메뉴 건너뛰기




Volumn 161, Issue 7, 2016, Pages 1751-1760

Glycosylation of dengue virus glycoproteins and their interactions with carbohydrate receptors: possible targets for antiviral therapy

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN BINDING; VIRAL PROTEIN; VIRUS RECEPTOR;

EID: 84962909517     PISSN: 03048608     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00705-016-2855-2     Document Type: Review
Times cited : (26)

References (113)
  • 1
    • 0036468861 scopus 로고    scopus 로고
    • Epidemic dengue/dengue hemorrhagic fever as a public health, social and economic problem in the 21st century
    • COI: 1:CAS:528:DC%2BD38XhvF2ltLc%3D, PID: 11827812
    • Gubler DJ (2002) Epidemic dengue/dengue hemorrhagic fever as a public health, social and economic problem in the 21st century. Trends Microbiol 10:100–103
    • (2002) Trends Microbiol , vol.10 , pp. 100-103
    • Gubler, D.J.1
  • 3
    • 0642287817 scopus 로고    scopus 로고
    • Neutralization and antibody-dependent enhancement of dengue viruses
    • COI: 1:CAS:528:DC%2BD2cXptFCqug%3D%3D, PID: 14689700
    • Halstead SB (2003) Neutralization and antibody-dependent enhancement of dengue viruses. Adv Virus Res 60:421–467
    • (2003) Adv Virus Res , vol.60 , pp. 421-467
    • Halstead, S.B.1
  • 7
    • 73249132734 scopus 로고    scopus 로고
    • The medicinal chemistry of dengue fever
    • COI: 1:CAS:528:DC%2BD1MXhtFWqu7zK, PID: 19739651
    • Stevens AJ, Gahan ME, Mahalingam S, Keller PA (2009) The medicinal chemistry of dengue fever. J Med Chem 52:7911–7926
    • (2009) J Med Chem , vol.52 , pp. 7911-7926
    • Stevens, A.J.1    Gahan, M.E.2    Mahalingam, S.3    Keller, P.A.4
  • 8
    • 0000163169 scopus 로고    scopus 로고
    • Flaviviridae: the viruses and their replication
    • Knipe DM, Howley PM, Griffin DE, Lamb RA, Martin MA, Roizman B, Straus SE, (eds), Lippincott Williams & Wilkins, Philadelphia
    • Lindenbach BD, Rich CM (2001) Flaviviridae: the viruses and their replication. In: Knipe DM, Howley PM, Griffin DE, Lamb RA, Martin MA, Roizman B, Straus SE (eds) Fields virology, 4th edn. Lippincott Williams & Wilkins, Philadelphia, pp 991–1041
    • (2001) Fields virology , pp. 991-1041
    • Lindenbach, B.D.1    Rich, C.M.2
  • 9
    • 5144228164 scopus 로고    scopus 로고
    • Enhancement of dengue virus translation: role of the 3′ untranslated region and the terminal 3′ stem-loop domain
    • COI: 1:CAS:528:DC%2BD2cXotlSkt7o%3D, PID: 15476880
    • Holden KL, Harris E (2004) Enhancement of dengue virus translation: role of the 3′ untranslated region and the terminal 3′ stem-loop domain. Virology 329:119–133
    • (2004) Virology , vol.329 , pp. 119-133
    • Holden, K.L.1    Harris, E.2
  • 10
    • 20744431725 scopus 로고    scopus 로고
    • Control of translation by the 5′- and 3′-terminal regions of the dengue virus genome
    • COI: 1:CAS:528:DC%2BD2MXlslGjurs%3D, PID: 15956576
    • Chiu WW, Kinney RM, Dreher TW (2005) Control of translation by the 5′- and 3′-terminal regions of the dengue virus genome. J Virol 79:8303–8315
    • (2005) J Virol , vol.79 , pp. 8303-8315
    • Chiu, W.W.1    Kinney, R.M.2    Dreher, T.W.3
  • 11
    • 1542723492 scopus 로고    scopus 로고
    • Solution structure of dengue virus capsid protein reveals another fold
    • COI: 1:CAS:528:DC%2BD2cXisFWmsL8%3D, PID: 14993605
    • Ma L, Jones CT, Groesch TD, Kuhn RJ, Post CB (2004) Solution structure of dengue virus capsid protein reveals another fold. Proc Natl Acad Sci USA 101:3414–3419
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 3414-3419
    • Ma, L.1    Jones, C.T.2    Groesch, T.D.3    Kuhn, R.J.4    Post, C.B.5
  • 14
    • 0028849770 scopus 로고
    • Evidence that flavivirus NS1-NS2A cleavage is mediated by a membrane-bound host protease in the endoplasmic reticulum
    • COI: 1:CAS:528:DyaK2MXoslWrs7s%3D, PID: 7474145
    • Falgout B, Markoff L (1995) Evidence that flavivirus NS1-NS2A cleavage is mediated by a membrane-bound host protease in the endoplasmic reticulum. J Virol 69:7232–7243
    • (1995) J Virol , vol.69 , pp. 7232-7243
    • Falgout, B.1    Markoff, L.2
  • 15
    • 0030218225 scopus 로고    scopus 로고
    • Mutagenesis of the N-linked glycosylation sites of the yellow fever virus NS1 protein: effects on virus replication and mouse neurovirulence
    • COI: 1:CAS:528:DyaK28XkvVCgsrY%3D, PID: 8806496
    • Muylaert IR, Chambers TJ, Galler R, Rice CM (1996) Mutagenesis of the N-linked glycosylation sites of the yellow fever virus NS1 protein: effects on virus replication and mouse neurovirulence. Virology 222:159–168
    • (1996) Virology , vol.222 , pp. 159-168
    • Muylaert, I.R.1    Chambers, T.J.2    Galler, R.3    Rice, C.M.4
  • 17
    • 84875777404 scopus 로고    scopus 로고
    • Membrane topology and function of dengue virus NS2A protein
    • COI: 1:CAS:528:DC%2BC3sXotVyqtLo%3D, PID: 23408612
    • Xie X, Gayen S, Kang C, Shi PY (2013) Membrane topology and function of dengue virus NS2A protein. J Virol 87:4609–4622
    • (2013) J Virol , vol.87 , pp. 4609-4622
    • Xie, X.1    Gayen, S.2    Kang, C.3    Shi, P.Y.4
  • 18
    • 0024372153 scopus 로고
    • Detection of a trypsin-like serine protease domain in flaviviruses and pestiviruses
    • COI: 1:CAS:528:DyaL1MXlt12ms7w%3D, PID: 2548336
    • Bazan JF, Fletterick RJ (1989) Detection of a trypsin-like serine protease domain in flaviviruses and pestiviruses. Virology 171:637–639
    • (1989) Virology , vol.171 , pp. 637-639
    • Bazan, J.F.1    Fletterick, R.J.2
  • 19
    • 0024341494 scopus 로고
    • N-terminal domains of putative helicases of flavi- and pestiviruses may be serine proteases
    • Gorbolenya AE, Donchenko AP, Koonin EV, Blinov VM (1989) N-terminal domains of putative helicases of flavi- and pestiviruses may be serine proteases. Nucleic Acids Res 17:3889–3897
    • (1989) Nucleic Acids Res , vol.17 , pp. 3889-3897
    • Gorbolenya, A.E.1    Donchenko, A.P.2    Koonin, E.V.3    Blinov, V.M.4
  • 20
    • 0033034992 scopus 로고    scopus 로고
    • Genetic interaction of flavivirus non-structural proteins NS1 and NS4A as a determinant of replicase function
    • COI: 1:CAS:528:DyaK1MXjtFertro%3D, PID: 10233920
    • Lindenbach BD, Rice CM (1999) Genetic interaction of flavivirus non-structural proteins NS1 and NS4A as a determinant of replicase function. J Virol 73:4611–4621
    • (1999) J Virol , vol.73 , pp. 4611-4621
    • Lindenbach, B.D.1    Rice, C.M.2
  • 21
    • 28444476999 scopus 로고    scopus 로고
    • Membrane curvature and mechanisms of dynamic cell membrane remodelling
    • COI: 1:CAS:528:DC%2BD2MXht1Gqs73N, PID: 16319878
    • McMahon HT, Gallop JL (2005) Membrane curvature and mechanisms of dynamic cell membrane remodelling. Nature 438:590–596
    • (2005) Nature , vol.438 , pp. 590-596
    • McMahon, H.T.1    Gallop, J.L.2
  • 22
    • 77953751833 scopus 로고    scopus 로고
    • Roles of amphipathic helices and the bin/amphiphysin/rvs (BAR) domain of endophilin in membrane curvature generation
    • COI: 1:CAS:528:DC%2BC3cXnsFygt7w%3D, PID: 20418375
    • Jao CC, Hedge BG, Gallop JL, Hegde PB, McMahon HT, Haworth IS, Langen R (2010) Roles of amphipathic helices and the bin/amphiphysin/rvs (BAR) domain of endophilin in membrane curvature generation. J Biol Chem 285:20164–20170
    • (2010) J Biol Chem , vol.285 , pp. 20164-20170
    • Jao, C.C.1    Hedge, B.G.2    Gallop, J.L.3    Hegde, P.B.4    McMahon, H.T.5    Haworth, I.S.6    Langen, R.7
  • 23
    • 0037013858 scopus 로고    scopus 로고
    • An RNA cap (nucleoside-2′-O-)-methyltransferase in the flavivirus RNA polymerase NS5: crystal structure and functional characterization
    • COI: 1:CAS:528:DC%2BD38XkvV2isL8%3D, PID: 12032088
    • Egloff MP, Benarroch D, Selisko B, Romette JL, Canard B (2002) An RNA cap (nucleoside-2′-O-)-methyltransferase in the flavivirus RNA polymerase NS5: crystal structure and functional characterization. EMBO J 21:2757–2768
    • (2002) EMBO J , vol.21 , pp. 2757-2768
    • Egloff, M.P.1    Benarroch, D.2    Selisko, B.3    Romette, J.L.4    Canard, B.5
  • 25
    • 33751508817 scopus 로고    scopus 로고
    • N-glycan processing in ER quality control
    • COI: 1:CAS:528:DC%2BD28Xht12hurrL, PID: 17074831
    • Ruddock LW, Molinari M (2006) N-glycan processing in ER quality control. J Cell Sci 119:4373–4380
    • (2006) J Cell Sci , vol.119 , pp. 4373-4380
    • Ruddock, L.W.1    Molinari, M.2
  • 26
    • 0029024748 scopus 로고
    • Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum
    • COI: 1:CAS:528:DyaK2MXlsFSrsLk%3D, PID: 7736594
    • Hebert DN, Foellmer B, Helenius A (1995) Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum. Cell 81:425–433
    • (1995) Cell , vol.81 , pp. 425-433
    • Hebert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 27
    • 0028103695 scopus 로고
    • Role of N-linked, glucose trimming, and calnexin in glycoprotein folding and quality control
    • COI: 1:CAS:528:DyaK2cXhvVOrtb8%3D, PID: 8302866
    • Hammond C, Braakman I, Helenius A (1994) Role of N-linked, glucose trimming, and calnexin in glycoprotein folding and quality control. Proc Natl Acad Sci USA 91:913–917
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 913-917
    • Hammond, C.1    Braakman, I.2    Helenius, A.3
  • 28
    • 0037495036 scopus 로고    scopus 로고
    • A ligand-binding pocket in the dengue virus envelope glycoprotein
    • COI: 1:CAS:528:DC%2BD3sXkslOntLg%3D, PID: 12759475
    • Modis Y, Ogata S, Clements D, Harrison SC (2003) A ligand-binding pocket in the dengue virus envelope glycoprotein. Proc Natl Acad Sci USA 100:6986–6991
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6986-6991
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 29
    • 11144244755 scopus 로고    scopus 로고
    • Variable surface epitopes in the crystal structure of dengue virus type 3 envelope glycoprotein
    • COI: 1:CAS:528:DC%2BD2MXlt12mtg%3D%3D, PID: 15613349
    • Modis Y, Ogata S, Clements D, Harrison SC (2005) Variable surface epitopes in the crystal structure of dengue virus type 3 envelope glycoprotein. J Virol 79:1223–1231
    • (2005) J Virol , vol.79 , pp. 1223-1231
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 30
    • 0025367812 scopus 로고
    • Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: implications for protein engineering
    • COI: 1:CAS:528:DyaK3cXksFCmu78%3D, PID: 2349213
    • Gavel Y, von Heijne G (1990) Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: implications for protein engineering. Protein Eng 3:433–442
    • (1990) Protein Eng , vol.3 , pp. 433-442
    • Gavel, Y.1    von Heijne, G.2
  • 31
    • 0028037768 scopus 로고
    • The envelope glycoproteins of dengue 1 and dengue 2 viruses grown in mosquito cells differ in their utilization of potential glycosylation sites
    • COI: 1:CAS:528:DyaK2cXlt12mur8%3D, PID: 8053148
    • Johnson AJ, Guirakhoo F, Roehrig JT (1994) The envelope glycoproteins of dengue 1 and dengue 2 viruses grown in mosquito cells differ in their utilization of potential glycosylation sites. Virology 203:241–249
    • (1994) Virology , vol.203 , pp. 241-249
    • Johnson, A.J.1    Guirakhoo, F.2    Roehrig, J.T.3
  • 32
    • 0035059088 scopus 로고    scopus 로고
    • Comparative sequences of two type 1 dengue virus strains possessing different growth characteristics in vitro
    • COI: 1:CAS:528:DC%2BD3MXjvVSitbY%3D, PID: 11386425
    • Ishak H, Takegami T, Kamimura K, Funada H (2001) Comparative sequences of two type 1 dengue virus strains possessing different growth characteristics in vitro. Microbiol Immunol 45:327–331
    • (2001) Microbiol Immunol , vol.45 , pp. 327-331
    • Ishak, H.1    Takegami, T.2    Kamimura, K.3    Funada, H.4
  • 33
    • 0027169938 scopus 로고
    • Selection and partial characterization of dengue 2 virus mutants that induce fusion at elevated pH
    • COI: 1:CAS:528:DyaK3sXisFWgurs%3D, PID: 8480420
    • Guirakhoo F, Hunt AR, Lewis JG, Roehrig JT (1993) Selection and partial characterization of dengue 2 virus mutants that induce fusion at elevated pH. Virology 194:219–223
    • (1993) Virology , vol.194 , pp. 219-223
    • Guirakhoo, F.1    Hunt, A.R.2    Lewis, J.G.3    Roehrig, J.T.4
  • 34
    • 0027453773 scopus 로고
    • Genetic determinants of dengue type 4 virus neurovirulence for mice
    • COI: 1:CAS:528:DyaK2cXisVOitg%3D%3D, PID: 8411360
    • Kawano H, Rostapshov V, Rosen L, Lai CJ (1993) Genetic determinants of dengue type 4 virus neurovirulence for mice. J Virol 67:6567–6575
    • (1993) J Virol , vol.67 , pp. 6567-6575
    • Kawano, H.1    Rostapshov, V.2    Rosen, L.3    Lai, C.J.4
  • 35
    • 0029862799 scopus 로고    scopus 로고
    • A single nucleotide change in the E protein gene of dengue virus 2 Mexican strain affects neurovirulence in mice
    • COI: 1:CAS:528:DyaK28XmtVOqt7k%3D, PID: 8887488
    • Sanchez IJ, Ruiz BH (1996) A single nucleotide change in the E protein gene of dengue virus 2 Mexican strain affects neurovirulence in mice. J Gen Virol 77:2541–2545
    • (1996) J Gen Virol , vol.77 , pp. 2541-2545
    • Sanchez, I.J.1    Ruiz, B.H.2
  • 36
    • 0024340421 scopus 로고
    • Genetic relatedness among structural protein genes of dengue 1 virus strains
    • COI: 1:CAS:528:DyaK3cXntFSqsw%3D%3D, PID: 2738579
    • Chu MC, O’Rourke EJ, Trent DW (1989) Genetic relatedness among structural protein genes of dengue 1 virus strains. J Gen Virol 70:1701–1712
    • (1989) J Gen Virol , vol.70 , pp. 1701-1712
    • Chu, M.C.1    O’Rourke, E.J.2    Trent, D.W.3
  • 37
    • 0025310447 scopus 로고
    • Complete nucleotide sequence of dengue type 3 virus genome RNA
    • COI: 1:CAS:528:DyaK3cXltFSju7o%3D, PID: 2345967
    • Osatomi K, Sumiyoshi H (1990) Complete nucleotide sequence of dengue type 3 virus genome RNA. Virology 176:643–647
    • (1990) Virology , vol.176 , pp. 643-647
    • Osatomi, K.1    Sumiyoshi, H.2
  • 38
    • 0024041312 scopus 로고
    • Nucleotide sequence and deduced amino-acid sequence of the nonstructural proteins of dengue type 2 virus, Jamaica genotype: comparative analysis of the full-length genome
    • COI: 1:CAS:528:DyaL1MXntVWitg%3D%3D, PID: 3388770
    • Deubel V, Kinney RM, Trent DW (1988) Nucleotide sequence and deduced amino-acid sequence of the nonstructural proteins of dengue type 2 virus, Jamaica genotype: comparative analysis of the full-length genome. Virology 165:234–244
    • (1988) Virology , vol.165 , pp. 234-244
    • Deubel, V.1    Kinney, R.M.2    Trent, D.W.3
  • 39
    • 0022996714 scopus 로고
    • Cloning full length dengue type 4 viral DNA sequences: analysis of genes coding for structural proteins
    • Zhao B, Mackow E, Buckler-White A, Markoff L, Chanock RM, Lai CJ, Makino Y (1986) Cloning full length dengue type 4 viral DNA sequences: analysis of genes coding for structural proteins. Virology 156:77–88
    • (1986) Virology , vol.156 , pp. 77-88
    • Zhao, B.1    Mackow, E.2    Buckler-White, A.3    Markoff, L.4    Chanock, R.M.5    Lai, C.J.6    Makino, Y.7
  • 41
    • 34250854515 scopus 로고    scopus 로고
    • Essential role of dengue virus envelope protein N glycosylation at asparagine-67 during viral propagation
    • COI: 1:CAS:528:DC%2BD2sXntVOitr0%3D, PID: 17459925
    • Mondotte JA, Lozach PY, Amara A, Gamarnik AV (2007) Essential role of dengue virus envelope protein N glycosylation at asparagine-67 during viral propagation. J Virol 81:7136–7148
    • (2007) J Virol , vol.81 , pp. 7136-7148
    • Mondotte, J.A.1    Lozach, P.Y.2    Amara, A.3    Gamarnik, A.V.4
  • 42
    • 34548605884 scopus 로고    scopus 로고
    • Glycosylation of the dengue 2 virus E protein at N67 is critical for virus growth in vitro but not for growth in intrathoracically inoculated Aedes aegypti mosquitoes
    • COI: 1:CAS:528:DC%2BD2sXhtVCmu7rI, PID: 17543367
    • Bryant JE, Calvert AE, Mesesan K, Crabtree MB, Volpe KE, Silengo S, Kinney RM, Huang CYH, Miller BR, Roehrig JT (2007) Glycosylation of the dengue 2 virus E protein at N67 is critical for virus growth in vitro but not for growth in intrathoracically inoculated Aedes aegypti mosquitoes. Virology 366:415–423
    • (2007) Virology , vol.366 , pp. 415-423
    • Bryant, J.E.1    Calvert, A.E.2    Mesesan, K.3    Crabtree, M.B.4    Volpe, K.E.5    Silengo, S.6    Kinney, R.M.7    Huang, C.Y.H.8    Miller, B.R.9    Roehrig, J.T.10
  • 43
    • 41349112506 scopus 로고    scopus 로고
    • The flavivirus precursor membrane-envelope protein complex: structure and maturation
    • COI: 1:CAS:528:DC%2BD1cXjs12ktr4%3D, PID: 18369147
    • Li L, Lok SM, Yu IM, Zhang Y, Kuhn R, Chen J, Rossmann MG (2008) The flavivirus precursor membrane-envelope protein complex: structure and maturation. Science 319:1830–1834
    • (2008) Science , vol.319 , pp. 1830-1834
    • Li, L.1    Lok, S.M.2    Yu, I.M.3    Zhang, Y.4    Kuhn, R.5    Chen, J.6    Rossmann, M.G.7
  • 44
    • 0033988280 scopus 로고    scopus 로고
    • α-Glucosidase inhibitors reduce dengue virus production by affecting the initial steps of virion morphogenesis in the endoplasmic reticulum
    • COI: 1:CAS:528:DC%2BD3cXkvV2i, PID: 10590151
    • Courageot MP, Frenkiel MP, Dos Santos CD, Deubel V, Després P (2000) α-Glucosidase inhibitors reduce dengue virus production by affecting the initial steps of virion morphogenesis in the endoplasmic reticulum. J Virol 74:564–572
    • (2000) J Virol , vol.74 , pp. 564-572
    • Courageot, M.P.1    Frenkiel, M.P.2    Dos Santos, C.D.3    Deubel, V.4    Després, P.5
  • 45
    • 0023857108 scopus 로고
    • Evidence that the mature form of the flavivirus non-structural protein NS1 is a dimer
    • COI: 1:CAS:528:DyaL1cXhsVKktbo%3D, PID: 2827377
    • Winkler G, Randolph VB, Cleaves GR, Ryan TE, Stollar V (1988) Evidence that the mature form of the flavivirus non-structural protein NS1 is a dimer. Virology 162:187–196
    • (1988) Virology , vol.162 , pp. 187-196
    • Winkler, G.1    Randolph, V.B.2    Cleaves, G.R.3    Ryan, T.E.4    Stollar, V.5
  • 46
    • 0027209027 scopus 로고
    • The effects of site-directed mutagenesis on the dimerization and secretion of the NS1 protein specified by dengue virus
    • COI: 1:CAS:528:DyaK3sXks1KjtrY%3D, PID: 8389081
    • Pryor MJ, Wright PJ (1993) The effects of site-directed mutagenesis on the dimerization and secretion of the NS1 protein specified by dengue virus. Virology 194:769–780
    • (1993) Virology , vol.194 , pp. 769-780
    • Pryor, M.J.1    Wright, P.J.2
  • 47
    • 0028345969 scopus 로고
    • Glycosylation mutants of dengue virus NS1 protein
    • COI: 1:CAS:528:DyaK2cXivFertLc%3D, PID: 8176380
    • Pryor MJ, Wright PJ (1994) Glycosylation mutants of dengue virus NS1 protein. J Gen Virol 75:1183–1187
    • (1994) J Gen Virol , vol.75 , pp. 1183-1187
    • Pryor, M.J.1    Wright, P.J.2
  • 48
    • 0032994359 scopus 로고    scopus 로고
    • Dengue virus type 1 nonstructural glycoprotein NS1 is secreted from mammalian cells as a soluble hexamer in a glycosylation-dependent fashion
    • COI: 1:CAS:528:DyaK1MXjvFyktbc%3D, PID: 10364366
    • Flamand M, Megret F, Mathieu M, Lepault J, Rey FA, Deubel V (1999) Dengue virus type 1 nonstructural glycoprotein NS1 is secreted from mammalian cells as a soluble hexamer in a glycosylation-dependent fashion. J Virol 73:6104–6110
    • (1999) J Virol , vol.73 , pp. 6104-6110
    • Flamand, M.1    Megret, F.2    Mathieu, M.3    Lepault, J.4    Rey, F.A.5    Deubel, V.6
  • 49
    • 79954633991 scopus 로고    scopus 로고
    • N-linked glycosylation of dengue virus NS1 protein modulates secretion, cell-surface expression, hexamer stability, and interactions with human complement
    • COI: 1:CAS:528:DC%2BC3MXkvFaltLs%3D, PID: 21429549
    • Somnuke P, Hauhart RE, Atkinson JP, Diamond MS, Avirutnam P (2011) N-linked glycosylation of dengue virus NS1 protein modulates secretion, cell-surface expression, hexamer stability, and interactions with human complement. Virology 413:253–264
    • (2011) Virology , vol.413 , pp. 253-264
    • Somnuke, P.1    Hauhart, R.E.2    Atkinson, J.P.3    Diamond, M.S.4    Avirutnam, P.5
  • 50
    • 33748195979 scopus 로고    scopus 로고
    • Glycosylation in cellular mechanisms of health and disease
    • COI: 1:CAS:528:DC%2BD28XpvVKitbo%3D, PID: 16959566
    • Ohtsubo K, Marth JD (2006) Glycosylation in cellular mechanisms of health and disease. Cell 126:855–867
    • (2006) Cell , vol.126 , pp. 855-867
    • Ohtsubo, K.1    Marth, J.D.2
  • 51
    • 0032763888 scopus 로고    scopus 로고
    • Evolutionary considerations in relating oligosaccharide diversity to biological function
    • COI: 1:CAS:528:DyaK1MXkslSks7g%3D, PID: 10406840
    • Gagneux P, Varki A (1999) Evolutionary considerations in relating oligosaccharide diversity to biological function. Glycobiology 9:747–755
    • (1999) Glycobiology , vol.9 , pp. 747-755
    • Gagneux, P.1    Varki, A.2
  • 52
    • 0034441282 scopus 로고    scopus 로고
    • The joys of HexNAc. The synthesis and function of N- and O-glycan branches
    • COI: 1:CAS:528:DC%2BD3MXksVOgtL4%3D, PID: 11421343
    • Schachter H (2000) The joys of HexNAc. The synthesis and function of N- and O-glycan branches. Glycoconj J 17:465–483
    • (2000) Glycoconj J , vol.17 , pp. 465-483
    • Schachter, H.1
  • 53
    • 13544268336 scopus 로고    scopus 로고
    • Unravelling the mechanism of protein N-glycosylation
    • COI: 1:CAS:528:DC%2BD2MXovVCktA%3D%3D, PID: 15590627
    • Yan A, Lennarz WJ (2005) Unravelling the mechanism of protein N-glycosylation. J Biol Chem 280:3121–3124
    • (2005) J Biol Chem , vol.280 , pp. 3121-3124
    • Yan, A.1    Lennarz, W.J.2
  • 54
    • 0035997376 scopus 로고    scopus 로고
    • Order out of chaos: assembly of ligand binding sites in heparan sulfate
    • COI: 1:CAS:528:DC%2BD38Xos1Cltrk%3D, PID: 12045103
    • Esko JD, Selleck SB (2002) Order out of chaos: assembly of ligand binding sites in heparan sulfate. Annu Rev Biochem 71:435–471
    • (2002) Annu Rev Biochem , vol.71 , pp. 435-471
    • Esko, J.D.1    Selleck, S.B.2
  • 55
    • 0036695829 scopus 로고    scopus 로고
    • Understanding the stepwise synthesis of glycolipids
    • COI: 1:CAS:528:DC%2BD38XntFGrsLo%3D, PID: 12374198
    • Maccioni HJ, Giraudo CG, Danniotti JL (2002) Understanding the stepwise synthesis of glycolipids. Neurochem Res 27:629–636
    • (2002) Neurochem Res , vol.27 , pp. 629-636
    • Maccioni, H.J.1    Giraudo, C.G.2    Danniotti, J.L.3
  • 56
    • 80052334710 scopus 로고    scopus 로고
    • Crystal structure of reovirus attachment protein σ1 in complex with sialylated oligosaccharides
    • COI: 1:CAS:528:DC%2BC3MXhtFWiurfF, PID: 21829363
    • Reiter DM, Frierson JM, Halvorson EE, Kobayashi T, Dermody TS, Stehle T (2011) Crystal structure of reovirus attachment protein σ1 in complex with sialylated oligosaccharides. PLoS Pathog 7:e1002166
    • (2011) PLoS Pathog , vol.7 , pp. e1002166
    • Reiter, D.M.1    Frierson, J.M.2    Halvorson, E.E.3    Kobayashi, T.4    Dermody, T.S.5    Stehle, T.6
  • 57
    • 0036500085 scopus 로고    scopus 로고
    • The rhesus rotavirus VP4 sialic acid binding domain has a galectin fold with a novel carbohydrate binding site
    • COI: 1:CAS:528:DC%2BD38XitFylsLo%3D, PID: 11867517
    • Dormitzer PR, Sun ZY, Wagner G, Harrison SC (2002) The rhesus rotavirus VP4 sialic acid binding domain has a galectin fold with a novel carbohydrate binding site. EMBO J 21:885–897
    • (2002) EMBO J , vol.21 , pp. 885-897
    • Dormitzer, P.R.1    Sun, Z.Y.2    Wagner, G.3    Harrison, S.C.4
  • 58
    • 0027988832 scopus 로고
    • Receptor specificity in human, avian, and equine H2 and H3 influenza virus isolates
    • COI: 1:CAS:528:DyaK2cXmvFKktbk%3D, PID: 7975212
    • Connor RJ, Kawaoka Y, Webster RG, Paulson JC (1994) Receptor specificity in human, avian, and equine H2 and H3 influenza virus isolates. Virology 205:17–23
    • (1994) Virology , vol.205 , pp. 17-23
    • Connor, R.J.1    Kawaoka, Y.2    Webster, R.G.3    Paulson, J.C.4
  • 59
    • 0026551062 scopus 로고
    • Cell surface receptors for herpes simplex virus are heparan sulfate proteoglycans
    • COI: 1:CAS:528:DyaK38XhtVemtLs%3D, PID: 1310996
    • Shieh MT, WuDunn D, Montgomery RI, Esko JD, Spearm PG (1992) Cell surface receptors for herpes simplex virus are heparan sulfate proteoglycans. J Cell Biol 116:1273–1281
    • (1992) J Cell Biol , vol.116 , pp. 1273-1281
    • Shieh, M.T.1    WuDunn, D.2    Montgomery, R.I.3    Esko, J.D.4    Spearm, P.G.5
  • 60
    • 0042195112 scopus 로고    scopus 로고
    • Parvovirus host range, cell tropism and evolution
    • COI: 1:CAS:528:DC%2BD3sXmslems7c%3D, PID: 12941411
    • Hueffer K, Parrishm CR (2003) Parvovirus host range, cell tropism and evolution. Curr Opin Microbiol 6:392–398
    • (2003) Curr Opin Microbiol , vol.6 , pp. 392-398
    • Hueffer, K.1    Parrishm, C.R.2
  • 61
    • 84861309287 scopus 로고    scopus 로고
    • Spike protein VP8* of human rotavirus recognizes histo-blood group antigens in a type-specific manner
    • COI: 1:CAS:528:DC%2BC38XmtFGls7s%3D, PID: 22345472
    • Huang P, Xia M, Tan M, Zhong W, Wei C, Wang L, Morrow A, Jiang X (2012) Spike protein VP8* of human rotavirus recognizes histo-blood group antigens in a type-specific manner. J Virol 86:4833–4843
    • (2012) J Virol , vol.86 , pp. 4833-4843
    • Huang, P.1    Xia, M.2    Tan, M.3    Zhong, W.4    Wei, C.5    Wang, L.6    Morrow, A.7    Jiang, X.8
  • 62
    • 84860786497 scopus 로고    scopus 로고
    • Cell attachment protein VP8* of a human rotavirus specifically interacts with A-type histo-blood group antigen
    • COI: 1:CAS:528:DC%2BC38XlslSis70%3D, PID: 22504179
    • Hu L, Crawford SE, Czako R, Cortes-Penfield NW, Smith DF, Le Pendu J, Estes MK, Prasad BV (2012) Cell attachment protein VP8* of a human rotavirus specifically interacts with A-type histo-blood group antigen. Nature 485:256–259
    • (2012) Nature , vol.485 , pp. 256-259
    • Hu, L.1    Crawford, S.E.2    Czako, R.3    Cortes-Penfield, N.W.4    Smith, D.F.5    Le Pendu, J.6    Estes, M.K.7    Prasad, B.V.8
  • 65
    • 33847654231 scopus 로고    scopus 로고
    • Dengue virus entry into liver (HepG2) cells is independent of hsp90 and hsp70
    • PID: 17311328
    • Cabrera-Hernandez A, Thepparit C, Suksanpaisan L, Smith DR (2007) Dengue virus entry into liver (HepG2) cells is independent of hsp90 and hsp70. J Med Virol 79:386–392
    • (2007) J Med Virol , vol.79 , pp. 386-392
    • Cabrera-Hernandez, A.1    Thepparit, C.2    Suksanpaisan, L.3    Smith, D.R.4
  • 66
    • 46949086037 scopus 로고    scopus 로고
    • Identification of dengue virus binding proteins using affinity chromatography
    • COI: 1:CAS:528:DC%2BD1cXosVymtro%3D, PID: 18562018
    • Upanan S, Kuadkitkan A, Smith DR (2008) Identification of dengue virus binding proteins using affinity chromatography. J Virol Methods 151:325–328
    • (2008) J Virol Methods , vol.151 , pp. 325-328
    • Upanan, S.1    Kuadkitkan, A.2    Smith, D.R.3
  • 67
    • 16244364801 scopus 로고    scopus 로고
    • Heat shock protein 90 and heat shock protein 70 are components of dengue virus receptor complex in human cells
    • COI: 1:CAS:528:DC%2BD2MXjt1Ghs74%3D, PID: 15795242
    • Reyes-Del Valle J, Chávez-Salinas S, Medina F, Del Angel RM (2005) Heat shock protein 90 and heat shock protein 70 are components of dengue virus receptor complex in human cells. J Virol 79:4557–4567
    • (2005) J Virol , vol.79 , pp. 4557-4567
    • Reyes-Del Valle, J.1    Chávez-Salinas, S.2    Medina, F.3    Del Angel, R.M.4
  • 68
    • 18944391706 scopus 로고    scopus 로고
    • Two dimensional VOPBA reveals laminin receptor (LAMR1) interaction with dengue virus serotypes 1, 2 and 3
    • PID: 15790424, COI: 1:CAS:528:DC%2BD2MXjsVahsr4%3D
    • Tio PH, Jong WW, Cardosa MJ (2005) Two dimensional VOPBA reveals laminin receptor (LAMR1) interaction with dengue virus serotypes 1, 2 and 3. Virol J 2:25
    • (2005) Virol J , vol.2 , pp. 25
    • Tio, P.H.1    Jong, W.W.2    Cardosa, M.J.3
  • 69
    • 0033015721 scopus 로고    scopus 로고
    • Bacterial lipopolysaccharide inhibits dengue virus infection of primary human monocytes/macrophages by blockade of virus entry via a CD14-dependent mechanism
    • COI: 1:CAS:528:DyaK1MXhvFynsrg%3D, PID: 10074110
    • Chen YC, Wang SY, King CC (1999) Bacterial lipopolysaccharide inhibits dengue virus infection of primary human monocytes/macrophages by blockade of virus entry via a CD14-dependent mechanism. J Virol 73:2650–2657
    • (1999) J Virol , vol.73 , pp. 2650-2657
    • Chen, Y.C.1    Wang, S.Y.2    King, C.C.3
  • 70
    • 0041563793 scopus 로고    scopus 로고
    • Dendritic-cell-specific ICAM3-grabbing non-integrin is essential for the productive infection of human dendritic cells by mosquito-cell-derived dengue viruses
    • COI: 1:CAS:528:DC%2BD3sXltVWhtbg%3D, PID: 12783086
    • Navarro-Sanchez E, Altmeyer R, Amara A, Schwartz O, Fieschi F, Virelizier JL, Arenzana-Seisdedos F, Desprès P (2003) Dendritic-cell-specific ICAM3-grabbing non-integrin is essential for the productive infection of human dendritic cells by mosquito-cell-derived dengue viruses. EMBO Rep 4:723–728
    • (2003) EMBO Rep , vol.4 , pp. 723-728
    • Navarro-Sanchez, E.1    Altmeyer, R.2    Amara, A.3    Schwartz, O.4    Fieschi, F.5    Virelizier, J.L.6    Arenzana-Seisdedos, F.7    Desprès, P.8
  • 72
    • 0030764559 scopus 로고    scopus 로고
    • Dengue virus infectivity depends on envelope protein binding to target cell heparan sulfate
    • COI: 1:CAS:528:DyaK2sXltVKqtb0%3D, PID: 9256277
    • Chen Y, Maguire T, Hileman RE, Fromm JR, Esko JD, Linhardt RJ, Marks RM (1997) Dengue virus infectivity depends on envelope protein binding to target cell heparan sulfate. Nat Med 3:866–871
    • (1997) Nat Med , vol.3 , pp. 866-871
    • Chen, Y.1    Maguire, T.2    Hileman, R.E.3    Fromm, J.R.4    Esko, J.D.5    Linhardt, R.J.6    Marks, R.M.7
  • 76
    • 7644219512 scopus 로고    scopus 로고
    • Serotype-specific entry of dengue virus into liver cells: identification of the 37-kilodalton/67-kilodalton high-affinity laminin receptor as a dengue virus serotype 1 receptor
    • COI: 1:CAS:528:DC%2BD2cXhtVWhu7fP, PID: 15507651
    • Thepparit C, Smith DR (2004) Serotype-specific entry of dengue virus into liver cells: identification of the 37-kilodalton/67-kilodalton high-affinity laminin receptor as a dengue virus serotype 1 receptor. J Virol 78:12647–12656
    • (2004) J Virol , vol.78 , pp. 12647-12656
    • Thepparit, C.1    Smith, D.R.2
  • 78
    • 0030768318 scopus 로고    scopus 로고
    • Identification of two surface proteins from C6/36 cells that bind dengue type 4 virus
    • Salas-Benito JS, del Angel RM (1997) Identification of two surface proteins from C6/36 cells that bind dengue type 4 virus. J Virol 71:7746–7752
    • (1997) J Virol , vol.71 , pp. 7746-7752
    • Salas-Benito, J.S.1    del Angel, R.M.2
  • 80
    • 0346727181 scopus 로고    scopus 로고
    • Isolation of putative dengue virus receptor molecules by affinity chromatography using a recombinant E protein ligand
    • COI: 1:CAS:528:DC%2BD2cXjsFShtQ%3D%3D, PID: 14715312
    • Reyes-del Valle J, del Angel RM (2004) Isolation of putative dengue virus receptor molecules by affinity chromatography using a recombinant E protein ligand. J Virol Methods 116:95–102
    • (2004) J Virol Methods , vol.116 , pp. 95-102
    • Reyes-del Valle, J.1    del Angel, R.M.2
  • 82
    • 0028788196 scopus 로고
    • Isolation and characterization of heparan sulfate from crude porcine intestinal mucosal peptidoglycan heparin
    • COI: 1:CAS:528:DyaK2MXptVanu7c%3D, PID: 8536254
    • Griffin CC, Linhardt RJ, Van Gorp CL, Toida T, Hileman RE, Schubert RL, Brown SE (1995) Isolation and characterization of heparan sulfate from crude porcine intestinal mucosal peptidoglycan heparin. Carbohydr Res 276:183–197
    • (1995) Carbohydr Res , vol.276 , pp. 183-197
    • Griffin, C.C.1    Linhardt, R.J.2    Van Gorp, C.L.3    Toida, T.4    Hileman, R.E.5    Schubert, R.L.6    Brown, S.E.7
  • 83
    • 38449102893 scopus 로고    scopus 로고
    • Analysis of the interaction of Ebola virus glycoprotein with DC-SIGN (dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin) and its homologue DC-SIGNR
    • COI: 1:CAS:528:DC%2BD2sXhsVamsr7J, PID: 17940955
    • Marzi A, Möller P, Hanna SL, Harrer T, Eisemann J, Steinkasserer A, Becker S, Baribaud F, Pöhlmann S (2007) Analysis of the interaction of Ebola virus glycoprotein with DC-SIGN (dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin) and its homologue DC-SIGNR. J Infect Dis 196:S237–S246
    • (2007) J Infect Dis , vol.196 , pp. S237-S246
    • Marzi, A.1    Möller, P.2    Hanna, S.L.3    Harrer, T.4    Eisemann, J.5    Steinkasserer, A.6    Becker, S.7    Baribaud, F.8    Pöhlmann, S.9
  • 86
    • 0141688292 scopus 로고    scopus 로고
    • DC-SIGN: escape mechanism for pathogens
    • PID: 12949494, COI: 1:CAS:528:DC%2BD3sXmvVWmtb8%3D
    • van Kooyk Geijtenbeek TB (2003) DC-SIGN: escape mechanism for pathogens. Nat Rev Immunol 3:697–709
    • (2003) Nat Rev Immunol , vol.3 , pp. 697-709
    • van Kooyk, G.T.B.1
  • 87
    • 70349332794 scopus 로고    scopus 로고
    • N-linked glycans on dengue viruses grown in mammalian and insect cells
    • COI: 1:CAS:528:DC%2BD1MXhtFehsbzE, PID: 19494052
    • Hacker K, White L, de Silva AM (2009) N-linked glycans on dengue viruses grown in mammalian and insect cells. J Gen Virol 90:2097–2106
    • (2009) J Gen Virol , vol.90 , pp. 2097-2106
    • Hacker, K.1    White, L.2    de Silva, A.M.3
  • 88
    • 21244462832 scopus 로고    scopus 로고
    • Dendritic cell-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN)-mediated enhancement of dengue virus infection is independent of DC-SIGN internalization signals
    • COI: 1:CAS:528:DC%2BD2MXltlKiu7k%3D, PID: 15855154
    • Lozach PY, Burleigh L, Staropoli I, Navarro-Sanchez E, Harriague J, Virelizier JL, Rey FA, Després P, Arenzana-Seisdedos F, Amara A (2005) Dendritic cell-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN)-mediated enhancement of dengue virus infection is independent of DC-SIGN internalization signals. J Biol Chem 280:23698–23708
    • (2005) J Biol Chem , vol.280 , pp. 23698-23708
    • Lozach, P.Y.1    Burleigh, L.2    Staropoli, I.3    Navarro-Sanchez, E.4    Harriague, J.5    Virelizier, J.L.6    Rey, F.A.7    Després, P.8    Arenzana-Seisdedos, F.9    Amara, A.10
  • 89
    • 0033578326 scopus 로고    scopus 로고
    • Myeloid DAP12-associating lectin (MDL)-1 is a cell surface receptor involved in the activation of myeloid cells
    • COI: 1:CAS:528:DyaK1MXlsVymtL4%3D, PID: 10449773
    • Bakker AB, Baker E, Sutherland GR, Phillips JH, Lanier LL (1999) Myeloid DAP12-associating lectin (MDL)-1 is a cell surface receptor involved in the activation of myeloid cells. Proc Natl Acad Sci USA 96:9792–9796
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 9792-9796
    • Bakker, A.B.1    Baker, E.2    Sutherland, G.R.3    Phillips, J.H.4    Lanier, L.L.5
  • 90
    • 0026317511 scopus 로고
    • Glycosidase inhibitors: inhibitors of N-linked oligosaccharide processing
    • COI: 1:CAS:528:DyaK38XnvV2hsA%3D%3D, PID: 1743438
    • Elbein AD (1991) Glycosidase inhibitors: inhibitors of N-linked oligosaccharide processing. FASEB J 5:3055–3063
    • (1991) FASEB J , vol.5 , pp. 3055-3063
    • Elbein, A.D.1
  • 91
    • 0024539433 scopus 로고
    • Structure–activity relationship of swainsonine. Inhibition of human α-mannosidases by swainsonine analogues
    • COI: 1:CAS:528:DyaL1MXktleisr4%3D, PID: 2499316
    • Cenci di Bello I, Fleet G, Namgoong SK, Tadano K, Winchester B (1989) Structure–activity relationship of swainsonine. Inhibition of human α-mannosidases by swainsonine analogues. Biochem J 259:855–861
    • (1989) Biochem J , vol.259 , pp. 855-861
    • Cenci di Bello, I.1    Fleet, G.2    Namgoong, S.K.3    Tadano, K.4    Winchester, B.5
  • 92
    • 0025063976 scopus 로고
    • Inhibition of α-l-fucosidase by derivatives of deoxyfuconojirimycin and deoxymannojirimycin
    • COI: 1:CAS:528:DyaK3cXlvVOjsb0%3D, PID: 2137330
    • Winchester B, Barker C, Baines S, Jacob GS, Namgoong SK, Fleet G (1990) Inhibition of α-l-fucosidase by derivatives of deoxyfuconojirimycin and deoxymannojirimycin. Biochem J 265:277–282
    • (1990) Biochem J , vol.265 , pp. 277-282
    • Winchester, B.1    Barker, C.2    Baines, S.3    Jacob, G.S.4    Namgoong, S.K.5    Fleet, G.6
  • 93
    • 0036196402 scopus 로고    scopus 로고
    • Antiviral effects of an iminosugar derivative on flavivirus infections
    • COI: 1:CAS:528:DC%2BD38XisVynurY%3D, PID: 11907199
    • Wu SF, Lee CJ, Liao CL, Dwek RA, Zitzmann N, Lin YL (2002) Antiviral effects of an iminosugar derivative on flavivirus infections. J Virol 76:3596–3604
    • (2002) J Virol , vol.76 , pp. 3596-3604
    • Wu, S.F.1    Lee, C.J.2    Liao, C.L.3    Dwek, R.A.4    Zitzmann, N.5    Lin, Y.L.6
  • 95
    • 47949093805 scopus 로고    scopus 로고
    • Simian immunodeficiency virus is susceptible to inhibition by carbohydrate-binding agents in a manner similar to that of HIV: implications for further preclinical drug development
    • PID: 18474667, COI: 1:CAS:528:DC%2BD1cXptF2gsr8%3D
    • François KO, Auwerx J, Schols D, Balzarini J (2008) Simian immunodeficiency virus is susceptible to inhibition by carbohydrate-binding agents in a manner similar to that of HIV: implications for further preclinical drug development. Mol Pharmacol 74:330–337
    • (2008) Mol Pharmacol , vol.74 , pp. 330-337
    • François, K.O.1    Auwerx, J.2    Schols, D.3    Balzarini, J.4
  • 96
    • 63549108516 scopus 로고    scopus 로고
    • Antiviral activity of carbohydrates-binding agents and the role of DC-SIGN in dengue virus infection
    • COI: 1:CAS:528:DC%2BD1MXkt1Sjs7k%3D, PID: 19264337
    • Alen MMF, Kaptein SJF, De Burghgraeve T, Balzarini J, Neyts J, Schols D (2009) Antiviral activity of carbohydrates-binding agents and the role of DC-SIGN in dengue virus infection. Virology 387:67–75
    • (2009) Virology , vol.387 , pp. 67-75
    • Alen, M.M.F.1    Kaptein, S.J.F.2    De Burghgraeve, T.3    Balzarini, J.4    Neyts, J.5    Schols, D.6
  • 97
    • 0033602564 scopus 로고    scopus 로고
    • Analysis of the steps involved in Dengue virus entry into host cells
    • COI: 1:CAS:528:DyaK1MXisVahsLw%3D, PID: 10208929
    • Hung SL, Lee PL, Chen LK, Kao CL, King CC (1999) Analysis of the steps involved in Dengue virus entry into host cells. Virology 257:156–167
    • (1999) Virology , vol.257 , pp. 156-167
    • Hung, S.L.1    Lee, P.L.2    Chen, L.K.3    Kao, C.L.4    King, C.C.5
  • 98
    • 77951712267 scopus 로고    scopus 로고
    • Narcissus tazetta lectin shows strong inhibitory effects against respiratory syncytial virus, influenza A (H1N1, H3N2, H5N1) and B viruses
    • COI: 1:CAS:528:DC%2BC3cXps1Wks7c%3D, PID: 20413914
    • Ooi LSM, Ho WS, Ngai KLK, Tian L, Chan PKS, Sun SSM, Ooi VEC (2010) Narcissus tazetta lectin shows strong inhibitory effects against respiratory syncytial virus, influenza A (H1N1, H3N2, H5N1) and B viruses. J Biosci 35:95–103
    • (2010) J Biosci , vol.35 , pp. 95-103
    • Ooi, L.S.M.1    Ho, W.S.2    Ngai, K.L.K.3    Tian, L.4    Chan, P.K.S.5    Sun, S.S.M.6    Ooi, V.E.C.7
  • 99
    • 79955749876 scopus 로고    scopus 로고
    • Cloning and functional characterization of a GNA-like lectin from Chinese narcissus (Narcissus tazetta var. Chinensis Roem)
    • COI: 1:CAS:528:DC%2BC3MXmvFeqsro%3D, PID: 21261630
    • Gao ZM, Zheng B, Wang WY, Li Q, Yuan QP (2011) Cloning and functional characterization of a GNA-like lectin from Chinese narcissus (Narcissus tazetta var. Chinensis Roem). Physiol Plant 142:193–204
    • (2011) Physiol Plant , vol.142 , pp. 193-204
    • Gao, Z.M.1    Zheng, B.2    Wang, W.Y.3    Li, Q.4    Yuan, Q.P.5
  • 100
    • 33845897631 scopus 로고    scopus 로고
    • Carbohydrate-binding agents efficiently prevent dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin (DC-SIGN)-directed HIV-1 transmission to T lymphocytes
    • COI: 1:CAS:528:DC%2BD2sXit1GksQ%3D%3D, PID: 17056872
    • Balzarini J, Van Herrewege Y, Vermeire K, Vanham G, Schols D (2007) Carbohydrate-binding agents efficiently prevent dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin (DC-SIGN)-directed HIV-1 transmission to T lymphocytes. Mol Pharmacol 71:3–11
    • (2007) Mol Pharmacol , vol.71 , pp. 3-11
    • Balzarini, J.1    Van Herrewege, Y.2    Vermeire, K.3    Vanham, G.4    Schols, D.5
  • 101
    • 0026532965 scopus 로고
    • n-specific plant lectin from Urtica dioica are potent and selective inhibitors of human immunodeficiency virus and cytomegalovirus replication in vitro
    • COI: 1:CAS:528:DyaK38Xks1agtLk%3D, PID: 1329650
    • n-specific plant lectin from Urtica dioica are potent and selective inhibitors of human immunodeficiency virus and cytomegalovirus replication in vitro. Antivir Res 18:191–207
    • (1992) Antivir Res , vol.18 , pp. 191-207
    • Balzarini, J.1    Neyts, J.2    Schols, D.3    Hosoya, M.4    van Damme, E.5    Peumans, W.6    de Clercq, E.7
  • 102
    • 34249738649 scopus 로고    scopus 로고
    • A novel mannose-binding tuber lectin from Typhonium divaricatum (L.) Decne (family Araceae) with antiviral activity against HSV-II and anti-proliferative effect on human cancer cell lines
    • COI: 1:CAS:528:DC%2BD2sXmslyhsr4%3D, PID: 17562287
    • Luo Y, Xu X, Liu J, Li J, Sun Y, Liu Z, Liu J, van Damme E, Balzarini J, Bao J (2007) A novel mannose-binding tuber lectin from Typhonium divaricatum (L.) Decne (family Araceae) with antiviral activity against HSV-II and anti-proliferative effect on human cancer cell lines. J Biochem Mol Biol 40:358–367
    • (2007) J Biochem Mol Biol , vol.40 , pp. 358-367
    • Luo, Y.1    Xu, X.2    Liu, J.3    Li, J.4    Sun, Y.5    Liu, Z.6    Liu, J.7    van Damme, E.8    Balzarini, J.9    Bao, J.10
  • 103
    • 4744364586 scopus 로고    scopus 로고
    • New mannose-binding lectin isolated from the rhizome of sarsaparilla Smilax glabra Roxb. (Liliaceae)
    • COI: 1:CAS:528:DC%2BD2cXnsVOntrg%3D, PID: 15453671
    • Ooi LSM, Sun SSM, Wang H, Ooi VEC (2004) New mannose-binding lectin isolated from the rhizome of sarsaparilla Smilax glabra Roxb. (Liliaceae). J Agric Food Chem 52:6091–6095
    • (2004) J Agric Food Chem , vol.52 , pp. 6091-6095
    • Ooi, L.S.M.1    Sun, S.S.M.2    Wang, H.3    Ooi, V.E.C.4
  • 104
    • 34249978146 scopus 로고    scopus 로고
    • In vitro activity evaluation of Parkia pendula seed lectin against human cytomegalovirus and herpes virus 6
    • COI: 1:CAS:528:DC%2BD2sXmsFKltrY%3D, PID: 17254798
    • Favacho ARM, Cintra EA, Coelho LCBB, Linhares MIS (2007) In vitro activity evaluation of Parkia pendula seed lectin against human cytomegalovirus and herpes virus 6. Biologicals 35:189–194
    • (2007) Biologicals , vol.35 , pp. 189-194
    • Favacho, A.R.M.1    Cintra, E.A.2    Coelho, L.C.B.B.3    Linhares, M.I.S.4
  • 105
    • 33644838985 scopus 로고    scopus 로고
    • Anti-HIV I/II activity and molecular cloning of a novel mannose/sialic acid-binding lectin from rhizome of Polygonatum cystonema Hua
    • COI: 1:CAS:528:DC%2BD28XisFequro%3D, PID: 16474897
    • An J, Liu J, Wu C, Li J, Dai L, van Damme E, Balzarini J, de Clercq E, Chen F, Bao J (2006) Anti-HIV I/II activity and molecular cloning of a novel mannose/sialic acid-binding lectin from rhizome of Polygonatum cystonema Hua. Acta Biochim Biophys Sin 38:70–78
    • (2006) Acta Biochim Biophys Sin , vol.38 , pp. 70-78
    • An, J.1    Liu, J.2    Wu, C.3    Li, J.4    Dai, L.5    van Damme, E.6    Balzarini, J.7    de Clercq, E.8    Chen, F.9    Bao, J.10
  • 106
    • 77950581739 scopus 로고    scopus 로고
    • A lectin isolated from bananas is a potent inhibitor of HIV replication
    • COI: 1:CAS:528:DC%2BC3cXjtFShs74%3D, PID: 20080975
    • Swanson MD, Winter HC, Goldstein IJ, Markovitz DM (2010) A lectin isolated from bananas is a potent inhibitor of HIV replication. J Biol Chem 285:8646–8655
    • (2010) J Biol Chem , vol.285 , pp. 8646-8655
    • Swanson, M.D.1    Winter, H.C.2    Goldstein, I.J.3    Markovitz, D.M.4
  • 108
    • 0033646649 scopus 로고    scopus 로고
    • Jackfruit lectin: properties of mitogenicity and the inhibition of herpesvirus infection
    • COI: 1:CAS:528:DC%2BD3MXltVSntw%3D%3D, PID: 11056557
    • Wetprasit N, Threesangsri W, Klamklai N, Chulavatnatol M (2000) Jackfruit lectin: properties of mitogenicity and the inhibition of herpesvirus infection. Jpn J Infect Dis 53:156–161
    • (2000) Jpn J Infect Dis , vol.53 , pp. 156-161
    • Wetprasit, N.1    Threesangsri, W.2    Klamklai, N.3    Chulavatnatol, M.4
  • 109
    • 79959757718 scopus 로고    scopus 로고
    • Broad antiviral activity of carbohydrate-binding agents against the four serotypes of dengue virus in monocyte-derived dendritic cells
    • COI: 1:CAS:528:DC%2BC3MXos12gurs%3D, PID: 21738755
    • Alen MMF, De Burghgraeve T, Kaptein SJF, Balzarini J, Neyts J, Schols D (2011) Broad antiviral activity of carbohydrate-binding agents against the four serotypes of dengue virus in monocyte-derived dendritic cells. PLoS One 6:e21658
    • (2011) PLoS One , vol.6 , pp. e21658
    • Alen, M.M.F.1    De Burghgraeve, T.2    Kaptein, S.J.F.3    Balzarini, J.4    Neyts, J.5    Schols, D.6
  • 110
    • 84879685472 scopus 로고    scopus 로고
    • Secondary infection as a risk factor for dengue hemorrhagic fever/dengue shock syndrome: an historical perspective and role of antibody-dependent enhancement of infection
    • COI: 1:CAS:528:DC%2BC3sXhtVCrtbvI, PID: 23471635
    • Guzman MG, Alvarez M, Halstead SB (2013) Secondary infection as a risk factor for dengue hemorrhagic fever/dengue shock syndrome: an historical perspective and role of antibody-dependent enhancement of infection. Arch Virol 158:1445–1459
    • (2013) Arch Virol , vol.158 , pp. 1445-1459
    • Guzman, M.G.1    Alvarez, M.2    Halstead, S.B.3
  • 111
    • 0024502091 scopus 로고
    • Maturation of Japanese encephalitis virus glycoproteins produced by infected mammalian and mosquito cells
    • COI: 1:CAS:528:DyaL1MXit1ynsro%3D, PID: 2523178
    • Mason P (1989) Maturation of Japanese encephalitis virus glycoproteins produced by infected mammalian and mosquito cells. Virology 169:354–364
    • (1989) Virology , vol.169 , pp. 354-364
    • Mason, P.1
  • 112
    • 0141534434 scopus 로고    scopus 로고
    • A sugar discriminating binuclear copper (II) complex
    • COI: 1:CAS:528:DC%2BD3sXmsl2nsbg%3D, PID: 13129353
    • Striegler S, Dittel M (2003) A sugar discriminating binuclear copper (II) complex. J Am Chem Soc 125:11518–11524
    • (2003) J Am Chem Soc , vol.125 , pp. 11518-11524
    • Striegler, S.1    Dittel, M.2
  • 113
    • 21244463409 scopus 로고    scopus 로고
    • Molecular recognition of carbohydrates with artificial receptors: mimicking the binding motifs found in the crystal structures of protein–carbohydrate complexes
    • COI: 1:CAS:528:DC%2BD2MXksl2msbk%3D, PID: 15969582
    • Mazik M, Cavqa H, Jones PG (2005) Molecular recognition of carbohydrates with artificial receptors: mimicking the binding motifs found in the crystal structures of protein–carbohydrate complexes. J Am Chem Soc 127:9045–9052
    • (2005) J Am Chem Soc , vol.127 , pp. 9045-9052
    • Mazik, M.1    Cavqa, H.2    Jones, P.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.