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Volumn 64, Issue 15, 2012, Pages 1759-1781

On the roles of polyvalent binding in immune recognition: Perspectives in the nanoscience of immunology and the immune response to nanomedicines

Author keywords

Adhesion molecules; Avidity; Immunoglobulins; Integrins; Mannan binding lectin; Nanotoxicology; Polyvalent binding

Indexed keywords

ADHESION MOLECULES; AVIDITY; IMMUNOGLOBULINS; INTEGRINS; MANNAN-BINDING LECTINS; NANOTOXICOLOGY; POLYVALENT BINDING;

EID: 84869201214     PISSN: 0169409X     EISSN: 18728294     Source Type: Journal    
DOI: 10.1016/j.addr.2012.06.003     Document Type: Review
Times cited : (43)

References (256)
  • 1
    • 0032476812 scopus 로고    scopus 로고
    • Polyvalent interactions in biological systems: Implications for design and use of multivalent ligands and inhibitors
    • Mammen M., Choi S.K., Whitesides G.M. Polyvalent interactions in biological systems: Implications for design and use of multivalent ligands and inhibitors. Angew. Chem. Int. Ed. 1998, 37:2755-2794.
    • (1998) Angew. Chem. Int. Ed. , vol.37 , pp. 2755-2794
    • Mammen, M.1    Choi, S.K.2    Whitesides, G.M.3
  • 2
    • 84869159943 scopus 로고
    • Studies in Anaphylaxis: XV. Equilibrium in Precipitation Reactions. Equilibrium in Combination
    • Weil R. Studies in Anaphylaxis: XV. Equilibrium in Precipitation Reactions. Equilibrium in Combination. J. Immunol. 1916, 1:19-34.
    • (1916) J. Immunol. , vol.1 , pp. 19-34
    • Weil, R.1
  • 3
    • 0017249449 scopus 로고
    • Multivalent binding and functional affinity
    • Karush F. Multivalent binding and functional affinity. Contemp. Top. Mol. Immunol. 1976, 5:217-228.
    • (1976) Contemp. Top. Mol. Immunol. , vol.5 , pp. 217-228
    • Karush, F.1
  • 5
    • 4043158815 scopus 로고
    • The constitution and fundamental properties of solids and liquids. Part I. Solids
    • Langmuir I. The constitution and fundamental properties of solids and liquids. Part I. Solids. J. Am. Chem. Soc. 1916, 38:2221-2295.
    • (1916) J. Am. Chem. Soc. , vol.38 , pp. 2221-2295
    • Langmuir, I.1
  • 6
    • 0015313012 scopus 로고
    • The influence of polyvalency on the binding properties of antibodies
    • Crothers D.M., Metzger H. The influence of polyvalency on the binding properties of antibodies. Immunochemistry 1972, 9:341-357.
    • (1972) Immunochemistry , vol.9 , pp. 341-357
    • Crothers, D.M.1    Metzger, H.2
  • 7
    • 0347694971 scopus 로고    scopus 로고
    • On the nature of the multivalency effect: a thermodynamic model
    • Kitov P.I., Bundle D.R. On the nature of the multivalency effect: a thermodynamic model. J. Am. Chem. Soc. 2003, 125:16271-16284.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 16271-16284
    • Kitov, P.I.1    Bundle, D.R.2
  • 8
    • 0011117902 scopus 로고
    • The interaction of purified antibody with homologous hapten; antibody valence and binding constant
    • Eisen H.N., Karush F. The interaction of purified antibody with homologous hapten; antibody valence and binding constant. J. Am. Chem. Soc. 1949, 71:363.
    • (1949) J. Am. Chem. Soc. , vol.71 , pp. 363
    • Eisen, H.N.1    Karush, F.2
  • 9
    • 70449276523 scopus 로고
    • The hydrolysis of rabbit y-globulin and antibodies with crystalline papain
    • Porter R.R. The hydrolysis of rabbit y-globulin and antibodies with crystalline papain. Biochem. J. 1959, 73:119-126.
    • (1959) Biochem. J. , vol.73 , pp. 119-126
    • Porter, R.R.1
  • 10
    • 0012569260 scopus 로고
    • The Arrangement of the Peptide Chains in Gamma-Globulin
    • Fleischman J.B., Porter R.R., Press E.M. The Arrangement of the Peptide Chains in Gamma-Globulin. Biochem. J. 1963, 88:220-228.
    • (1963) Biochem. J. , vol.88 , pp. 220-228
    • Fleischman, J.B.1    Porter, R.R.2    Press, E.M.3
  • 11
    • 0015315530 scopus 로고
    • Antibody affinity. 3. The role of multivalance
    • Hornick C.L., Karuch F. Antibody affinity. 3. The role of multivalance. Immunochemistry 1972, 9:325-340.
    • (1972) Immunochemistry , vol.9 , pp. 325-340
    • Hornick, C.L.1    Karuch, F.2
  • 12
    • 0016624901 scopus 로고
    • Binding energy, specificity, and enzymic catalysis - the circe effect
    • John Wiley and Sons, New York, A. Meister (Ed.)
    • Jencks W.P. Binding energy, specificity, and enzymic catalysis - the circe effect. Adv in Enzymol 1975, John Wiley and Sons, New York. A. Meister (Ed.).
    • (1975) Adv in Enzymol
    • Jencks, W.P.1
  • 13
    • 0018101150 scopus 로고
    • Models for the specific adhesion of cells to cells
    • Bell G.I. Models for the specific adhesion of cells to cells. Science 1978, 200:618-627.
    • (1978) Science , vol.200 , pp. 618-627
    • Bell, G.I.1
  • 14
    • 77954042425 scopus 로고    scopus 로고
    • Few and far between: how HIV may be evading antibody avidity
    • Klein J.S., Bjorkman P.J. Few and far between: how HIV may be evading antibody avidity. PLoS Pathog. 2010, 6:e1000908.
    • (2010) PLoS Pathog. , vol.6
    • Klein, J.S.1    Bjorkman, P.J.2
  • 15
    • 0014693139 scopus 로고
    • Conformation of the free and antigen-bound IgM antibody molecules
    • Feinstein A., Munn E.A. Conformation of the free and antigen-bound IgM antibody molecules. Nature 1969, 224:1307-1309.
    • (1969) Nature , vol.224 , pp. 1307-1309
    • Feinstein, A.1    Munn, E.A.2
  • 16
    • 0032850235 scopus 로고    scopus 로고
    • Immunoglobulin structure and function as revealed by electron microscopy
    • Roux K.H. Immunoglobulin structure and function as revealed by electron microscopy. Int. Arch. Allergy Immunol. 1999, 120:85-99.
    • (1999) Int. Arch. Allergy Immunol. , vol.120 , pp. 85-99
    • Roux, K.H.1
  • 17
    • 0019407381 scopus 로고
    • On the attribution and additivity of binding energies
    • Jencks W.P. On the attribution and additivity of binding energies. Proc. Natl. Acad. Sci. U. S. A. 1981, 78:4046-4050.
    • (1981) Proc. Natl. Acad. Sci. U. S. A. , vol.78 , pp. 4046-4050
    • Jencks, W.P.1
  • 18
    • 0018797909 scopus 로고
    • Evaluation of group contributions to ligand binding
    • Rappaport H.P. Evaluation of group contributions to ligand binding. J. Theor. Biol. 1979, 79:157-165.
    • (1979) J. Theor. Biol. , vol.79 , pp. 157-165
    • Rappaport, H.P.1
  • 19
    • 70450175085 scopus 로고    scopus 로고
    • Multivalent ligand presentation as a central concept to study intricate carbohydrate-protein interactions
    • Jayaraman N. Multivalent ligand presentation as a central concept to study intricate carbohydrate-protein interactions. Chem. Soc. Rev. 2009, 38:3463-3483.
    • (2009) Chem. Soc. Rev. , vol.38 , pp. 3463-3483
    • Jayaraman, N.1
  • 20
    • 0042971650 scopus 로고    scopus 로고
    • Molecular interactions mediating T cell antigen recognition
    • van der Merwe P.A., Davis S.J. Molecular interactions mediating T cell antigen recognition. Annu. Rev. Immunol. 2003, 21:659-684.
    • (2003) Annu. Rev. Immunol. , vol.21 , pp. 659-684
    • van der Merwe, P.A.1    Davis, S.J.2
  • 21
    • 0037167816 scopus 로고    scopus 로고
    • Direct observation of ligand recognition by T cells
    • Irvine D.J., Purbhoo M.A., Krogsgaard M., Davis M.M. Direct observation of ligand recognition by T cells. Nature 2002, 419:845-849.
    • (2002) Nature , vol.419 , pp. 845-849
    • Irvine, D.J.1    Purbhoo, M.A.2    Krogsgaard, M.3    Davis, M.M.4
  • 22
    • 41049113448 scopus 로고    scopus 로고
    • Blood cell interactions and segregation in flow
    • Munn L.L., Dupin M.M. Blood cell interactions and segregation in flow. Ann. Biomed. Eng. 2008, 36:534-544.
    • (2008) Ann. Biomed. Eng. , vol.36 , pp. 534-544
    • Munn, L.L.1    Dupin, M.M.2
  • 23
    • 0025182959 scopus 로고
    • Adhesion receptors of the immune system
    • Springer T.A. Adhesion receptors of the immune system. Nature 1990, 346:425-434.
    • (1990) Nature , vol.346 , pp. 425-434
    • Springer, T.A.1
  • 24
    • 84857478993 scopus 로고    scopus 로고
    • Leukocyte adhesion deficiencies
    • Hanna S., Etzioni A. Leukocyte adhesion deficiencies. Ann. N. Y. Acad. Sci. 2012, 1250:50-55.
    • (2012) Ann. N. Y. Acad. Sci. , vol.1250 , pp. 50-55
    • Hanna, S.1    Etzioni, A.2
  • 25
    • 35648977687 scopus 로고    scopus 로고
    • Alefacept for the treatment of psoriasis and other dermatologic diseases
    • Strober B.E., Menon K. Alefacept for the treatment of psoriasis and other dermatologic diseases. Dermatol. Ther. 2007, 20:270-276.
    • (2007) Dermatol. Ther. , vol.20 , pp. 270-276
    • Strober, B.E.1    Menon, K.2
  • 28
    • 0014943238 scopus 로고
    • Affinity and the immune response
    • Karush F. Affinity and the immune response. Ann. N. Y. Acad. Sci. 1970, 169:56-64.
    • (1970) Ann. N. Y. Acad. Sci. , vol.169 , pp. 56-64
    • Karush, F.1
  • 29
    • 0024955886 scopus 로고
    • Approaching the asymptote? Evolution and revolution in immunology
    • Janeway C.A. Approaching the asymptote? Evolution and revolution in immunology. Cold Spring Harb. Symp. Quant. Biol. 1989, 54(Pt 1):1-13.
    • (1989) Cold Spring Harb. Symp. Quant. Biol. , vol.54 , Issue.PART 1 , pp. 1-13
    • Janeway, C.A.1
  • 30
    • 77950343791 scopus 로고    scopus 로고
    • Pattern recognition receptors and inflammation
    • Takeuchi O., Akira S. Pattern recognition receptors and inflammation. Cell 2010, 140:805-820.
    • (2010) Cell , vol.140 , pp. 805-820
    • Takeuchi, O.1    Akira, S.2
  • 31
    • 25844454011 scopus 로고    scopus 로고
    • The Toll-like receptors: analysis by forward genetic methods
    • Beutler B. The Toll-like receptors: analysis by forward genetic methods. Immunogenetics 2005, 57:385-392.
    • (2005) Immunogenetics , vol.57 , pp. 385-392
    • Beutler, B.1
  • 32
    • 67349182481 scopus 로고    scopus 로고
    • The structural basis of lipopolysaccharide recognition by the TLR4-MD-2 complex
    • Park B.S., Song D.H., Kim H.M., Choi B.S., Lee H., Lee J.O. The structural basis of lipopolysaccharide recognition by the TLR4-MD-2 complex. Nature 2009, 458:1191-1195.
    • (2009) Nature , vol.458 , pp. 1191-1195
    • Park, B.S.1    Song, D.H.2    Kim, H.M.3    Choi, B.S.4    Lee, H.5    Lee, J.O.6
  • 36
    • 0037066427 scopus 로고    scopus 로고
    • The danger model: a renewed sense of self
    • Matzinger P. The danger model: a renewed sense of self. Science 2002, 296:301-305.
    • (2002) Science , vol.296 , pp. 301-305
    • Matzinger, P.1
  • 37
    • 0028533911 scopus 로고
    • Human mannose-binding protein carbohydrate recognition domain trimerizes through a triple alpha-helical coiled-coil
    • Sheriff S., Chang C.Y., Ezekowitz R.A. Human mannose-binding protein carbohydrate recognition domain trimerizes through a triple alpha-helical coiled-coil. Nat. Struct. Biol. 1994, 1:789-794.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 789-794
    • Sheriff, S.1    Chang, C.Y.2    Ezekowitz, R.A.3
  • 38
    • 0028774718 scopus 로고
    • Trimeric structure of a C-type mannose-binding protein
    • Weis W.I., Drickamer K. Trimeric structure of a C-type mannose-binding protein. Structure 1994, 2:1227-1240.
    • (1994) Structure , vol.2 , pp. 1227-1240
    • Weis, W.I.1    Drickamer, K.2
  • 40
    • 12844264792 scopus 로고    scopus 로고
    • Effect of capsulation of opportunistic pathogenic bacteria on binding of the pattern recognition molecules mannan-binding lectin, L-ficolin, and H-ficolin
    • Krarup A., Sorensen U.B., Matsushita M., Jensenius J.C., Thiel S. Effect of capsulation of opportunistic pathogenic bacteria on binding of the pattern recognition molecules mannan-binding lectin, L-ficolin, and H-ficolin. Infect. Immun. 2005, 73:1052-1060.
    • (2005) Infect. Immun. , vol.73 , pp. 1052-1060
    • Krarup, A.1    Sorensen, U.B.2    Matsushita, M.3    Jensenius, J.C.4    Thiel, S.5
  • 42
    • 0041534400 scopus 로고    scopus 로고
    • Collections and ficolins: humoral lectins of the innate immune defense
    • Holmskov U., Thiel S., Jensenius J.C. Collections and ficolins: humoral lectins of the innate immune defense. Annu. Rev. Immunol. 2003, 21:547-578.
    • (2003) Annu. Rev. Immunol. , vol.21 , pp. 547-578
    • Holmskov, U.1    Thiel, S.2    Jensenius, J.C.3
  • 43
    • 0008003814 scopus 로고
    • Inhibitory and activating action of normal ferret sera against an influenza virus strain
    • Burnet F.M., Mc C.J. Inhibitory and activating action of normal ferret sera against an influenza virus strain. Aust. J. Exp. Biol. Med. Sci. 1946, 24:277-282.
    • (1946) Aust. J. Exp. Biol. Med. Sci. , vol.24 , pp. 277-282
    • Burnet, F.M.1    Mc, C.J.2
  • 44
    • 0025298243 scopus 로고
    • Bovine and mouse serum beta inhibitors of influenza A viruses are mannose-binding lectins
    • Anders E.M., Hartley C.A., Jackson D.C. Bovine and mouse serum beta inhibitors of influenza A viruses are mannose-binding lectins. Proc. Natl. Acad. Sci. U. S. A. 1990, 87:4485-4489.
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 4485-4489
    • Anders, E.M.1    Hartley, C.A.2    Jackson, D.C.3
  • 45
    • 0025304137 scopus 로고
    • Refinement of the influenza virus hemagglutinin by simulated annealing
    • Weis W.I., Brunger A.T., Skehel J.J., Wiley D.C. Refinement of the influenza virus hemagglutinin by simulated annealing. J. Mol. Biol. 1990, 212:737-761.
    • (1990) J. Mol. Biol. , vol.212 , pp. 737-761
    • Weis, W.I.1    Brunger, A.T.2    Skehel, J.J.3    Wiley, D.C.4
  • 46
    • 80051921486 scopus 로고    scopus 로고
    • Specific sites of N-linked glycosylation on the hemagglutinin of H1N1 subtype influenza A virus determine sensitivity to inhibitors of the innate immune system and virulence in mice
    • Tate M.D., Brooks A.G., Reading P.C. Specific sites of N-linked glycosylation on the hemagglutinin of H1N1 subtype influenza A virus determine sensitivity to inhibitors of the innate immune system and virulence in mice. J. Immunol. 2011, 187:1884-1894.
    • (2011) J. Immunol. , vol.187 , pp. 1884-1894
    • Tate, M.D.1    Brooks, A.G.2    Reading, P.C.3
  • 49
    • 0033037036 scopus 로고    scopus 로고
    • Structure of a heterophilic adhesion complex between the human CD2 and CD58 (LFA-3) counterreceptors
    • Wang J.H., Smolyar A., Tan K., Liu J.H., Kim M., Sun Z.Y., Wagner G., Reinherz E.L. Structure of a heterophilic adhesion complex between the human CD2 and CD58 (LFA-3) counterreceptors. Cell 1999, 97:791-803.
    • (1999) Cell , vol.97 , pp. 791-803
    • Wang, J.H.1    Smolyar, A.2    Tan, K.3    Liu, J.H.4    Kim, M.5    Sun, Z.Y.6    Wagner, G.7    Reinherz, E.L.8
  • 50
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • Lo Conte L., Chothia C., Janin J. The atomic structure of protein-protein recognition sites. J. Mol. Biol. 1999, 285:2177-2198.
    • (1999) J. Mol. Biol. , vol.285 , pp. 2177-2198
    • Lo Conte, L.1    Chothia, C.2    Janin, J.3
  • 51
    • 0027932728 scopus 로고
    • Human cell-adhesion molecule CD2 binds CD58 (LFA-3) with a very low affinity and an extremely fast dissociation rate but does not bind CD48 or CD59
    • van der Merwe P.A., Barclay A.N., Mason D.W., Davies E.A., Morgan B.P., Tone M., Krishnam A.K., Ianelli C., Davis S.J. Human cell-adhesion molecule CD2 binds CD58 (LFA-3) with a very low affinity and an extremely fast dissociation rate but does not bind CD48 or CD59. Biochemistry 1994, 33:10149-10160.
    • (1994) Biochemistry , vol.33 , pp. 10149-10160
    • van der Merwe, P.A.1    Barclay, A.N.2    Mason, D.W.3    Davies, E.A.4    Morgan, B.P.5    Tone, M.6    Krishnam, A.K.7    Ianelli, C.8    Davis, S.J.9
  • 52
    • 0030679644 scopus 로고    scopus 로고
    • Low affinity interaction of human or rat T cell adhesion molecule CD2 with its ligand aligns adhering membranes to achieve high physiological affinity
    • Dustin M.L., Golan D.E., Zhu D.M., Miller J.M., Meier W., Davies E.A., van der Merwe P.A. Low affinity interaction of human or rat T cell adhesion molecule CD2 with its ligand aligns adhering membranes to achieve high physiological affinity. J. Biol. Chem. 1997, 272:30889-30898.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30889-30898
    • Dustin, M.L.1    Golan, D.E.2    Zhu, D.M.3    Miller, J.M.4    Meier, W.5    Davies, E.A.6    van der Merwe, P.A.7
  • 53
    • 33846818557 scopus 로고    scopus 로고
    • Analysis of two-dimensional dissociation constant of laterally mobile cell adhesion molecules
    • Zhu D.M., Dustin M.L., Cairo C.W., Golan D.E. Analysis of two-dimensional dissociation constant of laterally mobile cell adhesion molecules. Biophys. J. 2007, 92:1022-1034.
    • (2007) Biophys. J. , vol.92 , pp. 1022-1034
    • Zhu, D.M.1    Dustin, M.L.2    Cairo, C.W.3    Golan, D.E.4
  • 54
    • 33846812555 scopus 로고    scopus 로고
    • Mechanisms of Cellular Avidity Regulation in CD2-CD58-Mediated T Cell Adhesion
    • Zhu D.M., Dustin M.L., Cairo C.W., Thatte H.S., Golan D.E. Mechanisms of Cellular Avidity Regulation in CD2-CD58-Mediated T Cell Adhesion. ACS Chem. Biol. 2006, 1:649-658.
    • (2006) ACS Chem. Biol. , vol.1 , pp. 649-658
    • Zhu, D.M.1    Dustin, M.L.2    Cairo, C.W.3    Thatte, H.S.4    Golan, D.E.5
  • 55
    • 0026046515 scopus 로고
    • Influence of receptor lateral mobility on adhesion strengthening between membranes containing LFA-3 and CD2
    • Chan P.Y., Lawrence M.B., Dustin M.L., Ferguson L.M., Golan D.E., Springer T.A. Influence of receptor lateral mobility on adhesion strengthening between membranes containing LFA-3 and CD2. J. Cell Biol. 1991, 115:245-255.
    • (1991) J. Cell Biol. , vol.115 , pp. 245-255
    • Chan, P.Y.1    Lawrence, M.B.2    Dustin, M.L.3    Ferguson, L.M.4    Golan, D.E.5    Springer, T.A.6
  • 56
    • 79957621253 scopus 로고    scopus 로고
    • The insider's guide to leukocyte integrin signalling and function
    • Hogg N., Patzak I., Willenbrock F. The insider's guide to leukocyte integrin signalling and function. Nat. Rev. Immunol. 2011, 11:416-426.
    • (2011) Nat. Rev. Immunol. , vol.11 , pp. 416-426
    • Hogg, N.1    Patzak, I.2    Willenbrock, F.3
  • 57
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: bidirectional, allosteric signaling machines
    • Hynes R.O. Integrins: bidirectional, allosteric signaling machines. Cell 2002, 110:673-687.
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 58
    • 0028959231 scopus 로고
    • The protein fold of the von Willebrand factor type A domain is predicted to be similar to the open twisted beta-sheet flanked by alpha-helices found in human ras-p21
    • Edwards Y.J., Perkins S.J. The protein fold of the von Willebrand factor type A domain is predicted to be similar to the open twisted beta-sheet flanked by alpha-helices found in human ras-p21. FEBS Lett. 1995, 358:283-286.
    • (1995) FEBS Lett. , vol.358 , pp. 283-286
    • Edwards, Y.J.1    Perkins, S.J.2
  • 61
    • 0031013031 scopus 로고    scopus 로고
    • Folding of the N-terminal, ligand-binding region of integrin alpha-subunits into a beta-propeller domain
    • Springer T.A. Folding of the N-terminal, ligand-binding region of integrin alpha-subunits into a beta-propeller domain. Proc. Natl. Acad. Sci. U. S. A. 1997, 94:65-72.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 65-72
    • Springer, T.A.1
  • 62
    • 76349099822 scopus 로고    scopus 로고
    • Structure of an integrin with an alphaI domain, complement receptor type 4
    • Xie C., Zhu J., Chen X., Mi L., Nishida N., Springer T.A. Structure of an integrin with an alphaI domain, complement receptor type 4. EMBO J. 2010, 29:666-679.
    • (2010) EMBO J. , vol.29 , pp. 666-679
    • Xie, C.1    Zhu, J.2    Chen, X.3    Mi, L.4    Nishida, N.5    Springer, T.A.6
  • 63
    • 0034647506 scopus 로고    scopus 로고
    • Structural and functional studies with antibodies to the integrin beta 2 subunit. A model for the I-like domain
    • Huang C., Zang Q., Takagi J., Springer T.A. Structural and functional studies with antibodies to the integrin beta 2 subunit. A model for the I-like domain. J. Biol. Chem. 2000, 275:21514-21524.
    • (2000) J. Biol. Chem. , vol.275 , pp. 21514-21524
    • Huang, C.1    Zang, Q.2    Takagi, J.3    Springer, T.A.4
  • 65
    • 0021271957 scopus 로고
    • Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule
    • Pierschbacher M.D., Ruoslahti E. Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule. Nature 1984, 309:30-33.
    • (1984) Nature , vol.309 , pp. 30-33
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 66
    • 0344256437 scopus 로고    scopus 로고
    • The RGD story: a personal account
    • Ruoslahti E. The RGD story: a personal account. Matrix Biol. 2003, 22:459-465.
    • (2003) Matrix Biol. , vol.22 , pp. 459-465
    • Ruoslahti, E.1
  • 67
    • 0029775681 scopus 로고    scopus 로고
    • RGD and other recognition sequences for integrins
    • Ruoslahti E. RGD and other recognition sequences for integrins. Annu. Rev. Cell Dev. Biol. 1996, 12:697-715.
    • (1996) Annu. Rev. Cell Dev. Biol. , vol.12 , pp. 697-715
    • Ruoslahti, E.1
  • 70
    • 0027977974 scopus 로고
    • Transient intercellular adhesion: the importance of weak protein-protein interactions
    • van der Merwe P.A., Barclay A.N. Transient intercellular adhesion: the importance of weak protein-protein interactions. Trends Biochem. Sci. 1994, 19:354-358.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 354-358
    • van der Merwe, P.A.1    Barclay, A.N.2
  • 72
    • 5144233487 scopus 로고    scopus 로고
    • Mechanism of action of glatiramer acetate in multiple sclerosis and its potential for the development of new applications
    • Arnon R., Aharoni R. Mechanism of action of glatiramer acetate in multiple sclerosis and its potential for the development of new applications. Proc. Natl. Acad. Sci. U. S. A. 2004, 101(Suppl. 2):14593-14598.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , Issue.SUPPL. 2 , pp. 14593-14598
    • Arnon, R.1    Aharoni, R.2
  • 73
    • 13444294243 scopus 로고    scopus 로고
    • Exposure of acidic residues as a danger signal for recognition of fibrinogen and other macromolecules by integrin alphaXbeta2
    • Vorup-Jensen T., Carman C.V., Shimaoka M., Schuck P., Svitel J., Springer T.A. Exposure of acidic residues as a danger signal for recognition of fibrinogen and other macromolecules by integrin alphaXbeta2. Proc. Natl. Acad. Sci. U. S. A. 2005, 102:1614-1619.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 1614-1619
    • Vorup-Jensen, T.1    Carman, C.V.2    Shimaoka, M.3    Schuck, P.4    Svitel, J.5    Springer, T.A.6
  • 74
    • 80054741216 scopus 로고    scopus 로고
    • Surface plasmon resonance biosensing in studies of the binding between beta integrin I domains and their ligands
    • Vorup-Jensen T. Surface plasmon resonance biosensing in studies of the binding between beta integrin I domains and their ligands. Methods Mol. Biol. 2012, 757:55-71.
    • (2012) Methods Mol. Biol. , vol.757 , pp. 55-71
    • Vorup-Jensen, T.1
  • 78
    • 77953263435 scopus 로고    scopus 로고
    • The role of mass transport limitation and surface heterogeneity in the biophysical characterization of macromolecular binding processes by SPR biosensing
    • Schuck P., Zhao H. The role of mass transport limitation and surface heterogeneity in the biophysical characterization of macromolecular binding processes by SPR biosensing. Methods Mol. Biol. 2010, 627:15-54.
    • (2010) Methods Mol. Biol. , vol.627 , pp. 15-54
    • Schuck, P.1    Zhao, H.2
  • 79
    • 55549104031 scopus 로고    scopus 로고
    • Schuck, Bayesian analysis of heterogeneity in the distribution of binding properties of immobilized surface sites
    • Gorshkova J., Svitel F., Razjouyan P. Schuck, Bayesian analysis of heterogeneity in the distribution of binding properties of immobilized surface sites. Langmuir 2008, 24:11577-11586.
    • (2008) Langmuir , vol.24 , pp. 11577-11586
    • Gorshkova, J.1    Svitel, F.2    Razjouyan, P.3
  • 80
    • 0038778441 scopus 로고    scopus 로고
    • Combined affinity and rate constant distributions of ligand populations from experimental surface binding kinetics and equilibria
    • Svitel J., Balbo A., Mariuzza R.A., Gonzales N.R., Schuck P. Combined affinity and rate constant distributions of ligand populations from experimental surface binding kinetics and equilibria. Biophys. J. 2003, 84:4062-4077.
    • (2003) Biophys. J. , vol.84 , pp. 4062-4077
    • Svitel, J.1    Balbo, A.2    Mariuzza, R.A.3    Gonzales, N.R.4    Schuck, P.5
  • 81
    • 0018817278 scopus 로고
    • Localization of individual lysine-binding regions in human plasminogen and investigations on their complex-forming properties
    • Lerch P.G., Rickli E.E., Lergier W., Gillessen D. Localization of individual lysine-binding regions in human plasminogen and investigations on their complex-forming properties. Eur. J. Biochem. 1980, 107:7-13.
    • (1980) Eur. J. Biochem. , vol.107 , pp. 7-13
    • Lerch, P.G.1    Rickli, E.E.2    Lergier, W.3    Gillessen, D.4
  • 82
    • 0020539898 scopus 로고
    • Purification and molecular characterization of the brain synaptic membrane glutamate-binding protein
    • Michaelis E.K., Michaelis M.L., Stormann T.M., Chittenden W.L., Grubbs R.D. Purification and molecular characterization of the brain synaptic membrane glutamate-binding protein. J. Neurochem. 1983, 40:1742-1753.
    • (1983) J. Neurochem. , vol.40 , pp. 1742-1753
    • Michaelis, E.K.1    Michaelis, M.L.2    Stormann, T.M.3    Chittenden, W.L.4    Grubbs, R.D.5
  • 83
    • 0027982876 scopus 로고
    • Traffic signals for lymphocyte recirculation and leukocyte emigration: the multistep paradigm
    • Springer T.A. Traffic signals for lymphocyte recirculation and leukocyte emigration: the multistep paradigm. Cell 1994, 76:301-314.
    • (1994) Cell , vol.76 , pp. 301-314
    • Springer, T.A.1
  • 86
    • 33847630759 scopus 로고    scopus 로고
    • Critical residues of alphaX I-domain recognizing fibrinogen central domain
    • Lee J.H., Choi J., Nham S.U. Critical residues of alphaX I-domain recognizing fibrinogen central domain. Biochem. Biophys. Res. Commun. 2007, 355:1058-1063.
    • (2007) Biochem. Biophys. Res. Commun. , vol.355 , pp. 1058-1063
    • Lee, J.H.1    Choi, J.2    Nham, S.U.3
  • 87
    • 0029166397 scopus 로고
    • Heparin is an adhesive ligand for the leukocyte integrin Mac-1 (CD11b/CD1)
    • Diamond M.S., Alon R., Parkos C.A., Quinn M.T., Springer T.A. Heparin is an adhesive ligand for the leukocyte integrin Mac-1 (CD11b/CD1). J. Cell Biol. 1995, 130:1473-1482.
    • (1995) J. Cell Biol. , vol.130 , pp. 1473-1482
    • Diamond, M.S.1    Alon, R.2    Parkos, C.A.3    Quinn, M.T.4    Springer, T.A.5
  • 89
    • 70249092883 scopus 로고    scopus 로고
    • Free energy calculations of glycosaminoglycan-protein interactions
    • Gandhi N.S., Mancera R.L. Free energy calculations of glycosaminoglycan-protein interactions. Glycobiology 2009, 19:1103-1115.
    • (2009) Glycobiology , vol.19 , pp. 1103-1115
    • Gandhi, N.S.1    Mancera, R.L.2
  • 90
    • 80455127321 scopus 로고    scopus 로고
    • Biophysical investigations on the interaction of the major bovine seminal plasma protein, PDC-109, with heparin
    • Sankhala R.S., Damai R.S., Anbazhagan V., Kumar C.S., Bulusu G., Swamy M.J. Biophysical investigations on the interaction of the major bovine seminal plasma protein, PDC-109, with heparin. J. Phys. Chem. B 2011, 115:12954-12962.
    • (2011) J. Phys. Chem. B , vol.115 , pp. 12954-12962
    • Sankhala, R.S.1    Damai, R.S.2    Anbazhagan, V.3    Kumar, C.S.4    Bulusu, G.5    Swamy, M.J.6
  • 91
    • 0023840717 scopus 로고
    • Behavior of antithrombin III isoforms on immobilized heparins. Evidence that the isoforms bind to different numbers of low-affinity heparin sites
    • Carlson T.H., Babcock T., Atencio A.C., Levinson C., Mora H.R. Behavior of antithrombin III isoforms on immobilized heparins. Evidence that the isoforms bind to different numbers of low-affinity heparin sites. J. Biol. Chem. 1988, 263:2187-2194.
    • (1988) J. Biol. Chem. , vol.263 , pp. 2187-2194
    • Carlson, T.H.1    Babcock, T.2    Atencio, A.C.3    Levinson, C.4    Mora, H.R.5
  • 92
    • 0026736029 scopus 로고
    • The Mac-1 and p150,95 beta 2 integrins bind denatured proteins to mediate leukocyte cell-substrate adhesion
    • Davis G.E. The Mac-1 and p150,95 beta 2 integrins bind denatured proteins to mediate leukocyte cell-substrate adhesion. Exp. Cell Res. 1992, 200:242-252.
    • (1992) Exp. Cell Res. , vol.200 , pp. 242-252
    • Davis, G.E.1
  • 93
    • 0034698162 scopus 로고    scopus 로고
    • Folding and function of I domain-deleted Mac-1 and lymphocyte function-associated antigen-1
    • Yalamanchili P., Lu C., Oxvig C., Springer T.A. Folding and function of I domain-deleted Mac-1 and lymphocyte function-associated antigen-1. J. Biol. Chem. 2000, 275:21877-21882.
    • (2000) J. Biol. Chem. , vol.275 , pp. 21877-21882
    • Yalamanchili, P.1    Lu, C.2    Oxvig, C.3    Springer, T.A.4
  • 94
    • 12544252996 scopus 로고    scopus 로고
    • Distinct roles for the alpha and beta subunits in the functions of integrin alphaMbeta2
    • Solovjov D.A., Pluskota E., Plow E.F. Distinct roles for the alpha and beta subunits in the functions of integrin alphaMbeta2. J. Biol. Chem. 2005, 280:1336-1345.
    • (2005) J. Biol. Chem. , vol.280 , pp. 1336-1345
    • Solovjov, D.A.1    Pluskota, E.2    Plow, E.F.3
  • 95
    • 33747174596 scopus 로고    scopus 로고
    • Down-regulation of integrin alpha M beta 2 ligand-binding function by the urokinase-type plasminogen activator receptor
    • Tang M.L., Kong L.S., Law S.K., Tan S.M. Down-regulation of integrin alpha M beta 2 ligand-binding function by the urokinase-type plasminogen activator receptor. Biochem. Biophys. Res. Commun. 2006, 348:1184-1193.
    • (2006) Biochem. Biophys. Res. Commun. , vol.348 , pp. 1184-1193
    • Tang, M.L.1    Kong, L.S.2    Law, S.K.3    Tan, S.M.4
  • 96
    • 0026554217 scopus 로고
    • Affinity of integrins for damaged extracellular matrix: alpha v beta 3 binds to denatured collagen type I through RGD sites
    • Davis G.E. Affinity of integrins for damaged extracellular matrix: alpha v beta 3 binds to denatured collagen type I through RGD sites. Biochem. Biophys. Res. Commun. 1992, 182:1025-1031.
    • (1992) Biochem. Biophys. Res. Commun. , vol.182 , pp. 1025-1031
    • Davis, G.E.1
  • 97
    • 0030612478 scopus 로고    scopus 로고
    • The alpha4beta1 integrin can mediate leukocyte adhesion to casein and denatured protein substrates
    • Davis G.E., Thomas J.S., Madden S. The alpha4beta1 integrin can mediate leukocyte adhesion to casein and denatured protein substrates. J. Leukoc. Biol. 1997, 62:318-328.
    • (1997) J. Leukoc. Biol. , vol.62 , pp. 318-328
    • Davis, G.E.1    Thomas, J.S.2    Madden, S.3
  • 98
    • 64549135379 scopus 로고    scopus 로고
    • Proteolysis of fibrinogen deposits enables hydrogen peroxide-stimulated polymorphonuclear leukocytes to spread in an acidified environment
    • Suzuki K., Namiki H. Proteolysis of fibrinogen deposits enables hydrogen peroxide-stimulated polymorphonuclear leukocytes to spread in an acidified environment. Eur. J. Pharmacol. 2009, 609:140-147.
    • (2009) Eur. J. Pharmacol. , vol.609 , pp. 140-147
    • Suzuki, K.1    Namiki, H.2
  • 99
    • 0028986196 scopus 로고
    • Crystal structure of the A domain from the alpha subunit of integrin CR3 (CD11b/CD18)
    • Lee J.O., Rieu P., Arnaout M.A., Liddington R. Crystal structure of the A domain from the alpha subunit of integrin CR3 (CD11b/CD18). Cell 1995, 80:631-638.
    • (1995) Cell , vol.80 , pp. 631-638
    • Lee, J.O.1    Rieu, P.2    Arnaout, M.A.3    Liddington, R.4
  • 100
    • 0033900165 scopus 로고    scopus 로고
    • Computational design of an integrin I domain stabilized in the open high affinity conformation
    • Shimaoka M., Shifman J.M., Jing H., Takagi J., Mayo S.L., Springer T.A. Computational design of an integrin I domain stabilized in the open high affinity conformation. Nat. Struct. Biol. 2000, 7:674-678.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 674-678
    • Shimaoka, M.1    Shifman, J.M.2    Jing, H.3    Takagi, J.4    Mayo, S.L.5    Springer, T.A.6
  • 101
    • 0037168524 scopus 로고    scopus 로고
    • Stabilizing the integrin alpha M inserted domain in alternative conformations with a range of engineered disulfide bonds
    • Shimaoka M., Lu C., Salas A., Xiao T., Takagi J., Springer T.A. Stabilizing the integrin alpha M inserted domain in alternative conformations with a range of engineered disulfide bonds. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:16737-16741.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 16737-16741
    • Shimaoka, M.1    Lu, C.2    Salas, A.3    Xiao, T.4    Takagi, J.5    Springer, T.A.6
  • 102
    • 0035956969 scopus 로고    scopus 로고
    • An isolated, surface-expressed I domain of the integrin alphaLbeta2 is sufficient for strong adhesive function when locked in the open conformation with a disulfide bond
    • Lu C., Shimaoka M., Ferzly M., Oxvig C., Takagi J., Springer T.A. An isolated, surface-expressed I domain of the integrin alphaLbeta2 is sufficient for strong adhesive function when locked in the open conformation with a disulfide bond. Proc. Natl. Acad. Sci. U. S. A. 2001, 98:2387-2392.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 2387-2392
    • Lu, C.1    Shimaoka, M.2    Ferzly, M.3    Oxvig, C.4    Takagi, J.5    Springer, T.A.6
  • 103
    • 0035932996 scopus 로고    scopus 로고
    • Reversibly locking a protein fold in an active conformation with a disulfide bond: integrin alphaL I domains with high affinity and antagonist activity in vivo
    • Shimaoka M., Lu C., Palframan R.T., von Andrian U.H., McCormack A., Takagi J., Springer T.A. Reversibly locking a protein fold in an active conformation with a disulfide bond: integrin alphaL I domains with high affinity and antagonist activity in vivo. Proc. Natl. Acad. Sci. U. S. A. 2001, 98:6009-6014.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 6009-6014
    • Shimaoka, M.1    Lu, C.2    Palframan, R.T.3    von Andrian, U.H.4    McCormack, A.5    Takagi, J.6    Springer, T.A.7
  • 104
    • 33845566257 scopus 로고    scopus 로고
    • Importance of force linkage in mechanochemistry of adhesion receptors
    • Astrof N.S., Salas A., Shimaoka M., Chen J., Springer T.A. Importance of force linkage in mechanochemistry of adhesion receptors. Biochemistry 2006, 45:15020-15028.
    • (2006) Biochemistry , vol.45 , pp. 15020-15028
    • Astrof, N.S.1    Salas, A.2    Shimaoka, M.3    Chen, J.4    Springer, T.A.5
  • 107
    • 0034624058 scopus 로고    scopus 로고
    • An isoleucine-based allosteric switch controls affinity and shape shifting in integrin CD11b A-domain
    • Xiong J.P., Li R., Essafi M., Stehle T., Arnaout M.A. An isoleucine-based allosteric switch controls affinity and shape shifting in integrin CD11b A-domain. J. Biol. Chem. 2000, 275:38762-38767.
    • (2000) J. Biol. Chem. , vol.275 , pp. 38762-38767
    • Xiong, J.P.1    Li, R.2    Essafi, M.3    Stehle, T.4    Arnaout, M.A.5
  • 108
    • 34247891506 scopus 로고    scopus 로고
    • Structural basis of integrin regulation and signaling
    • Luo B.H., Carman C.V., Springer T.A. Structural basis of integrin regulation and signaling. Annu. Rev. Immunol. 2007, 25:619-647.
    • (2007) Annu. Rev. Immunol. , vol.25 , pp. 619-647
    • Luo, B.H.1    Carman, C.V.2    Springer, T.A.3
  • 109
    • 0037031906 scopus 로고    scopus 로고
    • Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling
    • Takagi J., Petre B.M., Walz T., Springer T.A. Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling. Cell 2002, 110:599-511.
    • (2002) Cell , vol.110 , pp. 599-511
    • Takagi, J.1    Petre, B.M.2    Walz, T.3    Springer, T.A.4
  • 110
    • 0141625303 scopus 로고    scopus 로고
    • Structure of integrin alpha5beta1 in complex with fibronectin
    • Takagi J., Strokovich K., Springer T.A., Walz T. Structure of integrin alpha5beta1 in complex with fibronectin. EMBO J. 2003, 22:4607-4615.
    • (2003) EMBO J. , vol.22 , pp. 4607-4615
    • Takagi, J.1    Strokovich, K.2    Springer, T.A.3    Walz, T.4
  • 111
    • 82455189778 scopus 로고    scopus 로고
    • Regulation of integrin affinity on cell surfaces
    • Schurpf T., Springer T.A. Regulation of integrin affinity on cell surfaces. EMBO J. 2011, 30:4712-4727.
    • (2011) EMBO J. , vol.30 , pp. 4712-4727
    • Schurpf, T.1    Springer, T.A.2
  • 112
    • 1542357680 scopus 로고    scopus 로고
    • Intersubunit signal transmission in integrins by a receptor-like interaction with a pull spring
    • Yang W., Shimaoka M., Salas A., Takagi J., Springer T.A. Intersubunit signal transmission in integrins by a receptor-like interaction with a pull spring. Proc. Natl. Acad. Sci. U. S. A. 2004, 101:2906-2911.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 2906-2911
    • Yang, W.1    Shimaoka, M.2    Salas, A.3    Takagi, J.4    Springer, T.A.5
  • 113
    • 1442306162 scopus 로고    scopus 로고
    • Activation of integrin beta-subunit I-like domains by one-turn C-terminal alpha-helix deletions
    • Yang W., Shimaoka M., Chen J., Springer T.A. Activation of integrin beta-subunit I-like domains by one-turn C-terminal alpha-helix deletions. Proc. Natl. Acad. Sci. U. S. A. 2004, 101:2333-2338.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 2333-2338
    • Yang, W.1    Shimaoka, M.2    Chen, J.3    Springer, T.A.4
  • 114
    • 0029646107 scopus 로고
    • Two conformations of the integrin A-domain (I-domain): a pathway for activation?
    • Lee J.O., Bankston L.A., Arnaout M.A., Liddington R.C. Two conformations of the integrin A-domain (I-domain): a pathway for activation?. Structure 1995, 3:1333-1340.
    • (1995) Structure , vol.3 , pp. 1333-1340
    • Lee, J.O.1    Bankston, L.A.2    Arnaout, M.A.3    Liddington, R.C.4
  • 116
    • 68149094151 scopus 로고    scopus 로고
    • Physiology of calcium, phosphate and magnesium
    • Allgrove J. Physiology of calcium, phosphate and magnesium. Endocr. Dev. 2009, 16:8-31.
    • (2009) Endocr. Dev. , vol.16 , pp. 8-31
    • Allgrove, J.1
  • 117
    • 0037366128 scopus 로고    scopus 로고
    • Principles governing Mg, Ca, and Zn binding and selectivity in proteins
    • Dudev T., Lim C. Principles governing Mg, Ca, and Zn binding and selectivity in proteins. Chem. Rev. 2003, 103:773-788.
    • (2003) Chem. Rev. , vol.103 , pp. 773-788
    • Dudev, T.1    Lim, C.2
  • 119
    • 0031952651 scopus 로고    scopus 로고
    • Are changes in integrin affinity and conformation overemphasized?
    • Bazzoni G., Hemler M.E. Are changes in integrin affinity and conformation overemphasized?. Trends Biochem. Sci. 1998, 23:30-34.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 30-34
    • Bazzoni, G.1    Hemler, M.E.2
  • 120
    • 0141756175 scopus 로고    scopus 로고
    • Integrin avidity regulation: are changes in affinity and conformation underemphasized?
    • Carman C.V., Springer T.A. Integrin avidity regulation: are changes in affinity and conformation underemphasized?. Curr. Opin. Cell Biol. 2003, 15:547-556.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 547-556
    • Carman, C.V.1    Springer, T.A.2
  • 121
    • 80052187643 scopus 로고    scopus 로고
    • Identification of integrin beta subunit mutations that alter affinity for extracellular matrix ligand
    • Kendall T., Mukai L., Jannuzi A.L., Bunch T.A. Identification of integrin beta subunit mutations that alter affinity for extracellular matrix ligand. J. Biol. Chem. 2011, 286:30981-30993.
    • (2011) J. Biol. Chem. , vol.286 , pp. 30981-30993
    • Kendall, T.1    Mukai, L.2    Jannuzi, A.L.3    Bunch, T.A.4
  • 122
    • 77949884325 scopus 로고    scopus 로고
    • Distinct roles for LFA-1 affinity regulation during T-cell adhesion, diapedesis, and interstitial migration in lymph nodes
    • Park E.J., Peixoto A., Imai Y., Goodarzi A., Cheng G., Carman C.V., von Andrian U.H., Shimaoka M. Distinct roles for LFA-1 affinity regulation during T-cell adhesion, diapedesis, and interstitial migration in lymph nodes. Blood 2010, 115:1572-1581.
    • (2010) Blood , vol.115 , pp. 1572-1581
    • Park, E.J.1    Peixoto, A.2    Imai, Y.3    Goodarzi, A.4    Cheng, G.5    Carman, C.V.6    von Andrian, U.H.7    Shimaoka, M.8
  • 125
    • 67649998388 scopus 로고    scopus 로고
    • Dynamic re-organization of individual adhesion nanoclusters in living cells by ligand-patterned surfaces
    • Diez-Ahedo R., Normanno D., Esteban O., Bakker G.J., Figdor C.G., Cambi A., Garcia-Parajo M.F. Dynamic re-organization of individual adhesion nanoclusters in living cells by ligand-patterned surfaces. Small 2009, 5:1258-1263.
    • (2009) Small , vol.5 , pp. 1258-1263
    • Diez-Ahedo, R.1    Normanno, D.2    Esteban, O.3    Bakker, G.J.4    Figdor, C.G.5    Cambi, A.6    Garcia-Parajo, M.F.7
  • 128
    • 77449114018 scopus 로고    scopus 로고
    • A nanometer scale optical view on the compartmentalization of cell membranes
    • van Zanten T.S., Cambi A., Garcia-Parajo M.F. A nanometer scale optical view on the compartmentalization of cell membranes. Biochim. Biophys. Acta 2010, 1798:777-787.
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 777-787
    • van Zanten, T.S.1    Cambi, A.2    Garcia-Parajo, M.F.3
  • 129
    • 59149102202 scopus 로고    scopus 로고
    • Disruption of the integrin alphaLbeta2 transmembrane domain interface by beta2 Thr-686 mutation activates alphaLbeta2 and promotes micro-clustering of the alphaL subunits
    • Vararattanavech A., Lin X., Torres J., Tan S.M. Disruption of the integrin alphaLbeta2 transmembrane domain interface by beta2 Thr-686 mutation activates alphaLbeta2 and promotes micro-clustering of the alphaL subunits. J. Biol. Chem. 2009, 284:3239-3249.
    • (2009) J. Biol. Chem. , vol.284 , pp. 3239-3249
    • Vararattanavech, A.1    Lin, X.2    Torres, J.3    Tan, S.M.4
  • 130
    • 11244274075 scopus 로고    scopus 로고
    • The primacy of affinity over clustering in regulation of adhesiveness of the integrin {alpha}L{beta}2
    • Kim M., Carman C.V., Yang W., Salas A., Springer T.A. The primacy of affinity over clustering in regulation of adhesiveness of the integrin {alpha}L{beta}2. J. Cell Biol. 2004, 167:1241-1253.
    • (2004) J. Cell Biol. , vol.167 , pp. 1241-1253
    • Kim, M.1    Carman, C.V.2    Yang, W.3    Salas, A.4    Springer, T.A.5
  • 131
    • 0028785507 scopus 로고
    • Intercellular adhesion molecule-1 dimerization and its consequences for adhesion mediated by lymphocyte function associated-1
    • Miller J., Knorr R., Ferrone M., Houdei R., Carron C.P., Dustin M.L. Intercellular adhesion molecule-1 dimerization and its consequences for adhesion mediated by lymphocyte function associated-1. J. Exp. Med. 1995, 182:1231-1241.
    • (1995) J. Exp. Med. , vol.182 , pp. 1231-1241
    • Miller, J.1    Knorr, R.2    Ferrone, M.3    Houdei, R.4    Carron, C.P.5    Dustin, M.L.6
  • 132
    • 0029013298 scopus 로고
    • The native structure of intercellular adhesion molecule-1 (ICAM-1) is a dimer. Correlation with binding to LFA-1
    • Reilly P.L., Woska J.R., Jeanfavre D.D., McNally E., Rothlein R., Bormann B.J. The native structure of intercellular adhesion molecule-1 (ICAM-1) is a dimer. Correlation with binding to LFA-1. J. Immunol. 1995, 155:529-532.
    • (1995) J. Immunol. , vol.155 , pp. 529-532
    • Reilly, P.L.1    Woska, J.R.2    Jeanfavre, D.D.3    McNally, E.4    Rothlein, R.5    Bormann, B.J.6
  • 136
    • 33746114879 scopus 로고    scopus 로고
    • The kinetic-segregation model: TCR triggering and beyond
    • Davis S.J., van der Merwe P.A. The kinetic-segregation model: TCR triggering and beyond. Nat. Immunol. 2006, 7:803-809.
    • (2006) Nat. Immunol. , vol.7 , pp. 803-809
    • Davis, S.J.1    van der Merwe, P.A.2
  • 137
    • 77949890193 scopus 로고    scopus 로고
    • Lectins as pattern recognition molecules: the effects of epitope density in innate immunity
    • Dam T.K., Brewer C.F. Lectins as pattern recognition molecules: the effects of epitope density in innate immunity. Glycobiology 2010, 20:270-279.
    • (2010) Glycobiology , vol.20 , pp. 270-279
    • Dam, T.K.1    Brewer, C.F.2
  • 138
    • 15744379234 scopus 로고    scopus 로고
    • Characterization of the oligomer structure of recombinant human mannan-binding lectin
    • Jensen P.H., Weilguny D., Matthiesen F., McGuire K.A., Shi L., Hojrup P. Characterization of the oligomer structure of recombinant human mannan-binding lectin. J. Biol. Chem. 2005, 280:11043-11051.
    • (2005) J. Biol. Chem. , vol.280 , pp. 11043-11051
    • Jensen, P.H.1    Weilguny, D.2    Matthiesen, F.3    McGuire, K.A.4    Shi, L.5    Hojrup, P.6
  • 139
    • 67651115625 scopus 로고    scopus 로고
    • Mannan-binding lectin: structure, oligomerization, and flexibility studied by atomic force microscopy
    • Jensenius H., Klein D.C., van Hecke M., Oosterkamp T.H., Schmidt T., Jensenius J.C. Mannan-binding lectin: structure, oligomerization, and flexibility studied by atomic force microscopy. J. Mol. Biol. 2009, 391:246-259.
    • (2009) J. Mol. Biol. , vol.391 , pp. 246-259
    • Jensenius, H.1    Klein, D.C.2    van Hecke, M.3    Oosterkamp, T.H.4    Schmidt, T.5    Jensenius, J.C.6
  • 140
    • 14044278783 scopus 로고    scopus 로고
    • The two major oligomeric forms of human mannan-binding lectin: chemical characterization, carbohydrate-binding properties, and interaction with MBL-associated serine proteases
    • Teillet F., Dublet B., Andrieu J.P., Gaboriaud C., Arlaud G.J., Thielens N.M. The two major oligomeric forms of human mannan-binding lectin: chemical characterization, carbohydrate-binding properties, and interaction with MBL-associated serine proteases. J. Immunol. 2005, 174:2870-2877.
    • (2005) J. Immunol. , vol.174 , pp. 2870-2877
    • Teillet, F.1    Dublet, B.2    Andrieu, J.P.3    Gaboriaud, C.4    Arlaud, G.J.5    Thielens, N.M.6
  • 144
    • 0026009904 scopus 로고
    • Solution structure of human and mouse immunoglobulin M by synchrotron X-ray scattering and molecular graphics modelling. A possible mechanism for complement activation
    • Perkins S.J., Nealis A.S., Sutton B.J., Feinstein A. Solution structure of human and mouse immunoglobulin M by synchrotron X-ray scattering and molecular graphics modelling. A possible mechanism for complement activation. J. Mol. Biol. 1991, 221:1345-1366.
    • (1991) J. Mol. Biol. , vol.221 , pp. 1345-1366
    • Perkins, S.J.1    Nealis, A.S.2    Sutton, B.J.3    Feinstein, A.4
  • 145
    • 70349284531 scopus 로고    scopus 로고
    • The human IgM pentamer is a mushroom-shaped molecule with a flexural bias
    • Czajkowsky D.M., Shao Z. The human IgM pentamer is a mushroom-shaped molecule with a flexural bias. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:14960-14965.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 14960-14965
    • Czajkowsky, D.M.1    Shao, Z.2
  • 147
    • 79960640479 scopus 로고    scopus 로고
    • Biology and physics of von Willebrand factor concatamers
    • Springer T.A. Biology and physics of von Willebrand factor concatamers. J. Thromb. Haemost. 2011, 9(Suppl. 1):130-143.
    • (2011) J. Thromb. Haemost. , vol.9 , Issue.SUPPL. 1 , pp. 130-143
    • Springer, T.A.1
  • 149
    • 80052144227 scopus 로고    scopus 로고
    • Protein ultrastructure and the nanoscience of complement activation
    • Vorup-Jensen T., Boesen T. Protein ultrastructure and the nanoscience of complement activation. Adv. Drug Deliv. Rev. 2011, 63:1008-1019.
    • (2011) Adv. Drug Deliv. Rev. , vol.63 , pp. 1008-1019
    • Vorup-Jensen, T.1    Boesen, T.2
  • 150
    • 84869197631 scopus 로고    scopus 로고
    • Wrong resemblance? Role of the immune system in biocompatibility of nanostructured materials
    • Pan Stanford Publishing, Singapore, D. Peer (Ed.)
    • Vorup-Jensen T. Wrong resemblance? Role of the immune system in biocompatibility of nanostructured materials. Handbook of harnessing biomaterials in nanomedicine 2012, 283-301. Pan Stanford Publishing, Singapore. D. Peer (Ed.).
    • (2012) Handbook of harnessing biomaterials in nanomedicine , pp. 283-301
    • Vorup-Jensen, T.1
  • 151
    • 79959397904 scopus 로고    scopus 로고
    • Mechanisms of membrane curvature sensing
    • Antonny B. Mechanisms of membrane curvature sensing. Annu. Rev. Biochem. 2011, 80:101-123.
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 101-123
    • Antonny, B.1
  • 152
    • 77950596053 scopus 로고    scopus 로고
    • Driving membrane curvature in clathrin-dependent and clathrin-independent endocytosis
    • Lundmark R., Carlsson S.R. Driving membrane curvature in clathrin-dependent and clathrin-independent endocytosis. Semin. Cell Dev. Biol. 2010, 21:363-370.
    • (2010) Semin. Cell Dev. Biol. , vol.21 , pp. 363-370
    • Lundmark, R.1    Carlsson, S.R.2
  • 154
    • 80855128787 scopus 로고    scopus 로고
    • Structural basis of mannan-binding lectin recognition by its associated serine protease MASP-1: implications for complement activation
    • Gingras A.R., Girija U.V., Keeble A.H., Panchal R., Mitchell D.A., Moody P.C., Wallis R. Structural basis of mannan-binding lectin recognition by its associated serine protease MASP-1: implications for complement activation. Structure 2011, 19:1635-1643.
    • (2011) Structure , vol.19 , pp. 1635-1643
    • Gingras, A.R.1    Girija, U.V.2    Keeble, A.H.3    Panchal, R.4    Mitchell, D.A.5    Moody, P.C.6    Wallis, R.7
  • 155
    • 0031847681 scopus 로고    scopus 로고
    • Structural specializations of immunoglobulin superfamily members for adhesion to integrins and viruses
    • Wang J., Springer T.A. Structural specializations of immunoglobulin superfamily members for adhesion to integrins and viruses. Immunol. Rev. 1998, 163:197-215.
    • (1998) Immunol. Rev. , vol.163 , pp. 197-215
    • Wang, J.1    Springer, T.A.2
  • 156
    • 0022453692 scopus 로고
    • A human intercellular adhesion molecule (ICAM-1) distinct from LFA-1
    • Rothlein R., Dustin M.L., Marlin S.D., Springer T.A. A human intercellular adhesion molecule (ICAM-1) distinct from LFA-1. J. Immunol. 1986, 137:1270-1274.
    • (1986) J. Immunol. , vol.137 , pp. 1270-1274
    • Rothlein, R.1    Dustin, M.L.2    Marlin, S.D.3    Springer, T.A.4
  • 157
    • 0030794169 scopus 로고    scopus 로고
    • A distinct profile of six soluble adhesion molecules (ICAM-1, ICAM-3, VCAM-1, E-selectin, L-selectin and P-selectin) in rheumatoid arthritis
    • Littler A.J., Buckley C.D., Wordsworth P., Collins I., Martinson J., Simmons D.L. A distinct profile of six soluble adhesion molecules (ICAM-1, ICAM-3, VCAM-1, E-selectin, L-selectin and P-selectin) in rheumatoid arthritis. Br. J. Rheumatol. 1997, 36:164-169.
    • (1997) Br. J. Rheumatol. , vol.36 , pp. 164-169
    • Littler, A.J.1    Buckley, C.D.2    Wordsworth, P.3    Collins, I.4    Martinson, J.5    Simmons, D.L.6
  • 158
    • 0025809398 scopus 로고
    • Circulating ICAM-1 isoforms: diagnostic prospects for inflammatory and immune disorders
    • Seth R., Raymond F.D., Makgoba M.W. Circulating ICAM-1 isoforms: diagnostic prospects for inflammatory and immune disorders. Lancet 1991, 338:83-84.
    • (1991) Lancet , vol.338 , pp. 83-84
    • Seth, R.1    Raymond, F.D.2    Makgoba, M.W.3
  • 159
    • 33846935498 scopus 로고    scopus 로고
    • Evidence for two distinct pathways in TNFalpha-induced membrane and soluble forms of ICAM-1 in human osteoblast-like cells isolated from osteoarthritic patients
    • Shi Q., Benderdour M., Lavigne P., Ranger P., Fernandes J.C. Evidence for two distinct pathways in TNFalpha-induced membrane and soluble forms of ICAM-1 in human osteoblast-like cells isolated from osteoarthritic patients. Osteoarthritis Cartilage 2007, 15:300-308.
    • (2007) Osteoarthritis Cartilage , vol.15 , pp. 300-308
    • Shi, Q.1    Benderdour, M.2    Lavigne, P.3    Ranger, P.4    Fernandes, J.C.5
  • 161
    • 0037043820 scopus 로고    scopus 로고
    • Matrix metalloproteinase 9 (MMP-9/gelatinase B) proteolytically cleaves ICAM-1 and participates in tumor cell resistance to natural killer cell-mediated cytotoxicity
    • Fiore E., Fusco C., Romero P., Stamenkovic I. Matrix metalloproteinase 9 (MMP-9/gelatinase B) proteolytically cleaves ICAM-1 and participates in tumor cell resistance to natural killer cell-mediated cytotoxicity. Oncogene 2002, 21:5213-5223.
    • (2002) Oncogene , vol.21 , pp. 5213-5223
    • Fiore, E.1    Fusco, C.2    Romero, P.3    Stamenkovic, I.4
  • 163
    • 0025269047 scopus 로고
    • The arrangement of the immunoglobulin-like domains of ICAM-1 and the binding sites for LFA-1 and rhinovirus
    • Staunton D.E., Dustin M.L., Erickson H.P., Springer T.A. The arrangement of the immunoglobulin-like domains of ICAM-1 and the binding sites for LFA-1 and rhinovirus. Cell 1990, 61:243-254.
    • (1990) Cell , vol.61 , pp. 243-254
    • Staunton, D.E.1    Dustin, M.L.2    Erickson, H.P.3    Springer, T.A.4
  • 164
    • 0025759969 scopus 로고
    • Binding of the integrin Mac-1 (CD11b/CD18) to the third immunoglobulin-like domain of ICAM-1 (CD54) and its regulation by glycosylation
    • Diamond M.S., Staunton D.E., Marlin S.D., Springer T.A. Binding of the integrin Mac-1 (CD11b/CD18) to the third immunoglobulin-like domain of ICAM-1 (CD54) and its regulation by glycosylation. Cell 1991, 65:961-971.
    • (1991) Cell , vol.65 , pp. 961-971
    • Diamond, M.S.1    Staunton, D.E.2    Marlin, S.D.3    Springer, T.A.4
  • 166
    • 0035800831 scopus 로고    scopus 로고
    • Ultrastructure and function of dimeric, soluble intercellular adhesion molecule-1 (ICAM-1)
    • Jun C.D., Carman C.V., Redick S.D., Shimaoka M., Erickson H.P., Springer T.A. Ultrastructure and function of dimeric, soluble intercellular adhesion molecule-1 (ICAM-1). J. Biol. Chem. 2001, 276:29019-29027.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29019-29027
    • Jun, C.D.1    Carman, C.V.2    Redick, S.D.3    Shimaoka, M.4    Erickson, H.P.5    Springer, T.A.6
  • 169
    • 0026694034 scopus 로고
    • Towards an understanding of the arginine-aspartate interaction
    • Mitchell J.B., Thornton J.M., Singh J., Price S.L. Towards an understanding of the arginine-aspartate interaction. J. Mol. Biol. 1992, 226:251-262.
    • (1992) J. Mol. Biol. , vol.226 , pp. 251-262
    • Mitchell, J.B.1    Thornton, J.M.2    Singh, J.3    Price, S.L.4
  • 170
    • 34848850459 scopus 로고    scopus 로고
    • Structural plasticity in Ig superfamily domain 4 of ICAM-1 mediates cell surface dimerization
    • Chen X., Kim T.D., Carman C.V., Mi L.Z., Song G., Springer T.A. Structural plasticity in Ig superfamily domain 4 of ICAM-1 mediates cell surface dimerization. Proc. Natl. Acad. Sci. U. S. A. 2007, 104:15358-15363.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 15358-15363
    • Chen, X.1    Kim, T.D.2    Carman, C.V.3    Mi, L.Z.4    Song, G.5    Springer, T.A.6
  • 171
    • 33646431420 scopus 로고    scopus 로고
    • Shedding of lymphocyte function-associated antigen-1 (LFA-1) in a human inflammatory response
    • Evans B.J., McDowall A., Taylor P.C., Hogg N., Haskard D.O., Landis R.C. Shedding of lymphocyte function-associated antigen-1 (LFA-1) in a human inflammatory response. Blood 2006, 107:3593-3599.
    • (2006) Blood , vol.107 , pp. 3593-3599
    • Evans, B.J.1    McDowall, A.2    Taylor, P.C.3    Hogg, N.4    Haskard, D.O.5    Landis, R.C.6
  • 174
    • 0141817946 scopus 로고    scopus 로고
    • Identification of a negatively charged peptide motif within the catalytic domain of progelatinases that mediates binding to leukocyte beta 2 integrins
    • Stefanidakis M., Bjorklund M., Ihanus E., Gahmberg C.G., Koivunen E. Identification of a negatively charged peptide motif within the catalytic domain of progelatinases that mediates binding to leukocyte beta 2 integrins. J. Biol. Chem. 2003, 278:34674-34684.
    • (2003) J. Biol. Chem. , vol.278 , pp. 34674-34684
    • Stefanidakis, M.1    Bjorklund, M.2    Ihanus, E.3    Gahmberg, C.G.4    Koivunen, E.5
  • 175
    • 37349023183 scopus 로고    scopus 로고
    • Fluid shear-induced activation and cleavage of CD18 during pseudopod retraction by human neutrophils
    • Shin H.Y., Simon S.I., Schmid-Schonbein G.W. Fluid shear-induced activation and cleavage of CD18 during pseudopod retraction by human neutrophils. J. Cell. Physiol. 2008, 214:528-536.
    • (2008) J. Cell. Physiol. , vol.214 , pp. 528-536
    • Shin, H.Y.1    Simon, S.I.2    Schmid-Schonbein, G.W.3
  • 176
    • 79955960587 scopus 로고    scopus 로고
    • Cleavage of the CD11b extracellular domain by the leukocyte serprocidins is critical for neutrophil detachment during chemotaxis
    • Zen K., Guo Y.L., Li L.M., Bian Z., Zhang C.Y., Liu Y. Cleavage of the CD11b extracellular domain by the leukocyte serprocidins is critical for neutrophil detachment during chemotaxis. Blood 2011, 117:4885-4894.
    • (2011) Blood , vol.117 , pp. 4885-4894
    • Zen, K.1    Guo, Y.L.2    Li, L.M.3    Bian, Z.4    Zhang, C.Y.5    Liu, Y.6
  • 177
    • 84856910083 scopus 로고    scopus 로고
    • Metalloproteinase-mediated Shedding of Integrin beta2 Promotes Macrophage Efflux from Inflammatory Sites
    • Gomez I.G., Tang J., Wilson C.L., Yan W., Heinecke J.W., Harlan J.M., Raines E.W. Metalloproteinase-mediated Shedding of Integrin beta2 Promotes Macrophage Efflux from Inflammatory Sites. J. Biol. Chem. 2012, 287:4581-4589.
    • (2012) J. Biol. Chem. , vol.287 , pp. 4581-4589
    • Gomez, I.G.1    Tang, J.2    Wilson, C.L.3    Yan, W.4    Heinecke, J.W.5    Harlan, J.M.6    Raines, E.W.7
  • 179
    • 33947261720 scopus 로고    scopus 로고
    • Integrin alpha6 cleavage: a novel modification to modulate cell migration
    • Pawar S.C., Demetriou M.C., Nagle R.B., Bowden G.T., Cress A.E. Integrin alpha6 cleavage: a novel modification to modulate cell migration. Exp. Cell Res. 2007, 313:1080-1089.
    • (2007) Exp. Cell Res. , vol.313 , pp. 1080-1089
    • Pawar, S.C.1    Demetriou, M.C.2    Nagle, R.B.3    Bowden, G.T.4    Cress, A.E.5
  • 181
    • 77958136190 scopus 로고    scopus 로고
    • Shedding of large functionally active CD11/CD18 Integrin complexes from leukocyte membranes during synovial inflammation distinguishes three types of arthritis through differential epitope exposure
    • Gjelstrup L.C., Boesen T., Kragstrup T.W., Jorgensen A., Klein N.J., Thiel S., Deleuran B.W., Vorup-Jensen T. Shedding of large functionally active CD11/CD18 Integrin complexes from leukocyte membranes during synovial inflammation distinguishes three types of arthritis through differential epitope exposure. J. Immunol. 2010, 185:4154-4168.
    • (2010) J. Immunol. , vol.185 , pp. 4154-4168
    • Gjelstrup, L.C.1    Boesen, T.2    Kragstrup, T.W.3    Jorgensen, A.4    Klein, N.J.5    Thiel, S.6    Deleuran, B.W.7    Vorup-Jensen, T.8
  • 182
    • 80052174164 scopus 로고    scopus 로고
    • Activation of complement by therapeutic liposomes and other lipid excipient-based therapeutic products: prediction and prevention
    • Szebeni J., Muggia F., Gabizon A., Barenholz Y. Activation of complement by therapeutic liposomes and other lipid excipient-based therapeutic products: prediction and prevention. Adv. Drug Deliv. Rev. 2011, 63:1020-1030.
    • (2011) Adv. Drug Deliv. Rev. , vol.63 , pp. 1020-1030
    • Szebeni, J.1    Muggia, F.2    Gabizon, A.3    Barenholz, Y.4
  • 183
    • 81855198887 scopus 로고    scopus 로고
    • Factors controlling nanoparticle pharmacokinetics: an integrated analysis and perspective
    • Moghimi S.M., Hunter A.C., Andresen T.L. Factors controlling nanoparticle pharmacokinetics: an integrated analysis and perspective. Annu. Rev. Pharmacol. Toxicol. 2012, 52:481-503.
    • (2012) Annu. Rev. Pharmacol. Toxicol. , vol.52 , pp. 481-503
    • Moghimi, S.M.1    Hunter, A.C.2    Andresen, T.L.3
  • 185
    • 77951619720 scopus 로고    scopus 로고
    • FDA report: Ferumoxytol for intravenous iron therapy in adult patients with chronic kidney disease
    • Lu M., Cohen M.H., Rieves D., Pazdur R. FDA report: Ferumoxytol for intravenous iron therapy in adult patients with chronic kidney disease. Am. J. Hematol. 2010, 85:315-319.
    • (2010) Am. J. Hematol. , vol.85 , pp. 315-319
    • Lu, M.1    Cohen, M.H.2    Rieves, D.3    Pazdur, R.4
  • 186
    • 67651098896 scopus 로고    scopus 로고
    • Safety and tolerability of ultrasmall superparamagnetic iron oxide contrast agent: comprehensive analysis of a clinical development program
    • Bernd H., De Kerviler E., Gaillard S., Bonnemain B. Safety and tolerability of ultrasmall superparamagnetic iron oxide contrast agent: comprehensive analysis of a clinical development program. Invest. Radiol. 2009, 44:336-342.
    • (2009) Invest. Radiol. , vol.44 , pp. 336-342
    • Bernd, H.1    De Kerviler, E.2    Gaillard, S.3    Bonnemain, B.4
  • 187
    • 81255166750 scopus 로고    scopus 로고
    • Carbohydrate-based nanoparticles for potential applications in medicine
    • Marradi M., Garcia I., Penades S. Carbohydrate-based nanoparticles for potential applications in medicine. Prog. Mol. Biol. Transl. Sci. 2011, 104:141-173.
    • (2011) Prog. Mol. Biol. Transl. Sci. , vol.104 , pp. 141-173
    • Marradi, M.1    Garcia, I.2    Penades, S.3
  • 189
    • 1642269075 scopus 로고    scopus 로고
    • Synthesis of ultrasmall superparamagnetic iron oxides using reduced polysaccharides
    • Paul K.G., Frigo T.B., Groman J.Y., Groman E.V. Synthesis of ultrasmall superparamagnetic iron oxides using reduced polysaccharides. Bioconjug. Chem. 2004, 15:394-401.
    • (2004) Bioconjug. Chem. , vol.15 , pp. 394-401
    • Paul, K.G.1    Frigo, T.B.2    Groman, J.Y.3    Groman, E.V.4
  • 190
    • 84863258679 scopus 로고    scopus 로고
    • Different effect of hydrogelation on antifouling and circulation properties of dextran-iron oxide nanoparticles
    • Karmali P.P., Chao Y., Park J.H., Sailor M.J., Ruoslahti E., Esener S.C., Simberg D. Different effect of hydrogelation on antifouling and circulation properties of dextran-iron oxide nanoparticles. Mol. Pharm. 2012, 9:539-545.
    • (2012) Mol. Pharm. , vol.9 , pp. 539-545
    • Karmali, P.P.1    Chao, Y.2    Park, J.H.3    Sailor, M.J.4    Ruoslahti, E.5    Esener, S.C.6    Simberg, D.7
  • 191
    • 79960966703 scopus 로고    scopus 로고
    • Multiple aspects of the interaction of biomacromolecules with inorganic surfaces
    • Fenoglio I., Fubini B., Ghibaudi E.M., Turci F. Multiple aspects of the interaction of biomacromolecules with inorganic surfaces. Adv. Drug Deliv. Rev. 2011, 63:1186-1209.
    • (2011) Adv. Drug Deliv. Rev. , vol.63 , pp. 1186-1209
    • Fenoglio, I.1    Fubini, B.2    Ghibaudi, E.M.3    Turci, F.4
  • 192
    • 67349133162 scopus 로고    scopus 로고
    • Differential proteomics analysis of the surface heterogeneity of dextran iron oxide nanoparticles and the implications for their in vivo clearance
    • Simberg D., Park J.H., Karmali P.P., Zhang W.M., Merkulov S., McCrae K., Bhatia S.N., Sailor M., Ruoslahti E. Differential proteomics analysis of the surface heterogeneity of dextran iron oxide nanoparticles and the implications for their in vivo clearance. Biomaterials 2009, 30:3926-3933.
    • (2009) Biomaterials , vol.30 , pp. 3926-3933
    • Simberg, D.1    Park, J.H.2    Karmali, P.P.3    Zhang, W.M.4    Merkulov, S.5    McCrae, K.6    Bhatia, S.N.7    Sailor, M.8    Ruoslahti, E.9
  • 193
    • 0029162188 scopus 로고
    • The occurrence of natural antibodies to minimal component of bacterial cell wall (N-acetylglucosaminyl-N-acetylmuramyl dipeptide) in sera from healthy humans
    • Pinegin B.V., Kulakov A.V., Makarov E.A., Ledger P.W., Khaitov R.M. The occurrence of natural antibodies to minimal component of bacterial cell wall (N-acetylglucosaminyl-N-acetylmuramyl dipeptide) in sera from healthy humans. Immunol. Lett. 1995, 47:33-37.
    • (1995) Immunol. Lett. , vol.47 , pp. 33-37
    • Pinegin, B.V.1    Kulakov, A.V.2    Makarov, E.A.3    Ledger, P.W.4    Khaitov, R.M.5
  • 194
    • 84855363576 scopus 로고    scopus 로고
    • Long-term maintenance of polysaccharide-specific antibodies by IgM-secreting cells
    • Foote J.B., Mahmoud T.I., Vale A.M., Kearney J.F. Long-term maintenance of polysaccharide-specific antibodies by IgM-secreting cells. J. Immunol. 2012, 188:57-67.
    • (2012) J. Immunol. , vol.188 , pp. 57-67
    • Foote, J.B.1    Mahmoud, T.I.2    Vale, A.M.3    Kearney, J.F.4
  • 195
    • 79951898882 scopus 로고    scopus 로고
    • Interactions of nanoparticles with plasma proteins: implication on clearance and toxicity of drug delivery systems
    • Karmali P.P., Simberg D. Interactions of nanoparticles with plasma proteins: implication on clearance and toxicity of drug delivery systems. Expert Opin. Drug Deliv. 2011, 8:343-357.
    • (2011) Expert Opin. Drug Deliv. , vol.8 , pp. 343-357
    • Karmali, P.P.1    Simberg, D.2
  • 196
    • 0002982888 scopus 로고
    • There's Plenty of Room at the Bottom
    • Feynman R. There's Plenty of Room at the Bottom. Eng. Sci. 1960, 23(23):22-36.
    • (1960) Eng. Sci. , vol.23 , Issue.23 , pp. 22-36
    • Feynman, R.1
  • 197
    • 79957768993 scopus 로고    scopus 로고
    • Production methods for nanodrug particles using the bottom-up approach
    • Chan H.K., Kwok P.C. Production methods for nanodrug particles using the bottom-up approach. Adv. Drug Deliv. Rev. 2011, 63:406-416.
    • (2011) Adv. Drug Deliv. Rev. , vol.63 , pp. 406-416
    • Chan, H.K.1    Kwok, P.C.2
  • 198
    • 77949762340 scopus 로고    scopus 로고
    • Targeting of drugs and nanoparticles to tumors
    • Ruoslahti E., Bhatia S.N., Sailor M.J. Targeting of drugs and nanoparticles to tumors. J. Cell Biol. 2010, 188:759-768.
    • (2010) J. Cell Biol. , vol.188 , pp. 759-768
    • Ruoslahti, E.1    Bhatia, S.N.2    Sailor, M.J.3
  • 199
    • 77953661858 scopus 로고    scopus 로고
    • Fabrication of micropatterns of nanoarrays on a polymeric gel surface
    • Liu P., Sun J., Huang J., Peng R., Tang J., Ding J. Fabrication of micropatterns of nanoarrays on a polymeric gel surface. Nanoscale 2010, 2:122-127.
    • (2010) Nanoscale , vol.2 , pp. 122-127
    • Liu, P.1    Sun, J.2    Huang, J.3    Peng, R.4    Tang, J.5    Ding, J.6
  • 200
    • 0035312624 scopus 로고    scopus 로고
    • The familiar and the unexpected in structures of icosahedral viruses
    • Harrison S.C. The familiar and the unexpected in structures of icosahedral viruses. Curr. Opin. Struct. Biol. 2001, 11:195-199.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 195-199
    • Harrison, S.C.1
  • 202
    • 70350322305 scopus 로고    scopus 로고
    • Cryo-electron microscopy structure of an adenovirus-integrin complex indicates conformational changes in both penton base and integrin
    • Lindert S., Silvestry M., Mullen T.M., Nemerow G.R., Stewart P.L. Cryo-electron microscopy structure of an adenovirus-integrin complex indicates conformational changes in both penton base and integrin. J. Virol. 2009, 83:11491-11501.
    • (2009) J. Virol. , vol.83 , pp. 11491-11501
    • Lindert, S.1    Silvestry, M.2    Mullen, T.M.3    Nemerow, G.R.4    Stewart, P.L.5
  • 203
    • 2442650314 scopus 로고    scopus 로고
    • Atomic force microscopy of cell growth and division in Staphylococcus aureus
    • Touhami A., Jericho M.H., Beveridge T.J. Atomic force microscopy of cell growth and division in Staphylococcus aureus. J. Bacteriol. 2004, 186:3286-3295.
    • (2004) J. Bacteriol. , vol.186 , pp. 3286-3295
    • Touhami, A.1    Jericho, M.H.2    Beveridge, T.J.3
  • 204
    • 73349083717 scopus 로고    scopus 로고
    • Toward the development of "nano-QSARs": advances and challenges
    • Puzyn T., Leszczynska D., Leszczynski J. Toward the development of "nano-QSARs": advances and challenges. Small 2009, 5:2494-2509.
    • (2009) Small , vol.5 , pp. 2494-2509
    • Puzyn, T.1    Leszczynska, D.2    Leszczynski, J.3
  • 207
    • 78650606928 scopus 로고    scopus 로고
    • Nanoparticle-induced unfolding of fibrinogen promotes Mac-1 receptor activation and inflammation
    • Deng Z.J., Liang M., Monteiro M., Toth I., Minchin R.F. Nanoparticle-induced unfolding of fibrinogen promotes Mac-1 receptor activation and inflammation. Nat. Nanotechnol. 2011, 6:39-44.
    • (2011) Nat. Nanotechnol. , vol.6 , pp. 39-44
    • Deng, Z.J.1    Liang, M.2    Monteiro, M.3    Toth, I.4    Minchin, R.F.5
  • 208
    • 84862586179 scopus 로고    scopus 로고
    • Physico-chemical characteristics of protein-NP bioconjugates: The role of particle curvature and solution conditions on human serum albumin conformation and fibrillogenesis inhibition
    • Goy-Lopez S., Juarez J., Alatorre-Meda M., Casals E., Puntes V.F., Taboada P., Mosquera V. Physico-chemical characteristics of protein-NP bioconjugates: The role of particle curvature and solution conditions on human serum albumin conformation and fibrillogenesis inhibition. Langmuir 2012, 28:9113-9126.
    • (2012) Langmuir , vol.28 , pp. 9113-9126
    • Goy-Lopez, S.1    Juarez, J.2    Alatorre-Meda, M.3    Casals, E.4    Puntes, V.F.5    Taboada, P.6    Mosquera, V.7
  • 209
    • 78650341420 scopus 로고    scopus 로고
    • The 1.5 A crystal structure of human receptor for advanced glycation endproducts (RAGE) ectodomains reveals unique features determining ligand binding
    • Park H., Adsit F.G., Boyington J.C. The 1.5 A crystal structure of human receptor for advanced glycation endproducts (RAGE) ectodomains reveals unique features determining ligand binding. J. Biol. Chem. 2011, 285:40762-40770.
    • (2011) J. Biol. Chem. , vol.285 , pp. 40762-40770
    • Park, H.1    Adsit, F.G.2    Boyington, J.C.3
  • 210
    • 10644245175 scopus 로고    scopus 로고
    • The recognition of adsorbed and denatured proteins of different topographies by beta2 integrins and effects on leukocyte adhesion and activation
    • Brevig T., Holst B., Ademovic Z., Rozlosnik N., Rohrmann J.H., Larsen N.B., Hansen O.C., Kingshott P. The recognition of adsorbed and denatured proteins of different topographies by beta2 integrins and effects on leukocyte adhesion and activation. Biomaterials 2005, 26:3039-3053.
    • (2005) Biomaterials , vol.26 , pp. 3039-3053
    • Brevig, T.1    Holst, B.2    Ademovic, Z.3    Rozlosnik, N.4    Rohrmann, J.H.5    Larsen, N.B.6    Hansen, O.C.7    Kingshott, P.8
  • 211
    • 0029918641 scopus 로고    scopus 로고
    • Molecular determinants of acute inflammatory responses to biomaterials
    • Tang L., Ugarova T.P., Plow E.F., Eaton J.W. Molecular determinants of acute inflammatory responses to biomaterials. J. Clin. Invest. 1996, 97:1329-1334.
    • (1996) J. Clin. Invest. , vol.97 , pp. 1329-1334
    • Tang, L.1    Ugarova, T.P.2    Plow, E.F.3    Eaton, J.W.4
  • 212
    • 0035883104 scopus 로고    scopus 로고
    • Molecular basis of biomaterial-mediated foreign body reactions
    • Hu W.J., Eaton J.W., Ugarova T.P., Tang L. Molecular basis of biomaterial-mediated foreign body reactions. Blood 2001, 98:1231-1238.
    • (2001) Blood , vol.98 , pp. 1231-1238
    • Hu, W.J.1    Eaton, J.W.2    Ugarova, T.P.3    Tang, L.4
  • 213
    • 10644241824 scopus 로고    scopus 로고
    • The attraction of Mac-1+ phagocytes during acute inflammation by methyl-coated self-assembled monolayers
    • Barbosa J.N., Madureira P., Barbosa M.A., Aguas A.P. The attraction of Mac-1+ phagocytes during acute inflammation by methyl-coated self-assembled monolayers. Biomaterials 2005, 26:3021-3027.
    • (2005) Biomaterials , vol.26 , pp. 3021-3027
    • Barbosa, J.N.1    Madureira, P.2    Barbosa, M.A.3    Aguas, A.P.4
  • 216
    • 78650831189 scopus 로고    scopus 로고
    • Leukocyte transepithelial migration in lung induced by DMSA functionalized magnetic nanoparticles
    • Azevedo R.B., Valois C.R., Chaves S.B., Silva J.R., Garcia M.P. Leukocyte transepithelial migration in lung induced by DMSA functionalized magnetic nanoparticles. Cell Adh. Migr. 2011, 5:29-33.
    • (2011) Cell Adh. Migr. , vol.5 , pp. 29-33
    • Azevedo, R.B.1    Valois, C.R.2    Chaves, S.B.3    Silva, J.R.4    Garcia, M.P.5
  • 217
    • 55849089267 scopus 로고    scopus 로고
    • Many cytokines are very useful therapeutic targets in disease
    • Feldmann M. Many cytokines are very useful therapeutic targets in disease. J. Clin. Invest. 2008, 118:3533-3536.
    • (2008) J. Clin. Invest. , vol.118 , pp. 3533-3536
    • Feldmann, M.1
  • 218
  • 220
    • 79952002733 scopus 로고    scopus 로고
    • Tunable physiologic interactions of adhesion molecules for inflamed cell-selective drug delivery
    • Kang S., Park T., Chen X., Dickens G., Lee B., Lu K., Rakhilin N., Daniel S., Jin M.M. Tunable physiologic interactions of adhesion molecules for inflamed cell-selective drug delivery. Biomaterials 2011, 32:3487-3498.
    • (2011) Biomaterials , vol.32 , pp. 3487-3498
    • Kang, S.1    Park, T.2    Chen, X.3    Dickens, G.4    Lee, B.5    Lu, K.6    Rakhilin, N.7    Daniel, S.8    Jin, M.M.9
  • 221
    • 77955768926 scopus 로고    scopus 로고
    • Self-assembled nanoplatform for targeted delivery of chemotherapy agents via affinity-regulated molecular interactions
    • Park S., Kang S., Veach A.J., Vedvyas Y., Zarnegar R., Kim J.Y., Jin M.M. Self-assembled nanoplatform for targeted delivery of chemotherapy agents via affinity-regulated molecular interactions. Biomaterials 2010, 31:7766-7775.
    • (2010) Biomaterials , vol.31 , pp. 7766-7775
    • Park, S.1    Kang, S.2    Veach, A.J.3    Vedvyas, Y.4    Zarnegar, R.5    Kim, J.Y.6    Jin, M.M.7
  • 223
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E., Henrick K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 2007, 372:774-797.
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 224
    • 3242879771 scopus 로고    scopus 로고
    • Computational alanine scanning of protein-protein interfaces
    • Kortemme T., Kim D.E., Baker D. Computational alanine scanning of protein-protein interfaces. Sci. STKE 2004, 2004:l2.
    • (2004) Sci. STKE , vol.2004
    • Kortemme, T.1    Kim, D.E.2    Baker, D.3
  • 225
    • 0037195144 scopus 로고    scopus 로고
    • A simple physical model for binding energy hot spots in protein-protein complexes
    • Kortemme T., Baker D. A simple physical model for binding energy hot spots in protein-protein complexes. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:14116-14121.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 14116-14121
    • Kortemme, T.1    Baker, D.2
  • 226
    • 0018859931 scopus 로고
    • Kinetics of the hormone-receptor interaction. Competition experiments with slowly equilibrating ligands
    • Aranyi P. Kinetics of the hormone-receptor interaction. Competition experiments with slowly equilibrating ligands. Biochim. Biophys. Acta 1980, 628:220-227.
    • (1980) Biochim. Biophys. Acta , vol.628 , pp. 220-227
    • Aranyi, P.1
  • 227
    • 3242801378 scopus 로고    scopus 로고
    • Characterization of plasminogen as an adhesive ligand for integrins alphaMbeta2 (Mac-1) and alpha5beta1 (VLA-5)
    • Lishko V.K., Novokhatny V.V., Yakubenko V.P., Skomorovska-Prokvolit H.V., Ugarova T.P. Characterization of plasminogen as an adhesive ligand for integrins alphaMbeta2 (Mac-1) and alpha5beta1 (VLA-5). Blood 2004, 104:719-726.
    • (2004) Blood , vol.104 , pp. 719-726
    • Lishko, V.K.1    Novokhatny, V.V.2    Yakubenko, V.P.3    Skomorovska-Prokvolit, H.V.4    Ugarova, T.P.5
  • 228
    • 36549000259 scopus 로고    scopus 로고
    • Identification of critical residues for plasminogen binding by the alphaX I-domain of the beta2 integrin, alphaXbeta2
    • Gang J., Choi J., Lee J.H., Nham S.U. Identification of critical residues for plasminogen binding by the alphaX I-domain of the beta2 integrin, alphaXbeta2. Mol. Cells 2007, 24:240-246.
    • (2007) Mol. Cells , vol.24 , pp. 240-246
    • Gang, J.1    Choi, J.2    Lee, J.H.3    Nham, S.U.4
  • 230
    • 35248867073 scopus 로고    scopus 로고
    • Characterization of two novel LPS-binding sites in leukocyte integrin betaA domain
    • Wong K.F., Luk J.M., Cheng R.H., Klickstein L.B., Fan S.T. Characterization of two novel LPS-binding sites in leukocyte integrin betaA domain. FASEB J. 2007, 21:3231-3239.
    • (2007) FASEB J. , vol.21 , pp. 3231-3239
    • Wong, K.F.1    Luk, J.M.2    Cheng, R.H.3    Klickstein, L.B.4    Fan, S.T.5
  • 232
    • 0036242232 scopus 로고    scopus 로고
    • Role of the lectin domain of Mac-1/CR3 (CD11b/CD18) in regulating intercellular adhesion
    • Ross G.D. Role of the lectin domain of Mac-1/CR3 (CD11b/CD18) in regulating intercellular adhesion. Immunol. Res. 2002, 25:219-227.
    • (2002) Immunol. Res. , vol.25 , pp. 219-227
    • Ross, G.D.1
  • 235
    • 0029034439 scopus 로고
    • The leukocyte integrin Mac-1 (CD11b/CD18) contributes to binding of human granulocytes to collagen
    • Walzog B., Schuppan D., Heimpel C., Hafezi-Moghadam A., Gaehtgens P., Ley K. The leukocyte integrin Mac-1 (CD11b/CD18) contributes to binding of human granulocytes to collagen. Exp. Cell Res. 1995, 218:28-38.
    • (1995) Exp. Cell Res. , vol.218 , pp. 28-38
    • Walzog, B.1    Schuppan, D.2    Heimpel, C.3    Hafezi-Moghadam, A.4    Gaehtgens, P.5    Ley, K.6
  • 236
    • 0037289806 scopus 로고    scopus 로고
    • The interplay between integrins alphaMbeta2 and alpha5beta1 during cell migration to fibronectin
    • Lishko V.K., Yakubenko V.P., Ugarova T.P. The interplay between integrins alphaMbeta2 and alpha5beta1 during cell migration to fibronectin. Exp. Cell Res. 2003, 283:116-126.
    • (2003) Exp. Cell Res. , vol.283 , pp. 116-126
    • Lishko, V.K.1    Yakubenko, V.P.2    Ugarova, T.P.3
  • 237
    • 0036718520 scopus 로고    scopus 로고
    • The junctional adhesion molecule 3 (JAM-3) on human platelets is a counterreceptor for the leukocyte integrin Mac-1
    • Santoso S., Sachs U.J., Kroll H., Linder M., Ruf A., Preissner K.T., Chavakis T. The junctional adhesion molecule 3 (JAM-3) on human platelets is a counterreceptor for the leukocyte integrin Mac-1. J. Exp. Med. 2002, 196:679-691.
    • (2002) J. Exp. Med. , vol.196 , pp. 679-691
    • Santoso, S.1    Sachs, U.J.2    Kroll, H.3    Linder, M.4    Ruf, A.5    Preissner, K.T.6    Chavakis, T.7
  • 239
  • 241
    • 33846261108 scopus 로고    scopus 로고
    • Red-cell ICAM-4 is a ligand for the monocyte/macrophage integrin CD11c/CD18: characterization of the binding sites on ICAM-4
    • Ihanus E., Uotila L.M., Toivanen A., Varis M., Gahmberg C.G. Red-cell ICAM-4 is a ligand for the monocyte/macrophage integrin CD11c/CD18: characterization of the binding sites on ICAM-4. Blood 2007, 109:802-810.
    • (2007) Blood , vol.109 , pp. 802-810
    • Ihanus, E.1    Uotila, L.M.2    Toivanen, A.3    Varis, M.4    Gahmberg, C.G.5
  • 243
    • 0346097974 scopus 로고    scopus 로고
    • Phorbol esters alter alpha4 and alphad integrin usage during eosinophil adhesion to VCAM-1
    • Kikuchi M., Tachimoto H., Nutku E., Hudson S.A., Bochner B.S. Phorbol esters alter alpha4 and alphad integrin usage during eosinophil adhesion to VCAM-1. Cell Commun. Adhes. 2003, 10:119-128.
    • (2003) Cell Commun. Adhes. , vol.10 , pp. 119-128
    • Kikuchi, M.1    Tachimoto, H.2    Nutku, E.3    Hudson, S.A.4    Bochner, B.S.5
  • 245
    • 0036008013 scopus 로고    scopus 로고
    • JAM-1 is a ligand of the beta(2) integrin LFA-1 involved in transendothelial migration of leukocytes
    • Ostermann G., Weber K.S., Zernecke A., Schroder A., Weber C. JAM-1 is a ligand of the beta(2) integrin LFA-1 involved in transendothelial migration of leukocytes. Nat. Immunol. 2002, 3:151-158.
    • (2002) Nat. Immunol. , vol.3 , pp. 151-158
    • Ostermann, G.1    Weber, K.S.2    Zernecke, A.3    Schroder, A.4    Weber, C.5
  • 247
    • 0027982055 scopus 로고
    • A functional integrin ligand on the surface of platelets: intercellular adhesion molecule-2
    • Diacovo T.G., deFougerolles A.R., Bainton D.F., Springer T.A. A functional integrin ligand on the surface of platelets: intercellular adhesion molecule-2. J. Clin. Invest. 1994, 94:1243-1251.
    • (1994) J. Clin. Invest. , vol.94 , pp. 1243-1251
    • Diacovo, T.G.1    deFougerolles, A.R.2    Bainton, D.F.3    Springer, T.A.4
  • 248
    • 33750962733 scopus 로고    scopus 로고
    • Levels of soluble vascular cell adhesion molecule-1 and soluble intercellular adhesion molecule-2 in plasma of patients with hemorrhagic fever with renal syndrome, and significance of the changes in level
    • Qi B.T., Wang P., Li J., Ren H.X., Xie M. Levels of soluble vascular cell adhesion molecule-1 and soluble intercellular adhesion molecule-2 in plasma of patients with hemorrhagic fever with renal syndrome, and significance of the changes in level. Viral Immunol. 2006, 19:565-569.
    • (2006) Viral Immunol. , vol.19 , pp. 565-569
    • Qi, B.T.1    Wang, P.2    Li, J.3    Ren, H.X.4    Xie, M.5
  • 249
    • 0026604790 scopus 로고
    • Intercellular adhesion molecule 3, a third adhesion counter-receptor for lymphocyte function-associated molecule 1 on resting lymphocytes
    • de Fougerolles A.R., Springer T.A. Intercellular adhesion molecule 3, a third adhesion counter-receptor for lymphocyte function-associated molecule 1 on resting lymphocytes. J. Exp. Med. 1992, 175:185-190.
    • (1992) J. Exp. Med. , vol.175 , pp. 185-190
    • de Fougerolles, A.R.1    Springer, T.A.2
  • 250
    • 0028922841 scopus 로고
    • Existence of a soluble form of CD50 (intercellular adhesion molecule-3) produced upon human lymphocyte activation. Present in normal human serum and levels are increased in the serum of systemic lupus erythematosus patients
    • Pino-Otin M.R., Vinas O., de la Fuente M.A., Juan M., Font J., Torradeflot M., Pallares L., Lozano F., Alberola-Ila J., Martorell J., et al. Existence of a soluble form of CD50 (intercellular adhesion molecule-3) produced upon human lymphocyte activation. Present in normal human serum and levels are increased in the serum of systemic lupus erythematosus patients. J. Immunol. 1995, 154:3015-3024.
    • (1995) J. Immunol. , vol.154 , pp. 3015-3024
    • Pino-Otin, M.R.1    Vinas, O.2    de la Fuente, M.A.3    Juan, M.4    Font, J.5    Torradeflot, M.6    Pallares, L.7    Lozano, F.8    Alberola-Ila, J.9    Martorell, J.10
  • 252
    • 0028874029 scopus 로고
    • Expression of VCAM-1 (CD106) by a subset of TCR gamma delta-bearing lymphocyte clones. Involvement of a metalloprotease in the specific hydrolytic release of the soluble isoform
    • Leca G., Mansur S.E., Bensussan A. Expression of VCAM-1 (CD106) by a subset of TCR gamma delta-bearing lymphocyte clones. Involvement of a metalloprotease in the specific hydrolytic release of the soluble isoform. J. Immunol. 1995, 154:1069-1077.
    • (1995) J. Immunol. , vol.154 , pp. 1069-1077
    • Leca, G.1    Mansur, S.E.2    Bensussan, A.3
  • 253
    • 66449098241 scopus 로고    scopus 로고
    • The detection of sLFA-3 in plasma of patients with hemorrhagic fever with renal syndrome
    • Xie M., Chen P., He L.J., Qi B.T., Wang P., Wang X.F., Ren H.X. The detection of sLFA-3 in plasma of patients with hemorrhagic fever with renal syndrome. Clin. Exp. Med. 2009, 9:67-71.
    • (2009) Clin. Exp. Med. , vol.9 , pp. 67-71
    • Xie, M.1    Chen, P.2    He, L.J.3    Qi, B.T.4    Wang, P.5    Wang, X.F.6    Ren, H.X.7
  • 254
    • 0024601050 scopus 로고
    • Endothelial leukocyte adhesion molecule 1: an inducible receptor for neutrophils related to complement regulatory proteins and lectins
    • Bevilacqua M.P., Stengelin S., Gimbrone M.A., Seed B. Endothelial leukocyte adhesion molecule 1: an inducible receptor for neutrophils related to complement regulatory proteins and lectins. Science 1989, 243:1160-1165.
    • (1989) Science , vol.243 , pp. 1160-1165
    • Bevilacqua, M.P.1    Stengelin, S.2    Gimbrone, M.A.3    Seed, B.4
  • 255
    • 0024391397 scopus 로고
    • Human homologue of mouse lymph node homing receptor: evolutionary conservation at tandem cell interaction domains
    • Siegelman M.H., Weissman I.L. Human homologue of mouse lymph node homing receptor: evolutionary conservation at tandem cell interaction domains. Proc. Natl. Acad. Sci. U. S. A. 1989, 86:5562-5566.
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 5562-5566
    • Siegelman, M.H.1    Weissman, I.L.2
  • 256
    • 0024558097 scopus 로고
    • Cloning of GMP-140, a granule membrane protein of platelets and endothelium: sequence similarity to proteins involved in cell adhesion and inflammation
    • Johnston G.I., Cook R.G., McEver R.P. Cloning of GMP-140, a granule membrane protein of platelets and endothelium: sequence similarity to proteins involved in cell adhesion and inflammation. Cell 1989, 56:1033-1044.
    • (1989) Cell , vol.56 , pp. 1033-1044
    • Johnston, G.I.1    Cook, R.G.2    McEver, R.P.3


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