메뉴 건너뛰기




Volumn 33, Issue 1, 2014, Pages 54-66

DC-SIGN, DC-SIGNR and LSECtin: C-type lectins for infection

Author keywords

DC SIGN; DC SIGNR; Gene structure; Infection; Lectins; LSECtin

Indexed keywords

ALLERGEN; CALCIUM ION; CD209 ANTIGEN; DC SIGNR PROTEIN; FUCOSE; LECTIN; LIGAND; LSECTIN PROTEIN; MANNOSE; UNCLASSIFIED DRUG;

EID: 84893121509     PISSN: 08830185     EISSN: 15635244     Source Type: Journal    
DOI: 10.3109/08830185.2013.834897     Document Type: Review
Times cited : (59)

References (80)
  • 1
    • 0035956986 scopus 로고    scopus 로고
    • Dc-signr, adc-sign homologue expressed in endothelial cells, binds to human and simianimmunodeficiency viruses and activates infection in trans
    • Pohlmann S, Soilleux EJ, Baribaud F, et al.DC-SIGNR, aDC-SIGN homologue expressed in endothelial cells, binds to human and simianimmunodeficiency viruses and activates infection in trans. Proc Natl Acad Sci USA 2001;98(5):2670-2675
    • (2001) Proc Natl Acad Sci USA , vol.98 , Issue.5 , pp. 2670-2675
    • Pohlmann, S.1    Soilleux, E.J.2    Baribaud, F.3
  • 2
    • 0034664758 scopus 로고    scopus 로고
    • DC-SIGN; a related gene, DC-SIGNR; and CD23 forma cluster on 19p13
    • Soilleux EJ, Barten R, Trowsdale J. DC-SIGN; a related gene, DC-SIGNR; and CD23 forma cluster on 19p13. J Immunol 2000;165(6):2937-2942
    • (2000) J Immunol , vol.165 , Issue.6 , pp. 2937-2942
    • Soilleux, E.J.1    Barten, R.2    Trowsdale, J.3
  • 3
    • 0037391145 scopus 로고    scopus 로고
    • Dc-sign (dendritic cell-specific icam-grabbing non-integrin) and dc-sign-related (dc-signr friend or foe
    • Soilleux EJ. DC-SIGN (dendritic cell-specific ICAM-grabbing non-integrin) and DC-SIGN-related (DC-SIGNR): Friend or foe Clin Sci (Lond) 2003;104(4):437-446
    • (2003) Clin Sci (Lond , vol.104 , Issue.4 , pp. 437-446
    • Soilleux, E.J.1
  • 4
    • 2442473249 scopus 로고    scopus 로고
    • Characterization of a novel C-type lectin-like gene, LSECtin: Demonstration of carbohydrate binding and expression in sinusoidal endothelial cells of liver and lymph node
    • Liu W, Tang L, Zhang G, et al. Characterization of a novel C-type lectin-like gene, LSECtin: Demonstration of carbohydrate binding and expression in sinusoidal endothelial cells of liver and lymph node. J Biol Chem 2004;279(18):18748-18758
    • (2004) J Biol Chem , vol.279 , Issue.18 , pp. 18748-18758
    • Liu, W.1    Tang, L.2    Zhang, G.3
  • 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, et al. DC-SIGN, a dendritic cell-specific HIV-1-binding protein that enhances trans-infection of T cells. Cell 2000;100(5):587-597
    • (2000) Cell , vol.100 , Issue.5 , pp. 587-597
    • Geijtenbeek, T.B.1    Kwon, D.S.2    Torensma, R.3
  • 6
    • 0036623112 scopus 로고    scopus 로고
    • DC-SIGN, a C-type lectin on dendritic cells that unveils many aspects of dendritic cell biology
    • Geijtenbeek TB, Engering A, Van Kooyk Y. DC-SIGN, a C-type lectin on dendritic cells that unveils many aspects of dendritic cell biology. J Leukoc Biol 2002;71(6):921-931
    • (2002) J Leukoc Biol , vol.71 , Issue.6 , pp. 921-931
    • Geijtenbeek, T.B.1    Engering, A.2    Van Kooyk, Y.3
  • 7
    • 40649123084 scopus 로고    scopus 로고
    • Interactions of LSECtin andDC-SIGN/DC-SIGNRwith viral ligands: Differential pHdependence, internalization and virion binding
    • Gramberg T, Soilleux E, Fisch T, et al. Interactions of LSECtin andDC-SIGN/DC-SIGNRwith viral ligands: Differential pHdependence, internalization and virion binding. Virology 2008;373(1):189-201
    • (2008) Virology , vol.373 , Issue.1 , pp. 189-201
    • Gramberg, T.1    Soilleux, E.2    Fisch, T.3
  • 8
    • 34250021363 scopus 로고    scopus 로고
    • The DC-SIGN-related lectin LSECtin mediates antigen capture and pathogen binding by human myeloid cells
    • Dominguez-Soto A, Aragoneses-Fenoll L, Martin-Gayo E, et al. The DC-SIGN-related lectin LSECtin mediates antigen capture and pathogen binding by human myeloid cells. Blood 2007;109(12):5337-5345
    • (2007) Blood , vol.109 , Issue.12 , pp. 5337-5345
    • Dominguez-Soto, A.1    Aragoneses-Fenoll, L.2    Martin-Gayo, E.3
  • 9
    • 67349253425 scopus 로고    scopus 로고
    • C-type lectin LSECtin interacts with DC-SIGNR and is involved in hepatitis C virus binding
    • 183-190
    • Li Y, Hao B, Kuai X, et al. C-type lectin LSECtin interacts with DC-SIGNR and is involved in hepatitis C virus binding.Mol Cell Biochem 2009;327(1-2):183-190
    • (2009) Mol Cell Biochem , vol.327 , pp. 1-2
    • Li, Y.1    Hao, B.2    Kuai, X.3
  • 10
    • 58949084492 scopus 로고    scopus 로고
    • The pathogen receptor liver and lymphnode sinusoidal endotelial cellC-type lectin is expressed in humanKupffer cells and regulated by PU1
    • Dominguez-Soto A, Aragoneses-Fenoll L, Ǵomez-Aguado F, et al. The pathogen receptor liver and lymphnode sinusoidal endotelial cellC-type lectin is expressed in humanKupffer cells and regulated by PU.1. Hepatology 2009;49(1):287-296
    • (2009) Hepatology , vol.49 , Issue.1 , pp. 287-296
    • Dominguez-Soto, A.1    Aragoneses-Fenoll, L.2    Ǵomez-Aguado, F.3
  • 11
    • 67349233479 scopus 로고    scopus 로고
    • Capture and transmission of HIV-1 by the C-type lectin L-SIGN (DC-SIGNR) is inhibited by carbohydrate-binding agents and polyanions
    • Auwerx J, François KO, Vanstreels E, et al. Capture and transmission of HIV-1 by the C-type lectin L-SIGN (DC-SIGNR) is inhibited by carbohydrate-binding agents and polyanions. Antiviral Res 2009;83(1):61-70
    • (2009) Antiviral Res , vol.83 , Issue.1 , pp. 61-70
    • Auwerx, J.1    François, K.O.2    Vanstreels, E.3
  • 12
    • 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, 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 ExpMed 2001;193(6):671-678
    • (2001) J ExpMed , vol.193 , Issue.6 , pp. 671-678
    • Bashirova, A.A.1    Geijtenbeek, T.B.2    Van Duijnhoven, G.C.3
  • 13
    • 0037447255 scopus 로고    scopus 로고
    • L-SIGN (CD 209L) is a liver-specific capture receptor for hepatitis C virus
    • Gardner JP, Durso RJ, Arrigale RR, et al. L-SIGN (CD 209L) is a liver-specific capture receptor for hepatitis C virus. Proc Natl Acad Sci USA 2003;100(8):4498-4503
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.8 , pp. 4498-4503
    • Gardner, J.P.1    Durso, R.J.2    Arrigale, R.R.3
  • 14
    • 0037379186 scopus 로고    scopus 로고
    • Hepatitis C virus glycoproteins interact with DC-SIGN and DC-SIGNR
    • Pohlmann S, Zhang J, Baribaud F, et al. Hepatitis C virus glycoproteins interact with DC-SIGN and DC-SIGNR. J Virol 2003;77(7):4070-4080
    • (2003) J Virol , vol.77 , Issue.7 , pp. 4070-4080
    • Pohlmann, S.1    Zhang, J.2    Baribaud, F.3
  • 15
    • 33745728738 scopus 로고    scopus 로고
    • Expression ofDC-SIGN andDC-SIGNR on human sinusoidal endothelium: A role for capturing hepatitis C virus particles
    • Lai WK, Sun PJ, Zhang J, et al. Expression ofDC-SIGN andDC-SIGNR on human sinusoidal endothelium: A role for capturing hepatitis C virus particles. AmJ Pathol 2006;169(1):200-208
    • (2006) AmJ Pathol , vol.169 , Issue.1 , pp. 200-208
    • Lai, W.K.1    Sun, P.J.2    Zhang, J.3
  • 16
    • 0344642934 scopus 로고    scopus 로고
    • DC-SIGN (CD209) mediates dengue virus infection of human dendritic cells
    • Tassaneetrithep B, Burgess TH, Granelli-Piperno A, et al. DC-SIGN (CD209) mediates dengue virus infection of human dendritic cells. J ExpMed 2003;197(7):823-829
    • (2003) J ExpMed , vol.197 , Issue.7 , pp. 823-829
    • Tassaneetrithep, B.1    Burgess, T.H.2    Granelli-Piperno, A.3
  • 17
    • 6344261967 scopus 로고    scopus 로고
    • DC-SIGN and DC-SIGNR interact with the glycoprotein of Marburg virus and the S protein of severe acute respiratory syndrome coronavirus
    • Marzi A, Gramberg T, Simmons G, et al. DC-SIGN and DC-SIGNR interact with the glycoprotein of Marburg virus and the S protein of severe acute respiratory syndrome coronavirus. J Virol 2004;78(21):12090-12095
    • (2004) J Virol , vol.78 , Issue.21 , pp. 12090-12095
    • Marzi, A.1    Gramberg, T.2    Simmons, G.3
  • 18
    • 29444444113 scopus 로고    scopus 로고
    • Homozygous L-SIGN (CLEC4M) plays a protective role in SARS coronavirus infection
    • Chan VS, Chan KY, Chen Y, et al. Homozygous L-SIGN (CLEC4M) plays a protective role in SARS coronavirus infection. Nat Genet 2006;38(1):38-46
    • (2006) Nat Genet , vol.38 , Issue.1 , pp. 38-46
    • Chan, V.S.1    Chan, K.Y.2    Chen, Y.3
  • 19
    • 84857081598 scopus 로고    scopus 로고
    • Identification of cell surface molecules involved in dystroglycan- independent Lassa virus cell entry
    • Shimojima M, Str?oher U, Ebihara H, et al. Identification of cell surface molecules involved in dystroglycan-independent Lassa virus cell entry. J Virol 2012;86(4):2067-2078
    • (2012) J Virol , vol.86 , Issue.4 , pp. 2067-2078
    • Shimojima, M.1    Stroher, U.2    Ebihara, H.3
  • 20
    • 0037237593 scopus 로고    scopus 로고
    • Mycobacteria target DC-SIGN to suppress dendritic cell function
    • Geijtenbeek TB, Van Vliet SJ, Koppel EA, et al. Mycobacteria target DC-SIGN to suppress dendritic cell function. J ExpMed 2003;197(1):7-17
    • (2003) J ExpMed , vol.197 , Issue.1 , pp. 7-17
    • Geijtenbeek, T.B.1    Van Vliet, S.J.2    Koppel, E.A.3
  • 21
    • 79953151566 scopus 로고    scopus 로고
    • Identification of four novel dc-sign ligands on mycobacterium bovis bcg
    • Carroll MV, Sim RB, Bigi F, et al. Identification of four novel DC-SIGN ligands on Mycobacterium bovis BCG. Protein Cell 2010;1(9):859-870
    • (2010) Protein Cell , vol.1 , Issue.9 , pp. 859-870
    • Carroll, M.V.1    Sim, R.B.2    Bigi, F.3
  • 22
    • 57549098955 scopus 로고    scopus 로고
    • Bchemical synthesis of all hosphatidylinositolmannoside (PIM) glycans fromMycobacterium tuberculosis
    • Boonyarattanakalin S, LiuX,Michieletti M, et al.Chemical synthesis of all phosphatidylinositolmannoside (PIM) glycans fromMycobacterium tuberculosis. J Am Chem Soc 2008;130(49):16791-16799
    • (2008) J Am Chem Soc , vol.130 , Issue.49 , pp. 16791-16799
    • Boonyarattanakalin, S.1    Liu, X.2    Michieletti, M.3
  • 23
    • 70349414430 scopus 로고    scopus 로고
    • Role of phosphatidylinositolmannosides in the interaction betweenmycobacteria and DC-SIGN
    • Driessen NN, Ummels R,Maaskant JJ, et al. Role of phosphatidylinositolmannosides in the interaction betweenmycobacteria and DC-SIGN. Infect Immun 2009;77(10):4538-4547
    • (2009) Infect Immun , vol.77 , Issue.10 , pp. 4538-4547
    • Driessen, N.N.1    Ummels, R.2    Maaskant, J.J.3
  • 24
    • 73649101258 scopus 로고    scopus 로고
    • Ehlers S.DC-SIGN Andmannosylated Surface Structures OfMycobacteriumtuberculosis: A Deceptive Liaison
    • Ehlers S.DC-SIGN andmannosylated surface structures ofMycobacteriumtuberculosis: A deceptive liaison. Eur J Cell Biol 2010;89(1):95-101
    • Eur J Cell Biol 2010 , vol.89 , Issue.1 , pp. 95-101
  • 25
    • 77949556108 scopus 로고    scopus 로고
    • Identification of mycobacterial alpha-glucan as a novel ligand for DC-SIGN: Involvement of mycobacterial capsular polysaccharides in host immune modulation
    • Geurtsen J, Chedammi S, Mesters J, et al. Identification of mycobacterial alpha-glucan as a novel ligand for DC-SIGN: Involvement of mycobacterial capsular polysaccharides in host immune modulation. J Immunol 2009;183(8):5221-5231
    • (2009) J Immunol , vol.183 , Issue.8 , pp. 5221-5231
    • Geurtsen, J.1    Chedammi, S.2    Mesters, J.3
  • 26
    • 0037442109 scopus 로고    scopus 로고
    • Cutting edge: Carbohydrate profiling identifies new pathogens that interact with dendritic cell-specific ICAM-3-grabbing nonintegrin on dendritic cells
    • Appelmelk BJ, van Die I, van Vliet SJ, et al. Cutting edge: Carbohydrate profiling identifies new pathogens that interact with dendritic cell-specific ICAM-3-grabbing nonintegrin on dendritic cells. J Immunol 2003;170(4):1635-1639
    • (2003) J Immunol , vol.170 , Issue.4 , pp. 1635-1639
    • Appelmelk, B.J.1    Van Die, I.2    Van Vliet, S.J.3
  • 27
    • 7244246930 scopus 로고    scopus 로고
    • Helicobacter pylorimodulates the T helper cell 1/T helper cell 2 balance through phase-variable interaction between lipopolysaccharide and DC-SIGN
    • BergmanMP, Engering A, Smits HH, et al.Helicobacter pylorimodulates the T helper cell 1/T helper cell 2 balance through phase-variable interaction between lipopolysaccharide and DC-SIGN. J Exp Med 2004;200(8):979-990
    • (2004) J Exp Med , vol.200 , Issue.8 , pp. 979-990
    • Bergman, M.P.1    Engering, A.2    Smits, H.H.3
  • 28
    • 33644821162 scopus 로고    scopus 로고
    • Neisseria meningitidis expressing lgtB lipopolysaccharide targets DC-SIGN and modulates dendritic cell function
    • Steeghs L, van Vliet S, Uronen-Hansson H, et al. Neisseria meningitidis expressing lgtB lipopolysaccharide targets DC-SIGN and modulates dendritic cell function. Cell Microbiol 2006;8(2):316-325
    • (2006) Cell Microbiol , vol.8 , Issue.2 , pp. 316-325
    • Steeghs, L.1    Van Vliet, S.2    Uronen-Hansson, H.3
  • 29
    • 0037331548 scopus 로고    scopus 로고
    • Thec-type lectindc-sign(cd209) is an antigen-uptake receptor for candida albicans on dendritic cells
    • CambiA,GijzenK,deVries IJ, et al.TheC-type lectinDC-SIGN(CD209) is an antigen-uptake receptor for Candida albicans on dendritic cells. Eur J Immunol 2003;33(2):532-538
    • (2003) Eur J Immunol , vol.33 , Issue.2 , pp. 532-538
    • Cambi, A.1    Gijzen, K.2    DeVries, I.J.3
  • 30
    • 6344268943 scopus 로고    scopus 로고
    • Dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrinmediates binding and internalization of Aspergillus fumigatus conidia by dendritic cells andmacrophages
    • Serrano-Gomez D, Doḿinguez-Soto A, Ancochea J, et al. Dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrinmediates binding and internalization of Aspergillus fumigatus conidia by dendritic cells andmacrophages. J Immunol 2004;173(9):5635-5643
    • (2004) J Immunol , vol.173 , Issue.9 , pp. 5635-5643
    • Serrano-Gomez, D.1    Doḿinguez-Soto, A.2    Ancochea, J.3
  • 31
    • 77950627537 scopus 로고    scopus 로고
    • Schistosoma mansoni worm glycolipids induce an inflammatory phenotype in human dendritic cells by cooperation of tlr4 and dc-sign
    • van Stijn CM, Meyer S, van den Broek M, et al. Schistosoma mansoni worm glycolipids induce an inflammatory phenotype in human dendritic cells by cooperation of TLR4 and DC-SIGN. Mol Immunol 2010;47(7-8):1544-1552
    • (2010) Mol Immunol , vol.47 , Issue.7-8 , pp. 1544-1552
    • Van Stijn, C.M.1    Meyer, S.2    Van Den Broek, M.3
  • 32
    • 27844597218 scopus 로고    scopus 로고
    • DC-SIGN mediates binding of dendritic cells to authentic pseudo-LewisY glycolipids of Schistosoma mansoni cercariae, the first parasite-specific ligand ofDCSIGN
    • Meyer S, van Liempt E, Imberty A, et al. DC-SIGN mediates binding of dendritic cells to authentic pseudo-LewisY glycolipids of Schistosoma mansoni cercariae, the first parasite-specific ligand ofDCSIGN. J Biol Chem 2005;280(45):37349-37359
    • (2005) J Biol Chem , vol.280 , Issue.45 , pp. 37349-37359
    • Meyer, S.1    Van Liempt, E.2    Imberty, A.3
  • 33
    • 0037183983 scopus 로고    scopus 로고
    • Dendritic cell (dc)-specific intercellular adhesion molecule 3 (icam-3)-grabbing nonintegrin (dc-sign, cd209), a c-type surface lectin in human dcs, is a receptor for leishmania amastigotes
    • Colmenares M, Puig-Kroger A, Pello OM, et al. Dendritic cell (DC)-specific intercellular adhesion molecule 3 (ICAM-3)-grabbing nonintegrin (DC-SIGN, CD209), a C-type surface lectin in human DCs, is a receptor for Leishmania amastigotes. J Biol Chem 2002;277(39):36766-36769
    • (2002) J Biol Chem , vol.277 , Issue.39 , pp. 36766-36769
    • Colmenares, M.1    Puig-Kroger, A.2    Pello, O.M.3
  • 34
    • 1942469317 scopus 로고    scopus 로고
    • Dynamic populations of dendritic cell-specific ICAM-3 grabbing nonintegrin-positive immature dendritic cells and liver/lymph node-specific ICAM-3 grabbing nonintegrin-positive endothelial cells in the outer zones of the paracortex of human lymph nodes
    • Engering A, vanVliet SJ,HebedaK, et al.Dynamic populations of dendritic cell-specific ICAM-3 grabbing nonintegrin-positive immature dendritic cells and liver/lymph node-specific ICAM-3 grabbing nonintegrin-positive endothelial cells in the outer zones of the paracortex of human lymph nodes. Am J Pathol 2004;164(5):1587-1595
    • (2004) Am J Pathol , vol.164 , Issue.5 , pp. 1587-1595
    • Engering, A.1    Vanvliet, S.J.2    Hebeda, K.3
  • 35
    • 8144221600 scopus 로고    scopus 로고
    • CD209L (L-SIGN) is a receptor for severe acute respiratory syndrome coronavirus
    • Jeffers SA, Tusell SM, Gillim-Ross L, et al. CD209L (L-SIGN) is a receptor for severe acute respiratory syndrome coronavirus. Proc Natl Acad Sci USA 2004;101(44):15748-15753
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.44 , pp. 15748-15753
    • Jeffers, S.A.1    Tusell, S.M.2    Gillim-Ross, L.3
  • 36
    • 79952410920 scopus 로고    scopus 로고
    • N-linked glycosylation facilitates sialic acid-independent attachment and entry of influenza A viruses into cells expressing DC-SIGN or L-SIGN
    • Londrigan SL, Turville SG, TateMD, et al. N-linked glycosylation facilitates sialic acid-independent attachment and entry of influenza A viruses into cells expressing DC-SIGN or L-SIGN. J Virol 2011;85(6):2990-3000
    • (2011) J Virol , vol.85 , Issue.6 , pp. 2990-3000
    • Londrigan, S.L.1    Turville, S.G.2    Tate, M.D.3
  • 37
    • 24944536732 scopus 로고    scopus 로고
    • LSECtin interacts with filovirus glycoproteins and the spike protein of SARS coronavirus
    • Gramberg T,HofmannH,Moller P, et al. LSECtin interacts with filovirus glycoproteins and the spike protein of SARS coronavirus. Virology 2005;340(2):224-236
    • (2005) Virology , vol.340 , Issue.2 , pp. 224-236
    • Gramberg, T.1    Hofmann, H.2    Moller, P.3
  • 38
    • 79956067859 scopus 로고    scopus 로고
    • Mouse lsectin as a model for a human ebola virus receptor
    • Pipirou Z, PowleslandAS, Steffen I, et al.Mouse LSECtin as a model for a human Ebola virus receptor. Glycobiology 2011;21(6):806-812
    • (2011) Glycobiology , vol.21 , Issue.6 , pp. 806-812
    • Pipirou, Z.1    Powlesland, A.S.2    Steffen, I.3
  • 39
    • 57149095908 scopus 로고    scopus 로고
    • Mutation in the DC-SIGN cytoplasmic triacidic cluster motif markedly attenuates receptor activity for phagocytosis and endocytosis of mannose-containing ligands by humanmyeloid cells
    • Azad AK, Torrelles JB, Schlesinger LS. Mutation in the DC-SIGN cytoplasmic triacidic cluster motif markedly attenuates receptor activity for phagocytosis and endocytosis of mannose-containing ligands by humanmyeloid cells. J Leukoc Biol 2008;84(6):1594-1603
    • (2008) J Leukoc Biol , vol.84 , Issue.6 , pp. 1594-1603
    • Azad, A.K.1    Torrelles, J.B.2    Schlesinger, L.S.3
  • 40
    • 13844322103 scopus 로고    scopus 로고
    • Distinct functions of DC-SIGN and its homologues L-SIGN (DC-SIGNR) and mSIGNR1 in pathogen recognition and immune regulation
    • Koppel EA, van Gisbergen KP, Geijtenbeek TB, van Kooyk Y. Distinct functions of DC-SIGN and its homologues L-SIGN (DC-SIGNR) and mSIGNR1 in pathogen recognition and immune regulation. CellMicrobiol 2005;7(2):157-165
    • (2005) CellMicrobiol , vol.7 , Issue.2 , pp. 157-165
    • Koppel, E.A.1    Van Gisbergen, K.P.2    Geijtenbeek, T.B.3    Van Kooyk, Y.4
  • 41
    • 61349116722 scopus 로고    scopus 로고
    • Identification of a porcine DC-SIGN-related C-type lectin, porcine CLEC4G (LSECtin), and its order of intron removal during splicing: Comparative genomic analyses of the cluster of genes CD23/CLEC4G/DC-SIGN among mammalian species
    • Huang YW, Meng XJ. Identification of a porcine DC-SIGN-related C-type lectin, porcine CLEC4G (LSECtin), and its order of intron removal during splicing: Comparative genomic analyses of the cluster of genes CD23/CLEC4G/DC-SIGN among mammalian species. Dev Comp Immunol 2009;33(6):747-760
    • (2009) Dev Comp Immunol , vol.33 , Issue.6 , pp. 747-760
    • Huang, Y.W.1    Meng, X.J.2
  • 42
    • 63449087888 scopus 로고    scopus 로고
    • Autonomous tetramerization domains in the glycanbinding receptors DC-SIGN and DC-SIGNR
    • Yu QD, Oldring AP, Powlesland AS, et al. Autonomous tetramerization domains in the glycanbinding receptors DC-SIGN and DC-SIGNR. JMol Biol 2009;387(5):1075-1080
    • (2009) JMol Biol , vol.387 , Issue.5 , pp. 1075-1080
    • Yu, Q.D.1    Oldring, A.P.2    Powlesland, A.S.3
  • 43
    • 0035800757 scopus 로고    scopus 로고
    • A novel mechanism of carbohydrate recognition by the Ctype 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 Ctype lectins DC-SIGN and DC-SIGNR: Subunit organization and binding to multivalent ligands. J Biol Chem 2001;276(31):28939-28945
    • (2001) J Biol Chem , vol.276 , Issue.31 , pp. 28939-28945
    • Mitchell, D.A.1    Fadden, A.J.2    Drickamer, K.3
  • 44
    • 70449533662 scopus 로고    scopus 로고
    • Segmented helical structure of the neck region of the glycanbinding receptor DC-SIGNR
    • Feinberg H, Tso CK, Taylor ME, et al. Segmented helical structure of the neck region of the glycanbinding receptor DC-SIGNR. JMol Biol 2009;394(4):613-620
    • (2009) JMol Biol , vol.394 , Issue.4 , pp. 613-620
    • Feinberg, H.1    Tso, C.K.2    Taylor, M.E.3
  • 45
    • 77949656707 scopus 로고    scopus 로고
    • Influence of polymorphism in dendritic cellspecific intercellular adhesionmolecule-3-grabbing nonintegrin-related (dc-signr) gene on hiv-1trans-infection
    • Zhu D, Kawana-Tachikawa A, Iwamoto A, Kitamura Y. Influence of polymorphism in dendritic cellspecific intercellular adhesionmolecule-3-grabbing nonintegrin-related (DC-SIGNR) gene on HIV-1trans-infection. Biochem Biophys Res Commun 2010;393(4):598-602
    • (2010) Biochem Biophys Res Commun , vol.393 , Issue.4 , pp. 598-602
    • Zhu, D.1    Kawana-Tachikawa, A.2    Iwamoto, A.3    Kitamura, Y.4
  • 46
    • 33646055497 scopus 로고    scopus 로고
    • Impact of polymorphisms in the DC-SIGNR neck domain on the interaction with pathogens
    • Gramberg T, Zhu T, Chaipan C, et al. Impact of polymorphisms in the DC-SIGNR neck domain on the interaction with pathogens. Virology 2006;347(2):354-363
    • (2006) Virology , vol.347 , Issue.2 , pp. 354-363
    • Gramberg, T.1    Zhu, T.2    Chaipan, C.3
  • 47
    • 84863375747 scopus 로고    scopus 로고
    • Relationship between intrauterine infection and the gene polymorphism of dc-signdc-signr in the pregnant women of hbv positive
    • Liu SR, Weng HB, Wu J, et al. Relationship between intrauterine infection and the gene polymorphism of DC-SIGN/DC-SIGNR in the pregnant women of HBV positive. Zhonghua Shi Yan He Lin Chuang Bing Du Xue Za Zhi 2011;25(5):331-333
    • (2011) Zhonghua Shi Yan He Lin Chuang Bing Du Xue Za Zhi , vol.25 , Issue.5 , pp. 331-333
    • Liu, S.R.1    Weng, H.B.2    Wu, J.3
  • 48
    • 77958156857 scopus 로고    scopus 로고
    • The association of genetic polymorphism of dendritic cellspecific ICAM-grabbing nonintegrin and hepatitis C infection
    • Wang M, Han HX, Lu J, et al. The association of genetic polymorphism of dendritic cellspecific ICAM-grabbing nonintegrin and hepatitis C infection. Zhonghua Gan Zang Bing Za Zhi 2009;17(9):645-648
    • (2009) Zhonghua Gan Zang Bing Za Zhi , vol.17 , Issue.9 , pp. 645-648
    • Wang, M.1    Han, H.X.2    Lu, J.3
  • 49
    • 12444347833 scopus 로고    scopus 로고
    • Extended neck regions stabilize tetramers of the receptors DC-SIGN and DC-SIGNR
    • Feinberg H, Guo Y, Mitchell DA, et al. Extended neck regions stabilize tetramers of the receptors DC-SIGN and DC-SIGNR. J Biol Chem 2005;280(2):1327-1335
    • (2005) J Biol Chem , vol.280 , Issue.2 , pp. 1327-1335
    • Feinberg, H.1    Guo, Y.2    Mitchell, D.A.3
  • 50
    • 73249137806 scopus 로고    scopus 로고
    • The neck-region polymorphism of dc-signr in peri-centenarian from han chinese population
    • Li H, Wang C-Y, Wang J-X, et al.The neck-region polymorphism of DC-SIGNR in peri-centenarian from Han Chinese population. BMCMed Genet 2009;10:134
    • (2009) BMCMed Genet , vol.10 , pp. 134
    • Li, H.1    Wang, C.-Y.2    Wang, J.-X.3
  • 51
    • 79959944073 scopus 로고    scopus 로고
    • Geometry and adhesion of extracellular domains of dc-signr neck length variants analyzed by force-distance measurements
    • Leckband DE, Menon S, Rosenberg K, et al. Geometry and adhesion of extracellular domains of DC-SIGNR neck length variants analyzed by force-distance measurements. Biochemistry 2011;50(27):6125-6132
    • (2011) Biochemistry , vol.50 , Issue.27 , pp. 6125-6132
    • Leckband, D.E.1    Menon, S.2    Rosenberg, K.3
  • 52
    • 0035824446 scopus 로고    scopus 로고
    • Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR
    • Feinberg H,Mitchell DA, Drickamer K,WeisWI. Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR. Science 2001;294(5549):2163-2166
    • (2001) Science , vol.294 , Issue.5549 , pp. 2163-2166
    • Feinberg, H.1    Mitchell, D.A.2    Drickamer, K.3    Weis, W.I.4
  • 53
    • 0035663209 scopus 로고    scopus 로고
    • Placental expression ofDC-SIGNmay mediate intrauterine vertical transmission of HIV
    • Soilleux EJ,Morris LS, LeeB, et al. Placental expression ofDC-SIGNmay mediate intrauterine vertical transmission of HIV. J Pathol 2001;195(5):586-592
    • (2001) J Pathol , vol.195 , Issue.5 , pp. 586-592
    • Soilleux, E.J.1    Morris, L.S.2    Lee, B.3
  • 54
    • 0036521487 scopus 로고    scopus 로고
    • Constitutive and induced expression of DC-SIGN on dendritic cell and macrophage subpopulations in situ and in vitro
    • Soilleux EJ, Morris LS, Leslie G, et al. Constitutive and induced expression of DC-SIGN on dendritic cell and macrophage subpopulations in situ and in vitro. J Leukoc Biol 2002;71(3):445-457
    • (2002) J Leukoc Biol , vol.71 , Issue.3 , pp. 445-457
    • Soilleux, E.J.1    Morris, L.S.2    Leslie, G.3
  • 55
    • 0036149902 scopus 로고    scopus 로고
    • Expression ofDC-SIGN by dendritic cells of intestinal and genitalmucosae in humans and rhesusmacaques
    • Jameson B, Baribaud F, Pohlmann S, et al. Expression ofDC-SIGN by dendritic cells of intestinal and genitalmucosae in humans and rhesusmacaques. J Virol 2002;76(4):1866-1875
    • (2002) J Virol , vol.76 , Issue.4 , pp. 1866-1875
    • Jameson, B.1    Baribaud, F.2    Pohlmann, S.3
  • 56
    • 15244356948 scopus 로고    scopus 로고
    • Characterization of DC-SIGN/R interaction with human immunodeficiency virus type 1 gp120 and ICAMmolecules favors the receptor's role as an antigencapturing rather than an adhesion receptor
    • Snyder GA, Ford J, Torabi-Parizi P, et al. Characterization of DC-SIGN/R interaction with human immunodeficiency virus type 1 gp120 and ICAMmolecules favors the receptor's role as an antigencapturing rather than an adhesion receptor. J Virol 2005;79(8):4589-4598
    • (2005) J Virol , vol.79 , Issue.8 , pp. 4589-4598
    • Snyder, G.A.1    Ford, J.2    Torabi-Parizi, P.3
  • 57
    • 84857262504 scopus 로고    scopus 로고
    • Retagging identifies dendritic cell-specific intercellular adhesion molecule-3 (ICAM3)-grabbing non-integrin (DC-SIGN) protein as a novel receptor for a major allergen from house dustmite
    • Emara M, Royer PJ, Mahdavi J, et al. Retagging identifies dendritic cell-specific intercellular adhesion molecule-3 (ICAM3)-grabbing non-integrin (DC-SIGN) protein as a novel receptor for a major allergen from house dustmite. J Biol Chem 2012;287(8):5756-5763
    • (2012) J Biol Chem , vol.287 , Issue.8 , pp. 5756-5763
    • Emara, M.1    Royer, P.J.2    Mahdavi, J.3
  • 58
    • 77951088538 scopus 로고    scopus 로고
    • The DC-SIGN family member LSECtin is a novel ligand of CD44 on activated T cells
    • Tang L, Yang J, Tang X, et al. The DC-SIGN family member LSECtin is a novel ligand of CD44 on activated T cells. Eur J Immunol 2010;40(4):1185-1191
    • (2010) Eur J Immunol , vol.40 , Issue.4 , pp. 1185-1191
    • Tang, L.1    Yang, J.2    Tang, X.3
  • 59
    • 70349432265 scopus 로고    scopus 로고
    • Liver sinusoidal endothelial cell lectin, LSECtin, negatively regulates hepatic T-cell immune response
    • e1-5
    • Tang L, Yang J, Liu W, et al. Liver sinusoidal endothelial cell lectin, LSECtin, negatively regulates hepatic T-cell immune response. Gastroenterology 2009;137(4):1498-1508; e1-5
    • (2009) Gastroenterology , vol.137 , Issue.4 , pp. 1498-1508
    • Tang, L.1    Yang, J.2    Liu, W.3
  • 60
    • 0036499125 scopus 로고    scopus 로고
    • The dendritic cell-specific adhesion receptorDC-SIGN internalizes antigen for presentation to T cells
    • Engering A,Geijtenbeek TB, vanVliet SJ, et al.The dendritic cell-specific adhesion receptorDC-SIGN internalizes antigen for presentation to T cells. J Immunol 2002;168(5):2118-2126
    • (2002) J Immunol , vol.168 , Issue.5 , pp. 2118-2126
    • Engering, A.1    Geijtenbeek, T.B.2    Vanvliet, S.J.3
  • 61
    • 3042788418 scopus 로고    scopus 로고
    • Hepatitis C virus targets DC-SIGN and L-SIGN to escape lysosomal degradation
    • Ludwig IS, Lekkerkerker AN, Depla E, et al. Hepatitis C virus targets DC-SIGN and L-SIGN to escape lysosomal degradation. J Virol 2004;78(15):8322- 8332
    • (2004) J Virol , vol.78 , Issue.15 , pp. 8322-8332
    • Ludwig, I.S.1    Lekkerkerker, A.N.2    Depla, E.3
  • 62
    • 0035655108 scopus 로고    scopus 로고
    • DC-SIGN and DC-SIGNR: Helping hands for HIV
    • Pohlmann S, Baribaud F, Doms RW. DC-SIGN and DC-SIGNR: Helping hands for HIV. Trends Immunol 2001;22(12):643-646
    • (2001) Trends Immunol , vol.22 , Issue.12 , pp. 643-646
    • Pohlmann, S.1    Baribaud, F.2    Doms, R.W.3
  • 63
    • 70350244342 scopus 로고    scopus 로고
    • Functional genetic variants in DC-SIGNR are associated with mother-to-child transmission of HIV-1
    • Boily-Larouche G, Iscache A-L, Zijenah LS, et al. Functional genetic variants in DC-SIGNR are associated with mother-to-child transmission of HIV-1. PLoS One 2009;4(10):e7211
    • (2009) PLoS One , vol.4 , Issue.10
    • Boily-Larouche, G.1    Iscache, A.-L.2    Zijenah, L.S.3
  • 64
    • 84863641055 scopus 로고    scopus 로고
    • Naturally-occurring genetic variants in human DCSIGN increase HIV-1 capture, cell-transfer and risk of mother-to-child transmission
    • Boily-Larouche G, Milev MP, Zijenah LS, et al. Naturally-occurring genetic variants in human DCSIGN increase HIV-1 capture, cell-transfer and risk of mother-to-child transmission. PLoS One 2012;7(7):e40706
    • (2012) PLoS One , vol.7 , Issue.7
    • Boily-Larouche, G.1    Milev, M.P.2    Zijenah, L.S.3
  • 65
    • 77953290976 scopus 로고    scopus 로고
    • The nine-repeat DC-SIGNR isoform is associated with increased HIV-RNA loads and HIV sexual transmission
    • Xu L, Li Q, Ye H, et al. The nine-repeat DC-SIGNR isoform is associated with increased HIV-RNA loads and HIV sexual transmission. J Clin Immunol 2010;30(3):402-407
    • (2010) J Clin Immunol , vol.30 , Issue.3 , pp. 402-407
    • Xu, L.1    Li, Q.2    Ye, H.3
  • 66
    • 84866039226 scopus 로고    scopus 로고
    • The VNTR polymorphism of the DC-SIGNR gene and susceptibility to HIV-1 infection: A meta-analysis
    • Li H, Yu XM, Wang JX, et al.The VNTR polymorphism of the DC-SIGNR gene and susceptibility to HIV-1 infection: A meta-analysis. PLoS One 2012;7(9):e42972
    • (2012) PLoS One , vol.7 , Issue.9
    • Li, H.1    Yu, X.M.2    Wang, J.X.3
  • 67
    • 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, et al. 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(22):12022-12032
    • (2003) J Virol , vol.77 , Issue.22 , pp. 12022-12032
    • Klimstra, W.B.1    Nangle, E.M.2    Smith, M.S.3
  • 68
    • 38449102893 scopus 로고    scopus 로고
    • Analysis of the interaction of Ebola virus glycoprotein with DCSIGN (dendritic cell-specific intercellular adhesionmolecule 3-grabbing nonintegrin) and its homologue DC-SIGNR
    • Marzi A, Moller P, Hanna SL, et al. Analysis of the interaction of Ebola virus glycoprotein with DCSIGN (dendritic cell-specific intercellular adhesionmolecule 3-grabbing nonintegrin) and its homologue DC-SIGNR. J Infect Dis 2007;196(Suppl 2):S237-S246
    • (2007) J Infect Dis , vol.196 , Issue.SUPPL. 2
    • Marzi, A.1    Moller, P.2    Hanna, S.L.3
  • 69
    • 84869067364 scopus 로고    scopus 로고
    • Cell surface molecules involved in infection mediated by lymphocytic choriomeningitis virus glycoprotein
    • Shimojima M, Kawaoka Y. Cell surface molecules involved in infection mediated by lymphocytic choriomeningitis virus glycoprotein. J VetMed Sci 2012;74(10):1363-1366
    • (2012) J VetMed Sci , vol.74 , Issue.10 , pp. 1363-1366
    • Shimojima, M.1    Kawaoka, Y.2
  • 70
    • 79957483733 scopus 로고    scopus 로고
    • Lectin switching during dengue virus infection
    • Dejnirattisai W, Webb AI, Chan V, et al. Lectin switching during dengue virus infection. J Infect Dis 2011;203(12):1775-1783
    • (2011) J Infect Dis , vol.203 , Issue.12 , pp. 1775-1783
    • Dejnirattisai, W.1    Webb, A.I.2    Chan, V.3
  • 71
    • 79959592623 scopus 로고    scopus 로고
    • Virus-receptor mediated transduction of dendritic cells by lentiviruses enveloped with glycoproteins derived from Semliki Forest virus
    • Froelich S, Tai A, Kennedy K, et al. Virus-receptor mediated transduction of dendritic cells by lentiviruses enveloped with glycoproteins derived from Semliki Forest virus. PLoS One 2011;6(6):e21491
    • (2011) PLoS One , vol.6 , Issue.6
    • Froelich, S.1    Tai, A.2    Kennedy, K.3
  • 72
    • 84862818159 scopus 로고    scopus 로고
    • Expression of theC-type lectinsDC-SIGNor L-SIGNalters host cell susceptibility for the avian coronavirus, infectious bronchitis virus
    • ZhangY,BucklesE,Whittaker GR.Expression of theC-type lectinsDC-SIGNor L-SIGNalters host cell susceptibility for the avian coronavirus, infectious bronchitis virus. VetMicrobiol 2012;167:285-293
    • (2012) VetMicrobiol , vol.167 , pp. 285-293
    • Zhang, Y.1    Buckles, E.2    Whittaker, G.R.3
  • 73
    • 84857082116 scopus 로고    scopus 로고
    • Respiratory syncytial virus glycoprotein G interacts with DCSIGN and L-SIGN to activate ERK1 and ERK2
    • Johnson TR,McLellan JS, Graham BS. Respiratory syncytial virus glycoprotein G interacts with DCSIGN and L-SIGN to activate ERK1 and ERK2. J Virol 2012;86(3):1339-1347
    • (2012) J Virol , vol.86 , Issue.3 , pp. 1339-1347
    • Johnson, T.R.1    Mclellan, J.S.2    Graham, B.S.3
  • 74
    • 84875633828 scopus 로고    scopus 로고
    • Glycan-based DC-SIGN targeting vaccines to enhance antigen cross-presentation
    • van Kooyk Y, Unger WW, Fehres CM, et al. Glycan-based DC-SIGN targeting vaccines to enhance antigen cross-presentation.Mol Immunol 2013;55(2):143-145
    • (2013) Mol Immunol , vol.55 , Issue.2 , pp. 143-145
    • Van Kooyk, Y.1    Unger, W.W.2    Fehres, C.M.3
  • 75
    • 38349082251 scopus 로고    scopus 로고
    • Glycan modification of the tumor antigen gp100targets DC-SIGN to enhance dendritic cell induced antigen presentation to T cells
    • Aarnoudse CA, BaxM, Śanchez-HerńandezM, et al. Glycan modification of the tumor antigen gp100targets DC-SIGN to enhance dendritic cell induced antigen presentation to T cells. Int J Cancer 2008;122(4):839-846
    • (2008) Int J Cancer , vol.122 , Issue.4 , pp. 839-846
    • Aarnoudse, C.A.1    Bax, M.2    Śanchez-Herńandez, M.3
  • 76
    • 70450277084 scopus 로고    scopus 로고
    • Targeting glycan modifiedovatomurinedc-signtransgenic dendritic cells enhances mhc class i and ii presentation
    • Singh SK, Stephani J, SchaeferM,et al.Targeting glycan modifiedOVAtomurineDC-SIGNtransgenic dendritic cells enhances MHC class I and II presentation.Mol Immunol 2009;47(2-3):164-174
    • (2009) Mol Immunol , vol.47 , Issue.2-3 , pp. 164-174
    • Singh, S.K.1    Stephani, J.2    Schaefer, M.3
  • 77
    • 84884287162 scopus 로고    scopus 로고
    • Targeting c-type lectin receptors with multivalent carbohydrate ligands
    • doi: 10.1016/j.addr.2013.05.007
    • Lepenies B, Lee J, Sonkaria S. Targeting C-type lectin receptors with multivalent carbohydrate ligands. Adv Drug Deliv Rev 2013; doi: 10.1016/j.addr.2013.05.007
    • (2013) Adv Drug Deliv Rev
    • Lepenies, B.1    Lee, J.2    Sonkaria, S.3
  • 78
    • 70350459593 scopus 로고    scopus 로고
    • A murine DC-SIGN homologue contributes to early host defense against Mycobacterium tuberculosis
    • Tanne A, Ma B, Boudou F, et al. A murine DC-SIGN homologue contributes to early host defense against Mycobacterium tuberculosis. J ExpMed 2009;206(10):2205-2220
    • (2009) J ExpMed , vol.206 , Issue.10 , pp. 2205-2220
    • Tanne, A.1    Ma, B.2    Boudou, F.3
  • 79
    • 84883714042 scopus 로고    scopus 로고
    • The C-type lectin receptor SIGNR3 binds to fungi present in commensal microbiota and influences immune regulation in experimental colitis
    • Eriksson M, Johannssen T, von Smolinski D, et al. The C-type lectin receptor SIGNR3 binds to fungi present in commensal microbiota and influences immune regulation in experimental colitis. Front Immunol 2013;4:196
    • (2013) Front Immunol , vol.4 , pp. 196
    • Eriksson, M.1    Johannssen, T.2    Von Smolinski, D.3
  • 80
    • 84878203462 scopus 로고    scopus 로고
    • The c-type lectin receptors dectin-1mr and signr3contribute both positively and negatively to themacrophage response to leishmania infantum
    • Lefevre L, Lugo-Villarino G,Meunier E, et al. The C-type lectin receptors dectin-1,MR, and SIGNR3contribute both positively and negatively to themacrophage response to Leishmania infantum. Immunity 2013;38(5):1038-1049
    • (2013) Immunity , vol.38 , Issue.5 , pp. 1038-1049
    • Lefevre, L.1    Lugo-Villarino, G.2    Meunier, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.