메뉴 건너뛰기




Volumn 1253, Issue 1, 2012, Pages 133-148

Glycans, galectins, and HIV-1 infection

Author keywords

Galectin; Glycobiology; HIV 1; Lectin

Indexed keywords

ANTIRETROVIRUS AGENT; GALECTIN; GALECTIN 1; GALECTIN 3; GLYCAN DERIVATIVE; GLYCOPROTEIN GP 120; LECTIN; MEMBRANE PROTEIN;

EID: 84860233524     PISSN: 00778923     EISSN: 17496632     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.2012.06475.x     Document Type: Review
Times cited : (55)

References (125)
  • 1
    • 77954391989 scopus 로고    scopus 로고
    • UNAIDS, J.U.N.P.o.H.A. Joint United Nations Programme on HIV/AIDS. Geneva, Switzerland
    • UNAIDS, J.U.N.P.o.H.A. 2009. 2009 AIDS Epidemic Update. Joint United Nations Programme on HIV/AIDS. Geneva, Switzerland.
    • (2009) 2009 AIDS Epidemic Update
  • 2
    • 84860235254 scopus 로고    scopus 로고
    • UNAIDS, J.U.N.P.o.H.A. Global report: UNAIDS report on the global AIDS epidemic 2010. Available at: Accessed 23 Nov 2010
    • UNAIDS, J.U.N.P.o.H.A. 2010. Global report: UNAIDS report on the global AIDS epidemic 2010. Available at: Accessed 23 Nov 2010.
    • (2010)
  • 3
    • 0035912248 scopus 로고    scopus 로고
    • Gulliver's travels in HIVland
    • Weiss, R.A. 2001. Gulliver's travels in HIVland. Nature 410: 963-967.
    • (2001) Nature , vol.410 , pp. 963-967
    • Weiss, R.A.1
  • 4
    • 34250372513 scopus 로고    scopus 로고
    • HIVs and their replication
    • 5th ed. D.M. Knipe & P.M. Howley, Eds.:. Lippincott Williams & Wilkins. Philadelphia
    • Freed, E.O. & Martin M.A. 2007. HIVs and their replication. In Fields Virology, 5th ed. D.M. Knipe & P.M. Howley, Eds.: 2107-2185. Lippincott Williams & Wilkins. Philadelphia.
    • (2007) Fields Virology , pp. 2107-2185
    • Freed, E.O.1    Martin, M.A.2
  • 5
    • 0034687168 scopus 로고    scopus 로고
    • Mass spectrometric characterization of the glycosylation pattern of HIV-gp120 expressed in CHO cells
    • Zhu, X., C. Borchers, R.J. Bienstock & K.B. Tomer. 2000. Mass spectrometric characterization of the glycosylation pattern of HIV-gp120 expressed in CHO cells. Biochemistry 39: 11194-11204.
    • (2000) Biochemistry , vol.39 , pp. 11194-11204
    • Zhu, X.1    Borchers, C.2    Bienstock, R.J.3    Tomer, K.B.4
  • 6
    • 34247636624 scopus 로고    scopus 로고
    • Exploiting the defensive sugars of HIV-1 for drug and vaccine design
    • Scanlan, C.N., J. Offer, N. Zitzmann & R.A. Dwek. 2007. Exploiting the defensive sugars of HIV-1 for drug and vaccine design. Nature 446: 1038-1045.
    • (2007) Nature , vol.446 , pp. 1038-1045
    • Scanlan, C.N.1    Offer, J.2    Zitzmann, N.3    Dwek, R.A.4
  • 7
    • 0031812844 scopus 로고    scopus 로고
    • The acquisition of host-encoded proteins by nascent HIV-1
    • Tremblay, M.J., J.F. Fortin & R. Cantin. 1998. The acquisition of host-encoded proteins by nascent HIV-1. Immunol. Today 19: 346-351.
    • (1998) Immunol. Today , vol.19 , pp. 346-351
    • Tremblay, M.J.1    Fortin, J.F.2    Cantin, R.3
  • 9
    • 18744391391 scopus 로고    scopus 로고
    • Plunder and stowaways: incorporation of cellular proteins by enveloped viruses
    • Cantin, R., S. Methot & M.J. Tremblay. 2005. Plunder and stowaways: incorporation of cellular proteins by enveloped viruses. J. Virol. 79: 6577-6587.
    • (2005) J. Virol. , vol.79 , pp. 6577-6587
    • Cantin, R.1    Methot, S.2    Tremblay, M.J.3
  • 10
    • 33745203490 scopus 로고    scopus 로고
    • Distribution and three-dimensional structure of AIDS virus envelope spikes
    • Zhu, P., J. Liu, J. Bess, Jr., et al. 2006. Distribution and three-dimensional structure of AIDS virus envelope spikes. Nature 441: 847-852.
    • (2006) Nature , vol.441 , pp. 847-852
    • Zhu, P.1    Liu, J.2    Bess Jr., J.3
  • 11
    • 33646146379 scopus 로고    scopus 로고
    • GP120: target for neutralizing HIV-1 antibodies
    • Pantophlet, R. & D.R. Burton. 2006. GP120: target for neutralizing HIV-1 antibodies. Annu. Rev. Immunol. 24: 739-769.
    • (2006) Annu. Rev. Immunol. , vol.24 , pp. 739-769
    • Pantophlet, R.1    Burton, D.R.2
  • 12
    • 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, C.K., M.W. Spellman, L. Riddle, et al. 1990. 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. 265: 10373-10382.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10373-10382
    • Leonard, C.K.1    Spellman, M.W.2    Riddle, L.3
  • 13
    • 70449534963 scopus 로고    scopus 로고
    • Proximal glycans outside of the epitopes regulate the presentation of HIV-1 envelope gp120 helper epitopes
    • Li, H., C.F. Xu, S. Blais, et al. 2009. Proximal glycans outside of the epitopes regulate the presentation of HIV-1 envelope gp120 helper epitopes. J. Immunol. 182: 6369-6378.
    • (2009) J. Immunol. , vol.182 , pp. 6369-6378
    • Li, H.1    Xu, C.F.2    Blais, S.3
  • 14
    • 0025075180 scopus 로고
    • The spectrum of N-linked oligosaccharide structures detected by enzymic microsequencing on a recombinant soluble CD4 glycoprotein from Chinese hamster ovary cells
    • Yuen, C.T., S.A. Carr & T. Feizi. 1990. The spectrum of N-linked oligosaccharide structures detected by enzymic microsequencing on a recombinant soluble CD4 glycoprotein from Chinese hamster ovary cells. Eur. J. Biochem. 192: 523-528.
    • (1990) Eur. J. Biochem. , vol.192 , pp. 523-528
    • Yuen, C.T.1    Carr, S.A.2    Feizi, T.3
  • 15
    • 80655137917 scopus 로고    scopus 로고
    • Glycomics analysis of HIV-1 gp120 glycoforms
    • Pang, P.C., H.R. Morris, S.M. Haslam, et al. 2007. Glycomics analysis of HIV-1 gp120 glycoforms. Glycobiology 17: 1274.
    • (2007) Glycobiology , vol.17 , pp. 1274
    • Pang, P.C.1    Morris, H.R.2    Haslam, S.M.3
  • 16
    • 80655125508 scopus 로고    scopus 로고
    • Host-soluble galectin-1 promotes HIV-1 replication through a direct interaction with glycans of viral gp120 and host CD4
    • St-Pierre, C., H. Manya, M. Ouellet, et al. 2011. Host-soluble galectin-1 promotes HIV-1 replication through a direct interaction with glycans of viral gp120 and host CD4. J. Virol. 85: 11742-11751.
    • (2011) J. Virol. , vol.85 , pp. 11742-11751
    • St-Pierre, C.1    Manya, H.2    Ouellet, M.3
  • 17
    • 80051677678 scopus 로고    scopus 로고
    • The glycan shield of HIV is predominantly oligomannose independently of production system or viral clade
    • Bonomelli, C., K.J. Doores, D.C. Dunlop, et al. 2011. The glycan shield of HIV is predominantly oligomannose independently of production system or viral clade. PLoS One 6: e23521.
    • (2011) PLoS One , vol.6
    • Bonomelli, C.1    Doores, K.J.2    Dunlop, D.C.3
  • 18
    • 77956385205 scopus 로고    scopus 로고
    • Envelope glycans of immunodeficiency virions are almost entirely oligomannose antigens
    • Doores, K.J., C. Bonomelli, D.J. Harvey, et al. 2010. Envelope glycans of immunodeficiency virions are almost entirely oligomannose antigens. Proc. Natl. Acad. Sci. U. S. A. 107: 13800-13805.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 13800-13805
    • Doores, K.J.1    Bonomelli, C.2    Harvey, D.J.3
  • 19
    • 15444380346 scopus 로고    scopus 로고
    • Galectin-1 acts as a soluble host factor that promotes HIV-1 infectivity through stabilization of virus attachment to host cells
    • Ouellet, M., S. Mercier, I. Pelletier, et al. 2005. Galectin-1 acts as a soluble host factor that promotes HIV-1 infectivity through stabilization of virus attachment to host cells. J. Immunol. 174: 4120-4126.
    • (2005) J. Immunol. , vol.174 , pp. 4120-4126
    • Ouellet, M.1    Mercier, S.2    Pelletier, I.3
  • 20
    • 0032543555 scopus 로고    scopus 로고
    • The antigenic structure of the HIV gp120 envelope glycoprotein
    • Wyatt, R., P.D. Kwong, E. Desjardins, et al. 1998. The antigenic structure of the HIV gp120 envelope glycoprotein. Nature 393: 705-711.
    • (1998) Nature , vol.393 , pp. 705-711
    • Wyatt, R.1    Kwong, P.D.2    Desjardins, E.3
  • 21
    • 13844267637 scopus 로고    scopus 로고
    • Determining the structure of an unliganded and fully glycosylated SIV gp120 envelope glycoprotein
    • Chen, B., E.M. Vogan, H. Gong, et al. 2005. Determining the structure of an unliganded and fully glycosylated SIV gp120 envelope glycoprotein. Structure 13: 197-211.
    • (2005) Structure , vol.13 , pp. 197-211
    • Chen, B.1    Vogan, E.M.2    Gong, H.3
  • 22
    • 36749070064 scopus 로고    scopus 로고
    • Toward a carbohydrate-based HIV-1 vaccine
    • American Chemical Society. Washington
    • Calarese, D., C. Scanlan, H.-K. Lee, et al. 2006. Toward a carbohydrate-based HIV-1 vaccine. In Carbohydrate Drug Design, 161-185. American Chemical Society. Washington.
    • (2006) Carbohydrate Drug Design , pp. 161-185
    • Calarese, D.1    Scanlan, C.2    Lee, H.-K.3
  • 23
    • 77950480397 scopus 로고    scopus 로고
    • Carbohydrate vaccines: developing sweet solutions to sticky situations?
    • Astronomo, R.D. & D.R. Burton. 2010. Carbohydrate vaccines: developing sweet solutions to sticky situations? Nat. Rev. Drug. Discov. 9: 308-324.
    • (2010) Nat. Rev. Drug. Discov. , vol.9 , pp. 308-324
    • Astronomo, R.D.1    Burton, D.R.2
  • 24
    • 78650062305 scopus 로고    scopus 로고
    • Yeast-elicited cross-reactive antibodies to HIV Env glycans efficiently neutralize virions expressing exclusively high-mannose N-linked glycans
    • Agrawal-Gamse, C., R.J. Luallen, B. Liu, et al. 2011. Yeast-elicited cross-reactive antibodies to HIV Env glycans efficiently neutralize virions expressing exclusively high-mannose N-linked glycans. J. Virol. 85: 470-480.
    • (2011) J. Virol. , vol.85 , pp. 470-480
    • Agrawal-Gamse, C.1    Luallen, R.J.2    Liu, B.3
  • 25
    • 0034598905 scopus 로고    scopus 로고
    • DC-SIGN, a dendritic cell-specific HIV-1-binding protein that enhances trans-infection of T cells
    • Geijtenbeek, T.B., D.S. Kwon, R. Torensma, et al. 2000. DC-SIGN, a dendritic cell-specific HIV-1-binding protein that enhances trans-infection of T cells. Cell 100: 587-597.
    • (2000) Cell , vol.100 , pp. 587-597
    • Geijtenbeek, T.B.1    Kwon, D.S.2    Torensma, R.3
  • 26
    • 33847755116 scopus 로고    scopus 로고
    • Langerin is a natural barrier to HIV-1 transmission by Langerhans cells
    • de Witte, L., A. Nabatov, M. Pion, et al. 2007. Langerin is a natural barrier to HIV-1 transmission by Langerhans cells. Nat. Med. 13: 367-371.
    • (2007) Nat. Med. , vol.13 , pp. 367-371
    • de Witte, L.1    Nabatov, A.2    Pion, M.3
  • 27
    • 51649113484 scopus 로고    scopus 로고
    • The C-type lectin surface receptor DCIR acts as a new attachment factor for HIV-1 in dendritic cells and contributes to trans- and cis-infection pathways
    • Lambert, A.A., C. Gilbert, M. Richard, et al. 2008. The C-type lectin surface receptor DCIR acts as a new attachment factor for HIV-1 in dendritic cells and contributes to trans- and cis-infection pathways. Blood 112: 1299-1307.
    • (2008) Blood , vol.112 , pp. 1299-1307
    • Lambert, A.A.1    Gilbert, C.2    Richard, M.3
  • 28
    • 36048945481 scopus 로고    scopus 로고
    • The interaction of HIV with dendritic cells: outcomes and pathways
    • Piguet, V. & R.M. Steinman. 2007. The interaction of HIV with dendritic cells: outcomes and pathways. Trends Immunol. 28: 503-510.
    • (2007) Trends Immunol. , vol.28 , pp. 503-510
    • Piguet, V.1    Steinman, R.M.2
  • 29
    • 33750378183 scopus 로고    scopus 로고
    • Dendritic-cell interactions with HIV: infection and viral dissemination
    • Wu, L. & V.N. KewalRamani. 2006. Dendritic-cell interactions with HIV: infection and viral dissemination. Nat. Rev. Immunol. 6: 859-868.
    • (2006) Nat. Rev. Immunol. , vol.6 , pp. 859-868
    • Wu, L.1    KewalRamani, V.N.2
  • 30
    • 0033566807 scopus 로고    scopus 로고
    • APCs express DCIR, a novel C-type lectin surface receptor containing an immunoreceptor tyrosine-based inhibitory motif
    • Bates, E.E., N. Fournier, E. Garcia, et al. 1999. APCs express DCIR, a novel C-type lectin surface receptor containing an immunoreceptor tyrosine-based inhibitory motif. J. Immunol. 163: 1973-1983.
    • (1999) J. Immunol. , vol.163 , pp. 1973-1983
    • Bates, E.E.1    Fournier, N.2    Garcia, E.3
  • 31
    • 0024385412 scopus 로고
    • Involvement of a leukocyte adhesion receptor (LFA-1) in HIV-induced syncytium formation
    • Hildreth, J.E. & R.J. Orentas. 1989. Involvement of a leukocyte adhesion receptor (LFA-1) in HIV-induced syncytium formation. Science 244: 1075-1078.
    • (1989) Science , vol.244 , pp. 1075-1078
    • Hildreth, J.E.1    Orentas, R.J.2
  • 32
    • 39449098115 scopus 로고    scopus 로고
    • HIV-1 envelope protein binds to and signals through integrin alpha4beta7, the gut mucosal homing receptor for peripheral T cells
    • Arthos, J., C. Cicala, E. Martinelli, et al. 2008. HIV-1 envelope protein binds to and signals through integrin alpha4beta7, the gut mucosal homing receptor for peripheral T cells. Nat. Immunol. 9: 301-309.
    • (2008) Nat. Immunol. , vol.9 , pp. 301-309
    • Arthos, J.1    Cicala, C.2    Martinelli, E.3
  • 33
    • 79251526530 scopus 로고    scopus 로고
    • HIV-1 envelope, integrins and co-receptor use in mucosal transmission of HIV
    • Cicala, C., J. Arthos & A.S. Fauci. 2011. HIV-1 envelope, integrins and co-receptor use in mucosal transmission of HIV. J. Transl. Med. 9(Suppl. 1): S2.
    • (2011) J. Transl. Med. , vol.9 , Issue.SUPPL. 1
    • Cicala, C.1    Arthos, J.2    Fauci, A.S.3
  • 34
    • 0037237790 scopus 로고    scopus 로고
    • Syndecan captures, protects, and transmits HIV to T lymphocytes
    • Bobardt, M.D., A.C. Saphire, H.C. Hung, et al. 2003. Syndecan captures, protects, and transmits HIV to T lymphocytes. Immunity 18: 27-39.
    • (2003) Immunity , vol.18 , pp. 27-39
    • Bobardt, M.D.1    Saphire, A.C.2    Hung, H.C.3
  • 35
    • 2542422996 scopus 로고    scopus 로고
    • Syndecans and HIV-1 pathogenesis
    • Gallay, P. 2004. Syndecans and HIV-1 pathogenesis. Microbes. Infect. 6: 617-622.
    • (2004) Microbes. Infect. , vol.6 , pp. 617-622
    • Gallay, P.1
  • 36
    • 37649009793 scopus 로고    scopus 로고
    • Syndecan-3 is a dendritic cell-specific attachment receptor for HIV-1
    • de Witte, L., M. Bobardt, U. Chatterji, et al. 2007. Syndecan-3 is a dendritic cell-specific attachment receptor for HIV-1. Proc. Natl. Acad. Sci. U S A. 104: 19464-19469.
    • (2007) Proc. Natl. Acad. Sci. U S A. , vol.104 , pp. 19464-19469
    • de Witte, L.1    Bobardt, M.2    Chatterji, U.3
  • 37
    • 37849027311 scopus 로고    scopus 로고
    • Galectin-1 promotes HIV-1 infectivity in macrophages through stabilization of viral adsorption
    • Mercier, S., C. St-Pierre, I. Pelletier, et al. 2008. Galectin-1 promotes HIV-1 infectivity in macrophages through stabilization of viral adsorption. Virology 371: 121-129.
    • (2008) Virology , vol.371 , pp. 121-129
    • Mercier, S.1    St-Pierre, C.2    Pelletier, I.3
  • 38
    • 84455161715 scopus 로고    scopus 로고
    • Galectin-1 specific inhibitors as a new class of compounds to treat HIV-1 infection
    • St-Pierre, C., M. Ouellet, D. Giguere, et al. 2012. Galectin-1 specific inhibitors as a new class of compounds to treat HIV-1 infection. Antimicrob. Agents Chemother. 56: 154-162.
    • (2012) Antimicrob. Agents Chemother , vol.56 , pp. 154-162
    • St-Pierre, C.1    Ouellet, M.2    Giguere, D.3
  • 40
    • 69549116580 scopus 로고    scopus 로고
    • Genetic and antigenic features of the transmitted virus
    • Keele, B.F. & C.A. Derdeyn. 2009. Genetic and antigenic features of the transmitted virus. Curr. Opin. HIV AIDS 4: 352-357.
    • (2009) Curr. Opin. HIV AIDS , vol.4 , pp. 352-357
    • Keele, B.F.1    Derdeyn, C.A.2
  • 41
    • 66049139947 scopus 로고    scopus 로고
    • Genetic identity, biological phenotype, and evolutionary pathways of transmitted/founder viruses in acute and early HIV-1 infection
    • Salazar-Gonzalez, J.F., M.G. Salazar, B.F. Keele, et al. 2009. Genetic identity, biological phenotype, and evolutionary pathways of transmitted/founder viruses in acute and early HIV-1 infection. J. Exp. Med. 206: 1273-1289.
    • (2009) J. Exp. Med. , vol.206 , pp. 1273-1289
    • Salazar-Gonzalez, J.F.1    Salazar, M.G.2    Keele, B.F.3
  • 42
    • 79251508013 scopus 로고    scopus 로고
    • Selective transmission of R5 HIV-1 variants: where is the gatekeeper?
    • Grivel, J.C., R.J. Shattock & L.B. Margolis. 2011. Selective transmission of R5 HIV-1 variants: where is the gatekeeper? J. Transl. Med. 9 (Suppl. 1): S6.
    • (2011) J. Transl. Med. , vol.9 , Issue.SUPPL. 1
    • Grivel, J.C.1    Shattock, R.J.2    Margolis, L.B.3
  • 43
    • 0033919404 scopus 로고    scopus 로고
    • Oligomeric modeling and electrostatic analysis of the gp120 envelope glycoprotein of human immunodeficiency virus
    • Kwong, P.D., R. Wyatt, Q.J. Sattentau, J. Sodroski et al. 2000. Oligomeric modeling and electrostatic analysis of the gp120 envelope glycoprotein of human immunodeficiency virus. J. Virol. 74: 1961-1972.
    • (2000) J. Virol. , vol.74 , pp. 1961-1972
    • Kwong, P.D.1    Wyatt, R.2    Sattentau, Q.J.3    Sodroski, J.4
  • 44
    • 0033920212 scopus 로고    scopus 로고
    • Selective interactions of polyanions with basic surfaces on human immunodeficiency virus type 1 gp120
    • Moulard, M., H. Lortat-Jacob, I. Mondor, et al. 2000. Selective interactions of polyanions with basic surfaces on human immunodeficiency virus type 1 gp120. J. Virol. 74: 1948-1960.
    • (2000) J. Virol. , vol.74 , pp. 1948-1960
    • Moulard, M.1    Lortat-Jacob, H.2    Mondor, I.3
  • 45
    • 12144289425 scopus 로고    scopus 로고
    • Envelope-constrained neutralization-sensitive HIV-1 after heterosexual transmission
    • Derdeyn, C.A., J.M. Decker, F. Bibollet-Ruche, et al. 2004. Envelope-constrained neutralization-sensitive HIV-1 after heterosexual transmission. Science 303: 2019-2022.
    • (2004) Science , vol.303 , pp. 2019-2022
    • Derdeyn, C.A.1    Decker, J.M.2    Bibollet-Ruche, F.3
  • 46
    • 42649129348 scopus 로고    scopus 로고
    • Env length and N-linked glycosylation following transmission of human immunodeficiency virus Type 1 subtype B viruses
    • Liu, Y., M.E. Curlin, K. Diem, et al. 2008. Env length and N-linked glycosylation following transmission of human immunodeficiency virus Type 1 subtype B viruses. Virology 374: 229-233.
    • (2008) Virology , vol.374 , pp. 229-233
    • Liu, Y.1    Curlin, M.E.2    Diem, K.3
  • 47
    • 77950493667 scopus 로고    scopus 로고
    • Donor and recipient envs from heterosexual human immunodeficiency virus subtype C transmission pairs require high receptor levels for entry
    • Alexander, M., R. Lynch, J. Mulenga, et al. 2010. Donor and recipient envs from heterosexual human immunodeficiency virus subtype C transmission pairs require high receptor levels for entry. J. Virol. 84: 4100-4104.
    • (2010) J. Virol. , vol.84 , pp. 4100-4104
    • Alexander, M.1    Lynch, R.2    Mulenga, J.3
  • 48
    • 0032742547 scopus 로고    scopus 로고
    • Sexual transmission and propagation of SIV and HIV in resting and activated CD4+ T cells
    • Zhang, Z., T. Schuler, M. Zupancic, et al. 1999. Sexual transmission and propagation of SIV and HIV in resting and activated CD4+ T cells. Science 286: 1353-1357.
    • (1999) Science , vol.286 , pp. 1353-1357
    • Zhang, Z.1    Schuler, T.2    Zupancic, M.3
  • 49
    • 77949409948 scopus 로고    scopus 로고
    • Targeting early infection to prevent HIV-1 mucosal transmission
    • Haase, A.T. 2010. Targeting early infection to prevent HIV-1 mucosal transmission. Nature 464: 217-223.
    • (2010) Nature , vol.464 , pp. 217-223
    • Haase, A.T.1
  • 50
    • 80555154835 scopus 로고    scopus 로고
    • HIV-1 N-glycan composition governs a balance between dendritic cell-mediated viral transmission and antigen presentation
    • van Montfort, T., D. Eggink, M. Boot, et al. 2011. HIV-1 N-glycan composition governs a balance between dendritic cell-mediated viral transmission and antigen presentation. J. Immunol. 187: 4676-4685.
    • (2011) J. Immunol. , vol.187 , pp. 4676-4685
    • van Montfort, T.1    Eggink, D.2    Boot, M.3
  • 51
    • 73949112038 scopus 로고    scopus 로고
    • The integrin alpha4beta7 forms a complex with cell-surface CD4 and defines a T-cell subset that is highly susceptible to infection by HIV-1
    • Cicala, C., E. Martinelli, J. P. McNally, et al. 2009. The integrin alpha4beta7 forms a complex with cell-surface CD4 and defines a T-cell subset that is highly susceptible to infection by HIV-1. Proc. Natl. Acad. Sci. U. S. A. 106: 20877-20882.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 20877-20882
    • Cicala, C.1    Martinelli, E.2    McNally, J.P.3
  • 52
    • 0026562144 scopus 로고
    • Comparison of female to male and male to female transmission of HIV in 563 stable couples.
    • European Study Group on Heterosexual Transmission of HIV
    • European Study Group on Heterosexual Transmission of HIV. 1992. Comparison of female to male and male to female transmission of HIV in 563 stable couples. BMJ 304: 809-813.
    • (1992) BMJ , vol.304 , pp. 809-813
  • 53
    • 0032127568 scopus 로고    scopus 로고
    • Heterosexual transmission of human immunodeficiency virus: variability of infectivity throughout the course of infection. European Study Group on Heterosexual Transmission of HIV
    • Leynaert, B., A.M. Downs & I. de Vincenzi. 1998. Heterosexual transmission of human immunodeficiency virus: variability of infectivity throughout the course of infection. European Study Group on Heterosexual Transmission of HIV. Am J Epidemiol 148: 88-96.
    • (1998) Am J Epidemiol , vol.148 , pp. 88-96
    • Leynaert, B.1    Downs, A.M.2    de Vincenzi, I.3
  • 54
    • 0036144814 scopus 로고    scopus 로고
    • Reducing the risk of sexual HIV transmission: quantifying the per-act risk for HIV on the basis of choice of partner, sex act, and condom use
    • Varghese, B., J.E. Maher, T.A. Peterman, et al. 2002. Reducing the risk of sexual HIV transmission: quantifying the per-act risk for HIV on the basis of choice of partner, sex act, and condom use. Sex. Transm. Dis. 29: 38-43.
    • (2002) Sex. Transm. Dis. , vol.29 , pp. 38-43
    • Varghese, B.1    Maher, J.E.2    Peterman, T.A.3
  • 55
    • 58549113211 scopus 로고    scopus 로고
    • Heterosexual risk of HIV-1 infection per sexual act: systematic review and meta-analysis of observational studies
    • Boily, M.C., R.F. Baggaley, L. Wang, et al. 2009. Heterosexual risk of HIV-1 infection per sexual act: systematic review and meta-analysis of observational studies. Lancet Infect. Dis. 9: 118-129.
    • (2009) Lancet Infect. Dis. , vol.9 , pp. 118-129
    • Boily, M.C.1    Baggaley, R.F.2    Wang, L.3
  • 56
    • 33747875872 scopus 로고    scopus 로고
    • Hepatitis B virus infection: epidemiology and vaccination
    • Shepard, C.W., E.P. Simard, L. Finelli, et al. 2006. Hepatitis B virus infection: epidemiology and vaccination. Epidemiol. Rev. 28: 112-125.
    • (2006) Epidemiol. Rev , vol.28 , pp. 112-125
    • Shepard, C.W.1    Simard, E.P.2    Finelli, L.3
  • 57
    • 0025264623 scopus 로고
    • Hepatitis B: transmission by sexual contact and needle sharing
    • discussion S41-33.
    • Piot, P., C. Goilav & E. Kegels. 1990. Hepatitis B: transmission by sexual contact and needle sharing. Vaccine 8(Suppl.): S37-40; discussion S41-33.
    • (1990) Vaccine , vol.8 , Issue.SUPPL.
    • Piot, P.1    Goilav, C.2    Kegels, E.3
  • 58
    • 17844374605 scopus 로고    scopus 로고
    • Massive infection and loss of memory CD4+ T cells in multiple tissues during acute SIV infection
    • Mattapallil, J.J., D.C. Douek, B. Hill, et al. 2005. Massive infection and loss of memory CD4+ T cells in multiple tissues during acute SIV infection. Nature 434: 1093-1097.
    • (2005) Nature , vol.434 , pp. 1093-1097
    • Mattapallil, J.J.1    Douek, D.C.2    Hill, B.3
  • 59
    • 4644342929 scopus 로고    scopus 로고
    • CD4+ T cell depletion during all stages of HIV disease occurs predominantly in the gastrointestinal tract
    • J.M. Brenchley, T.W. Schacker, L.E. Ruff, et al. 2004. CD4+ T cell depletion during all stages of HIV disease occurs predominantly in the gastrointestinal tract. J. Exp. Med. 200: 749-759.
    • (2004) J. Exp. Med. , vol.200 , pp. 749-759
    • Brenchley, J.M.1    Schacker, T.W.2    Ruff, L.E.3
  • 60
    • 0032540418 scopus 로고    scopus 로고
    • Gastrointestinal tract as a major site of CD4+ T cell depletion and viral replication in SIV infection
    • Veazey, R.S., M. DeMaria, L.V. Chalifoux, et al. 1998. Gastrointestinal tract as a major site of CD4+ T cell depletion and viral replication in SIV infection. Science 280: 427-431.
    • (1998) Science , vol.280 , pp. 427-431
    • Veazey, R.S.1    DeMaria, M.2    Chalifoux, L.V.3
  • 61
    • 33746892252 scopus 로고    scopus 로고
    • HIV infection: first battle decides the war
    • Hel, Z., J.R. McGhee & J. Mestecky. 2006. HIV infection: first battle decides the war. Trends Immunol. 27: 274-281.
    • (2006) Trends Immunol. , vol.27 , pp. 274-281
    • Hel, Z.1    McGhee, J.R.2    Mestecky, J.3
  • 62
    • 44649102135 scopus 로고    scopus 로고
    • Identification and characterization of transmitted and early founder virus envelopes in primary HIV-1 infection
    • Keele, B.F., E.E. Giorgi, J.F. Salazar-Gonzalez, et al. 2008. Identification and characterization of transmitted and early founder virus envelopes in primary HIV-1 infection. Proc. Natl. Acad. Sci. U. S. A. 105: 7552-7557.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 7552-7557
    • Keele, B.F.1    Giorgi, E.E.2    Salazar-Gonzalez, J.F.3
  • 63
    • 0031976829 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 attachment to HeLa CD4 cells is CD4 independent and gp120 dependent and requires cell surface heparans
    • Mondor, I., S. Ugolini & Q.J. Sattentau. 1998. Human immunodeficiency virus type 1 attachment to HeLa CD4 cells is CD4 independent and gp120 dependent and requires cell surface heparans. J. Virol. 72: 3623-3634.
    • (1998) J. Virol. , vol.72 , pp. 3623-3634
    • Mondor, I.1    Ugolini, S.2    Sattentau, Q.J.3
  • 64
    • 38349081511 scopus 로고    scopus 로고
    • The challenges of eliciting neutralizing antibodies to HIV-1 and to influenza virus
    • Karlsson Hedestam, G.B., R.A. Fouchier, S. Phogat, et al. 2008. The challenges of eliciting neutralizing antibodies to HIV-1 and to influenza virus. Nat. Rev. Microbiol. 6: 143-155.
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 143-155
    • Karlsson Hedestam, G.B.1    Fouchier, R.A.2    Phogat, S.3
  • 65
    • 25844482131 scopus 로고    scopus 로고
    • Perils at mucosal front lines for HIV and SIV and their hosts
    • Haase, A.T. 2005. Perils at mucosal front lines for HIV and SIV and their hosts. Nat. Rev. Immunol. 5: 783-792.
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 783-792
    • Haase, A.T.1
  • 66
    • 72949117233 scopus 로고    scopus 로고
    • The immune response during acute HIV-1 infection: clues for vaccine development
    • McMichael, A. J., P. Borrow, G.D. Tomaras, et al. 2010. The immune response during acute HIV-1 infection: clues for vaccine development. Nat. Rev. Immunol. 10: 11-23.
    • (2010) Nat. Rev. Immunol. , vol.10 , pp. 11-23
    • McMichael, A.J.1    Borrow, P.2    Tomaras, G.D.3
  • 67
    • 0345569681 scopus 로고    scopus 로고
    • Inhibiting sexual transmission of HIV-1 infection
    • Shattock, R.J. & J.P. Moore. 2003. Inhibiting sexual transmission of HIV-1 infection. Nat. Rev. Microbiol. 1: 25-34.
    • (2003) Nat. Rev. Microbiol. , vol.1 , pp. 25-34
    • Shattock, R.J.1    Moore, J.P.2
  • 68
    • 79960601577 scopus 로고    scopus 로고
    • Galectin-9 binding to cell surface protein disulfide isomerase regulates the redox environment to enhance T-cell migration and HIV entry
    • Bi, S., P.W. Hong, B. Lee & L.G. Baum. 2011. Galectin-9 binding to cell surface protein disulfide isomerase regulates the redox environment to enhance T-cell migration and HIV entry. Proc. Natl. Acad. Sci. U. S. A. 108: 10650-10655.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 10650-10655
    • Bi, S.1    Hong, P.W.2    Lee, B.3    Baum, L.G.4
  • 69
    • 0027169990 scopus 로고
    • The family of metazoan metal-independent beta-galactoside-binding lectins: structure, function and molecular evolution
    • Hirabayashi, J. & K. Kasai. 1993. The family of metazoan metal-independent beta-galactoside-binding lectins: structure, function and molecular evolution. Glycobiology 3: 297-304.
    • (1993) Glycobiology , vol.3 , pp. 297-304
    • Hirabayashi, J.1    Kasai, K.2
  • 71
    • 4644268104 scopus 로고    scopus 로고
    • Special issue on galectins
    • Leffler, H. 2004. Special issue on galectins. Glycoconj. J. 19: 433-638.
    • (2004) Glycoconj. J. , vol.19 , pp. 433-638
    • Leffler, H.1
  • 72
    • 67349258025 scopus 로고    scopus 로고
    • Turning 'sweet' on immunity: galectin-glycan interactions in immune tolerance and inflammation
    • Rabinovich, G.A. & M.A. Toscano. 2009. Turning 'sweet' on immunity: galectin-glycan interactions in immune tolerance and inflammation. Nat. Rev. Immunol. 9: 338-352.
    • (2009) Nat. Rev. Immunol. , vol.9 , pp. 338-352
    • Rabinovich, G.A.1    Toscano, M.A.2
  • 73
    • 1542337781 scopus 로고    scopus 로고
    • Seeing strangers or announcing "danger": galectin-3 in two models of innate immunity
    • Sato, S. & J. Nieminen. 2004. Seeing strangers or announcing "danger": galectin-3 in two models of innate immunity. Glycoconj. J. 19: 583-591.
    • (2004) Glycoconj. J , vol.19 , pp. 583-591
    • Sato, S.1    Nieminen, J.2
  • 74
    • 33847718338 scopus 로고    scopus 로고
    • Visualization of galectin-3 oligomerization on the surface of neutrophils and endothelial cells using fluorescence resonance energy transfer
    • Nieminen, J., A. Kuno, J. Hirabayashi & S. Sato. 2007. Visualization of galectin-3 oligomerization on the surface of neutrophils and endothelial cells using fluorescence resonance energy transfer. J. Biol. Chem. 282: 1374-1383.
    • (2007) J. Biol. Chem. , vol.282 , pp. 1374-1383
    • Nieminen, J.1    Kuno, A.2    Hirabayashi, J.3    Sato, S.4
  • 75
    • 27644480032 scopus 로고    scopus 로고
    • Galectin-3 interacts with naive and primed neutrophils, inducing innate immune responses
    • Nieminen, J., C. St-Pierre & S. Sato. 2005. Galectin-3 interacts with naive and primed neutrophils, inducing innate immune responses. J. Leukoc. Biol. 78: 1127-1135.
    • (2005) J. Leukoc. Biol. , vol.78 , pp. 1127-1135
    • Nieminen, J.1    St-Pierre, C.2    Sato, S.3
  • 77
    • 75749101401 scopus 로고    scopus 로고
    • Galectins: regulators of acute and chronic inflammation
    • Liu F.T. & G.A. Rabinovich. 2010. Galectins: regulators of acute and chronic inflammation. Ann. N. Y. Acad. Sci. 1183: 158-182.
    • (2010) Ann. N. Y. Acad. Sci. , vol.1183 , pp. 158-182
    • Liu, F.T.1    Rabinovich, G.A.2
  • 78
    • 67649774331 scopus 로고    scopus 로고
    • Galectins in innate immunity: dual functions of host soluble beta-galactoside-binding lectins as damage-associated molecular patterns (DAMPs) and as receptors for pathogen-associated molecular patterns (PAMPs)
    • Sato, S., C. St-Pierre, P. Bhaumik & J. Nieminen. 2009. Galectins in innate immunity: dual functions of host soluble beta-galactoside-binding lectins as damage-associated molecular patterns (DAMPs) and as receptors for pathogen-associated molecular patterns (PAMPs). Immunol. Rev. 230: 172-187.
    • (2009) Immunol. Rev , vol.230 , pp. 172-187
    • Sato, S.1    St-Pierre, C.2    Bhaumik, P.3    Nieminen, J.4
  • 79
    • 65649109738 scopus 로고    scopus 로고
    • Roles of galectins in infection
    • Vasta, G.R. 2009. Roles of galectins in infection. Nat. Rev. Microbiol. 7: 424-438.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 424-438
    • Vasta, G.R.1
  • 80
    • 0029944559 scopus 로고    scopus 로고
    • Regulated expression of a 16-kd galectin-like protein in activated rat macrophages
    • Rabinovich, G., L. Castagna, C. Landa, et al. 1996. Regulated expression of a 16-kd galectin-like protein in activated rat macrophages. J. Leukoc. Biol. 59: 363-370.
    • (1996) J. Leukoc. Biol. , vol.59 , pp. 363-370
    • Rabinovich, G.1    Castagna, L.2    Landa, C.3
  • 81
    • 0029257527 scopus 로고
    • Human thymic epithelial cells express an endogenous lectin, galectin-1, which binds to core 2 O-glycans on thymocytes and T lymphoblastoid cells
    • Baum, L.G., M. Pang, N.L. Perillo, et al. 1995. Human thymic epithelial cells express an endogenous lectin, galectin-1, which binds to core 2 O-glycans on thymocytes and T lymphoblastoid cells. J. Exp. Med. 181: 877-887.
    • (1995) J. Exp. Med. , vol.181 , pp. 877-887
    • Baum, L.G.1    Pang, M.2    Perillo, N.L.3
  • 82
    • 0034974155 scopus 로고    scopus 로고
    • Regulated expression of galectin-1 during B-cell activation and implications for T-cell apoptosis
    • Zuniga, E., G.A. Rabinovich, M.M. Iglesias & A. Gruppi. 2001. Regulated expression of galectin-1 during B-cell activation and implications for T-cell apoptosis. J. Leukoc. Biol. 70: 73-79.
    • (2001) J. Leukoc. Biol. , vol.70 , pp. 73-79
    • Zuniga, E.1    Rabinovich, G.A.2    Iglesias, M.M.3    Gruppi, A.4
  • 83
    • 0031928667 scopus 로고    scopus 로고
    • Beta-galactoside-binding protein secreted by activated T cells inhibits antigen-induced proliferation of T cells
    • Blaser, C., M. Kaufmann, C. Muller, et al. 1998. Beta-galactoside-binding protein secreted by activated T cells inhibits antigen-induced proliferation of T cells. Eur. J. Immunol. 28: 2311-2319.
    • (1998) Eur. J. Immunol. , vol.28 , pp. 2311-2319
    • Blaser, C.1    Kaufmann, M.2    Muller, C.3
  • 84
    • 0037230314 scopus 로고    scopus 로고
    • Regulated expression and ultrastructural localization of galectin-1, a proapoptotic beta-galactoside-binding lectin, during spermatogenesis in rat testis
    • Dettin, L., N. Rubinstein, A. Aoki, et al. 2003. Regulated expression and ultrastructural localization of galectin-1, a proapoptotic beta-galactoside-binding lectin, during spermatogenesis in rat testis. Biol. Reprod 68: 51-59.
    • (2003) Biol. Reprod , vol.68 , pp. 51-59
    • Dettin, L.1    Rubinstein, N.2    Aoki, A.3
  • 85
    • 3142694898 scopus 로고    scopus 로고
    • Binding of galectin-1 (gal-1) on trophoblast cells and inhibition of hormone production of trophoblast tumor cells in vitro by gal-1
    • Jeschke, U., T. Reimer, C. Bergemann, et al. 2004. Binding of galectin-1 (gal-1) on trophoblast cells and inhibition of hormone production of trophoblast tumor cells in vitro by gal-1. Histochem. Cell. Biol. 121: 501-508.
    • (2004) Histochem. Cell. Biol. , vol.121 , pp. 501-508
    • Jeschke, U.1    Reimer, T.2    Bergemann, C.3
  • 86
    • 30744445427 scopus 로고    scopus 로고
    • Galectin-3 and galectin-1 bind distinct cell surface glycoprotein receptors to induce T cell death
    • Stillman, B.N., D.K. Hsu, M. Pang, et al. 2006. Galectin-3 and galectin-1 bind distinct cell surface glycoprotein receptors to induce T cell death. J. Immunol. 176: 778-789.
    • (2006) J. Immunol. , vol.176 , pp. 778-789
    • Stillman, B.N.1    Hsu, D.K.2    Pang, M.3
  • 87
    • 80051923641 scopus 로고    scopus 로고
    • Nuclear factor (NF)-kappaB controls expression of the immunoregulatory glycan-binding protein galectin-1
    • Toscano, M.A., L. Campagna, L.L. Molinero, et al. 2011. Nuclear factor (NF)-kappaB controls expression of the immunoregulatory glycan-binding protein galectin-1. Mol. Immunol. 48: 1940-1949.
    • (2011) Mol. Immunol. , vol.48 , pp. 1940-1949
    • Toscano, M.A.1    Campagna, L.2    Molinero, L.L.3
  • 88
    • 58149102754 scopus 로고    scopus 로고
    • Immunohistochemical localization of six galectin subtypes in the mouse digestive tract
    • Nio-Kobayashi, J., H., Takahashi-Iwanaga & T. Iwanaga. 2009. Immunohistochemical localization of six galectin subtypes in the mouse digestive tract. J. Histochem. Cytochem. 57: 41-50.
    • (2009) J. Histochem. Cytochem. , vol.57 , pp. 41-50
    • Nio-Kobayashi, J.1    Takahashi-Iwanaga, H.2    Iwanaga, T.3
  • 89
    • 59449109414 scopus 로고    scopus 로고
    • Structural details and composition of Trichomonas vaginalis lipophosphoglycan in relevance to the epithelial immune function
    • Singh, B.N., G.R. Hayes, J.J. Lucas, et al. 2009. Structural details and composition of Trichomonas vaginalis lipophosphoglycan in relevance to the epithelial immune function. Glycoconj. J. 26: 3-17.
    • (2009) Glycoconj. J. , vol.26 , pp. 3-17
    • Singh, B.N.1    Hayes, G.R.2    Lucas, J.J.3
  • 90
    • 70450223320 scopus 로고    scopus 로고
    • Impact of T. vaginalis infection on innate immune responses and reproductive outcome
    • Fichorova, R.N. 2009. Impact of T. vaginalis infection on innate immune responses and reproductive outcome. J. Reprod. Immunol. 83: 185-189.
    • (2009) J. Reprod. Immunol. , vol.83 , pp. 185-189
    • Fichorova, R.N.1
  • 91
    • 0032959619 scopus 로고    scopus 로고
    • The tat protein of HIV-1 induces galectin-3 expression
    • Fogel, S., M. Guittaut, A. Legrand, et al. 1999. The tat protein of HIV-1 induces galectin-3 expression. Glycobiology 9: 383-387.
    • (1999) Glycobiology , vol.9 , pp. 383-387
    • Fogel, S.1    Guittaut, M.2    Legrand, A.3
  • 92
    • 70349382257 scopus 로고    scopus 로고
    • Efficient magnetic bead-based separation of HIV-1-infected cells using an improved reporter virus system reveals that p53 up-regulation occurs exclusively in the virus-expressing cell population
    • Imbeault, M., R. Lodge, M. Ouellet & M.J. Tremblay. 2009. Efficient magnetic bead-based separation of HIV-1-infected cells using an improved reporter virus system reveals that p53 up-regulation occurs exclusively in the virus-expressing cell population. Virology 393: 160-167.
    • (2009) Virology , vol.393 , pp. 160-167
    • Imbeault, M.1    Lodge, R.2    Ouellet, M.3    Tremblay, M.J.4
  • 93
    • 0028074969 scopus 로고
    • Regulation of secretion and surface expression of Mac-2, a galactoside-binding protein of macrophages
    • Sato, S. & R.C. Hughes. 1994. Regulation of secretion and surface expression of Mac-2, a galactoside-binding protein of macrophages. J. Biol. Chem. 269: 4424-4430.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4424-4430
    • Sato, S.1    Hughes, R.C.2
  • 94
    • 78651356179 scopus 로고    scopus 로고
    • Regulated expression of galectin-3, a multifunctional glycan-binding protein, in haematopoietic and non-haematopoietic tissues
    • Sundblad, V., D.O. Croci & G.A. Rabinovich. 2011. Regulated expression of galectin-3, a multifunctional glycan-binding protein, in haematopoietic and non-haematopoietic tissues. Histol. Histopathol 26: 247-265.
    • (2011) Histol. Histopathol , vol.26 , pp. 247-265
    • Sundblad, V.1    Croci, D.O.2    Rabinovich, G.A.3
  • 95
    • 33847785649 scopus 로고    scopus 로고
    • Selective ablation of proliferating microglial cells exacerbates ischemic injury in the brain
    • Lalancette-Hébert, M., G. Gowing, A. Simard, et al. 2007. Selective ablation of proliferating microglial cells exacerbates ischemic injury in the brain. J. Neurosci. 27: 2596-2605.
    • (2007) J. Neurosci. , vol.27 , pp. 2596-2605
    • Lalancette-Hébert, M.1    Gowing, G.2    Simard, A.3
  • 96
    • 18244404848 scopus 로고    scopus 로고
    • Regulatory roles of galectins in the immune response
    • Liu, F.T. 2005. Regulatory roles of galectins in the immune response. Int. Arch. Allergy. Immunol. 136, 385-400.
    • (2005) Int. Arch. Allergy. Immunol. , vol.136 , pp. 385-400
    • Liu, F.T.1
  • 97
    • 0036767357 scopus 로고    scopus 로고
    • Galectin as a molecule of danger signal, which could evoke immune response to infection
    • Sato, S. 2002. Galectin as a molecule of danger signal, which could evoke immune response to infection. Trends Glycosci. Glycotechnol. 14: 285-301.
    • (2002) Trends Glycosci. Glycotechnol , vol.14 , pp. 285-301
    • Sato, S.1
  • 98
    • 0030989330 scopus 로고    scopus 로고
    • Developmental regulation, expression, and apoptotic potential of galectin-9, a beta-galactoside binding lectin
    • Wada, J., K. Ota, A. Kumar, et al. 1997. Developmental regulation, expression, and apoptotic potential of galectin-9, a beta-galactoside binding lectin. J. Clin. Invest. 99: 2452-2461.
    • (1997) J. Clin. Invest. , vol.99 , pp. 2452-2461
    • Wada, J.1    Ota, K.2    Kumar, A.3
  • 99
    • 0032479178 scopus 로고    scopus 로고
    • Human ecalectin, a variant of human galectin-9, is a novel eosinophil chemoattractant produced by T lymphocytes
    • Matsumoto, R., H. Matsumoto, M. Seki, et al. 1998. Human ecalectin, a variant of human galectin-9, is a novel eosinophil chemoattractant produced by T lymphocytes. J. Biol. Chem. 273: 16976-16984.
    • (1998) J. Biol. Chem , vol.273 , pp. 16976-16984
    • Matsumoto, R.1    Matsumoto, H.2    Seki, M.3
  • 100
    • 62649106103 scopus 로고    scopus 로고
    • HIV-1 and microvesicles from T cells share a common glycome, arguing for a common origin
    • Krishnamoorthy, L., J.W. Bess, Jr., A.B. Preston, et al. 2009. HIV-1 and microvesicles from T cells share a common glycome, arguing for a common origin. Nat. Chem. Biol. 5: 244-250.
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 244-250
    • Krishnamoorthy, L.1    Bess Jr., J.W.2    Preston, A.B.3
  • 101
    • 0023664406 scopus 로고
    • Multiple soluble beta-galactoside-binding lectins from human lung
    • Sparrow, C.P., H. Leffler & S.H. Barondes. 1987. Multiple soluble beta-galactoside-binding lectins from human lung. J. Biol. Chem. 262: 7383-7390.
    • (1987) J. Biol. Chem. , vol.262 , pp. 7383-7390
    • Sparrow, C.P.1    Leffler, H.2    Barondes, S.H.3
  • 102
    • 0027965708 scopus 로고
    • Galectins. Structure and function of a large family of animal lectins
    • Barondes, S.H., D.N. Cooper, M.A. Gitt & H. Leffler. 1994. Galectins. Structure and function of a large family of animal lectins. J. Biol. Chem. 269: 20807-20810.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20807-20810
    • Barondes, S.H.1    Cooper, D.N.2    Gitt, M.A.3    Leffler, H.4
  • 103
    • 0036606914 scopus 로고    scopus 로고
    • Galectins and their ligands: amplifiers, silencers or tuners of the inflammatory response?
    • Rabinovich, G.A., L.G. Baum, N. Tinari, et al. 2002. Galectins and their ligands: amplifiers, silencers or tuners of the inflammatory response? Trends Immunol. 23: 313-320.
    • (2002) Trends Immunol. , vol.23 , pp. 313-320
    • Rabinovich, G.A.1    Baum, L.G.2    Tinari, N.3
  • 104
    • 0037136406 scopus 로고    scopus 로고
    • Oligosaccharide specificity of galectins: a search by frontal affinity chromatography
    • Hirabayashi, J., T. Hashidate, Y. Arata, et al. 2002. Oligosaccharide specificity of galectins: a search by frontal affinity chromatography. Biochim. Biophys. Acta. 1572: 232-254.
    • (2002) Biochim. Biophys. Acta. , vol.1572 , pp. 232-254
    • Hirabayashi, J.1    Hashidate, T.2    Arata, Y.3
  • 105
    • 44049104824 scopus 로고    scopus 로고
    • Galectin-1, -2, and -3 exhibit differential recognition of sialylated glycans and blood group antigens
    • Stowell, S.R., C.M. Arthur, P. Mehta, et al. 2008. Galectin-1, -2, and -3 exhibit differential recognition of sialylated glycans and blood group antigens. J. Biol. Chem. 283: 10109-10123.
    • (2008) J. Biol. Chem. , vol.283 , pp. 10109-10123
    • Stowell, S.R.1    Arthur, C.M.2    Mehta, P.3
  • 106
    • 33845976972 scopus 로고    scopus 로고
    • Human galectin-1, -2, and -4 induce surface exposure of phosphatidylserine in activated human neutrophils but not in activated T cells
    • Stowell, S.R., S. Karmakar, C.J. Stowell, et al. 2007. Human galectin-1, -2, and -4 induce surface exposure of phosphatidylserine in activated human neutrophils but not in activated T cells. Blood 109: 219-227.
    • (2007) Blood , vol.109 , pp. 219-227
    • Stowell, S.R.1    Karmakar, S.2    Stowell, C.J.3
  • 107
    • 0026673762 scopus 로고
    • Binding specificity of a baby hamster kidney lectin for H type I and II chains, polylactosamine glycans, and appropriately glycosylated forms of laminin and fibronectin
    • Sato, S. & R.C. Hughes. 1992. Binding specificity of a baby hamster kidney lectin for H type I and II chains, polylactosamine glycans, and appropriately glycosylated forms of laminin and fibronectin. J. Biol. Chem. 267: 6983-6990.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6983-6990
    • Sato, S.1    Hughes, R.C.2
  • 108
    • 0037124095 scopus 로고    scopus 로고
    • Specific recognition and cleavage of galectin-3 by Leishmania major through species-specific polygalactose epitope
    • Pelletier, I. & S. Sato. 2002. Specific recognition and cleavage of galectin-3 by Leishmania major through species-specific polygalactose epitope. J. Biol. Chem. 277: 17663-17670.
    • (2002) J. Biol. Chem. , vol.277 , pp. 17663-17670
    • Pelletier, I.1    Sato, S.2
  • 109
    • 0038605468 scopus 로고    scopus 로고
    • Specific recognition of Leishmania major poly-beta-galactosyl epitopes by galectin-9: possible implication of galectin-9 in interaction between L. major and host cells
    • Pelletier, I., T. Hashidate, T. Urashima, et al. 2003. Specific recognition of Leishmania major poly-beta-galactosyl epitopes by galectin-9: possible implication of galectin-9 in interaction between L. major and host cells. J. Biol. Chem. 278: 22223-22230.
    • (2003) J. Biol. Chem. , vol.278 , pp. 22223-22230
    • Pelletier, I.1    Hashidate, T.2    Urashima, T.3
  • 110
    • 34547099820 scopus 로고    scopus 로고
    • Differential glycosylation of T(H)1, T(H)2 and T(H)-17 effector cells selectively regulates susceptibility to cell death
    • Toscano, M.A., G.A. Bianco, J.M. Ilarregui, et al. 2007. Differential glycosylation of T(H)1, T(H)2 and T(H)-17 effector cells selectively regulates susceptibility to cell death. Nat. Immunol. 8: 825-834.
    • (2007) Nat. Immunol. , vol.8 , pp. 825-834
    • Toscano, M.A.1    Bianco, G.A.2    Ilarregui, J.M.3
  • 111
    • 17644441326 scopus 로고    scopus 로고
    • Altered T cell surface glycosylation in HIV-1 infection results in increased susceptibility to galectin-1-induced cell death
    • Lanteri, M., V. Giordanengo, N. Hiraoka, et al. 2003. Altered T cell surface glycosylation in HIV-1 infection results in increased susceptibility to galectin-1-induced cell death. Glycobiology 13: 909-918.
    • (2003) Glycobiology , vol.13 , pp. 909-918
    • Lanteri, M.1    Giordanengo, V.2    Hiraoka, N.3
  • 112
    • 0037155878 scopus 로고    scopus 로고
    • Syncytium formation and HIV-1 replication are both accentuated by purified influenza and virus-associated neuraminidase
    • Sun, J., B. Barbeau, S. Sato, et al. 2002. Syncytium formation and HIV-1 replication are both accentuated by purified influenza and virus-associated neuraminidase. J. Biol. Chem. 277: 9825-9833.
    • (2002) J. Biol. Chem. , vol.277 , pp. 9825-9833
    • Sun, J.1    Barbeau, B.2    Sato, S.3
  • 113
    • 0035947107 scopus 로고    scopus 로고
    • Neuraminidase from a bacterial source enhances both HIV-1-mediated syncytium formation and the virus binding/entry process
    • Sun, J., B. Barbeau, S. Sato & M.J. Tremblay. 2001. Neuraminidase from a bacterial source enhances both HIV-1-mediated syncytium formation and the virus binding/entry process. Virology 284: 26-36.
    • (2001) Virology , vol.284 , pp. 26-36
    • Sun, J.1    Barbeau, B.2    Sato, S.3    Tremblay, M.J.4
  • 114
    • 0024460246 scopus 로고
    • Conserved sequences in bacterial and viral sialidases
    • Roggentin, P., B. Rothe, J.B. Kaper, et al. 1989. Conserved sequences in bacterial and viral sialidases. Glycoconj. J. 6: 349-353.
    • (1989) Glycoconj. J , vol.6 , pp. 349-353
    • Roggentin, P.1    Rothe, B.2    Kaper, J.B.3
  • 115
    • 0027185635 scopus 로고
    • The sialidase superfamily and its spread by horizontal gene transfer
    • Roggentin, P., R. Schauer, L.L. Hoyer & E.R. Vimr. 1993. The sialidase superfamily and its spread by horizontal gene transfer. Mol. Microbiol. 9: 915-921.
    • (1993) Mol. Microbiol. , vol.9 , pp. 915-921
    • Roggentin, P.1    Schauer, R.2    Hoyer, L.L.3    Vimr, E.R.4
  • 116
    • 33746692516 scopus 로고    scopus 로고
    • Bacterial neuraminidase facilitates mucosal infection by participating in biofilm production
    • Soong, G., A. Muir, M.I. Gomez, et al. 2006. Bacterial neuraminidase facilitates mucosal infection by participating in biofilm production. J. Clin. Invest. 116: 2297-2305.
    • (2006) J. Clin. Invest. , vol.116 , pp. 2297-2305
    • Soong, G.1    Muir, A.2    Gomez, M.I.3
  • 117
    • 0019294102 scopus 로고
    • Structural studies of the sugar chains of cold-insoluble globulin isolated from human plasma
    • Takasaki, S., K. Yamashita, K. Suzuki & A. Kobata. 1980. Structural studies of the sugar chains of cold-insoluble globulin isolated from human plasma. J. Biochem. 88: 1587-1594.
    • (1980) J. Biochem. , vol.88 , pp. 1587-1594
    • Takasaki, S.1    Yamashita, K.2    Suzuki, K.3    Kobata, A.4
  • 118
    • 0024335289 scopus 로고
    • Structures of asparagine-linked oligosaccharides of human placental fibronectin
    • Takamoto, M., T. Endo, M. Isemura, et al. 1989. Structures of asparagine-linked oligosaccharides of human placental fibronectin. J. Biochem. 105: 742-750.
    • (1989) J. Biochem. , vol.105 , pp. 742-750
    • Takamoto, M.1    Endo, T.2    Isemura, M.3
  • 119
    • 70449590867 scopus 로고    scopus 로고
    • Discovery and classification of glycan-binding proteins
    • 2nd ed. A. Varki, R.D. Cummings, J. Esko, H.H. Freeze, P. Stanley, C.R. G. Bertozzi, W. Hart, & M.E. Etzler, Eds.:. Cold Spring Harbor Laboratory Press. New York
    • Varki, A., M.E. Etzler, R.D. Cummings & J.D. Esko. 2009. Discovery and classification of glycan-binding proteins. In Essentials of Glycobiology, 2nd ed. A. Varki, R.D. Cummings, J. Esko, H.H. Freeze, P. Stanley, C.R. G. Bertozzi, W. Hart, & M.E. Etzler, Eds.: 375-386. Cold Spring Harbor Laboratory Press. New York.
    • (2009) Essentials of Glycobiology , pp. 375-386
    • Varki, A.1    Etzler, M.E.2    Cummings, R.D.3    Esko, J.D.4
  • 121
    • 69249122444 scopus 로고    scopus 로고
    • Association of cell surface mucins with galectin-3 contributes to the ocular surface epithelial barrier
    • Argueso, P., A. Guzman-Aranguez, F. Mantelli, et al. 2009. Association of cell surface mucins with galectin-3 contributes to the ocular surface epithelial barrier. J. Biol. Chem. 284: 23037-23045.
    • (2009) J. Biol. Chem. , vol.284 , pp. 23037-23045
    • Argueso, P.1    Guzman-Aranguez, A.2    Mantelli, F.3
  • 122
    • 33646946320 scopus 로고    scopus 로고
    • Synthesis of multivalent lactose derivatives by 1,3-dipolar cycloadditions: selective galectin-1 inhibition
    • Tejler, J., E. Tullberg, T. Frejd, et al. 2006. Synthesis of multivalent lactose derivatives by 1, 3-dipolar cycloadditions: selective galectin-1 inhibition. Carbohydr. Res. 341: 1353-1362.
    • (2006) Carbohydr. Res , vol.341 , pp. 1353-1362
    • Tejler, J.1    Tullberg, E.2    Frejd, T.3
  • 123
    • 33744908340 scopus 로고    scopus 로고
    • Carbohydrate triazoles and isoxazoles as inhibitors of galectins-1 and -3
    • Giguere, D., R. Patnam, M.A. Bellefleur, et al. 2006. Carbohydrate triazoles and isoxazoles as inhibitors of galectins-1 and -3. Chem. Commun. (Camb). 22: 2379-2381.
    • (2006) Chem. Commun. (Camb). , vol.22 , pp. 2379-2381
    • Giguere, D.1    Patnam, R.2    Bellefleur, M.A.3
  • 124
    • 32144452076 scopus 로고    scopus 로고
    • Aryl O- and S-galactosides and lactosides as specific inhibitors of human galectins-1 and -3: role of electrostatic potential at O-3
    • Giguere, D., S. Sato, St-Pierre, C., et al. 2006. Aryl O- and S-galactosides and lactosides as specific inhibitors of human galectins-1 and -3: role of electrostatic potential at O-3. Bioorg. Med. Chem. Lett. 16: 1668-1672.
    • (2006) Bioorg. Med. Chem. Lett. , vol.16 , pp. 1668-1672
    • Giguere, D.1    Sato, S.2    St-Pierre, C.3
  • 125
    • 49349096307 scopus 로고    scopus 로고
    • Synthesis of stable and selective inhibitors of human galectins-1 and -3
    • Giguere, D., M.A. Bonin, P. Cloutier, et al. 2008. Synthesis of stable and selective inhibitors of human galectins-1 and -3. Bioorg. Med. Chem. 16: 7811-7823.
    • (2008) Bioorg. Med. Chem. , vol.16 , pp. 7811-7823
    • Giguere, D.1    Bonin, M.A.2    Cloutier, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.