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Volumn 50, Issue 27, 2011, Pages 6125-6132

Geometry and adhesion of extracellular domains of DC-SIGNR neck length variants analyzed by force-distance measurements

Author keywords

[No Author keywords available]

Indexed keywords

CARBOHYDRATE-RECOGNITION DOMAINS; CONFORMATIONAL CHANGE; CRYSTALLOGRAPHIC STUDIES; DENDRITIC CELLS; EXTRACELLULAR DOMAINS; GENETIC POLYMORPHISMS; LENGTH VARIANTS;

EID: 79959944073     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi2003444     Document Type: Article
Times cited : (14)

References (33)
  • 3
    • 0036326535 scopus 로고    scopus 로고
    • Expression of human immunodeficiency virus (HIV)-binding lectin DC-SIGNR: Consequences for HIV infection and immunity
    • DOI 10.1053/hupa.2002.124036
    • Soilleux, E. J., Morris, L. S., Rushbrook, S., Lee, B., and Coleman, N. (2002) Expression of human immunodeficiency virus (HIV)-binding lectin DC-SIGNR: Consequences for HIV infection and immunity Hum. Pathol. 33, 652-659 (Pubitemid 34827548)
    • (2002) Human Pathology , vol.33 , Issue.6 , pp. 652-659
    • Soilleux, E.J.1    Morris, L.S.2    Rushbrook, S.3    Lee, B.4    Coleman, N.5
  • 5
    • 31144445030 scopus 로고    scopus 로고
    • West nile virus discriminates between DC-SIGN and DC-SIGNR for cellular attachment and infection
    • DOI 10.1128/JVI.80.3.1290-1301.2006
    • Davis, C. W., Nguyen, H. Y., Hanna, S. L., Sanchez, M. D., Doms, R. W., and Pierson, T. C. (2006) West Nile virus discriminates between DC-SIGN and DC-SIGNR for cellular attachment and infection J. Virol. 80, 1290-1301 (Pubitemid 43134086)
    • (2006) Journal of Virology , vol.80 , Issue.3 , pp. 1290-1301
    • Davis, C.W.1    Nguyen, H.-Y.2    Hanna, S.L.3    Sanchez, M.D.4    Doms, R.W.5    Pierson, T.C.6
  • 6
    • 48149094568 scopus 로고    scopus 로고
    • DC-SIGN and L-SIGN: The SIGNs for infection
    • Khoo, U. S., Chan, K. Y., Chan, V. S., and Lin, C. L. (2008) DC-SIGN and L-SIGN: the SIGNs for infection J. Mol. Med. 86, 861-874
    • (2008) J. Mol. Med. , vol.86 , pp. 861-874
    • Khoo, U.S.1    Chan, K.Y.2    Chan, V.S.3    Lin, C.L.4
  • 8
    • 0037391145 scopus 로고    scopus 로고
    • DC-SIGN (dendritic cell-specific ICAM-grabbing non-integrin) and DC-SIGN-related (DC-SIGNR): Friend or foe?
    • DOI 10.1042/CS20020092
    • Soilleux, E. J. (2003) DC-SIGN (dendritic cell-specific ICAM-grabbing non-integrin) and DC-SIGN-related (DC-SIGNR): friend or foe? Clin. Sci. 104, 437-446 (Pubitemid 36458072)
    • (2003) Clinical Science , vol.104 , Issue.4 , pp. 437-446
    • Soilleux, E.J.1
  • 10
    • 27844597218 scopus 로고    scopus 로고
    • Y glycolipids of Schistosoma mansoni cercariae, the first parasite-specific ligand of DC-SIGN
    • DOI 10.1074/jbc.M507100200
    • Meyer, S., van Liempt, E., Imberty, A., van Kooyk, Y., Geyer, H., Geyer, R., and van Die, I. (2005) DC-SIGN mediates binding of dendritic cells to authentic pseudo-LewisY glycolipids of Schistosoma mansoni cercariae, the first parasite-specific ligand of DC-SIGN J. Biol. Chem. 280, 37349-37359 (Pubitemid 41642340)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.45 , pp. 37349-37359
    • Meyer, S.1    Van Liempt, E.2    Imberty, A.3    Van Kooyk, Y.4    Geyer, H.5    Geyer, R.6    Van Die, I.7
  • 11
    • 35148816072 scopus 로고    scopus 로고
    • The C-type lectin L-SIGN differentially recognizes glycan antigens on egg glycosphingolipids and soluble egg glycoproteins from Schistosoma mansoni
    • DOI 10.1093/glycob/cwm073
    • Meyer, S., Tefsen, B., Imberty, A., Geyer, R., and van Die, I. (2007) The C-type lectin L-SIGN differentially recognizes glycan antigens on egg glycosphingolipids and soluble egg glycoproteins from Schistosoma mansoni Glycobiology 17, 1104-1119 (Pubitemid 47543404)
    • (2007) Glycobiology , vol.17 , Issue.10 , pp. 1104-1119
    • Meyer, S.1    Tefsen, B.2    Imberty, A.3    Geyer, R.4    Van Die, I.5
  • 12
    • 0037623506 scopus 로고    scopus 로고
    • The tandem-repeat polymorphism of the DC-SIGNR gene does not affect the susceptibility to HIV infection and the progression to AIDS
    • DOI 10.1016/S1521-6616(02)00050-5
    • Lichterfeld, M., Nischalke, H. D., van Lunzen, J., Sohne, J., Schmeisser, N., Woitas, R., Sauerbruch, T., Rockstroh, J. K., and Spengler, U. (2003) The tandem-repeat polymorphism of the DC-SIGNR gene does not affect the susceptibility to HIV infection and the progression to AIDS Clin. Immunol. 107, 55-59 (Pubitemid 36539446)
    • (2003) Clinical Immunology , vol.107 , Issue.1 , pp. 55-59
    • Lichterfeld, M.1    Nischalke, H.D.2    Van Lunzen, J.3    Sohne, J.4    Schmeisser, N.5    Woitas, R.6    Sauerbruch, T.7    Rockstroh, J.K.8    Spengler, U.9
  • 14
    • 33750993048 scopus 로고    scopus 로고
    • Preparation of Neoglycolipids with Ring-Closed Cores via Chemoselective Oxime-Ligation for Microarray Analysis of Carbohydrate-Protein Interactions
    • DOI 10.1016/S0076-6879(06)15020-X, PII S007668790615020X, Glycobiology
    • Liu, Y., Chai, W., Childs, R. A., and Feizi, T. (2006) Preparation of neoglycolipids with ring-closed cores via chemoselective oxime-ligation for microarray analysis of carbohydrate-protein interactions Methods Enzymol. 415, 326-340 (Pubitemid 44751106)
    • (2006) Methods in Enzymology , vol.415 , pp. 326-340
    • Liu, Y.1    Chai, W.2    Childs, R.A.3    Feizi, T.4
  • 17
    • 70449533662 scopus 로고    scopus 로고
    • Segmented helical structure of the neck region of the glycan-binding receptor DC-SIGNR
    • Feinberg, H., Tso, C. K., Taylor, M. E., Drickamer, K., and Weis, W. I. (2009) Segmented helical structure of the neck region of the glycan-binding receptor DC-SIGNR J. Mol. Biol. 394, 613-620
    • (2009) J. Mol. Biol. , vol.394 , pp. 613-620
    • Feinberg, H.1    Tso, C.K.2    Taylor, M.E.3    Drickamer, K.4    Weis, W.I.5
  • 19
    • 33745219458 scopus 로고    scopus 로고
    • All but the shortest polymorphic forms of the viral receptor DC-SIGNR assemble into stable homo- and heterotetramers
    • Guo, Y., Atkinson, C. E., Taylor, M. E., and Drickamer, K. (2006) All but the shortest polymorphic forms of the viral receptor DC-SIGNR assemble into stable homo- and heterotetramers J. Biol. Chem. 281, 16794-16798
    • (2006) J. Biol. Chem. , vol.281 , pp. 16794-16798
    • Guo, Y.1    Atkinson, C.E.2    Taylor, M.E.3    Drickamer, K.4
  • 20
    • 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, D. A., Fadden, A. J., and Drickamer, K. (2001) 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. 276, 28939-28945
    • (2001) J. Biol. Chem. , vol.276 , pp. 28939-28945
    • Mitchell, D.A.1    Fadden, A.J.2    Drickamer, K.3
  • 21
    • 0033891706 scopus 로고    scopus 로고
    • Optical and direct force measurements of the interactions between monolayers of aromatic macrocycles on surfactant monolayers
    • DOI 10.1021/la9904612
    • Lavrik, N. and Leckband, D. (2000) Optical and direct force measurements of the interaction between monolayers of aromatic macrocycles on surfactant monolayers Langmuir 16, 1842-1851 (Pubitemid 30590684)
    • (2000) Langmuir , vol.16 , Issue.4 , pp. 1842-1851
    • Lavrik, N.1    Leckband, D.2
  • 22
    • 0031881294 scopus 로고    scopus 로고
    • 2 surface
    • DOI 10.1007/s001140050459
    • Ball, V. and Ramsden, J. J. (1998) Influence of D(-) and L(+) tartaric acid on lysozyme adsorption onto a Si(Ti)-O2 surface Naturwissenschaften 85, 87-89 (Pubitemid 28136613)
    • (1998) Naturwissenschaften , vol.85 , Issue.2 , pp. 87-89
    • Ball, V.1    Ramsden, J.J.2
  • 23
    • 2542516405 scopus 로고    scopus 로고
    • The density and refractive index of adsorbing protein layers
    • DOI 10.1529/biophysj.103.030072
    • Voros, J. (2004) The density and refractive index of adsorbing protein layers Biophys. J. 57, 553-561 (Pubitemid 38880108)
    • (2004) Biophysical Journal , vol.87 , Issue.1 , pp. 553-561
    • Voros, J.1
  • 24
    • 70449246528 scopus 로고
    • Phosphorus assay in column chromatography
    • Bartlett, G. (1959) Phosphorus assay in column chromatography J. Biol. Chem. 234, 466-468
    • (1959) J. Biol. Chem. , vol.234 , pp. 466-468
    • Bartlett, G.1
  • 25
    • 17644448651 scopus 로고
    • Thin film studies using multiple-beam interferometry
    • Israelachvili, J. (1973) Thin film studies using multiple-beam interferometry J. Colloid Interface Sci. 44, 259-272
    • (1973) J. Colloid Interface Sci. , vol.44 , pp. 259-272
    • Israelachvili, J.1
  • 26
    • 0021972793 scopus 로고
    • Direct measurements of forces between phosphatidylcholine and phosphatidylethanolamine bilayers in aqueous electrolyte solutions
    • DOI 10.1021/bi00338a020
    • Marra, J. and Israelachvili, J. (1985) Direct measurements of forces between phosphatidylcholine and phosphatidylethanolamine bilayers in aqueous electrolyte solutions Biochemistry 24, 4608-4618 (Pubitemid 15233711)
    • (1985) Biochemistry , vol.24 , Issue.17 , pp. 4608-4618
    • Marra, J.1    Israelachvili, J.2
  • 27
    • 35348863025 scopus 로고    scopus 로고
    • X-ray reflectivity investigations of two-dimensional assemblies of C-cadherins: First steps in structural and functional studies
    • Martel, L., Johnson, C., Boutet, S., al-Kurdi, R., Konavalov, O., Robinson, I., Leckband, D., and Legrand, J. (2002) X-ray reflectivity investigations of two-dimensional assemblies of C-cadherins: First steps in structural and functional studies J. Phys. IV 12, 365-377
    • (2002) J. Phys. IV , vol.12 , pp. 365-377
    • Martel, L.1    Johnson, C.2    Boutet, S.3    Al-Kurdi, R.4    Konavalov, O.5    Robinson, I.6    Leckband, D.7    Legrand, J.8
  • 29
    • 0026342025 scopus 로고
    • Structure of the calcium-dependent lectin domain from a rat mannose-binding protein determined by MAD phasing
    • Weis, W. I., Kahn, R., Fourme, R., Drickamer, K., and Hendrickson, W. A. (1991) Structure of the calcium-dependent lectin domain from a rat mannose-binding protein determined by MAD phasing Science 254, 1608-1615 (Pubitemid 21917498)
    • (1991) Science , vol.254 , Issue.5038 , pp. 1608-1615
    • Weis, W.I.1    Kahn, R.2    Fourme, R.3    Drickamer, K.4    Hendrickson, W.A.5
  • 30
    • 0031016904 scopus 로고    scopus 로고
    • Direct measurement of a tethered ligand-receptor interaction potential
    • DOI 10.1126/science.275.5301.820
    • Wong, J., Kuhl, T., Israelachvili, J., Mullah, N., and Zalipsky, S. (1997) Direct measurement of a tethered ligand-receptor interaction potential Science 275, 820-822 (Pubitemid 27074880)
    • (1997) Science , vol.275 , Issue.5301 , pp. 820-822
    • Wong, J.Y.1    Kuhl, T.L.2    Israelachvili, J.N.3    Mullah, N.4    Zalipsky, S.5
  • 31
    • 0029120757 scopus 로고
    • Molecular mechanisms determining the strength of receptor-mediated intermembrane adhesion
    • Leckband, D., Muller, W., Schmitt, F. J., and Ringsdorf, H. (1995) Molecular mechanisms determining the strength of receptor-mediated intermembrane adhesion Biophys. J. 69, 1162-1169
    • (1995) Biophys. J. , vol.69 , pp. 1162-1169
    • Leckband, D.1    Muller, W.2    Schmitt, F.J.3    Ringsdorf, H.4
  • 32
  • 33
    • 12444347833 scopus 로고    scopus 로고
    • Extended neck regions stabilize tetramers of the receptors DC-SIGN and DC-SIGNR
    • Feinberg, H., Guo, Y., Mitchell, D., Drickamer, K., and Weis, W. (2005) Extended neck regions stabilize tetramers of the receptors DC-SIGN and DC-SIGNR J. Biol. Chem. 280, 1327-1335
    • (2005) J. Biol. Chem. , vol.280 , pp. 1327-1335
    • Feinberg, H.1    Guo, Y.2    Mitchell, D.3    Drickamer, K.4    Weis, W.5


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