplex virus glycoprotein D to nectin-1 exploits host cell adhesion

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; GLYCOPROTEIN D; HOMODIMER; NECTIN 1; CELL ADHESION MOLECULE; GLYCOPROTEIN D, HUMAN HERPESVIRUS 1; NECTINS; RECOMBINANT PROTEIN; VIRUS ENVELOPE PROTEIN; VIRUS RECEPTOR;

EID: 84455194239     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms1571     Document Type: Article
Times cited : (87)

References (59)
  • 1
    • 0004250834 scopus 로고    scopus 로고
    • (eds D. M. Knipe & P. M. Howley) Lippincott Williams & Wilkins
    • Roizman, B., Knipe, D. M. & Whitley, J. R. in Field's Virology (eds D. M. Knipe & P. M. Howley) 2503-2576 Lippincott Williams & Wilkins, 2007.
    • (2007) Field's Virology , pp. 2503-2576
    • Roizman, B.1    Knipe, D.M.2    Whitley, J.R.3
  • 2
    • 37349036293 scopus 로고    scopus 로고
    • Genital herpes
    • DOI 10.1016/S0140-6736(07)61908-4, PII S0140673607619084
    • Gupta, R., Warren, T. & Wald, A. Genital herpes. Lancet 370, 2127-2137 (2007). (Pubitemid 350296304)
    • (2007) Lancet , vol.370 , Issue.9605 , pp. 2127-2137
    • Gupta, R.1    Warren, T.2    Wald, A.3
  • 3
    • 0019235642 scopus 로고
    • Herpes simplex virus latency: The cellular location of virus in dorsal root ganglia and the fate of the infected cell following virus activation
    • McLennan, J. L. & Darby, G. Herpes simplex virus latency: the cellular location of virus in dorsal root ganglia and the fate of the infected cell following virus activation. J. Gen. Virol. 51, 233-243 (1980). (Pubitemid 13240025)
    • (1980) Journal of General Virology , vol.51 , Issue.2 , pp. 233-243
    • McLennan, J.L.1    Darby, G.2
  • 4
    • 44749091723 scopus 로고    scopus 로고
    • Entry of herpesviruses into mammalian cells
    • Heldwein, E. E. & Krummenacher, C. Entry of herpesviruses into mammalian cells. Cell. Mol. Life. Sci. 65, 1653-1668 (2008).
    • (2008) Cell. Mol. Life. Sci. , vol.65 , pp. 1653-1668
    • Heldwein, E.E.1    Krummenacher, C.2
  • 5
    • 79954617024 scopus 로고    scopus 로고
    • Fusing structure and function: A structural view of the herpesvirus entry machinery
    • Connolly, S. A., Jackson, J. O., Jardetzky, T. S. & Longnecker, R. Fusing structure and function: a structural view of the herpesvirus entry machinery. Nat. Rev. Microbiol. 9, 369-381 (2011).
    • (2011) Nat. Rev. Microbiol. , vol.9 , pp. 369-381
    • Connolly, S.A.1    Jackson, J.O.2    Jardetzky, T.S.3    Longnecker, R.4
  • 6
    • 1842850945 scopus 로고    scopus 로고
    • Herpes simplex virus: Receptors and ligands for cell entry
    • DOI 10.1111/j.1462-5822.2004.00389.x
    • Spear, P. G. Herpes simplex virus: receptors and ligands for cell entry. Cell Microbiol. 6, 401-410 (2004). (Pubitemid 38488933)
    • (2004) Cellular Microbiology , vol.6 , Issue.5 , pp. 401-410
    • Spear, P.G.1
  • 7
    • 0031746910 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycan binding by herpes simplex virus type 1 glycoproteins B and C, which differ in their contributions to virus attachment, penetration, and cell-to-cell spread
    • Laquerre, S. et al. Heparan sulfate proteoglycan binding by herpes simplex virus type 1 glycoproteins B and C, which differ in their contributions to virus attachment, penetration, and cell-to-cell spread. J. Virol. 72, 6119-6130 (1998). (Pubitemid 28283402)
    • (1998) Journal of Virology , vol.72 , Issue.7 , pp. 6119-6130
    • Laquerre, S.1    Argnani, R.2    Anderson, D.B.3    Zucchini, S.4    Manservigi, R.5    Glorioso, J.C.6
  • 8
    • 0026308922 scopus 로고
    • Involvement of glycoprotein C (gC) in adsorption of herpes simplex virus type 1 (HSV-1) to the cell
    • Svennerholm, B., Jeansson, S., Vahlne, A. & Lycke, E. Involvement of glycoprotein C (gC) in adsorption of herpes simplex virus type 1 (HSV-1) to the cell. A rch. Virol. 120, 273-279 (1991).
    • (1991) Arch. Virol , vol.120 , pp. 273-279
    • Svennerholm, B.1    Jeansson, S.2    Vahlne, A.3    Lycke, E.4
  • 9
    • 77957960097 scopus 로고    scopus 로고
    • Non-muscle myosin IIA is a functional entry receptor for herpes simplex virus-1
    • Arii, J. et al. Non-muscle myosin IIA is a functional entry receptor for herpes simplex virus-1. Nature 467, 859-862 (2010).
    • (2010) Nature , vol.467 , pp. 859-862
    • Arii, J.1
  • 10
    • 0031963977 scopus 로고    scopus 로고
    • Glycoproteins gB, gD, and gHgL of herpes simplex virus type 1 are necessary and sufficient to mediate membrane fusion in a Cos cell transfection system
    • Turner, A., Bruun, B., Minson, T. & Browne, H. Glycoproteins gB, gD, and gHgL of herpes simplex virus type 1 are necessary and sufficient to mediate membrane fusion in a Cos cell transfection system. J. Virol. 72, 873-875 (1998). (Pubitemid 28048916)
    • (1998) Journal of Virology , vol.72 , Issue.1 , pp. 873-875
    • Turner, A.1    Bruun, B.2    Minson, T.3    Browne, H.4
  • 11
    • 77954385082 scopus 로고    scopus 로고
    • Crystal structure of the conserved herpesvirus fusion regulator complex gh-gl
    • Chowdary, T. K. et al. Crystal structure of the conserved herpesvirus fusion regulator complex gH-gL. Nat. Struct. Mol. Biol. 17, 882-888 (2010).
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 882-888
    • Chowdary, T.K.1
  • 15
    • 0034665214 scopus 로고    scopus 로고
    • Three classes of cell surface receptors for alphaherpesvirus entry
    • Spear, P. G., Eisenberg, R. J. & Cohen, G. H. Th ree classes of cell surface receptors for alphaherpesvirus entry. Virology 275, 1-8 (2000).
    • (2000) Virology , vol.275 , pp. 1-8
    • Spear, P.G.1    Eisenberg, R.J.2    Cohen, G.H.3
  • 17
    • 47749149269 scopus 로고    scopus 로고
    • Nectins and nectin-like molecules: Roles in contact inhibition of cell movement and proliferation
    • DOI 10.1038/nrm2457, PII NRM2457
    • Takai, Y., Miyoshi, J., Ikeda, W. & Ogita, H. Nectins and nectin-like molecules: roles in contact inhibition of cell movement and proliferation. Nat. Rev. Mol. Cell Biol. 9, 603-615 (2008). (Pubitemid 352032927)
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , Issue.8 , pp. 603-615
    • Takai, Y.1    Miyoshi, J.2    Ikeda, W.3    Ogita, H.4
  • 18
    • 33745083716 scopus 로고    scopus 로고
    • Nectins and nectin-like molecules: Roles in cell adhesion, polarization, movement, and proliferation
    • DOI 10.1080/15216540600719622, PII H8823508212364
    • Ogita, H. & Takai, Y. Nectins and nectin-like molecules: roles in cell adhesion, polarization, movement, and proliferation. I UBMB Life 58, 334-343 (2006). (Pubitemid 43880026)
    • (2006) IUBMB Life , vol.58 , Issue.5-6 , pp. 334-343
    • Ogita, H.1    Takai, Y.2
  • 19
    • 0037232646 scopus 로고    scopus 로고
    • Nectin and afadin: Novel organizers of intracellular junctions
    • DOI 10.1242/jcs.00167
    • Takai, Y. & Nakanishi, H. Nectin and afadin: novel organizers of intercellular junctions. J. Cell Sci. 116, 17-27 (2003). (Pubitemid 36113961)
    • (2003) Journal of Cell Science , vol.116 , Issue.1 , pp. 17-27
    • Takai, Y.1    Nakanishi, H.2
  • 20
    • 55849135745 scopus 로고    scopus 로고
    • The immunoglobulin-like cell adhesion molecule nectin and its associated protein afadin
    • Takai, Y., Ikeda, W., Ogita, H. & Rikitake, Y. The immunoglobulin-like cell adhesion molecule nectin and its associated protein afadin. Annu. Rev. Cell Dev. Biol. 24, 309-342 (2008).
    • (2008) Annu. Rev. Cell Dev. Biol. , vol.24 , pp. 309-342
    • Takai, Y.1    Ikeda, W.2    Ogita, H.3    Rikitake, Y.4
  • 21
    • 79953332147 scopus 로고    scopus 로고
    • Crystal structure of the cis-dimer of nectin-1: Implications for the architecture of cell-cell junctions
    • Narita, H. et al. Crystal structure of the cis-dimer of Nectin-1: implications for the architecture of cell-cell junctions. J. Biol. Chem. 286, 12659-12669 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 12659-12669
    • Narita, H.1
  • 23
    • 0036173066 scopus 로고    scopus 로고
    • Effects of herpes simplex virus on structure and function of nectin-1/HveC
    • DOI 10.1128/jvi.76.5.2424-2433.2002
    • Krummenacher, C., Baribaud, I., Sanzo, J. F., Cohen, G. H. & Eisenberg, R. J. Effects of herpes simplex virus on structure and function of nectin-1/HveC. J. Virol. 76, 2424-2433 (2002). (Pubitemid 34150710)
    • (2002) Journal of Virology , vol.76 , Issue.5 , pp. 2424-2433
    • Krummenacher, C.1    Baribaud, I.2    Sanzo, J.F.3    Cohen, G.H.4    Eisenberg, R.J.5
  • 26
    • 33645778936 scopus 로고    scopus 로고
    • Soluble v domain of nectin-1/hvec enables entry of herpes simplex virus type 1 (HSV-1) into hsv-resistant cells by binding to viral glycoprotein d
    • Kwon, H. et al. Soluble v domain of nectin-1/HveC enables entry of herpes simplex virus type 1 (HSV-1) into HSV-resistant cells by binding to viral glycoprotein D. J. Virol. 80, 138-148 (2006).
    • (2006) J. Virol. , vol.80 , pp. 138-148
    • Kwon, H.1
  • 27
    • 0036631777 scopus 로고    scopus 로고
    • Amino acid substitutions in the v domain of nectin-1 (HveC) that impair entry activity for herpes simplex virus types 1 and 2 but not for pseudorabies virus or bovine herpesvirus 1
    • Martinez, W. M. & Spear, P. G. Amino acid substitutions in the V domain of nectin-1 (HveC) that impair entry activity for herpes simplex virus types 1 and 2 but not for Pseudorabies virus or bovine herpesvirus 1. J. Virol. 76, 7255-7262 (2002).
    • (2002) J. Virol. , vol.76 , pp. 7255-7262
    • Martinez, W.M.1    Spear, P.G.2
  • 28
    • 0041701432 scopus 로고    scopus 로고
    • Cellular localization of nectin-1 and glycoprotein D during herpes simplex virus infection
    • DOI 10.1128/JVI.77.16.8985-8999.2003
    • Krummenacher, C., Baribaud, I., Eisenberg, R. J. & Cohen, G. H. Cellular localization of nectin-1 and glycoprotein D during herpes simplex virus infection. J. Virol. 77, 8985-8999 (2003). (Pubitemid 36939158)
    • (2003) Journal of Virology , vol.77 , Issue.16 , pp. 8985-8999
    • Krummenacher, C.1    Baribaud, I.2    Eisenberg, R.J.3    Cohen, G.H.4
  • 29
    • 0043210408 scopus 로고    scopus 로고
    • Function of herpes simplex virus type 1 gD mutants with different receptor-binding affinities in virus entry and fusion
    • DOI 10.1128/JVI.77.16.8962-8972.2003
    • Milne, R. S. et al. Function of herpes simplex virus type 1 gD mutants with different receptor-binding affinities in virus entry and fusion. J. Virol. 77, 8962-8972 (2003). (Pubitemid 36936106)
    • (2003) Journal of Virology , vol.77 , Issue.16 , pp. 8962-8972
    • Milne, R.S.B.1    Hanna, S.L.2    Rux, A.H.3    Willis, S.H.4    Cohen, G.H.5    Eisenberg, R.J.6
  • 30
    • 29144441087 scopus 로고    scopus 로고
    • Different receptors binding to distinct interfaces on herpes simplex virus gD can trigger events leading to cell fusion and viral entry
    • DOI 10.1016/j.virol.2005.09.016, PII S0042682205005842
    • Spear, P. G. et al. Different receptors binding to distinct interfaces on herpes simplex virus gD can trigger events leading to cell fusion and viral entry. Virology 344, 17-24 (2006). (Pubitemid 41814445)
    • (2006) Virology , vol.344 , Issue.1 , pp. 17-24
    • Spear, P.G.1    Manoj, S.2    Yoon, M.3    Jogger, C.R.4    Zago, A.5    Myscofski, D.6
  • 31
    • 0034109367 scopus 로고    scopus 로고
    • Cell-to-cell spread of wild-type herpes simplex virus type 1, but not of syncytial strains, is mediated by the immunoglobulin-like receptors that mediate virion entry, Nectin1 (PRR1/HveC/HIgR) and Nectin2 (PRR2/HveB)
    • DOI 10.1128/JVI.74.8.3909-3917.2000
    • Cocchi, F., Menotti, L., Dubreuil, P., Lopez, M. & Campadelli-Fiume, G. Cellto-cell spread of wild-type herpes simplex virus type 1, but not of syncytial strains, is mediated by the immunoglobulin-like receptors that mediate virion entry, nectin1 (PRR1/HveC/HIgR) and nectin2 (PRR2/HveB). J. Virol. 74, 3909-3917 (2000). (Pubitemid 30180336)
    • (2000) Journal of Virology , vol.74 , Issue.8 , pp. 3909-3917
    • Cocchi, F.1    Menotti, L.2    Dubreuil, P.3    Lopez, M.4    Campadelli-Fiume, G.5
  • 32
    • 0036632634 scopus 로고    scopus 로고
    • Disruption of adherens junctions liberates nectin-1 to serve as receptor for herpes simplex virus and pseudorabies virus entry
    • Yoon, M. & Spear, P. G. Disruption of adherens junctions liberates nectin-1 to serve as receptor for herpes simplex virus and pseudorabies virus entry. J. Virol. 76, 7203-7208 (2002).
    • (2002) J. Virol. , vol.76 , pp. 7203-7208
    • Yoon, M.1    Spear, P.G.2
  • 34
    • 34547735905 scopus 로고    scopus 로고
    • Multiple receptor interactions trigger release of membrane and intracellular calcium stores critical for herpes simplex virus entry
    • DOI 10.1091/mbc.E07-01-0062
    • Cheshenko, N., Liu, W., Satlin, L. M. & Herold, B. C. Multiple receptor interactions trigger release of membrane and intracellular calcium stores critical for herpes simplex virus entry. Mol. Biol. Cell 18, 3119-3130 (2007). (Pubitemid 47235316)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.8 , pp. 3119-3130
    • Cheshenko, N.1    Liu, W.2    Satlin, L.M.3    Herold, B.C.4
  • 35
    • 33744511706 scopus 로고    scopus 로고
    • Crystal structure of the V domain of human nectin-like molecule-1/syncam3/ Tsll1/Igsf4b, a neural tissue-specific immunoglobulin-like cell-cell adhesion molecule
    • DOI 10.1074/jbc.M513459200
    • Dong, X. et al. Crystal structure of the V domain of human nectin-like molecule-1/Syncam3/Tsll1/Igsf4b, a neural tissue-specific immunoglobulin-like cell-cell adhesion molecule. J. Biol. Chem. 281, 10610-10617 (2006). (Pubitemid 43864603)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.15 , pp. 10610-10617
    • Dong, X.1    Xu, F.2    Gong, Y.3    Gao, J.4    Lin, P.5    Chen, T.6    Peng, Y.7    Qiang, B.8    Yuan, J.9    Peng, X.10    Rao, Z.11
  • 36
    • 79953146572 scopus 로고    scopus 로고
    • A dimeric structure of pd-l1: Functional units or evolutionary relics?
    • Chen, Y. et al. A dimeric structure of PD-L1: functional units or evolutionary relics? Protein Cell 1, 153-160 (2010).
    • (2010) Protein Cell , vol.1 , pp. 153-160
    • Chen, Y.1
  • 37
    • 0038758772 scopus 로고    scopus 로고
    • Structure-based mutagenesis of herpes simplex virus glycoprotein D defines three critical regions at the gD-HveA/HVEM binding interface
    • DOI 10.1128/JVI.77.14.8127-8140.2003
    • Connolly, S. A. et al. Structure-based mutagenesis of herpes simplex virus glycoprotein D defines three critical regions at the gD-HveA/HVEM binding interface. J. Virol. 77, 8127-8140 (2003). (Pubitemid 36792808)
    • (2003) Journal of Virology , vol.77 , Issue.14 , pp. 8127-8140
    • Connolly, S.A.1    Landsburg, D.J.2    Carfi, A.3    Wiley, D.C.4    Cohen, G.H.5    Eisenberg, R.J.6
  • 39
    • 10344264483 scopus 로고    scopus 로고
    • Random mutagenesis of the gene encoding a viral ligand for multiple cell entry receptors to obtain viral mutants altered for receptor usage
    • DOI 10.1073/pnas.0407892101
    • Yoon, M. & Spear, P. G. Random mutagenesis of the gene encoding a viral ligand for multiple cell entry receptors to obtain viral mutants altered for receptor usage. Proc. Natl Acad. Sci. USA 101, 17252-17257 (2004). (Pubitemid 39627806)
    • (2004) Proceedings of the National Academy of Sciences of the United States of America , vol.101 , Issue.49 , pp. 17252-17257
    • Yoon, M.1    Spear, P.G.2
  • 40
    • 0028212250 scopus 로고
    • Identification of functional regions of herpes simplex virus glycoprotein gD by using linker-insertion mutagenesis
    • Chiang, H. Y., Cohen, G. H. & Eisenberg, R. J. Identification of functional regions of herpes simplex virus glycoprotein gD by using linker-insertion mutagenesis. J. Virol. 68, 2529-2543 (1994). (Pubitemid 24091933)
    • (1994) Journal of Virology , vol.68 , Issue.4 , pp. 2529-2543
    • Chiang, H.-Y.1    Cohen, G.H.2    Eisenberg, R.J.3
  • 41
    • 34247191887 scopus 로고    scopus 로고
    • Separation of receptor-binding and profusogenic domains of glycoprotein D of herpes simplex virus 1 into distinct interacting proteins
    • DOI 10.1073/pnas.0611565104
    • Zhou, G. & Roizman, B. Separation of receptor-binding and profusogenic domains of glycoprotein D of herpes simplex virus 1 into distinct interacting proteins. Proc. Natl Acad. Sci. USA 104, 4142-4146 (2007). (Pubitemid 47181592)
    • (2007) Proceedings of the National Academy of Sciences of the United States of America , vol.104 , Issue.10 , pp. 4142-4146
    • Zhou, G.1    Roizman, B.2
  • 43
    • 0036892864 scopus 로고    scopus 로고
    • Mutations in the N-terminal domains of nectin-1 and nectin-2 reveal differences in requirements for entry of various alphaherpesviruses and for nectin-nectin interactions
    • DOI 10.1128/JVI.76.24.12940-12950.2002
    • Struyf, F., Martinez, W. M. & Spear, P. G. Mutations in the N-terminal domains of nectin-1 and nectin-2 reveal differences in requirements for entry of various alphaherpesviruses and for nectin-nectin interactions. J. Virol. 76, 12940-12950 (2002). (Pubitemid 35386978)
    • (2002) Journal of Virology , vol.76 , Issue.24 , pp. 12940-12950
    • Struyf, F.1    Martinez, W.M.2    Spear, P.G.3
  • 44
    • 0032486317 scopus 로고    scopus 로고
    • Entry of alphaherpesviruses mediated by poliovirus receptor-related protein 1 and poliovirus receptor
    • DOI 10.1126/science.280.5369.1618
    • Geraghty, R. J., Krummenacher, C., Cohen, G. H., Eisenberg, R. J. & Spear, P. G. Entry of alphaherpesviruses mediated by poliovirus receptor-related protein 1 and poliovirus receptor. Science 280, 1618-1620 (1998). (Pubitemid 28277708)
    • (1998) Science , vol.280 , Issue.5369 , pp. 1618-1620
    • Geraghty, R.J.1    Krummenacher, C.2    Cohen, G.H.3    Eisenberg, R.J.4    Spear, P.G.5
  • 45
    • 33646452443 scopus 로고    scopus 로고
    • Expression of entry receptor nectin-1 of Herpes simplex virus 1 and/or Herpes simplex virus 2 in normal and neoplastic human nervous system tissues
    • Guzman, G., Oh, S., Shukla, D., Engelhard, H. H. & Valyi-Nagy, T. Expression of entry receptor nectin-1 of herpes simplex virus 1 and/or herpes simplex virus 2 in normal and neoplastic human nervous system tissues. Acta. Virol. 50, 59-66 (2006). (Pubitemid 47434340)
    • (2006) Acta Virologica , vol.50 , Issue.1 , pp. 59-66
    • Guzman, G.1    Oh, S.2    Shukla, D.3    Engelhard, H.H.4    Valyi-Nagy, T.5
  • 46
    • 0030298375 scopus 로고    scopus 로고
    • Herpes simplex virus-1 entry into cells mediated by a novel member of the TNF/NGF receptor family
    • DOI 10.1016/S0092-8674(00)81363-X
    • Montgomery, R. I., Warner, M. S., Lum, B. J. & Spear, P. G. Herpes simplex virus-1 entry into cells mediated by a novel member of the TNF/NGF receptor family. Cell 87, 427-436 (1996). (Pubitemid 26374317)
    • (1996) Cell , vol.87 , Issue.3 , pp. 427-436
    • Montgomery, R.I.1    Warner, M.S.2    Lum, B.J.3    Spear, P.G.4
  • 47
    • 26444445063 scopus 로고    scopus 로고
    • A role for herpesvirus entry mediator as the receptor for herpes simplex virus 1 entry into primary human trabecular meshwork cells
    • DOI 10.1128/JVI.79.20.13173-13179.2005
    • Tiwari, V. et al. A role for herpesvirus entry mediator as the receptor for herpes simplex virus 1 entry into primary human trabecular meshwork cells. J. Virol. 79, 13173-13179 (2005). (Pubitemid 41433235)
    • (2005) Journal of Virology , vol.79 , Issue.20 , pp. 13173-13179
    • Tiwari, V.1    Clement, C.2    Scanlan, P.M.3    Kowlessur, D.4    Yue, B.Y.J.T.5    Shukla, D.6
  • 48
    • 0037069501 scopus 로고    scopus 로고
    • Engineered herpes simplex virus 1 is dependent on IL13Rα2 receptor for cell entry and independent of glycoprotein d receptor interaction
    • DOI 10.1073/pnas.232588699
    • Zhou, G., Ye, G. J., Debinski, W. & Roizman, B. Engineered herpes simplex virus 1 is dependent on IL13Ralpha 2 receptor for cell entry and independent of glycoprotein D receptor interaction. Proc. Natl Acad. Sci. USA 99, 15124-15129 (2002). (Pubitemid 35334620)
    • (2002) Proceedings of the National Academy of Sciences of the United States of America , vol.99 , Issue.23 , pp. 15124-15129
    • Zhou, G.1    Ye, G.-J.2    Debinski, W.3    Roizman, B.4
  • 49
    • 53749099520 scopus 로고    scopus 로고
    • Construction of a fully retargeted herpes simplex virus 1 recombinant capable of entering cells solely via human epidermal growth factor receptor 2
    • Menotti, L., Cerretani, A., Hengel, H. & Campadelli-Fiume, G. Construction of a fully retargeted herpes simplex virus 1 recombinant capable of entering cells solely via human epidermal growth factor receptor 2. J. Virol. 82, 10153-10161 (2008).
    • (2008) J. Virol. , vol.82 , pp. 10153-10161
    • Menotti, L.1    Cerretani, A.2    Hengel, H.3    Campadelli-Fiume, G.4
  • 50
    • 77957816428 scopus 로고    scopus 로고
    • Crystal structure of the swine-origin A (H1N1)-2009 influenza A virus hemagglutinin (HA) reveals similar antigenicity to that of the 1918 pandemic virus. P rotein
    • Zhang, W. et al. Crystal structure of the swine-origin A (H1N1)-2009 influenza A virus hemagglutinin (HA) reveals similar antigenicity to that of the 1918 pandemic virus. P rotein Cell 1, 459-467 (2010).
    • (2010) Cell , vol.1 , pp. 459-467
    • Zhang, W.1
  • 51
    • 79961185765 scopus 로고    scopus 로고
    • Influenza a virus N5 neuraminidase has an extended 150-cavity
    • Wang, M. et al. Influenza a virus n5 neuraminidase has an extended 150-cavity. J. Virol. 85, 8431-8435 (2011).
    • (2011) J. Virol. , vol.85 , pp. 8431-8435
    • Wang, M.1
  • 52
    • 77957767268 scopus 로고    scopus 로고
    • The 2009 pandemic h1n1 neuraminidase N1 lacks the 150-cavity in its active site
    • Li, Q. et al. The 2009 pandemic H1N1 neuraminidase N1 lacks the 150-cavity in its active site. Nat. Struct. Mol. Biol. 17, 1266-1268 (2010).
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 1266-1268
    • Li, Q.1
  • 53
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997). (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 54
    • 0035788107 scopus 로고    scopus 로고
    • Pushing the boundaries of molecular replacement with maximum likelihood
    • DOI 10.1107/S0907444901012471
    • Read, R. J. Pushing the boundaries of molecular replacement with maximum likelihood. Acta Crystallogr. D Biol. Crystallogr. 57, 1373-1382 (2001). (Pubitemid 36117185)
    • (2001) Acta Crystallographica Section D: Biological Crystallography , vol.57 , Issue.10 , pp. 1373-1382
    • Read, R.J.1
  • 55
    • 0028103275 scopus 로고
    • Collaborative Computational Project, Number 4. The ccp4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 58
    • 76449098262 scopus 로고    scopus 로고
    • Phenix: A comprehensive python-based system for macromolecular structure solution
    • Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213-221 (2010).
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 59
    • 0000243829 scopus 로고
    • Procheck - A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., Macarthur, M. W., Moss, D. S. & Th ornton, J. M. Procheck-a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291 (1993).
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4


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