메뉴 건너뛰기




Volumn 15, Issue 5, 2016, Pages 959-967

Erratum: A Molecular-Level Account of the Antigenic Hantaviral Surface (Cell Reports (2016) 15(5) (959–967)(S2211124716303849)(10.1016/j.celrep.2016.03.082));A Molecular-Level Account of the Antigenic Hantaviral Surface

Author keywords

[No Author keywords available]

Indexed keywords

GC GLYCOPROTEIN; GN GLYCOPROTEIN; TETRAMER; UNCLASSIFIED DRUG; VIRUS GLYCOPROTEIN; EPITOPE; GLYCOPROTEIN; POLYSACCHARIDE; VIRAL PROTEIN; VIRUS ANTIBODY; VIRUS ANTIGEN;

EID: 84963986274     PISSN: None     EISSN: 22111247     Source Type: Journal    
DOI: 10.1016/j.celrep.2016.06.039     Document Type: Erratum
Times cited : (51)

References (62)
  • 1
    • 84946865951 scopus 로고    scopus 로고
    • Acidification triggers Andes hantavirus membrane fusion and rearrangement of Gc into a stable post-fusion homotrimer
    • Acuña R., Bignon E.A., Mancini R., Lozach P.Y., Tischler N.D. Acidification triggers Andes hantavirus membrane fusion and rearrangement of Gc into a stable post-fusion homotrimer. J. Gen. Virol. 2015, 96:3192-3197.
    • (2015) J. Gen. Virol. , vol.96 , pp. 3192-3197
    • Acuña, R.1    Bignon, E.A.2    Mancini, R.3    Lozach, P.Y.4    Tischler, N.D.5
  • 2
    • 33745912405 scopus 로고    scopus 로고
    • A time- and cost-efficient system for high-level protein production in mammalian cells
    • Aricescu A.R., Lu W., Jones E.Y. A time- and cost-efficient system for high-level protein production in mammalian cells. Acta Crystallogr. D Biol. Crystallogr. 2006, 62:1243-1250.
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 1243-1250
    • Aricescu, A.R.1    Lu, W.2    Jones, E.Y.3
  • 3
    • 0024564146 scopus 로고
    • Characterization of Hantaan virus envelope glycoprotein antigenic determinants defined by monoclonal antibodies
    • Arikawa J., Schmaljohn A.L., Dalrymple J.M., Schmaljohn C.S. Characterization of Hantaan virus envelope glycoprotein antigenic determinants defined by monoclonal antibodies. J. Gen. Virol. 1989, 70:615-624.
    • (1989) J. Gen. Virol. , vol.70 , pp. 615-624
    • Arikawa, J.1    Schmaljohn, A.L.2    Dalrymple, J.M.3    Schmaljohn, C.S.4
  • 4
    • 77954257799 scopus 로고    scopus 로고
    • ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids
    • Ashkenazy H., Erez E., Martz E., Pupko T., Ben-Tal N. ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids. Nucleic Acids Res. 2010, 38:W529-W533.
    • (2010) Nucleic Acids Res. , vol.38 , pp. W529-W533
    • Ashkenazy, H.1    Erez, E.2    Martz, E.3    Pupko, T.4    Ben-Tal, N.5
  • 5
    • 84862803501 scopus 로고    scopus 로고
    • Direct electron detection yields cryo-EM reconstructions at resolutions beyond 3/4 Nyquist frequency
    • Bammes B.E., Rochat R.H., Jakana J., Chen D.H., Chiu W. Direct electron detection yields cryo-EM reconstructions at resolutions beyond 3/4 Nyquist frequency. J. Struct. Biol. 2012, 177:589-601.
    • (2012) J. Struct. Biol. , vol.177 , pp. 589-601
    • Bammes, B.E.1    Rochat, R.H.2    Jakana, J.3    Chen, D.H.4    Chiu, W.5
  • 8
    • 77952691868 scopus 로고    scopus 로고
    • Dimeric architecture of the Hendra virus attachment glycoprotein: evidence for a conserved mode of assembly
    • Bowden T.A., Crispin M., Harvey D.J., Jones E.Y., Stuart D.I. Dimeric architecture of the Hendra virus attachment glycoprotein: evidence for a conserved mode of assembly. J. Virol. 2010, 84:6208-6217.
    • (2010) J. Virol. , vol.84 , pp. 6208-6217
    • Bowden, T.A.1    Crispin, M.2    Harvey, D.J.3    Jones, E.Y.4    Stuart, D.I.5
  • 10
    • 77953082677 scopus 로고    scopus 로고
    • Recognition of decay accelerating factor and alpha(v)beta(3) by inactivated hantaviruses: Toward the development of high-throughput screening flow cytometry assays
    • Buranda T., Wu Y., Perez D., Jett S.D., BonduHawkins V., Ye C., Edwards B., Hall P., Larson R.S., Lopez G.P., et al. Recognition of decay accelerating factor and alpha(v)beta(3) by inactivated hantaviruses: Toward the development of high-throughput screening flow cytometry assays. Anal. Biochem. 2010, 402:151-160.
    • (2010) Anal. Biochem. , vol.402 , pp. 151-160
    • Buranda, T.1    Wu, Y.2    Perez, D.3    Jett, S.D.4    BonduHawkins, V.5    Ye, C.6    Edwards, B.7    Hall, P.8    Larson, R.S.9    Lopez, G.P.10
  • 11
    • 84860574289 scopus 로고    scopus 로고
    • Dynamo: a flexible, user-friendly development tool for subtomogram averaging of cryo-EM data in high-performance computing environments
    • Castaño-Díez D., Kudryashev M., Arheit M., Stahlberg H. Dynamo: a flexible, user-friendly development tool for subtomogram averaging of cryo-EM data in high-performance computing environments. J. Struct. Biol. 2012, 178:139-151.
    • (2012) J. Struct. Biol. , vol.178 , pp. 139-151
    • Castaño-Díez, D.1    Kudryashev, M.2    Arheit, M.3    Stahlberg, H.4
  • 12
    • 54549083102 scopus 로고    scopus 로고
    • A hantavirus causing hemorrhagic fever with renal syndrome requires gC1qR/p32 for efficient cell binding and infection
    • Choi Y., Kwon Y.C., Kim S.I., Park J.M., Lee K.H., Ahn B.Y. A hantavirus causing hemorrhagic fever with renal syndrome requires gC1qR/p32 for efficient cell binding and infection. Virology 2008, 381:178-183.
    • (2008) Virology , vol.381 , pp. 178-183
    • Choi, Y.1    Kwon, Y.C.2    Kim, S.I.3    Park, J.M.4    Lee, K.H.5    Ahn, B.Y.6
  • 13
    • 0022706389 scopus 로고
    • The relation between the divergence of sequence and structure in proteins
    • Chothia C., Lesk A.M. The relation between the divergence of sequence and structure in proteins. EMBO J. 1986, 5:823-826.
    • (1986) EMBO J. , vol.5 , pp. 823-826
    • Chothia, C.1    Lesk, A.M.2
  • 15
    • 84873205968 scopus 로고    scopus 로고
    • Crystal structure of glycoprotein C from Rift Valley fever virus
    • Dessau M., Modis Y. Crystal structure of glycoprotein C from Rift Valley fever virus. Proc. Natl. Acad. Sci. USA 2013, 110:1696-1701.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 1696-1701
    • Dessau, M.1    Modis, Y.2
  • 16
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • Edgar R.C. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 2004, 32:1792-1797.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 17
    • 67649825692 scopus 로고    scopus 로고
    • The Hantavirus Glycoprotein G1 Tail Contains Dual CCHC-type Classical Zinc Fingers
    • Estrada D.F., Boudreaux D.M., Zhong D., St Jeor S.C., De Guzman R.N. The Hantavirus Glycoprotein G1 Tail Contains Dual CCHC-type Classical Zinc Fingers. J. Biol. Chem. 2009, 284:8654-8660.
    • (2009) J. Biol. Chem. , vol.284 , pp. 8654-8660
    • Estrada, D.F.1    Boudreaux, D.M.2    Zhong, D.3    St Jeor, S.C.4    De Guzman, R.N.5
  • 18
    • 84864067332 scopus 로고    scopus 로고
    • The structure of the hantavirus zinc finger domain is conserved and represents the only natively folded region of the Gn cytoplasmic tail
    • Estrada D.F., Conner M., Jeor S.C., Guzman R.N. The structure of the hantavirus zinc finger domain is conserved and represents the only natively folded region of the Gn cytoplasmic tail. Front. Microbiol. 2011, 2:251.
    • (2011) Front. Microbiol. , vol.2 , pp. 251
    • Estrada, D.F.1    Conner, M.2    Jeor, S.C.3    Guzman, R.N.4
  • 20
    • 0033619114 scopus 로고    scopus 로고
    • Phage-displayed peptides mimicking the discontinuous neutralization sites of puumala Hantavirus envelope glycoproteins
    • Heiskanen T., Lundkvist A., Soliymani R., Koivunen E., Vaheri A., Lankinen H. Phage-displayed peptides mimicking the discontinuous neutralization sites of puumala Hantavirus envelope glycoproteins. Virology 1999, 262:321-332.
    • (1999) Virology , vol.262 , pp. 321-332
    • Heiskanen, T.1    Lundkvist, A.2    Soliymani, R.3    Koivunen, E.4    Vaheri, A.5    Lankinen, H.6
  • 21
    • 0043268749 scopus 로고    scopus 로고
    • Improvement of binding of Puumala virus neutralization site resembling peptide with a second-generation phage library
    • Heiskanen T., Li X.D., Hepojoki J., Gustafsson E., Lundkvist A., Vaheri A., Lankinen H. Improvement of binding of Puumala virus neutralization site resembling peptide with a second-generation phage library. Protein Eng. 2003, 16:443-450.
    • (2003) Protein Eng. , vol.16 , pp. 443-450
    • Heiskanen, T.1    Li, X.D.2    Hepojoki, J.3    Gustafsson, E.4    Lundkvist, A.5    Vaheri, A.6    Lankinen, H.7
  • 22
    • 72849128417 scopus 로고    scopus 로고
    • Interactions and oligomerization of hantavirus glycoproteins
    • Hepojoki J., Strandin T., Vaheri A., Lankinen H. Interactions and oligomerization of hantavirus glycoproteins. J. Virol. 2010, 84:227-242.
    • (2010) J. Virol. , vol.84 , pp. 227-242
    • Hepojoki, J.1    Strandin, T.2    Vaheri, A.3    Lankinen, H.4
  • 23
    • 0031127099 scopus 로고    scopus 로고
    • Single amino acid substitutions in Puumala virus envelope glycoproteins G1 and G2 eliminate important neutralization epitopes
    • Hörling J., Lundkvist A. Single amino acid substitutions in Puumala virus envelope glycoproteins G1 and G2 eliminate important neutralization epitopes. Virus Res. 1997, 48:89-100.
    • (1997) Virus Res. , vol.48 , pp. 89-100
    • Hörling, J.1    Lundkvist, A.2
  • 25
    • 84908326020 scopus 로고    scopus 로고
    • Averaging of viral envelope glycoprotein spikes from electron cryotomography reconstructions using Jsubtomo
    • Huiskonen J.T., Parsy M.L., Li S., Bitto D., Renner M., Bowden T.A. Averaging of viral envelope glycoprotein spikes from electron cryotomography reconstructions using Jsubtomo. J. Vis. Exp. 2014, 92:e51714.
    • (2014) J. Vis. Exp. , vol.92 , pp. e51714
    • Huiskonen, J.T.1    Parsy, M.L.2    Li, S.3    Bitto, D.4    Renner, M.5    Bowden, T.A.6
  • 26
    • 0028271715 scopus 로고
    • Characterization of human antibody responses to four corners hantavirus infections among patients with hantavirus pulmonary syndrome
    • Jenison S., Yamada T., Morris C., Anderson B., Torrez-Martinez N., Keller N., Hjelle B. Characterization of human antibody responses to four corners hantavirus infections among patients with hantavirus pulmonary syndrome. J. Virol. 1994, 68:3000-3006.
    • (1994) J. Virol. , vol.68 , pp. 3000-3006
    • Jenison, S.1    Yamada, T.2    Morris, C.3    Anderson, B.4    Torrez-Martinez, N.5    Keller, N.6    Hjelle, B.7
  • 28
    • 4444300614 scopus 로고    scopus 로고
    • Complete gene sequence of a human Puumala hantavirus isolate, Puumala Umeå/hu: sequence comparison and characterisation of encoded gene products
    • Johansson P., Olsson M., Lindgren L., Ahlm C., Elgh F., Holmström A., Bucht G. Complete gene sequence of a human Puumala hantavirus isolate, Puumala Umeå/hu: sequence comparison and characterisation of encoded gene products. Virus Res. 2004, 105:147-155.
    • (2004) Virus Res. , vol.105 , pp. 147-155
    • Johansson, P.1    Olsson, M.2    Lindgren, L.3    Ahlm, C.4    Elgh, F.5    Holmström, A.6    Bucht, G.7
  • 29
    • 77950651664 scopus 로고    scopus 로고
    • A global perspective on hantavirus ecology, epidemiology, and disease
    • Jonsson C.B., Figueiredo L.T., Vapalahti O. A global perspective on hantavirus ecology, epidemiology, and disease. Clin. Microbiol. Rev. 2010, 23:412-441.
    • (2010) Clin. Microbiol. Rev. , vol.23 , pp. 412-441
    • Jonsson, C.B.1    Figueiredo, L.T.2    Vapalahti, O.3
  • 31
    • 0037473316 scopus 로고    scopus 로고
    • Human recombinant neutralizing antibodies against hantaan virus G2 protein
    • Koch J., Liang M., Queitsch I., Kraus A.A., Bautz E.K. Human recombinant neutralizing antibodies against hantaan virus G2 protein. Virology 2003, 308:64-73.
    • (2003) Virology , vol.308 , pp. 64-73
    • Koch, J.1    Liang, M.2    Queitsch, I.3    Kraus, A.A.4    Bautz, E.K.5
  • 32
    • 17744396121 scopus 로고    scopus 로고
    • Not so different after all: a comparison of methods for detecting amino acid sites under selection
    • Kosakovsky Pond S.L., Frost S.D. Not so different after all: a comparison of methods for detecting amino acid sites under selection. Mol. Biol. Evol. 2005, 22:1208-1222.
    • (2005) Mol. Biol. Evol. , vol.22 , pp. 1208-1222
    • Kosakovsky Pond, S.L.1    Frost, S.D.2
  • 33
    • 0029879295 scopus 로고    scopus 로고
    • Computer visualization of three-dimensional image data using IMOD
    • Kremer J.R., Mastronarde D.N., McIntosh J.R. Computer visualization of three-dimensional image data using IMOD. J. Struct. Biol. 1996, 116:71-76.
    • (1996) J. Struct. Biol. , vol.116 , pp. 71-76
    • Kremer, J.R.1    Mastronarde, D.N.2    McIntosh, J.R.3
  • 34
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes
    • Krogh A., Larsson B., von Heijne G., Sonnhammer E.L. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 2001, 305:567-580.
    • (2001) J. Mol. Biol. , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    von Heijne, G.3    Sonnhammer, E.L.4
  • 35
    • 45849154166 scopus 로고    scopus 로고
    • An improved general amino acid replacement matrix
    • Le S.Q., Gascuel O. An improved general amino acid replacement matrix. Mol. Biol. Evol. 2008, 25:1307-1320.
    • (2008) Mol. Biol. Evol. , vol.25 , pp. 1307-1320
    • Le, S.Q.1    Gascuel, O.2
  • 36
    • 0037280525 scopus 로고    scopus 로고
    • Hantaviruses. a short review
    • Lednicky J.A. Hantaviruses. a short review. Arch. Pathol. Lab. Med. 2003, 127:30-35.
    • (2003) Arch. Pathol. Lab. Med. , vol.127 , pp. 30-35
    • Lednicky, J.A.1
  • 37
    • 0020402444 scopus 로고
    • Laboratory-acquired infections with Hantaan virus, the etiologic agent of Korean hemorrhagic fever
    • Lee H.W., Johnson K.M. Laboratory-acquired infections with Hantaan virus, the etiologic agent of Korean hemorrhagic fever. J. Infect. Dis. 1982, 146:645-651.
    • (1982) J. Infect. Dis. , vol.146 , pp. 645-651
    • Lee, H.W.1    Johnson, K.M.2
  • 38
    • 78649891889 scopus 로고    scopus 로고
    • Structural changes of envelope proteins during alphavirus fusion
    • Li L., Jose J., Xiang Y., Kuhn R.J., Rossmann M.G. Structural changes of envelope proteins during alphavirus fusion. Nature 2010, 468:705-708.
    • (2010) Nature , vol.468 , pp. 705-708
    • Li, L.1    Jose, J.2    Xiang, Y.3    Kuhn, R.J.4    Rossmann, M.G.5
  • 39
    • 84880848354 scopus 로고    scopus 로고
    • Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM
    • Li X., Mooney P., Zheng S., Booth C.R., Braunfeld M.B., Gubbens S., Agard D.A., Cheng Y. Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM. Nat. Methods 2013, 10:584-590.
    • (2013) Nat. Methods , vol.10 , pp. 584-590
    • Li, X.1    Mooney, P.2    Zheng, S.3    Booth, C.R.4    Braunfeld, M.B.5    Gubbens, S.6    Agard, D.A.7    Cheng, Y.8
  • 41
    • 0037211471 scopus 로고    scopus 로고
    • Generation of an HFRS patient-derived neutralizing recombinant antibody to Hantaan virus G1 protein and definition of the neutralizing domain
    • Liang M., Mahler M., Koch J., Ji Y., Li D., Schmaljohn C., Bautz E.K. Generation of an HFRS patient-derived neutralizing recombinant antibody to Hantaan virus G1 protein and definition of the neutralizing domain. J. Med. Virol. 2003, 69:99-107.
    • (2003) J. Med. Virol. , vol.69 , pp. 99-107
    • Liang, M.1    Mahler, M.2    Koch, J.3    Ji, Y.4    Li, D.5    Schmaljohn, C.6    Bautz, E.K.7
  • 42
    • 0035950598 scopus 로고    scopus 로고
    • The Hantaan virus glycoprotein precursor is cleaved at the conserved pentapeptide WAASA
    • Löber C., Anheier B., Lindow S., Klenk H.D., Feldmann H. The Hantaan virus glycoprotein precursor is cleaved at the conserved pentapeptide WAASA. Virology 2001, 289:224-229.
    • (2001) Virology , vol.289 , pp. 224-229
    • Löber, C.1    Anheier, B.2    Lindow, S.3    Klenk, H.D.4    Feldmann, H.5
  • 43
    • 0026481821 scopus 로고
    • Bank vole monoclonal antibodies against Puumala virus envelope glycoproteins: identification of epitopes involved in neutralization
    • Lundkvist A., Niklasson B. Bank vole monoclonal antibodies against Puumala virus envelope glycoproteins: identification of epitopes involved in neutralization. Arch. Virol. 1992, 126:93-105.
    • (1992) Arch. Virol. , vol.126 , pp. 93-105
    • Lundkvist, A.1    Niklasson, B.2
  • 44
    • 0027249313 scopus 로고
    • Neutralizing human monoclonal antibodies against Puumala virus, causative agent of nephropathia epidemica: a novel method using antigen-coated magnetic beads for specific B cell isolation
    • Lundkvist A., Hörling J., Athlin L., Rosén A., Niklasson B. Neutralizing human monoclonal antibodies against Puumala virus, causative agent of nephropathia epidemica: a novel method using antigen-coated magnetic beads for specific B cell isolation. J. Gen. Virol. 1993, 74:1303-1310.
    • (1993) J. Gen. Virol. , vol.74 , pp. 1303-1310
    • Lundkvist, A.1    Hörling, J.2    Athlin, L.3    Rosén, A.4    Niklasson, B.5
  • 45
    • 25644458666 scopus 로고    scopus 로고
    • Automated electron microscope tomography using robust prediction of specimen movements
    • Mastronarde D.N. Automated electron microscope tomography using robust prediction of specimen movements. J. Struct. Biol. 2005, 152:36-51.
    • (2005) J. Struct. Biol. , vol.152 , pp. 36-51
    • Mastronarde, D.N.1
  • 46
    • 4143051195 scopus 로고    scopus 로고
    • Comparison of site-specific rate-inference methods for protein sequences: empirical Bayesian methods are superior
    • Mayrose I., Graur D., Ben-Tal N., Pupko T. Comparison of site-specific rate-inference methods for protein sequences: empirical Bayesian methods are superior. Mol. Biol. Evol. 2004, 21:1781-1791.
    • (2004) Mol. Biol. Evol. , vol.21 , pp. 1781-1791
    • Mayrose, I.1    Graur, D.2    Ben-Tal, N.3    Pupko, T.4
  • 48
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: discriminating signal peptides from transmembrane regions
    • Petersen T.N., Brunak S., von Heijne G., Nielsen H. SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat. Methods 2011, 8:785-786.
    • (2011) Nat. Methods , vol.8 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 50
    • 77952581453 scopus 로고    scopus 로고
    • Quantitative analysis of cryo-EM density map segmentation by watershed and scale-space filtering, and fitting of structures by alignment to regions
    • Pintilie G.D., Zhang J., Goddard T.D., Chiu W., Gossard D.C. Quantitative analysis of cryo-EM density map segmentation by watershed and scale-space filtering, and fitting of structures by alignment to regions. J. Struct. Biol. 2010, 170:427-438.
    • (2010) J. Struct. Biol. , vol.170 , pp. 427-438
    • Pintilie, G.D.1    Zhang, J.2    Goddard, T.D.3    Chiu, W.4    Gossard, D.C.5
  • 51
    • 15844406550 scopus 로고    scopus 로고
    • HyPhy: hypothesis testing using phylogenies
    • Pond S.L., Frost S.D., Muse S.V. HyPhy: hypothesis testing using phylogenies. Bioinformatics 2005, 21:676-679.
    • (2005) Bioinformatics , vol.21 , pp. 676-679
    • Pond, S.L.1    Frost, S.D.2    Muse, S.V.3
  • 52
    • 12844253063 scopus 로고    scopus 로고
    • Pathogenic hantaviruses bind plexin-semaphorin-integrin domains present at the apex of inactive, bent alphavbeta3 integrin conformers
    • Raymond T., Gorbunova E., Gavrilovskaya I.N., Mackow E.R. Pathogenic hantaviruses bind plexin-semaphorin-integrin domains present at the apex of inactive, bent alphavbeta3 integrin conformers. Proc. Natl. Acad. Sci. USA 2005, 102:1163-1168.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 1163-1168
    • Raymond, T.1    Gorbunova, E.2    Gavrilovskaya, I.N.3    Mackow, E.R.4
  • 53
    • 59449110909 scopus 로고    scopus 로고
    • DOG 1.0: illustrator of protein domain structures
    • Ren J., Wen L., Gao X., Jin C., Xue Y., Yao X. DOG 1.0: illustrator of protein domain structures. Cell Res. 2009, 19:271-273.
    • (2009) Cell Res. , vol.19 , pp. 271-273
    • Ren, J.1    Wen, L.2    Gao, X.3    Jin, C.4    Xue, Y.5    Yao, X.6
  • 54
    • 0023092796 scopus 로고
    • Hantaan virus M RNA: coding strategy, nucleotide sequence, and gene order
    • Schmaljohn C.S., Schmaljohn A.L., Dalrymple J.M. Hantaan virus M RNA: coding strategy, nucleotide sequence, and gene order. Virology 1987, 157:31-39.
    • (1987) Virology , vol.157 , pp. 31-39
    • Schmaljohn, C.S.1    Schmaljohn, A.L.2    Dalrymple, J.M.3
  • 55
    • 0025286385 scopus 로고
    • Antigenic subunits of Hantaan virus expressed by baculovirus and vaccinia virus recombinants
    • Schmaljohn C.S., Chu Y.K., Schmaljohn A.L., Dalrymple J.M. Antigenic subunits of Hantaan virus expressed by baculovirus and vaccinia virus recombinants. J. Virol. 1990, 64:3162-3170.
    • (1990) J. Virol. , vol.64 , pp. 3162-3170
    • Schmaljohn, C.S.1    Chu, Y.K.2    Schmaljohn, A.L.3    Dalrymple, J.M.4
  • 56
    • 2342629333 scopus 로고    scopus 로고
    • Analysis of N-linked glycosylation of hantaan virus glycoproteins and the role of oligosaccharide side chains in protein folding and intracellular trafficking
    • Shi X., Elliott R.M. Analysis of N-linked glycosylation of hantaan virus glycoproteins and the role of oligosaccharide side chains in protein folding and intracellular trafficking. J. Virol. 2004, 78:5414-5422.
    • (2004) J. Virol. , vol.78 , pp. 5414-5422
    • Shi, X.1    Elliott, R.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.