메뉴 건너뛰기




Volumn 10, Issue 30, 2004, Pages 3701-3712

Virus attachment and entry offer numerous targets for antiviral therapy

Author keywords

[No Author keywords available]

Indexed keywords

1,1' [1,4 PHENYLENEBIS(METHYLENE)]BIS(1,4,8,11 TETRAAZACYCLOTETRADECANE); 4 [1 [(2,4 DIMETHYL 3 PYRIDINYL)CARBONYL] 4 METHYL 4 PIPERIDINYL] 2 METHYL 1 [1 [4 (TRIFLUOOROMETHYL)PHENYL]ETHYL]PIPERAZINE; 4 BENZOYL 1 [(4 METHOXY 1H PYRROLO[2,3 B]PYRIDIN 3 YL)OXOACETYL] 2 METHYLPIPERAZINE; 4 METHOXY 7 AZAINDOLE DERIVATIVE; ANTI HUMAN IMMUNODEFICIENCY VIRUS AGENT; ANTIVIRUS AGENT; CD4 IMMUNOGLOBULIN; CD4 IMMUNOGLOBULIN G2; CHEMOKINE RECEPTOR CCR5; ENFUVIRTIDE; GLYCOPROTEIN GP 120; GLYCOPROTEIN GP 41; INTERFERON; LECTIN; LOW DENSITY LIPOPROTEIN RECEPTOR; MEMBRANE PROTEIN; N [4 [[[6,7 DIHYDRO 2 (4 METHYLPHENYL) 5H BENZOCYCLOHEPTEN 8 YL]CARBONYL]AMINO]BENZYL] N,N DIMETHYL 2H TETRAHYDROPYRAN 4 AMINIUM CHLORIDE; PROTEIN INHIBITOR; PROTEINASE; RIBAVIRIN; SCH C; T 1249; T 134; T 22; TETRASPANIN; UNCLASSIFIED DRUG; UNINDEXED DRUG; VIRUS ENVELOPE PROTEIN; VIRUS FUSION PROTEIN; VIRUS RECEPTOR; VIRUS RNA;

EID: 6944223883     PISSN: 13816128     EISSN: None     Source Type: Journal    
DOI: 10.2174/1381612043382729     Document Type: Review
Times cited : (54)

References (155)
  • 2
    • 0026465468 scopus 로고
    • A synthetic peptide inhibitor of human immunodeficiency virus replication: Correlation between solution structure and viral inhibition
    • Wild C, Oas T, McDanal C, Bolognesi D, Matthews T. A synthetic peptide inhibitor of human immunodeficiency virus replication: correlation between solution structure and viral inhibition. Proc Natl Acad Sci USA 1992; 89: 10537-41.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10537-10541
    • Wild, C.1    Oas, T.2    McDanal, C.3    Bolognesi, D.4    Matthews, T.5
  • 3
    • 0031729823 scopus 로고    scopus 로고
    • Potent suppression of HIV-1 replication in humans by T-20, a peptide inhibitor of gp41-mediated virus entry
    • Kilby JM, Hopkins S, Venetta TM, DiMassimo B, Cloud GA, Lee JY, et al. Potent suppression of HIV-1 replication in humans by T-20, a peptide inhibitor of gp41-mediated virus entry. Nat Med 1998; 4: 1302-7.
    • (1998) Nat. Med. , vol.4 , pp. 1302-1307
    • Kilby, J.M.1    Hopkins, S.2    Venetta, T.M.3    DiMassimo, B.4    Cloud, G.A.5    Lee, J.Y.6
  • 4
    • 0038407687 scopus 로고    scopus 로고
    • DC-SIGN: A novel HIV receptor on DCs that mediates HIV-1 transmission
    • Geijtenbeek TB, van Kooyk Y. DC-SIGN: a novel HIV receptor on DCs that mediates HIV-1 transmission. Curr Top Microbiol Immunol 2003; 276: 31-54.
    • (2003) Curr. Top Microbiol. Immunol. , vol.276 , pp. 31-54
    • Geijtenbeek, T.B.1    van Kooyk, Y.2
  • 5
    • 0034598905 scopus 로고    scopus 로고
    • DC-SIGN, a dendritic cell-specific HIV-1-binding protein that enhances trans-infection of T cells
    • Geijtenbeek TB, Kwon DS, Torensma R, van Vliet SJ, van Duijnhoven GC, Middel J, et al. DC-SIGN, a dendritic cell-specific HIV-1-binding protein that enhances trans-infection of T cells. Cell 2000; 100: 587-97.
    • (2000) Cell , vol.100 , pp. 587-597
    • Geijtenbeek, T.B.1    Kwon, D.S.2    Torensma, R.3    van Vliet, S.J.4    van Duijnhoven, G.C.5    Middel, J.6
  • 7
    • 0034598934 scopus 로고    scopus 로고
    • Identification of DC-SIGN, a novel dendritic cell-specific ICAM-3 receptor that supports primary immune responses
    • Geijtenbeek TB, Torensma R, van Vliet SJ, van Duijnhoven GC, Adema GJ, van Kooyk Y, et al. Identification of DC-SIGN, a novel dendritic cell-specific ICAM-3 receptor that supports primary immune responses. Cell 2000; 100: 575-85.
    • (2000) Cell , vol.100 , pp. 575-585
    • Geijtenbeek, T.B.1    Torensma, R.2    van Vliet, S.J.3    van Duijnhoven, G.C.4    Adema, G.J.5    van Kooyk, Y.6
  • 8
    • 0344643425 scopus 로고    scopus 로고
    • Unique appearance of proliferating antigen-presenting cells expressing DC-SIGN (CD209) in the decidua of early human pregnancy
    • Kammerer U, Eggert AO, Kapp M, McLellan AD, Geijtenbeek TB, Dietl J, et al. Unique appearance of proliferating antigen-presenting cells expressing DC-SIGN (CD209) in the decidua of early human pregnancy. Am J Pathol 2003; 162: 887-96.
    • (2003) Am. J. Pathol. , vol.162 , pp. 887-896
    • Kammerer, U.1    Eggert, A.O.2    Kapp, M.3    McLellan, A.D.4    Geijtenbeek, T.B.5    Dietl, J.6
  • 9
    • 0036499125 scopus 로고    scopus 로고
    • The dendritic cell-specific adhesion receptor DC-SIGN internalizes antigen for presentation to T cells
    • Engering A, Geijtenbeek TB, van Vliet SJ, Wijers M, van Liempt E, Demaurex N, et al. The dendritic cell-specific adhesion receptor DC-SIGN internalizes antigen for presentation to T cells. J Immunol 2002; 168: 2118-26.
    • (2002) J. Immunol. , vol.168 , pp. 2118-2126
    • Engering, A.1    Geijtenbeek, T.B.2    van Vliet, S.J.3    Wijers, M.4    van Liempt, E.5    Demaurex, N.6
  • 12
    • 0036278649 scopus 로고    scopus 로고
    • C-type lectins DC-SIGN and L-SIGN mediate cellular entry by Ebola virus in cis and in trans
    • Alvarez CP, Lasala F, Carrillo J, Muniz O, Corbi AL, Delgado R. C-type lectins DC-SIGN and L-SIGN mediate cellular entry by Ebola virus in cis and in trans. J Virol 2002; 76: 6841-4.
    • (2002) J. Virol. , vol.76 , pp. 6841-6844
    • Alvarez, C.P.1    Lasala, F.2    Carrillo, J.3    Muniz, O.4    Corbi, A.L.5    Delgado, R.6
  • 15
    • 0037379186 scopus 로고    scopus 로고
    • Hepatitis C virus glycoproteins interact with DC-SIGN and DC-SIGNR
    • Pohlmann S, Zhang J, Baribaud F, Chen Z, Leslie GJ, Lin G, et al. Hepatitis C virus glycoproteins interact with DC-SIGN and DC-SIGNR. J Virol 2003; 77: 4070-80.
    • (2003) J. Virol. , vol.77 , pp. 4070-4080
    • Pohlmann, S.1    Zhang, J.2    Baribaud, F.3    Chen, Z.4    Leslie, G.J.5    Lin, G.6
  • 16
    • 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
    • Navarro-Sanchez E, Altmeyer R, Amara A, Schwartz O, Fieschi F, Virelizier JL, et al. 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 2003; 4: 723-8.
    • (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
  • 18
    • 18744366087 scopus 로고    scopus 로고
    • Human cytomegalovirus binding to DC-SIGN is required for dendritic cell infection and target cell trans-infection
    • Halary F, Amara A, Lortat-Jacob H, Messerle M, Delaunay T, Houles C, et al. Human cytomegalovirus binding to DC-SIGN is required for dendritic cell infection and target cell trans-infection. Immunity 2002; 17: 653-64.
    • (2002) Immunity , vol.17 , pp. 653-664
    • Halary, F.1    Amara, A.2    Lortat-Jacob, H.3    Messerle, M.4    Delaunay, T.5    Houles, C.6
  • 19
    • 0035800757 scopus 로고    scopus 로고
    • A novel mechanism of carbohydrate recognition by the C-type lectins DC-SIGN and DC-SIGNR. Subunit organization and binding to multivalent ligands
    • Mitchell DA, Fadden AJ, Drickamer K. A novel mechanism of carbohydrate recognition by the C-type lectins DC-SIGN and DC-SIGNR. Subunit organization and binding to multivalent ligands. J Biol Chem 2001; 276: 28939-45.
    • (2001) J. Biol. Chem. , vol.276 , pp. 28939-28945
    • Mitchell, D.A.1    Fadden, A.J.2    Drickamer, K.3
  • 20
    • 0035824446 scopus 로고    scopus 로고
    • Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR
    • Feinberg H, Mitchell DA, Drickamer K, Weis WI. Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR. Science 2001; 294: 2163-6.
    • (2001) Science , vol.294 , pp. 2163-2166
    • Feinberg, H.1    Mitchell, D.A.2    Drickamer, K.3    Weis, W.I.4
  • 21
    • 0035956986 scopus 로고    scopus 로고
    • DC-SIGNR, a DC-SIGN homologue expressed in endothelial cells, binds to human and simian immunodeficiency viruses and activates infection in trans
    • Pohlmann S, Soilleux EJ, Baribaud F, Leslie GJ, Morris LS, Trowsdale J, et al. DC-SIGNR, a DC-SIGN homologue expressed in endothelial cells, binds to human and simian immunodeficiency viruses and activates infection in trans. Proc Natl Acad Sci USA 2001; 98: 2670-5.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2670-2675
    • Pohlmann, S.1    Soilleux, E.J.2    Baribaud, F.3    Leslie, G.J.4    Morris, L.S.5    Trowsdale, J.6
  • 22
    • 0035911220 scopus 로고    scopus 로고
    • A dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin (DC-SIGN)-related protein is highly expressed on human liver sinusoidal endothelial cells and promotes HIV-1 infection
    • Bashirova AA, Geijtenbeek TB, van Duijnhoven GC, van Vliet SJ, Eilering JB, Martin MP, et al. A dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin (DC-SIGN)-related protein is highly expressed on human liver sinusoidal endothelial cells and promotes HIV-1 infection. J Exp Med 2001; 193: 671-8.
    • (2001) J. Exp. Med. , vol.193 , pp. 671-678
    • Bashirova, A.A.1    Geijtenbeek, T.B.2    van Duijnhoven, G.C.3    van Vliet, S.J.4    Eilering, J.B.5    Martin, M.P.6
  • 23
    • 0034813206 scopus 로고    scopus 로고
    • Endothelial cell-mediated uptake of a hepatitis B virus: A new concept of liver targeting of hepatotropic microorganisms
    • Breiner KM, Schaller H, Knolle PA. Endothelial cell-mediated uptake of a hepatitis B virus: a new concept of liver targeting of hepatotropic microorganisms. Hepatology 2001; 34: 803-8.
    • (2001) Hepatology , vol.34 , pp. 803-808
    • Breiner, K.M.1    Schaller, H.2    Knolle, P.A.3
  • 24
    • 0031820273 scopus 로고    scopus 로고
    • The C-type lectin superfamily in the immune system
    • Weis WI, Taylor ME, Drickamer K. The C-type lectin superfamily in the immune system. Immunol Rev 1998; 163: 19-34.
    • (1998) Immunol. Rev. , vol.163 , pp. 19-34
    • Weis, W.I.1    Taylor, M.E.2    Drickamer, K.3
  • 25
    • 0028232179 scopus 로고
    • Binding of sugar ligands to Ca(2+)-dependent animal lectins. I. Analysis of mannose binding by site-directed mutagenesis and NMR
    • Iobst ST, Wormald MR, Weis WI, Dwek RA, Drickamer K. Binding of sugar ligands to Ca(2+)-dependent animal lectins. I. Analysis of mannose binding by site-directed mutagenesis and NMR. J Biol Chem 1994; 269: 15505-11.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15505-15511
    • Iobst, S.T.1    Wormald, M.R.2    Weis, W.I.3    Dwek, R.A.4    Drickamer, K.5
  • 26
    • 18544381567 scopus 로고    scopus 로고
    • The macrophage C-type lectin specific for galactose/N-acetylgalactosamine is an endocytic receptor expressed on monocyte-derived immature dendritic cells
    • Higashi N, Fujioka K, Denda-Nagai K, Hashimoto S, Nagai S, Sato T, et al. The macrophage C-type lectin specific for galactose/N-acetylgalactosamine is an endocytic receptor expressed on monocyte-derived immature dendritic cells. J Biol Chem 2002; 277: 20686-93.
    • (2002) J. Biol. Chem. , vol.277 , pp. 20686-20693
    • Higashi, N.1    Fujioka, K.2    Denda-Nagai, K.3    Hashimoto, S.4    Nagai, S.5    Sato, T.6
  • 27
    • 0035988217 scopus 로고    scopus 로고
    • Human macrophage lectin specific for galactose/N-acetylgalactosamine is a marker for cells at an intermediate stage in their differentiation from monocytes into macrophages
    • Higashi N, Morikawa A, Fujioka K, Fujita Y, Sano Y, Miyata-Takeuchi M, et al. Human macrophage lectin specific for galactose/N-acetylgalactosamine is a marker for cells at an intermediate stage in their differentiation from monocytes into macrophages. Int Immunol 2002; 14: 545-54.
    • (2002) Int. Immunol. , vol.14 , pp. 545-554
    • Higashi, N.1    Morikawa, A.2    Fujioka, K.3    Fujita, Y.4    Sano, Y.5    Miyata-Takeuchi, M.6
  • 28
    • 0037227929 scopus 로고    scopus 로고
    • Differential N-linked glycosylation of human immunodeficiency virus and Ebola virus envelope glycoproteins modulates interactions with DC-SIGN and DC-SIGNR
    • Lin G, Simmons G, Pohlmann S, Baribaud F, Ni H, Leslie GJ, et al. Differential N-linked glycosylation of human immunodeficiency virus and Ebola virus envelope glycoproteins modulates interactions with DC-SIGN and DC-SIGNR. J Virol 2003; 77: 1337-46.
    • (2003) J. Virol. , vol.77 , pp. 1337-1346
    • Lin, G.1    Simmons, G.2    Pohlmann, S.3    Baribaud, F.4    Ni, H.5    Leslie, G.J.6
  • 29
    • 0026756506 scopus 로고
    • Sequence and expression of a membrane-associated C-type lectin that exhibits CD4-independent binding of human immunodeficiency virus envelope glycoprotein gp120
    • Curtis BM, Scharnowske S, Watson AJ. Sequence and expression of a membrane-associated C-type lectin that exhibits CD4-independent binding of human immunodeficiency virus envelope glycoprotein gp120. Proc Natl Acad Sci USA 1992; 89: 8356-60.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8356-8360
    • Curtis, B.M.1    Scharnowske, S.2    Watson, A.J.3
  • 30
    • 0025292252 scopus 로고
    • Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells
    • Leonard CK, Spellman MW, Riddle L, Harris RJ, Thomas JN, Gregory TJ. Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells. J Biol Chem 1990; 265: 10373-82.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10373-10382
    • Leonard, C.K.1    Spellman, M.W.2    Riddle, L.3    Harris, R.J.4    Thomas, J.N.5    Gregory, T.J.6
  • 31
    • 0036314488 scopus 로고    scopus 로고
    • Differential transmission of human immunodeficiency virus type 1 by distinct subsets of effector dendritic cells
    • Sanders RW, de Jong EC, Baldwin CE, Schuitemaker JH, Kapsenberg ML, Berkhout B. Differential transmission of human immunodeficiency virus type 1 by distinct subsets of effector dendritic cells. J Virol 2002; 76: 7812-21.
    • (2002) J. Virol. , vol.76 , pp. 7812-7821
    • Sanders, R.W.1    de Jong, E.C.2    Baldwin, C.E.3    Schuitemaker, J.H.4    Kapsenberg, M.L.5    Berkhout, B.6
  • 33
    • 0036172314 scopus 로고    scopus 로고
    • DC-SIGN-mediated internalization of HIV is required for trans-enhancement of T cell infection
    • Kwon DS, Gregorio G, Bitton N, Hendrickson WA, Littman DR. DC-SIGN-mediated internalization of HIV is required for trans-enhancement of T cell infection. Immunity 2002; 16: 135-44.
    • (2002) Immunity , vol.16 , pp. 135-144
    • Kwon, D.S.1    Gregorio, G.2    Bitton, N.3    Hendrickson, W.A.4    Littman, D.R.5
  • 34
    • 0035194354 scopus 로고    scopus 로고
    • cis Expression of DC-SIGN allows for more efficient entry of human and simian immunodeficiency viruses via CD4 and a coreceptor
    • Lee B, Leslie G, Soilleux E, O'Doherty U, Baik S, Levroney E, et al. cis Expression of DC-SIGN allows for more efficient entry of human and simian immunodeficiency viruses via CD4 and a coreceptor. J Virol 2001; 75: 12028-38.
    • (2001) J. Virol. , vol.75 , pp. 12028-12038
    • Lee, B.1    Leslie, G.2    Soilleux, E.3    O'Doherty, U.4    Baik, S.5    Levroney, E.6
  • 36
    • 0036889170 scopus 로고    scopus 로고
    • Capture and transfer of simian immunodeficiency virus by macaque dendritic cells is enhanced by DC-SIGN
    • Yu Kimata MT, Cella M, Biggins JE, Rorex C, White R, Hicks S, et al. Capture and transfer of simian immunodeficiency virus by macaque dendritic cells is enhanced by DC-SIGN. J Virol 2002; 76: 11827-36.
    • (2002) J. Virol. , vol.76 , pp. 11827-11836
    • Yu Kimata, M.T.1    Cella, M.2    Biggins, J.E.3    Rorex, C.4    White, R.5    Hicks, S.6
  • 37
    • 0034051289 scopus 로고    scopus 로고
    • Simian immunodeficiency virus rapidly penetrates the cervicovaginal mucosa after intravaginal inoculation and infects intraepithelial dendritic cells
    • Hu J, Gardner MB, Miller CJ. Simian immunodeficiency virus rapidly penetrates the cervicovaginal mucosa after intravaginal inoculation and infects intraepithelial dendritic cells. J Virol 2000; 74: 6087-95.
    • (2000) J. Virol. , vol.74 , pp. 6087-6095
    • Hu, J.1    Gardner, M.B.2    Miller, C.J.3
  • 38
    • 1342290514 scopus 로고    scopus 로고
    • Productive infection of dendritic cells by simian immunodeficiency virus in macaque intestinal tissues
    • Choi YK, Whelton KM, Mlechick B, Murphey-Corb MA, Reinhart TA. Productive infection of dendritic cells by simian immunodeficiency virus in macaque intestinal tissues. J Pathol 2003; 201: 616-28.
    • (2003) J. Pathol. , vol.201 , pp. 616-628
    • Choi, Y.K.1    Whelton, K.M.2    Mlechick, B.3    Murphey-Corb, M.A.4    Reinhart, T.A.5
  • 39
    • 0036387133 scopus 로고    scopus 로고
    • Distribution and immunophenotype of DC-SIGN-expressing cells in SIV-infected and uninfected macaques
    • Schwartz AJ, Alvarez X, Lackner AA. Distribution and immunophenotype of DC-SIGN-expressing cells in SIV-infected and uninfected macaques. AIDS Res Hum Retroviruses 2002; 18: 1021-9.
    • (2002) AIDS Res. Hum. Retroviruses , vol.18 , pp. 1021-1029
    • Schwartz, A.J.1    Alvarez, X.2    Lackner, A.A.3
  • 40
    • 0036149902 scopus 로고    scopus 로고
    • Expression of DC-SIGN by dendritic cells of intestinal and genital mucosae in humans and rhesus macaques
    • Jameson B, Baribaud F, Pohlmann S, Ghavimi D, Mortari F, Doms RW, et al. Expression of DC-SIGN by dendritic cells of intestinal and genital mucosae in humans and rhesus macaques. J Virol 2002; 76: 1866-75.
    • (2002) J. Virol. , vol.76 , pp. 1866-1875
    • Jameson, B.1    Baribaud, F.2    Pohlmann, S.3    Ghavimi, D.4    Mortari, F.5    Doms, R.W.6
  • 42
    • 18344387519 scopus 로고    scopus 로고
    • Structure of dengue virus: Implications for flavivirus organization, maturation, and fusion
    • Kuhn RJ, Zhang W, Rossmann MG, Pletnev SV, Corver J, Lenches E, et al. Structure of dengue virus: implications for flavivirus organization, maturation, and fusion. Cell 2002; 108: 717-25.
    • (2002) Cell , vol.108 , pp. 717-725
    • Kuhn, R.J.1    Zhang, W.2    Rossmann, M.G.3    Pletnev, S.V.4    Corver, J.5    Lenches, E.6
  • 43
    • 0033602564 scopus 로고    scopus 로고
    • Analysis of the steps involved in Dengue virus entry into host cells
    • Hung SL, Lee PL, Chen HW, Chen LK, Kao CL, King CC. Analysis of the steps involved in Dengue virus entry into host cells. Virology 1999; 257: 156-67.
    • (1999) Virology , vol.257 , pp. 156-167
    • Hung, S.L.1    Lee, P.L.2    Chen, H.W.3    Chen, L.K.4    Kao, C.L.5    King, C.C.6
  • 44
    • 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
    • Johnson AJ, Guirakhoo F, Roehrig JT. The envelope glycoproteins of dengue 1 and dengue 2 viruses grown in mosquito cells differ in their utilization of potential glycosylation sites. Virology 1994; 203: 241-9.
    • (1994) Virology , vol.203 , pp. 241-249
    • Johnson, A.J.1    Guirakhoo, F.2    Roehrig, J.T.3
  • 46
    • 0033915304 scopus 로고    scopus 로고
    • Dengue virus and dendritic cells
    • Palucka AK. Dengue virus and dendritic cells. Nat Med 2000; 6: 748-9.
    • (2000) Nat. Med. , vol.6 , pp. 748-749
    • Palucka, A.K.1
  • 49
    • 0242363253 scopus 로고    scopus 로고
    • DC-SIGN and L-SIGN can act as attachment receptors for alphaviruses and distinguish between mosquito cell- and mammalian cell-derived viruses
    • Klimstra WB, Nangle EM, Smith MS, Yurochko AD, Ryman KD. DC-SIGN and L-SIGN can act as attachment receptors for alphaviruses and distinguish between mosquito cell- and mammalian cell-derived viruses. J Virol 2003; 77: 12022-32.
    • (2003) J. Virol. , vol.77 , pp. 12022-12032
    • Klimstra, W.B.1    Nangle, E.M.2    Smith, M.S.3    Yurochko, A.D.4    Ryman, K.D.5
  • 51
    • 0001606930 scopus 로고    scopus 로고
    • Hepatitis C Viruses
    • Knipe, editor. Philadelphia: Lippincott Williams & Wilkins
    • Major ME, Rehermann B, Feinstone SM. Hepatitis C Viruses. In: Knipe, editor. Fields Virology. Philadelphia: Lippincott Williams & Wilkins; 2001; p. 1127-1162.
    • (2001) Fields Virology , pp. 1127-1162
    • Major, M.E.1    Rehermann, B.2    Feinstone, S.M.3
  • 52
    • 0034023295 scopus 로고    scopus 로고
    • The role of the hepatitis C virus glycoproteins in infection
    • Flint M, McKeating JA. The role of the hepatitis C virus glycoproteins in infection. Rev Med Virol 2000; 10: 101-17.
    • (2000) Rev. Med. Virol. , vol.10 , pp. 101-117
    • Flint, M.1    McKeating, J.A.2
  • 53
    • 0034775964 scopus 로고    scopus 로고
    • Biogenesis of hepatitis C virus envelope glycoproteins
    • Op De Beeck A, Cocquerel L, Dubuisson J. Biogenesis of hepatitis C virus envelope glycoproteins. J Gen Virol 2001; 82: 2589-95.
    • (2001) J. Gen. Virol. , vol.82 , pp. 2589-2595
    • Op De Beeck, A.1    Cocquerel, L.2    Dubuisson, J.3
  • 54
    • 0033992596 scopus 로고    scopus 로고
    • Folding, assembly and subcellular localization of hepatitis C virus glycoproteins
    • Dubuisson J. Folding, assembly and subcellular localization of hepatitis C virus glycoproteins. Curr Top Microbiol Immunol 2000; 242: 135-48.
    • (2000) Curr. Top Microbiol. Immunol. , vol.242 , pp. 135-148
    • Dubuisson, J.1
  • 55
    • 0040211559 scopus 로고    scopus 로고
    • The transmembrane domains of hepatitis C virus envelope glycoproteins E1 and E2 play a major role in heterodimerization
    • Op De Beeck A, Montserret R, Duvet S, Cocquerel L, Cacan R, Barberot B, et al. The transmembrane domains of hepatitis C virus envelope glycoproteins E1 and E2 play a major role in heterodimerization. J Biol Chem 2000; 275: 31428-37.
    • (2000) J. Biol. Chem. , vol.275 , pp. 31428-31437
    • Op De Beeck, A.1    Montserret, R.2    Duvet, S.3    Cocquerel, L.4    Cacan, R.5    Barberot, B.6
  • 56
    • 0037124347 scopus 로고    scopus 로고
    • Topological changes in the transmembrane domains of hepatitis C virus envelope glycoproteins
    • Cocquerel L, Op de Beeck A, Lambot M, Roussel J, Delgrange D, Pillez A, et al. Topological changes in the transmembrane domains of hepatitis C virus envelope glycoproteins. EMBO J 2002; 21: 2893-902.
    • (2002) EMBO J. , vol.21 , pp. 2893-2902
    • Cocquerel, L.1    Op de Beeck, A.2    Lambot, M.3    Roussel, J.4    Delgrange, D.5    Pillez, A.6
  • 57
    • 0031911782 scopus 로고    scopus 로고
    • A retention signal necessary and sufficient for endoplasmic reticulum localization maps to the transmembrane domain of hepatitis C virus glycoprotein E2
    • Cocquerel L, Meunier JC, Pillez A, Wychowski C, Dubuisson J. A retention signal necessary and sufficient for endoplasmic reticulum localization maps to the transmembrane domain of hepatitis C virus glycoprotein E2. J Virol 1998; 72: 2183-91.
    • (1998) J. Virol. , vol.72 , pp. 2183-2191
    • Cocquerel, L.1    Meunier, J.C.2    Pillez, A.3    Wychowski, C.4    Dubuisson, J.5
  • 58
    • 0033050645 scopus 로고    scopus 로고
    • The transmembrane domain of hepatitis C virus glycoprotein E1 is a signal for static retention in the endoplasmic reticulum
    • Cocquerel L, Duvet S, Meunier JC, Pillez A, Cacan R, Wychowski C, et al. The transmembrane domain of hepatitis C virus glycoprotein E1 is a signal for static retention in the endoplasmic reticulum. J Virol 1999; 73: 2641-9.
    • (1999) J. Virol. , vol.73 , pp. 2641-2649
    • Cocquerel, L.1    Duvet, S.2    Meunier, J.C.3    Pillez, A.4    Cacan, R.5    Wychowski, C.6
  • 59
    • 0036145390 scopus 로고    scopus 로고
    • Binding of hepatitis C virus-like particles derived from infectious clone H77C to defined human cell lines
    • Wellnitz S, Klumpp B, Barth H, Ito S, Depla E, Dubuisson J, et al. Binding of hepatitis C virus-like particles derived from infectious clone H77C to defined human cell lines. J Virol 2002; 76: 1181-93.
    • (2002) J. Virol. , vol.76 , pp. 1181-1193
    • Wellnitz, S.1    Klumpp, B.2    Barth, H.3    Ito, S.4    Depla, E.5    Dubuisson, J.6
  • 60
    • 0031977996 scopus 로고    scopus 로고
    • Hepatitis C virus structural proteins assemble into viruslike particles in insect cells
    • Baumert TF, Ito S, Wong DT, Liang TJ. Hepatitis C virus structural proteins assemble into viruslike particles in insect cells. J Virol 1998; 72: 3827-36.
    • (1998) J. Virol. , vol.72 , pp. 3827-3836
    • Baumert, T.F.1    Ito, S.2    Wong, D.T.3    Liang, T.J.4
  • 62
    • 0033932001 scopus 로고    scopus 로고
    • Recovery, persistence, and sequelae in hepatitis C virus infection: A perspective on long-term outcome
    • Alter HJ, Seeff LB. Recovery, persistence, and sequelae in hepatitis C virus infection: a perspective on long-term outcome. Semin Liver Dis 2000; 20: 17-35.
    • (2000) Semin. Liver Dis. , vol.20 , pp. 17-35
    • Alter, H.J.1    Seeff, L.B.2
  • 63
    • 0031904712 scopus 로고    scopus 로고
    • Detection of widespread hepatocyte infection in chronic hepatitis C
    • Agnello V, Abel G, Knight GB, Muchmore E. Detection of widespread hepatocyte infection in chronic hepatitis C. Hepatology 1998; 28: 573-84.
    • (1998) Hepatology , vol.28 , pp. 573-584
    • Agnello, V.1    Abel, G.2    Knight, G.B.3    Muchmore, E.4
  • 64
    • 0027935048 scopus 로고
    • Demonstration of in vitro infection of chimpanzee hepatocytes with hepatitis C virus using strand-specific RT/PCR
    • Lanford RE, Sureau C, Jacob JR, White R, Fuerst TR. Demonstration of in vitro infection of chimpanzee hepatocytes with hepatitis C virus using strand-specific RT/PCR. Virology 1994; 202: 606-14.
    • (1994) Virology , vol.202 , pp. 606-614
    • Lanford, R.E.1    Sureau, C.2    Jacob, J.R.3    White, R.4    Fuerst, T.R.5
  • 65
    • 0032525264 scopus 로고    scopus 로고
    • In vivo tropism of hepatitis C virus genomic sequences in hematopoietic cells: Influence of viral load, viral genotype, and cell phenotype
    • Lerat H, Rumin S, Habersetzer F, Berby F, Trabaud MA, Trepo C, et al. In vivo tropism of hepatitis C virus genomic sequences in hematopoietic cells: influence of viral load, viral genotype, and cell phenotype. Blood 1998; 91: 3841-9.
    • (1998) Blood , vol.91 , pp. 3841-3849
    • Lerat, H.1    Rumin, S.2    Habersetzer, F.3    Berby, F.4    Trabaud, M.A.5    Trepo, C.6
  • 67
    • 0037416146 scopus 로고    scopus 로고
    • Infectious hepatitis C virus pseudo-particles containing functional E1-E2 envelope protein complexes
    • Bartosch B, Dubuisson J, Cosset FL. Infectious hepatitis C virus pseudo-particles containing functional E1-E2 envelope protein complexes. J Exp Med 2003; 197: 633-42.
    • (2003) J. Exp. Med. , vol.197 , pp. 633-642
    • Bartosch, B.1    Dubuisson, J.2    Cosset, F.L.3
  • 68
    • 0344011988 scopus 로고    scopus 로고
    • Mannosyl Glycodendritic Structure Inhibits DC-SIGN-Mediated Ebola Virus Infection in cis and in trans
    • Lasala F, Arce E, Otero JR, Rojo J, Delgado R. Mannosyl Glycodendritic Structure Inhibits DC-SIGN-Mediated Ebola Virus Infection in cis and in trans. Antimicrob Agents Chemother 2003; 47: 3970-2.
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 3970-3972
    • Lasala, F.1    Arce, E.2    Otero, J.R.3    Rojo, J.4    Delgado, R.5
  • 69
    • 0037592165 scopus 로고    scopus 로고
    • Oligolysine-based oligosaccharide clusters: Selective recognition and endocytosis by the mannose receptor and dendritic cell-specific intercellular adhesion molecule 3 (ICAM-3)-grabbing nonintegrin
    • Frison N, Taylor ME, Soilleux E, Bousser MT, Mayer R, Monsigny M, et al. Oligolysine-based oligosaccharide clusters: selective recognition and endocytosis by the mannose receptor and dendritic cell-specific intercellular adhesion molecule 3 (ICAM-3)-grabbing nonintegrin. J Biol Chem 2003; 278: 23922-9.
    • (2003) J. Biol. Chem. , vol.278 , pp. 23922-23929
    • Frison, N.1    Taylor, M.E.2    Soilleux, E.3    Bousser, M.T.4    Mayer, R.5    Monsigny, M.6
  • 70
    • 0035815282 scopus 로고    scopus 로고
    • The Fusion glycoprotein shell of Semliki Forest virus: An icosahedral assembly primed for fusogenic activation at endosomal pH
    • Lescar J, Roussel A, Wien MW, Navaza J, Fuller SD, Wengler G, et al. The Fusion glycoprotein shell of Semliki Forest virus: an icosahedral assembly primed for fusogenic activation at endosomal pH. Cell 2001; 105: 137-48.
    • (2001) Cell , vol.105 , pp. 137-148
    • Lescar, J.1    Roussel, A.2    Wien, M.W.3    Navaza, J.4    Fuller, S.D.5    Wengler, G.6
  • 71
    • 0032431055 scopus 로고    scopus 로고
    • Coiled coils in both intracellular vesicle and viral membrane fusion
    • Skehel JJ, Wiley DC. Coiled coils in both intracellular vesicle and viral membrane fusion. Cell 1998; 95: 871-4.
    • (1998) Cell , vol.95 , pp. 871-874
    • Skehel, J.J.1    Wiley, D.C.2
  • 72
    • 0029014434 scopus 로고
    • The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution
    • Rey FA, Heinz FX, Mandl C, Kunz C, Harrison SC. The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution. Nature 1995; 375: 291-8.
    • (1995) Nature , vol.375 , pp. 291-298
    • Rey, F.A.1    Heinz, F.X.2    Mandl, C.3    Kunz, C.4    Harrison, S.C.5
  • 74
    • 0038810275 scopus 로고    scopus 로고
    • Dengue virus envelope glycoprotein structure: New insight into its interactions during viral entry
    • Rey FA. Dengue virus envelope glycoprotein structure: new insight into its interactions during viral entry. Proc Natl Acad Sci USA 2003; 100: 6899-901.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6899-6901
    • Rey, F.A.1
  • 75
    • 0034634615 scopus 로고    scopus 로고
    • Processing, stability, and receptor binding properties of oligomeric envelope glycoprotein from a primary HIV-1 isolate
    • Staropoli I, Chanel C, Girard M, Altmeyer R. Processing, stability, and receptor binding properties of oligomeric envelope glycoprotein from a primary HIV-1 isolate. J Biol Chem 2000; 275: 35137-45.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35137-35145
    • Staropoli, I.1    Chanel, C.2    Girard, M.3    Altmeyer, R.4
  • 76
    • 0025095635 scopus 로고
    • Oligomeric structure of the human immunodeficiency virus type 1 envelope glycoprotein
    • Earl PL, Doms RW, Moss B. Oligomeric structure of the human immunodeficiency virus type 1 envelope glycoprotein. Proc Natl Acad Sci USA 1990; 87: 648-52.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 648-652
    • Earl, P.L.1    Doms, R.W.2    Moss, B.3
  • 77
    • 0026029621 scopus 로고
    • Folding, interaction with GRP78-BiP, assembly, and transport of the human immunodeficiency virus type 1 envelope protein
    • Earl PL, Moss B, Doms RW. Folding, interaction with GRP78-BiP, assembly, and transport of the human immunodeficiency virus type 1 envelope protein. J Virol 1991; 65: 2047-55.
    • (1991) J. Virol. , vol.65 , pp. 2047-2055
    • Earl, P.L.1    Moss, B.2    Doms, R.W.3
  • 78
    • 0026716831 scopus 로고
    • Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gp160
    • Hallenberger S, Bosch V, Angliker H, Shaw E, Klenk HD, Garten W. Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gp160. Nature 1992; 360: 358-61.
    • (1992) Nature , vol.360 , pp. 358-361
    • Hallenberger, S.1    Bosch, V.2    Angliker, H.3    Shaw, E.4    Klenk, H.D.5    Garten, W.6
  • 80
    • 0029964418 scopus 로고    scopus 로고
    • Biophysical characterization of recombinant proteins expressing the leucine zipper-like domain of the human immunodeficiency virus type 1 transmembrane protein gp41
    • Shugars DC, Wild CT, Greenwell TK, Matthews TJ. Biophysical characterization of recombinant proteins expressing the leucine zipper-like domain of the human immunodeficiency virus type 1 transmembrane protein gp41. Journal of Virology 1996; 70: 2982-91.
    • (1996) Journal of Virology , vol.70 , pp. 2982-2991
    • Shugars, D.C.1    Wild, C.T.2    Greenwell, T.K.3    Matthews, T.J.4
  • 81
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan DC, Fass D, Berger JM, Kim PS. Core structure of gp41 from the HIV envelope glycoprotein. Cell 1997; 89: 263-73.
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 82
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • Skehel JJ, Wiley DC. Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin. Annual Review of Biochemistry 2000; 69: 531-569.
    • (2000) Annual Review of Biochemistry , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 83
    • 0026069632 scopus 로고
    • Human immunodeficiency virus type 1 gp120 envelope glycoprotein regions important for association with the gp41 transmembrane glycoprotein
    • Helseth E, Olshevsky U, Furman C, Sodroski J. Human immunodeficiency virus type 1 gp120 envelope glycoprotein regions important for association with the gp41 transmembrane glycoprotein. Journal of Virology 1991; 65: 2119-23.
    • (1991) Journal of Virology , vol.65 , pp. 2119-2123
    • Helseth, E.1    Olshevsky, U.2    Furman, C.3    Sodroski, J.4
  • 84
    • 0032546844 scopus 로고    scopus 로고
    • The HIV-1 envelope glycoproteins: Fusogens, antigens, and immunogens
    • [Review]
    • Wyatt R, Sodroski J. The HIV-1 envelope glycoproteins: Fusogens, antigens, and immunogens [Review]. Science 1998; 280: 1884-1888.
    • (1998) Science , vol.280 , pp. 1884-1888
    • Wyatt, R.1    Sodroski, J.2
  • 85
    • 0023028190 scopus 로고
    • The T4 gene encodes the AIDS virus receptor and is expressed in the immune system and the brain
    • Maddon PJ, Dalgleish AG, McDougal JS, Clapham PR, Weiss RA, Axel R. The T4 gene encodes the AIDS virus receptor and is expressed in the immune system and the brain. Cell 1986; 47: 333-48.
    • (1986) Cell , vol.47 , pp. 333-348
    • Maddon, P.J.1    Dalgleish, A.G.2    McDougal, J.S.3    Clapham, P.R.4    Weiss, R.A.5    Axel, R.6
  • 86
    • 15844419153 scopus 로고    scopus 로고
    • Identification of a major co-receptor for primary isolates of HIV-1
    • [see comments]
    • Deng H, Liu R, Ellmeier W, Choe S, Unutmaz D, Burkhart M, et al. Identification of a major co-receptor for primary isolates of HIV-1 [see comments]. Nature 1996; 381: 661-6.
    • (1996) Nature , vol.381 , pp. 661-666
    • Deng, H.1    Liu, R.2    Ellmeier, W.3    Choe, S.4    Unutmaz, D.5    Burkhart, M.6
  • 87
    • 0030002637 scopus 로고    scopus 로고
    • HIV-1 entry cofactor: Functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor
    • [see comments]
    • Feng Y, Broder CC, Kennedy PE, Berger EA. HIV-1 entry cofactor: functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor [see comments]. Science 1996; 272: 872-7.
    • (1996) Science , vol.272 , pp. 872-877
    • Feng, Y.1    Broder, C.C.2    Kennedy, P.E.3    Berger, E.A.4
  • 88
    • 0030604727 scopus 로고    scopus 로고
    • A dual-tropic primary HIV-1 isolate that uses fusin and the beta-chemokine receptors CKR-5, CKR-3, and CKR-2b as fusion cofactors
    • Doranz BJ, Rucker J, Yi Y, Smyth RJ, Samson M, Peiper SC, et al. A dual-tropic primary HIV-1 isolate that uses fusin and the beta-chemokine receptors CKR-5, CKR-3, and CKR-2b as fusion cofactors. Cell 1996; 85: 1149-58.
    • (1996) Cell , vol.85 , pp. 1149-1158
    • Doranz, B.J.1    Rucker, J.2    Yi, Y.3    Smyth, R.J.4    Samson, M.5    Peiper, S.C.6
  • 89
    • 0032543307 scopus 로고    scopus 로고
    • Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
    • Kwong PD, Wyatt R, Robinson J, Sweet RW, Sodroski J, Hendrickson WA. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 1998; 393: 648-59.
    • (1998) Nature , vol.393 , pp. 648-659
    • Kwong, P.D.1    Wyatt, R.2    Robinson, J.3    Sweet, R.W.4    Sodroski, J.5    Hendrickson, W.A.6
  • 90
    • 0032546952 scopus 로고    scopus 로고
    • A conserved HIV gp120 glycoprotein structure involved in chemokine receptor binding
    • [see comments]
    • Rizzuto CD, Wyatt R, Hernandez-Ramos N, Sun Y, Kwong PD, Hendrickson WA, et al. A conserved HIV gp120 glycoprotein structure involved in chemokine receptor binding [see comments]. Science 1998; 280: 1949-53.
    • (1998) Science , vol.280 , pp. 1949-1953
    • Rizzuto, C.D.1    Wyatt, R.2    Hernandez-Ramos, N.3    Sun, Y.4    Kwong, P.D.5    Hendrickson, W.A.6
  • 91
    • 16044370087 scopus 로고    scopus 로고
    • The CXC chemokine SDF-1 is the ligand for LESTR/fusin and prevents infection by T-cell-line-adapted HIV-1
    • Oberlin E, Amara A, Bachelerie F, Bessia C, Virelizier JL, Arenzana-Seisdedos F, et al. The CXC chemokine SDF-1 is the ligand for LESTR/fusin and prevents infection by T-cell-line-adapted HIV-1. Nature 1996; 382: 833-5.
    • (1996) Nature , vol.382 , pp. 833-835
    • Oberlin, E.1    Amara, A.2    Bachelerie, F.3    Bessia, C.4    Virelizier, J.L.5    Arenzana-Seisdedos, F.6
  • 92
    • 0031710044 scopus 로고    scopus 로고
    • Use of coreceptors other than CCR5 by non-syncytium-inducing adult and pediatric isolates of human immunodeficiency virus type 1 is rare in vitro
    • Zhang YJ, Dragic T, Can YZ, Kostrikis L, Kwon DS, Littman DR, et al. Use of coreceptors other than CCR5 by non-syncytium-inducing adult and pediatric isolates of human immunodeficiency virus type 1 is rare in vitro. Journal of Virology 1998; 72: 9337-9344.
    • (1998) Journal of Virology , vol.72 , pp. 9337-9344
    • Zhang, Y.J.1    Dragic, T.2    Can, Y.Z.3    Kostrikis, L.4    Kwon, D.S.5    Littman, D.R.6
  • 94
    • 0041920924 scopus 로고    scopus 로고
    • Structure-based, targeted deglycosylation of HIV-1 gp120 and effects on neutralization sensitivity and antibody recognition
    • Koch M, Pancera M, Kwong PD, Kolchinsky P, Grundner C, Wang L, et al. Structure-based, targeted deglycosylation of HIV-1 gp120 and effects on neutralization sensitivity and antibody recognition. Virology 2003; 313: 387-400.
    • (2003) Virology , vol.313 , pp. 387-400
    • Koch, M.1    Pancera, M.2    Kwong, P.D.3    Kolchinsky, P.4    Grundner, C.5    Wang, L.6
  • 95
    • 0242270786 scopus 로고    scopus 로고
    • Epitope mapping and characterization of a novel CD4-induced human monoclonal antibody capable of neutralizing primary HIV-1 strains
    • Xiang SH, Wang L, Abreu M, Huang CC, Kwong PD, Rosenberg E, et al. Epitope mapping and characterization of a novel CD4-induced human monoclonal antibody capable of neutralizing primary HIV-1 strains. Virology 2003; 315: 124-34.
    • (2003) Virology , vol.315 , pp. 124-134
    • Xiang, S.H.1    Wang, L.2    Abreu, M.3    Huang, C.C.4    Kwong, P.D.5    Rosenberg, E.6
  • 96
    • 0141521564 scopus 로고    scopus 로고
    • Access of antibody molecules to the conserved coreceptor binding site on glycoprotein gp120 is sterically restricted on primary human immunodeficiency virus type 1
    • Labrijn AF, Poignard P, Raja A, Zwick MB, Delgado K, Franti M, et al. Access of antibody molecules to the conserved coreceptor binding site on glycoprotein gp120 is sterically restricted on primary human immunodeficiency virus type 1. J Virol 2003; 77: 10557-65.
    • (2003) J. Virol. , vol.77 , pp. 10557-10565
    • Labrijn, A.F.1    Poignard, P.2    Raja, A.3    Zwick, M.B.4    Delgado, K.5    Franti, M.6
  • 97
    • 0034984290 scopus 로고    scopus 로고
    • Structural flexibility and functional valence of CD4-IgG2 (PRO 542): Potential for cross-linking human immunodeficiency virus type 1 envelope spikes
    • Zhu P, Olson WC, Roux KH. Structural flexibility and functional valence of CD4-IgG2 (PRO 542): potential for cross-linking human immunodeficiency virus type 1 envelope spikes. J Virol 2001; 75: 6682-6.
    • (2001) J. Virol. , vol.75 , pp. 6682-6686
    • Zhu, P.1    Olson, W.C.2    Roux, K.H.3
  • 98
    • 0033914939 scopus 로고    scopus 로고
    • Single-dose safety, pharmacology, and antiviral activity of the human immunodeficiency virus (HIV) type 1 entry inhibitor PRO 542 in HIV-infected adults
    • Jacobson JM, Lowy I, Fletcher CV, O'Neill TJ, Tran DN, Ketas TJ, et al. Single-dose safety, pharmacology, and antiviral activity of the human immunodeficiency virus (HIV) type 1 entry inhibitor PRO 542 in HIV-infected adults. J Infect Dis 2000; 182: 326-9.
    • (2000) J. Infect. Dis. , vol.182 , pp. 326-329
    • Jacobson, J.M.1    Lowy, I.2    Fletcher, C.V.3    O'Neill, T.J.4    Tran, D.N.5    Ketas, T.J.6
  • 99
    • 12244281787 scopus 로고    scopus 로고
    • Rational design of a CD4 mimic that inhibits HIV-1 entry and exposes cryptic neutralization epitopes
    • Martin L, Stricher F, Misse D, Sironi F, Pugniere M, Barthe P, et al. Rational design of a CD4 mimic that inhibits HIV-1 entry and exposes cryptic neutralization epitopes. Nat Biotechnol 2003; 21: 71-6.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 71-76
    • Martin, L.1    Stricher, F.2    Misse, D.3    Sironi, F.4    Pugniere, M.5    Barthe, P.6
  • 100
    • 13044292627 scopus 로고    scopus 로고
    • Rational engineering of a miniprotein that reproduces the core of the CD4 site interacting with HIV-1 envelope glycoprotein
    • Vita C, Drakopoulou E, Vizzavona J, Rochette S, Martin L, Menez A, et al. Rational engineering of a miniprotein that reproduces the core of the CD4 site interacting with HIV-1 envelope glycoprotein. Proc Natl Acad Sci USA 1999; 96: 13091-6.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13091-13096
    • Vita, C.1    Drakopoulou, E.2    Vizzavona, J.3    Rochette, S.4    Martin, L.5    Menez, A.6
  • 101
    • 0141703204 scopus 로고    scopus 로고
    • A small molecule HIV-1 inhibitor that targets the HIV-1 envelope and inhibits CD4 receptor binding
    • Lin PF, Blair W, Wang T, Spicer T, Guo Q, Zhou N, et al. A small molecule HIV-1 inhibitor that targets the HIV-1 envelope and inhibits CD4 receptor binding. Proc Natl Acad Sci USA 2003; 100: 11013-8.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 11013-11018
    • Lin, P.F.1    Blair, W.2    Wang, T.3    Spicer, T.4    Guo, Q.5    Zhou, N.6
  • 102
    • 0141680855 scopus 로고    scopus 로고
    • Discovery of 4-benzoyl-1-[(4-methoxy-1H- pyrrolo[2,3-b]pyridin-3-yl)oxoacetyl]-2-(R)-methylpiperazine (BMS-378806): A novel HIV-1 attachment inhibitor that interferes with CD4-gp120 interactions
    • Wang T, Zhang Z, Wallace OB, Deshpande M, Fang H, Yang Z, et al. Discovery of 4-benzoyl-1-[(4-methoxy-1H- pyrrolo[2,3-b]pyridin-3-yl)oxoacetyl]-2-(R)-methylpiperazine (BMS-378806): a novel HIV-1 attachment inhibitor that interferes with CD4-gp120 interactions. J Med Chem 2003; 46: 4236-9.
    • (2003) J. Med. Chem. , vol.46 , pp. 4236-4239
    • Wang, T.1    Zhang, Z.2    Wallace, O.B.3    Deshpande, M.4    Fang, H.5    Yang, Z.6
  • 103
    • 0141856289 scopus 로고    scopus 로고
    • Biochemical and genetic characterizations of a novel human immunodeficiency virus type 1 inhibitor that blocks gp120-CD4 interactions
    • Guo Q, Ho HT, Dicker I, Fan L, Zhou N, Friborg J, et al. Biochemical and genetic characterizations of a novel human immunodeficiency virus type 1 inhibitor that blocks gp120-CD4 interactions. J Virol 2003; 77: 10528-36.
    • (2003) J. Virol. , vol.77 , pp. 10528-10536
    • Guo, Q.1    Ho, H.T.2    Dicker, I.3    Fan, L.4    Zhou, N.5    Friborg, J.6
  • 104
    • 16044373004 scopus 로고    scopus 로고
    • Resistance to HIV-1 infection in caucasian individuals bearing mutant alleles of the CCR-5 chemokine receptor gene
    • Samson M, Libert F, Doranz BJ, Rucker J, Liesnard C, Farber CM, et al. Resistance to HIV-1 infection in caucasian individuals bearing mutant alleles of the CCR-5 chemokine receptor gene. Nature 1996; 382: 722-5.
    • (1996) Nature , vol.382 , pp. 722-725
    • Samson, M.1    Libert, F.2    Doranz, B.J.3    Rucker, J.4    Liesnard, C.5    Farber, C.M.6
  • 105
    • 13044256383 scopus 로고    scopus 로고
    • A small-molecule, nonpeptide CCR5 antagonist with highly potent and selective anti-HIV-1 activity
    • Baba M, Nishimura O, Kanzaki N, Okamoto M, Sawada H, Iizawa Y, et al. A small-molecule, nonpeptide CCR5 antagonist with highly potent and selective anti-HIV-1 activity. Proc Natl Acad Sci USA 1999; 96: 5698-703.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 5698-5703
    • Baba, M.1    Nishimura, O.2    Kanzaki, N.3    Okamoto, M.4    Sawada, H.5    Iizawa, Y.6
  • 107
    • 0035940445 scopus 로고    scopus 로고
    • SCH-C (SCH 351125), an orally bioavailable, small molecule antagonist of the chemokine receptor CCR5, is a potent inhibitor of HIV-1 infection in vitro and in vivo
    • Strizki JM, Xu S, Wagner NE, Wojcik L, Liu J, Hou Y, et al. SCH-C (SCH 351125), an orally bioavailable, small molecule antagonist of the chemokine receptor CCR5, is a potent inhibitor of HIV-1 infection in vitro and in vivo. Proc Natl Acad Sci USA 2001; 98: 12718-23.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 12718-12723
    • Strizki, J.M.1    Xu, S.2    Wagner, N.E.3    Wojcik, L.4    Liu, J.5    Hou, Y.6
  • 109
    • 0037404511 scopus 로고    scopus 로고
    • Analysis of the mechanism by which the small-molecule CCR5 antagonists SCH-351125 and SCH-350581 inhibit human immunodeficiency virus type 1 entry
    • Tsamis F, Gavrilov S, Kajumo F, Seibert C, Kuhmann S, Ketas T, et al. Analysis of the mechanism by which the small-molecule CCR5 antagonists SCH-351125 and SCH-350581 inhibit human immunodeficiency virus type 1 entry. J Virol 2003; 77: 5201-8.
    • (2003) J. Virol. , vol.77 , pp. 5201-5208
    • Tsamis, F.1    Gavrilov, S.2    Kajumo, F.3    Seibert, C.4    Kuhmann, S.5    Ketas, T.6
  • 113
    • 0032954383 scopus 로고    scopus 로고
    • T134, a small-molecule CXCR4 inhibitor, has no cross-drug resistance with AMD3100, a CXCR4 antagonist with a different structure
    • Arakaki R, Tamamura H, Premanathan M, Kanbara K, Ramanan S, Mochizuki K, et al. T134, a small-molecule CXCR4 inhibitor, has no cross-drug resistance with AMD3100, a CXCR4 antagonist with a different structure. J Virol 1999; 73: 1719-23.
    • (1999) J. Virol. , vol.73 , pp. 1719-1723
    • Arakaki, R.1    Tamamura, H.2    Premanathan, M.3    Kanbara, K.4    Ramanan, S.5    Mochizuki, K.6
  • 114
    • 0030773515 scopus 로고    scopus 로고
    • A small-molecule inhibitor directed against the chemokine receptor CXCR4 prevents its use as an HIV-1 coreceptor
    • Doranz BJ, Grovit-Ferbas K, Sharron MP, Mao SH, Goetz MB, Daar ES, et al. A small-molecule inhibitor directed against the chemokine receptor CXCR4 prevents its use as an HIV-1 coreceptor. J Exp Med 1997; 186: 1395-400.
    • (1997) J. Exp. Med. , vol.186 , pp. 1395-1400
    • Doranz, B.J.1    Grovit-Ferbas, K.2    Sharron, M.P.3    Mao, S.H.4    Goetz, M.B.5    Daar, E.S.6
  • 115
    • 0037025357 scopus 로고    scopus 로고
    • A point mutation that confers constitutive activity to CXCR4 reveals that T140 is an inverse agonist and that AMD3100 and ALX40-4C are weak partial agonists
    • Zhang WB, Navenot JM, Haribabu B, Tamamura H, Hiramatu K, Omagari A, et al. A point mutation that confers constitutive activity to CXCR4 reveals that T140 is an inverse agonist and that AMD3100 and ALX40-4C are weak partial agonists. J Biol Chem 2002; 277: 24515-21.
    • (2002) J. Biol. Chem. , vol.277 , pp. 24515-24521
    • Zhang, W.B.1    Navenot, J.M.2    Haribabu, B.3    Tamamura, H.4    Hiramatu, K.5    Omagari, A.6
  • 116
    • 0141814730 scopus 로고    scopus 로고
    • The entry of entry inhibitors: A fusion of science and medicine
    • Moore JP, Doms RW. The entry of entry inhibitors: a fusion of science and medicine. Proc Natl Acad Sci USA 2003; 100: 10598-602.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 10598-10602
    • Moore, J.P.1    Doms, R.W.2
  • 117
    • 0027692502 scopus 로고
    • A synthetic peptide from HIV-1 gp41 is a potent inhibitor of virus-mediated cell-cell fusion
    • Wild C, Greenwell T, Matthews T. A synthetic peptide from HIV-1 gp41 is a potent inhibitor of virus-mediated cell-cell fusion. AIDS Res Hum Retroviruses 1993; 9: 1051-3.
    • (1993) AIDS Res. Hum. Retroviruses , vol.9 , pp. 1051-1053
    • Wild, C.1    Greenwell, T.2    Matthews, T.3
  • 118
    • 0038467539 scopus 로고    scopus 로고
    • Direct evidence that C-peptide inhibitors of human immunodeficiency virus type 1 entry bind to the gp41 N-helical domain in receptor-activated viral envelope
    • Kilgore NR, Salzwedel K, Reddick M, Allaway GP, Wild CT. Direct evidence that C-peptide inhibitors of human immunodeficiency virus type 1 entry bind to the gp41 N-helical domain in receptor-activated viral envelope. J Virol 2003; 77: 7669-72.
    • (2003) J. Virol. , vol.77 , pp. 7669-7672
    • Kilgore, N.R.1    Salzwedel, K.2    Reddick, M.3    Allaway, G.P.4    Wild, C.T.5
  • 119
    • 0037936885 scopus 로고    scopus 로고
    • C-terminal octylation rescues an inactive T20 mutant: Implications for the mechanism of HIV/SIMIAN immunodeficiency virus-induced membrane fusion
    • Peisajovich SG, Gallo SA, Blumenthal R, Shai Y. C-terminal octylation rescues an inactive T20 mutant: implications for the mechanism of HIV/SIMIAN immunodeficiency virus-induced membrane fusion. J Biol Chem 2003; 278: 21012-7.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21012-21017
    • Peisajovich, S.G.1    Gallo, S.A.2    Blumenthal, R.3    Shai, Y.4
  • 120
    • 0036066762 scopus 로고    scopus 로고
    • The safety, plasma pharmacokinetics, and antiviral activity of subcutaneous enfuvirtide (T-20), a peptide inhibitor of gp41-mediated virus fusion, in HIV-infected adults
    • Kilby JM, Lalezari JP, Eron JJ, Carlson M, Cohen C, Arduino RC, et al. The safety, plasma pharmacokinetics, and antiviral activity of subcutaneous enfuvirtide (T-20), a peptide inhibitor of gp41-mediated virus fusion, in HIV-infected adults. AIDS Res Hum Retroviruses 2002; 18: 685-93.
    • (2002) AIDS Res. Hum. Retroviruses , vol.18 , pp. 685-693
    • Kilby, J.M.1    Lalezari, J.P.2    Eron, J.J.3    Carlson, M.4    Cohen, C.5    Arduino, R.C.6
  • 121
    • 0038279960 scopus 로고    scopus 로고
    • Clinical safety and efficacy of enfuvirtide (T-20), a new fusion inhibitor. A review of tile presentation at the satellite symposium "New hope: Advancing care in HIV infection" at the 15th annual Association of Nurses in AIDS Care conference, November 2002
    • Lalezari JP. Clinical safety and efficacy of enfuvirtide (T-20), a new fusion inhibitor. A review of tile presentation at the satellite symposium "New hope: advancing care in HIV infection" at the 15th annual Association of Nurses in AIDS Care conference, November 2002. AIDS Read 2003; 13: S9-13.
    • (2003) AIDS Read , vol.13
    • Lalezari, J.P.1
  • 122
    • 10744229122 scopus 로고    scopus 로고
    • A controlled Phase II trial assessing three doses of enfuvirtide (T-20) in combination with abacavir, amprenavir, ritonavir and efavirenz in non-nucleoside reverse transcriptase inhibitor-naive HIV-infected adults
    • Lalezari JP, DeJesus E, Northfelt DW, Richmond G, Wolfe P, Haubrich R, et al. A controlled Phase II trial assessing three doses of enfuvirtide (T-20) in combination with abacavir, amprenavir, ritonavir and efavirenz in non-nucleoside reverse transcriptase inhibitor-naive HIV-infected adults. Antivir Ther 2003; 8: 279-87.
    • (2003) Antivir. Ther. , vol.8 , pp. 279-287
    • Lalezari, J.P.1    DeJesus, E.2    Northfelt, D.W.3    Richmond, G.4    Wolfe, P.5    Haubrich, R.6
  • 123
    • 0031883832 scopus 로고    scopus 로고
    • Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides
    • Rimsky LT, Shugars DC, Matthews TJ. Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides. J Virol 1998; 72: 986-93.
    • (1998) J. Virol. , vol.72 , pp. 986-993
    • Rimsky, L.T.1    Shugars, D.C.2    Matthews, T.J.3
  • 124
    • 0037119027 scopus 로고    scopus 로고
    • Minimal variation in T-20 binding domain of different HIV-1 subtypes from antiretroviral-naive and -experienced patients
    • Xu L, Hue S, Taylor S, Ratcliffe D, Workman JA, Jackson S, et al. Minimal variation in T-20 binding domain of different HIV-1 subtypes from antiretroviral-naive and -experienced patients. Aids 2002; 16: 1684-6.
    • (2002) Aids , vol.16 , pp. 1684-1686
    • Xu, L.1    Hue, S.2    Taylor, S.3    Ratcliffe, D.4    Workman, J.A.5    Jackson, S.6
  • 126
    • 0036090585 scopus 로고    scopus 로고
    • Emergence of resistant human immunodeficiency virus type 1 in patients receiving fusion inhibitor (T-20) monotherapy
    • Wei X, Decker JM, Liu H, Zhang Z, Arani RB, Kilby JM, et al. Emergence of resistant human immunodeficiency virus type 1 in patients receiving fusion inhibitor (T-20) monotherapy. Antimicrob Agents Chemother 2002; 46: 1896-905.
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 1896-1905
    • Wei, X.1    Decker, J.M.2    Liu, H.3    Zhang, Z.4    Arani, R.B.5    Kilby, J.M.6
  • 127
    • 0037059049 scopus 로고    scopus 로고
    • Sensitivity of HIV-1 to entry inhibitors correlates with envelope/coreceptor affinity, receptor density, and fusion kinetics
    • Reeves JD, Gallo SA, Ahmad N, Miamidian JL, Harvey PE, Sharron M, et al. Sensitivity of HIV-1 to entry inhibitors correlates with envelope/coreceptor affinity, receptor density, and fusion kinetics. Proc Natl Acad Sci USA 2002; 99: 16249-54.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 16249-16254
    • Reeves, J.D.1    Gallo, S.A.2    Ahmad, N.3    Miamidian, J.L.4    Harvey, P.E.5    Sharron, M.6
  • 128
    • 0037470227 scopus 로고    scopus 로고
    • The prefusogenic intermediate of HIV-1 gp41 contains exposed C-peptide regions
    • Koshiba T, Chan DC. The prefusogenic intermediate of HIV-1 gp41 contains exposed C-peptide regions. J Biol Chem 2003; 278: 7573-9.
    • (2003) J. Biol. Chem. , vol.278 , pp. 7573-7579
    • Koshiba, T.1    Chan, D.C.2
  • 129
    • 0035793406 scopus 로고    scopus 로고
    • Protein design of an HIV-1 entry inhibitor
    • Root MJ, Kay MS, Kim PS. Protein design of an HIV-1 entry inhibitor. Science 2001; 291: 884-8.
    • (2001) Science , vol.291 , pp. 884-888
    • Root, M.J.1    Kay, M.S.2    Kim, P.S.3
  • 130
    • 0037966960 scopus 로고    scopus 로고
    • Targeting therapeutics to an exposed and conserved binding element of the HIV-1 fusion protein
    • Root MJ, Hamer DH. Targeting therapeutics to an exposed and conserved binding element of the HIV-1 fusion protein. Proc Natl Acad Sci USA 2003; 100: 5016-21.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 5016-5021
    • Root, M.J.1    Hamer, D.H.2
  • 131
    • 0042208243 scopus 로고    scopus 로고
    • The coronavirus spike protein is a class I virus fusion protein: Structural and functional characterization of the fusion core complex
    • Bosch BJ, van der Zee R, de Haan CA, Rottier PJ. The coronavirus spike protein is a class I virus fusion protein: structural and functional characterization of the fusion core complex. J Virol 2003; 77: 8801-11.
    • (2003) J. Virol. , vol.77 , pp. 8801-8811
    • Bosch, B.J.1    van der Zee, R.2    de Haan, C.A.3    Rottier, P.J.4
  • 132
    • 0034905041 scopus 로고    scopus 로고
    • The machinery for flavivirus fusion with host cell membranes
    • Heinz FX, Allison SL. The machinery for flavivirus fusion with host cell membranes. Curr Opin Microbiol 2001; 4: 450-5.
    • (2001) Curr. Opin. Microbiol. , vol.4 , pp. 450-455
    • Heinz, F.X.1    Allison, S.L.2
  • 133
    • 0034567567 scopus 로고    scopus 로고
    • Structures and mechanisms in flavivirus fusion
    • Heinz FX, Allison SL. Structures and mechanisms in flavivirus fusion. Adv Virus Res 2000; 55: 231-69.
    • (2000) Adv. Virus Res. , vol.55 , pp. 231-269
    • Heinz, F.X.1    Allison, S.L.2
  • 134
    • 0032813509 scopus 로고    scopus 로고
    • Functional analysis of cell surface-expressed hepatitis C virus E2 glycoprotein
    • Flint M, Thomas JM, Maidens CM, Shotton C, Levy S, Barclay WS, et al. Functional analysis of cell surface-expressed hepatitis C virus E2 glycoprotein. J Virol 1999; 73: 6782-90.
    • (1999) J. Virol. , vol.73 , pp. 6782-6790
    • Flint, M.1    Thomas, J.M.2    Maidens, C.M.3    Shotton, C.4    Levy, S.5    Barclay, W.S.6
  • 135
    • 0037444329 scopus 로고    scopus 로고
    • Proteomics computational analyses suggest that hepatitis C virus E1 and pestivirus E2 envelope glycoproteins are truncated class II fusion proteins
    • Garry RF, Dash S. Proteomics computational analyses suggest that hepatitis C virus E1 and pestivirus E2 envelope glycoproteins are truncated class II fusion proteins. Virology 2003; 307: 255-65.
    • (2003) Virology , vol.307 , pp. 255-265
    • Garry, R.F.1    Dash, S.2
  • 136
    • 0033607281 scopus 로고    scopus 로고
    • Hepatitis C virus and other flaviviridae viruses enter cells via low density lipoprotein receptor
    • Agnello V, Abel G, Elfahal M, Knight GB, Zhang QX. Hepatitis C ] virus and other flaviviridae viruses enter cells via low density lipoprotein receptor. Proc Natl Acad Sci USA 1999; 96: 12766-71.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12766-12771
    • Agnello, V.1    Abel, G.2    Elfahal, M.3    Knight, G.B.4    Zhang, Q.X.5
  • 137
    • 0345251979 scopus 로고    scopus 로고
    • Low density lipoprotein receptor as a candidate receptor for hepatitis C virus
    • Monazahian M, Bohme I, Bonk S, Koch A, Scholz C, Grethe S, et al. Low density lipoprotein receptor as a candidate receptor for hepatitis C virus. J Med Virol 1999; 57: 223-9.
    • (1999) J. Med. Virol. , vol.57 , pp. 223-229
    • Monazahian, M.1    Bohme, I.2    Bonk, S.3    Koch, A.4    Scholz, C.5    Grethe, S.6
  • 139
    • 17944385968 scopus 로고    scopus 로고
    • Structure-function analysis of hepatitis C virus envelope-CD81 binding
    • Petracca R, Falugi F, Galli G, Norais N, Rosa D, Campagnoli S, et al. Structure-function analysis of hepatitis C virus envelope-CD81 binding. J Virol 2000; 74: 4824-30.
    • (2000) J. Virol. , vol.74 , pp. 4824-4830
    • Petracca, R.1    Falugi, F.2    Galli, G.3    Norais, N.4    Rosa, D.5    Campagnoli, S.6
  • 140
    • 0037301359 scopus 로고    scopus 로고
    • Binding of the hepatitis C virus E2 glycoprotein to CD81 is strain specific and is modulated by a complex interplay between hypervariable regions 1 and 2
    • Roccasecca R, Ansuini H, Vitelli A, Meola A, Scarselli E, Acali S, et al. Binding of the hepatitis C virus E2 glycoprotein to CD81 is strain specific and is modulated by a complex interplay between hypervariable regions 1 and 2. J Virol 2003; 77: 1856-67.
    • (2003) J. Virol. , vol.77 , pp. 1856-1867
    • Roccasecca, R.1    Ansuini, H.2    Vitelli, A.3    Meola, A.4    Scarselli, E.5    Acali, S.6
  • 142
    • 18644378971 scopus 로고    scopus 로고
    • The human scavenger receptor class B type I is a novel candidate receptor for the hepatitis C virus
    • Scarselli E, Ansuini H, Cerino R, Roccasecca RM, Acali S, Filocamo G, et al. The human scavenger receptor class B type I is a novel candidate receptor for the hepatitis C virus. EMBO J 2002; 21: 5017-25.
    • (2002) EMBO J. , vol.21 , pp. 5017-5025
    • Scarselli, E.1    Ansuini, H.2    Cerino, R.3    Roccasecca, R.M.4    Acali, S.5    Filocamo, G.6
  • 143
    • 0037136420 scopus 로고    scopus 로고
    • Glycans as endocytosis signals: The cases of the asialoglycoprotein and hyaluronan/chondroitin sulfate receptors
    • Weigel PH, Yik JH. Glycans as endocytosis signals: the cases of the asialoglycoprotein and hyaluronan/chondroitin sulfate receptors. Biochim Biophys Acta 2002; 1572: 341-63.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 341-363
    • Weigel, P.H.1    Yik, J.H.2
  • 144
    • 0038471344 scopus 로고    scopus 로고
    • Hepatitis C virus glycoproteins mediate pH-dependent cell entry of pseudotyped retroviral particles
    • Hsu M, Zhang J, Flint M, Logvinoff C, Cheng-Mayer C, Rice CM, et al. Hepatitis C virus glycoproteins mediate pH-dependent cell entry of pseudotyped retroviral particles. Proc Natl Acad Sci USA 2003; 100: 7271-6.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 7271-7276
    • Hsu, M.1    Zhang, J.2    Flint, M.3    Logvinoff, C.4    Cheng-Mayer, C.5    Rice, C.M.6
  • 145
    • 18644378971 scopus 로고    scopus 로고
    • The human scavenger receptor class B type I is a novel candidate receptor for the hepatitis C virus
    • Scarselli E, Ansuini H, Cerino R, Roccasecca RM, Acali S, Filocamo G, et al. The human scavenger receptor class B type I is a novel candidate receptor for the hepatitis C virus. EMBO J 2002; 21: 5017-25.
    • (2002) EMBO J. , vol.21 , pp. 5017-5025
    • Scarselli, E.1    Ansuini, H.2    Cerino, R.3    Roccasecca, R.M.4    Acali, S.5    Filocamo, G.6
  • 146
    • 0142242265 scopus 로고    scopus 로고
    • Cell entry of hepatitis C virus requires a set of co-receptors that include the CD81 tetraspanin and the SR-B1 scavenger receptor
    • Bartosch B, Vitelli A, Granier C, Goujon C, Dubuisson J, Pascale S, et al. Cell entry of hepatitis C virus requires a set of co-receptors that include the CD81 tetraspanin and the SR-B1 scavenger receptor. J Biol Chem 2003; 278: 41624-30.
    • (2003) J. Biol. Chem. , vol.278 , pp. 41624-41630
    • Bartosch, B.1    Vitelli, A.2    Granier, C.3    Goujon, C.4    Dubuisson, J.5    Pascale, S.6
  • 147
    • 0037213932 scopus 로고    scopus 로고
    • Role of the asialoglycoprotein receptor in binding and entry of hepatitis C virus structural proteins in cultured human hepatocytes
    • Saunier B, Triyatni M, Ulianich L, Maruvada P, Yen P, Kohn LD. Role of the asialoglycoprotein receptor in binding and entry of hepatitis C virus structural proteins in cultured human hepatocytes. J Virol 2003; 77: 546-59.
    • (2003) J. Virol. , vol.77 , pp. 546-559
    • Saunier, B.1    Triyatni, M.2    Ulianich, L.3    Maruvada, P.4    Yen, P.5    Kohn, L.D.6
  • 148
    • 3042637779 scopus 로고    scopus 로고
    • Structural basis for distinct ligand-binding and targeting properties of the receptors DC-SIGN and DC-SIGNR
    • Guo Y, Feinberg H, Conroy E, Mitchell DA, Alvarez R, Blixt O, et al. Structural basis for distinct ligand-binding and targeting properties of the receptors DC-SIGN and DC-SIGNR. Nat Struct Mol Biol 2004; 11: 591-8.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 591-598
    • Guo, Y.1    Feinberg, H.2    Conroy, E.3    Mitchell, D.A.4    Alvarez, R.5    Blixt, O.6
  • 152
    • 1842526097 scopus 로고    scopus 로고
    • Structure of a flavivirus envelope glycoprotein in its low-pH-induced membrane fusion conformation
    • Bressanelli S, Stiasny K, Allison SL, Stura EA, Duquerroy S, Lescar J, et al. Structure of a flavivirus envelope glycoprotein in its low-pH-induced membrane fusion conformation. EMBO J 2004; 23: 728-38.
    • (2004) EMBO J. , vol.23 , pp. 728-738
    • Bressanelli, S.1    Stiasny, K.2    Allison, S.L.3    Stura, E.A.4    Duquerroy, S.5    Lescar, J.6
  • 153
    • 0038714246 scopus 로고    scopus 로고
    • Potential drug targets on the HIV-1 envelope glycoproteins, gp120 and gp41
    • Huang L, Zhang L, Chen CH. Potential drug targets on the HIV-1 envelope glycoproteins, gp120 and gp41. Curr Pharm Design 2003; 9(18): 1453-62.
    • (2003) Curr. Pharm. Design , vol.9 , Issue.18 , pp. 1453-1462
    • Huang, L.1    Zhang, L.2    Chen, C.H.3
  • 154
  • 155
    • 0036234876 scopus 로고    scopus 로고
    • Drug delivery system to control infectious diseases
    • Shoji Y, Shimada J, Mizushima Y. Drug delivery system to control infectious diseases. Curr Pharm Design 2002; 8(6): 455-65.
    • (2002) Curr. Pharm. Design , vol.8 , Issue.6 , pp. 455-465
    • Shoji, Y.1    Shimada, J.2    Mizushima, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.