메뉴 건너뛰기




Volumn 113, Issue 11, 2004, Pages 1596-1606

Leukocyte engagement of fibrin(ogen) via the integrin receptor αMβ2/Mac-1 is critical for host inflammatory response in vivo

Author keywords

[No Author keywords available]

Indexed keywords

CD11B ANTIGEN; FIBRIN; FIBRINOGEN;

EID: 85047691114     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI20741     Document Type: Article
Times cited : (375)

References (52)
  • 1
    • 0027982876 scopus 로고
    • Traffic signals for lymphocyte recirculation and leukocyte emigration: The multi-step paradigm
    • Springer, T.A. 1994. Traffic signals for lymphocyte recirculation and leukocyte emigration: the multi-step paradigm. Cell. 76:301-314.
    • (1994) Cell , vol.76 , pp. 301-314
    • Springer, T.A.1
  • 2
    • 0002790968 scopus 로고
    • Leukocyte adhesion deficiency and other disorders of leukocyte adherence and motility
    • W.S. Sly, C.R. Scriver, A.L. Beaudet, and D. Valle, editors. McGraw-Hill. New York, New York, USA
    • Anderson, D.C., Kishimoto, T.K., and Smith, C.W. 1995. Leukocyte adhesion deficiency and other disorders of leukocyte adherence and motility. In The metabolic and molecular bases of inherited disease. W.S. Sly, C.R. Scriver, A.L. Beaudet, and D. Valle, editors. McGraw-Hill. New York, New York, USA. 3955-3994.
    • (1995) The Metabolic and Molecular Bases of Inherited Disease , pp. 3955-3994
    • Anderson, D.C.1    Kishimoto, T.K.2    Smith, C.W.3
  • 3
    • 0025195764 scopus 로고
    • Structure and function of leukocyte integrins
    • Larson, R.S., and Springer, T.A. 1990. Structure and function of leukocyte integrins. Immunol. Rev. 114:181-217.
    • (1990) Immunol. Rev. , vol.114 , pp. 181-217
    • Larson, R.S.1    Springer, T.A.2
  • 4
    • 0029198299 scopus 로고
    • A novel leukointegrin, αdβ2, binds preferentially to ICAM-3
    • Van der Vieren, M., et al. 1995. A novel leukointegrin, αdβ2, binds preferentially to ICAM-3. Immunity. 3:683-690.
    • (1995) Immunity , vol.3 , pp. 683-690
    • Van Der Vieren, M.1
  • 5
    • 0030483324 scopus 로고    scopus 로고
    • A novel role for the β2 integrin CD11b/CD18 in neutrophil apoptosis: A homeostatic mechanism in inflammation
    • Coxon, A., et al. 1996. A novel role for the β2 integrin CD11b/CD18 in neutrophil apoptosis: a homeostatic mechanism in inflammation. Immunity. 5:653-666.
    • (1996) Immunity , vol.5 , pp. 653-666
    • Coxon, A.1
  • 6
    • 0030731918 scopus 로고    scopus 로고
    • Neutrophil emigration in the skin, lungs, and peritoneum: Different requirements for CD11/CD18 revealed by CD18-deficient mice
    • Mizgerd, J.P., et al. 1997. Neutrophil emigration in the skin, lungs, and peritoneum: different requirements for CD11/CD18 revealed by CD18-deficient mice J. Exp. Med. 186:1357-1364.
    • (1997) J. Exp. Med. , vol.186 , pp. 1357-1364
    • Mizgerd, J.P.1
  • 7
    • 0031000635 scopus 로고    scopus 로고
    • LFA-1 is sufficient in mediating neutrophil emigration in Mac-1-deficient mice
    • Lu, H., et al. 1997. LFA-1 is sufficient in mediating neutrophil emigration in Mac-1-deficient mice. J. Clin. Invest. 99:1340-1350.
    • (1997) J. Clin. Invest. , vol.99 , pp. 1340-1350
    • Lu, H.1
  • 8
    • 0032729875 scopus 로고    scopus 로고
    • Relative contribution of LFA-1 and Mac-1 to neutrophil adhesion and migration
    • Ding, Z.M., et al. 1999. Relative contribution of LFA-1 and Mac-1 to neutrophil adhesion and migration. J. Immunol. 163:5029-5038.
    • (1999) J. Immunol. , vol.163 , pp. 5029-5038
    • Ding, Z.M.1
  • 9
    • 0031280365 scopus 로고    scopus 로고
    • β2 integrins (CD11/CD18) promote apoptosis of human neutrophils
    • Walzog, B., Jeblonski, F., Zakrzewicz, A., and Gaehtgens, P. 1997. β2 integrins (CD11/CD18) promote apoptosis of human neutrophils. FASEB J. 11:1177-1186.
    • (1997) FASEB J. , vol.11 , pp. 1177-1186
    • Walzog, B.1    Jeblonski, F.2    Zakrzewicz, A.3    Gaehtgens, P.4
  • 10
    • 0036090346 scopus 로고    scopus 로고
    • Control of leukocyte rolling velocity in TNF-alpha-induced inflammation by LFA-1 and Mac-1
    • Dunne, J.L., Ballantyne, C.M., Beaudet, A.L., and Ley, K. 2002. Control of leukocyte rolling velocity in TNF-alpha-induced inflammation by LFA-1 and Mac-1. Blood. 99:336-341.
    • (2002) Blood , vol.99 , pp. 336-341
    • Dunne, J.L.1    Ballantyne, C.M.2    Beaudet, A.L.3    Ley, K.4
  • 11
    • 0035898301 scopus 로고    scopus 로고
    • The use of lymphocyte function-associated antigen (LFA)-1-deficient mice to determine the role of LFA-1, Mac-1, and α4 integrin in the inflammatory response of neutrophils
    • Henderson, R.B., et al. 2001. The use of lymphocyte function-associated antigen (LFA)-1-deficient mice to determine the role of LFA-1, Mac-1, and α4 integrin in the inflammatory response of neutrophils. J. Exp. Med. 194:219-226.
    • (2001) J. Exp. Med. , vol.194 , pp. 219-226
    • Henderson, R.B.1
  • 13
    • 0035927074 scopus 로고    scopus 로고
    • Integrin αMβ2-mediated cell migration to fibrinogen and its recognition peptides
    • Forsyth, C.B., Solovjov, D.A., Ugarova, T.P., and Plow, E.F. 2001. Integrin αMβ2-mediated cell migration to fibrinogen and its recognition peptides. J. Exp. Med. 193:1123-1133.
    • (2001) J. Exp. Med. , vol.193 , pp. 1123-1133
    • Forsyth, C.B.1    Solovjov, D.A.2    Ugarova, T.P.3    Plow, E.F.4
  • 14
    • 0027318675 scopus 로고
    • Fibrinogen mediates leukocyte adhesion to vascular endothelium through an ICAM-1-dependent pathway
    • Languino, L.R., et al. 1993. Fibrinogen mediates leukocyte adhesion to vascular endothelium through an ICAM-1-dependent pathway. Cell. 73:1423-1434.
    • (1993) Cell , vol.73 , pp. 1423-1434
    • Languino, L.R.1
  • 15
    • 0035834822 scopus 로고    scopus 로고
    • Leukocyte integrin Mac-1 recruits toll/interleukin-1 receptor superfamily signaling intermediates to modulate NF-κB activity
    • Shi, C., Zhang, X., Chen, Z., Robinson, M.K., and Simon, D.I. 2001. Leukocyte integrin Mac-1 recruits toll/interleukin-1 receptor superfamily signaling intermediates to modulate NF-κB activity. Circ. Res. 89:859-865.
    • (2001) Circ. Res. , vol.89 , pp. 859-865
    • Shi, C.1    Zhang, X.2    Chen, Z.3    Robinson, M.K.4    Simon, D.I.5
  • 16
    • 0035253366 scopus 로고    scopus 로고
    • Fibrinogen promotes neutrophil activation and delays apoptosis
    • Rubel, C., et al. 2001. Fibrinogen promotes neutrophil activation and delays apoptosis. J. Immunol. 166:2002-2010.
    • (2001) J. Immunol. , vol.166 , pp. 2002-2010
    • Rubel, C.1
  • 17
    • 0036533481 scopus 로고    scopus 로고
    • Soluble fibrinogen modulates neutrophil functionality through the activation of an extracellular signal-regulated kinase-dependent pathway
    • Rubel, C., et al. 2002. Soluble fibrinogen modulates neutrophil functionality through the activation of an extracellular signal-regulated kinase-dependent pathway. J. Immunol. 168:3527-3535.
    • (2002) J. Immunol. , vol.168 , pp. 3527-3535
    • Rubel, C.1
  • 18
    • 0035451118 scopus 로고    scopus 로고
    • Fibrinogen stimulates macrophage chemokine secretion through toll-like receptor 4
    • Smiley, S.T., King, J.A., and Hancock, W.W. 2001. Fibrinogen stimulates macrophage chemokine secretion through toll-like receptor 4. J. Immunol. 167:2887-2894.
    • (2001) J. Immunol. , vol.167 , pp. 2887-2894
    • Smiley, S.T.1    King, J.A.2    Hancock, W.W.3
  • 19
    • 0027052126 scopus 로고
    • The role of protected extracellular compartments in interactions between leukocytes, and platelets, and fibrin/fibrinogen matrices
    • Loike, J.D., et al. 1992. The role of protected extracellular compartments in interactions between leukocytes, and platelets, and fibrin/fibrinogen matrices. Ann. N. Y. Acad. Sci. 667:163-172.
    • (1992) Ann. N. Y. Acad. Sci. , vol.667 , pp. 163-172
    • Loike, J.D.1
  • 20
    • 0037195265 scopus 로고    scopus 로고
    • Regulated unmasking of the cryptic binding site for integrin αMβ2 in the γ C-domain of fibrinogen
    • Lishko, V.K., Kudryk, B., Yakubenko, V.P., Yee, V.C., and Ugarova, T.P. 2002. Regulated unmasking of the cryptic binding site for integrin αMβ2 in the γ C-domain of fibrinogen. Biochemistry. 41:12942-12951.
    • (2002) Biochemistry , vol.41 , pp. 12942-12951
    • Lishko, V.K.1    Kudryk, B.2    Yakubenko, V.P.3    Yee, V.C.4    Ugarova, T.P.5
  • 21
    • 0032575509 scopus 로고    scopus 로고
    • Identification of a novel recognition sequence for integrin αMβ2 within the γ-chain of fibrinogen
    • Ugarova, T.P., et al. 1998. Identification of a novel recognition sequence for integrin αMβ2 within the γ-chain of fibrinogen. J. Biol. Chem. 273:22519-22527.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22519-22527
    • Ugarova, T.P.1
  • 22
    • 0042573729 scopus 로고    scopus 로고
    • Sequence γ 377-395(P2), but not γ 190-202(P1), is the binding site for the αM I-domain of integrin αMβ2 in the γ C-domain of fibrinogen
    • Ugarova, T.P., et al. 2003. Sequence γ 377-395(P2), but not γ 190-202(P1), is the binding site for the αM I-domain of integrin αMβ2 in the γ C-domain of fibrinogen. Biochemistry. 42:9365-9373.
    • (2003) Biochemistry , vol.42 , pp. 9365-9373
    • Ugarova, T.P.1
  • 23
    • 0029906976 scopus 로고    scopus 로고
    • Impaired platelet aggregation and sustained bleeding in mice lacking the fibrinogen motif bound by integrin αIIbβ3
    • Holmback, K., Danton, M.J., Suh, T.T., Daugherty, C.C., and Degen, J.L. 1996. Impaired platelet aggregation and sustained bleeding in mice lacking the fibrinogen motif bound by integrin αIIbβ3. EMBO J. 15:5760-5771.
    • (1996) EMBO J. , vol.15 , pp. 5760-5771
    • Holmback, K.1    Danton, M.J.2    Suh, T.T.3    Daugherty, C.C.4    Degen, J.L.5
  • 24
    • 0023150598 scopus 로고
    • HPRT-deficient (Lesch-Nyhan) mouse embryos derived from germline colonization by cultured cells
    • Hooper, M., Hardy, K., Handyside, A., Hunter, S., and Monk, M. 1987. HPRT-deficient (Lesch-Nyhan) mouse embryos derived from germline colonization by cultured cells: Nature. 326:292-295.
    • (1987) Nature , vol.326 , pp. 292-295
    • Hooper, M.1    Hardy, K.2    Handyside, A.3    Hunter, S.4    Monk, M.5
  • 25
    • 0029147959 scopus 로고
    • Resolution of spontaneous bleeding events but failure of pregnancy in fibrinogen-deficient mice
    • Suh, T.T., et al. 1995. Resolution of spontaneous bleeding events but failure of pregnancy in fibrinogen-deficient mice. Genes Dev. 9:2020-2033.
    • (1995) Genes Dev. , vol.9 , pp. 2020-2033
    • Suh, T.T.1
  • 26
    • 0028052961 scopus 로고
    • Binding of recombinant fibrinogen mutants to platelets
    • Farrell, D.H., and Thiagarajan, P. 1994. Binding of recombinant fibrinogen mutants to platelets. J. Biol. Chem. 269:226-231.
    • (1994) J. Biol. Chem. , vol.269 , pp. 226-231
    • Farrell, D.H.1    Thiagarajan, P.2
  • 27
    • 1542373667 scopus 로고    scopus 로고
    • Antibody blockade or mutation of the fibrinogen γ chain C-terminus are more effective in inhibiting murine arterial thrombus formation than complete absence of fibrinogen
    • Jirousková, M., Chereshnev, I., Väänänen, H., Degen, J.L., and Coller, B.S. 2004. Antibody blockade or mutation of the fibrinogen γ chain C-terminus are more effective in inhibiting murine arterial thrombus formation than complete absence of fibrinogen. Blood. 103:1995-2002.
    • (2004) Blood , vol.103 , pp. 1995-2002
    • Jirousková, M.1    Chereshnev, I.2    Väänänen, H.3    Degen, J.L.4    Coller, B.S.5
  • 28
    • 0029905283 scopus 로고    scopus 로고
    • Overlapping, but not identical, sites are involved in the recognition of C3bi, neutrophil inhibitory factor, and adhesive ligands by the αMβ2 integrin
    • Zhang, L., and Plow, E.F. 1996. Overlapping, but not identical, sites are involved in the recognition of C3bi, neutrophil inhibitory factor, and adhesive ligands by the αMβ2 integrin. J. Biol. Chem. 271:18211-18216.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18211-18216
    • Zhang, L.1    Plow, E.F.2
  • 29
    • 0018646905 scopus 로고
    • Pretreatment of plastic Petri dishes with fetal calf serum. A simple method for macrophage isolation
    • Kumagai, K., Itoh, K., Hinuma, S., and Tada, M. 1979. Pretreatment of plastic Petri dishes with fetal calf serum. A simple method for macrophage isolation. J. Immunol. Methods. 29:17-25.
    • (1979) J. Immunol. Methods , vol.29 , pp. 17-25
    • Kumagai, K.1    Itoh, K.2    Hinuma, S.3    Tada, M.4
  • 31
  • 32
    • 0005482819 scopus 로고
    • Complement receptor type three (CD11b/CD18) of human polymorphonuclear leukocytes recognizes fibrinogen
    • Wright, S.D., et al. 1988. Complement receptor type three (CD11b/CD18) of human polymorphonuclear leukocytes recognizes fibrinogen. Proc. Natl. Acad. Sci. U. S. A. 85:7734-7738.
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 7734-7738
    • Wright, S.D.1
  • 33
    • 0027468975 scopus 로고
    • The structural motif glycine 190-valine 202 of the fibrinogen γ chain interacts with CD11b/CD18 integrin (alpha;Mβ2, Mac-1) and promotes leukocyte adhesion
    • Altieri, D.C., Plescia, J., and Plow, E.F. 1993. The structural motif glycine 190-valine 202 of the fibrinogen γ chain interacts with CD11b/CD18 integrin (alpha;Mβ2, Mac-1) and promotes leukocyte adhesion. J. Biol. Chem. 268:1847-1853.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1847-1853
    • Altieri, D.C.1    Plescia, J.2    Plow, E.F.3
  • 34
    • 0030749838 scopus 로고    scopus 로고
    • Identification and reconstruction of the binding site within αMβ2 for a specific and high affinity ligand, NIF
    • Zhang, L., and Plow, E.F. 1997. Identification and reconstruction of the binding site within αMβ2 for a specific and high affinity ligand, NIF. J. Biol. Chem. 272:17558-17564.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17558-17564
    • Zhang, L.1    Plow, E.F.2
  • 35
    • 0025678813 scopus 로고
    • ICAM-1 (CD54): A counter-receptor for Mac-1 (CD11b/CD18)
    • Diamond, M.S., et al. 1990. ICAM-1 (CD54): a counter-receptor for Mac-1 (CD11b/CD18). J. Cell Biol. 111:3129-3139.
    • (1990) J. Cell Biol. , vol.111 , pp. 3129-3139
    • Diamond, M.S.1
  • 36
    • 0037073752 scopus 로고    scopus 로고
    • A molecular basis for integrin alpha;M;β2 ligand binding promiscuity
    • Yakubenko, V.P., Lishko, V.K., Lam, S.C., and Ugarova, T.P. 2002. A molecular basis for integrin alpha;M;β2 ligand binding promiscuity. J. Biol. Chem. 277:48635-48642.
    • (2002) J. Biol. Chem. , vol.277 , pp. 48635-48642
    • Yakubenko, V.P.1    Lishko, V.K.2    Lam, S.C.3    Ugarova, T.P.4
  • 37
    • 0036135609 scopus 로고    scopus 로고
    • Complementary adhesion molecules promote neutrophil-Kupffer cell interaction and the elimination of bacteria taken up by the liver
    • Gregory, S.H., et al. 2002. Complementary adhesion molecules promote neutrophil-Kupffer cell interaction and the elimination of bacteria taken up by the liver. J. Immunol. 168:308-315.
    • (2002) J. Immunol. , vol.168 , pp. 308-315
    • Gregory, S.H.1
  • 38
    • 0038326555 scopus 로고    scopus 로고
    • Neutrophilia in LFA-1-deficient mice confers resistance to listeriosis: Possible contribution of granulocyte-colony-stimulating factor and IL-17
    • Miyamoto, M., et al. 2003. Neutrophilia in LFA-1-deficient mice confers resistance to listeriosis: possible contribution of granulocyte-colony- stimulating factor and IL-17. J. Immunol 170:5228-5234.
    • (2003) J. Immunol. , vol.170 , pp. 5228-5234
    • Miyamoto, M.1
  • 39
    • 0035876921 scopus 로고    scopus 로고
    • The differential roles of LFA-1 and Mac-1 in host defense against systemic infection with Streptococcus pneumoniae
    • Prince, J.E., et al. 2001. The differential roles of LFA-1 and Mac-1 in host defense against systemic infection with Streptococcus pneumoniae. J. Immunol. 166:7362-7369.
    • (2001) J. Immunol. , vol.166 , pp. 7362-7369
    • Prince, J.E.1
  • 40
    • 0032146709 scopus 로고    scopus 로고
    • Fibrinogen activates NF-κ transcription factors in mononuclear phagocytes
    • Sitrin, R.G., Pan, P.M., Srikanth, S., and Todd, R.F., 3rd. 1998. Fibrinogen activates NF-κ transcription factors in mononuclear phagocytes. J. Immunol. 161:1462-1470.
    • (1998) J. Immunol. , vol.161 , pp. 1462-1470
    • Sitrin, R.G.1    Pan, P.M.2    Srikanth, S.3    Todd III, R.F.4
  • 41
    • 0036464689 scopus 로고    scopus 로고
    • Roles for thrombin and fibrin(ogen) in cytokine/chemokine production and macrophage adhesion in vivo
    • Szaba, F.M., and Smiley, S.T. 2002. Roles for thrombin and fibrin(ogen) in cytokine/chemokine production and macrophage adhesion in vivo. Blood. 99:1053-1059.
    • (2002) Blood , vol.99 , pp. 1053-1059
    • Szaba, F.M.1    Smiley, S.T.2
  • 42
    • 0036569440 scopus 로고    scopus 로고
    • Signaling pathways involved in IL-8-dependent activation of adhesion through Mac-1
    • Takami, M., Terry, V., and Petruzzelli, L. 2002. Signaling pathways involved in IL-8-dependent activation of adhesion through Mac-1. J. Immunol. 168:4559-4566.
    • (2002) J. Immunol. , vol.168 , pp. 4559-4566
    • Takami, M.1    Terry, V.2    Petruzzelli, L.3
  • 43
    • 0035889160 scopus 로고    scopus 로고
    • The alternatively spliced αE C domain of human fibrinogen-420 is a novel ligand for leukocyte integrins alpha;Mβ2 and αXβ2
    • Lishko, V.K., Yakubenko, V.P., Hertzberg, K.M., Grieninger, G., and Ugarova, T.P. 2001. The alternatively spliced αE C domain of human fibrinogen-420 is a novel ligand for leukocyte integrins alpha;Mβ2 and αXβ2. Blood. 98:2448-2455.
    • (2001) Blood , vol.98 , pp. 2448-2455
    • Lishko, V.K.1    Yakubenko, V.P.2    Hertzberg, K.M.3    Grieninger, G.4    Ugarova, T.P.5
  • 44
  • 45
    • 18244415152 scopus 로고    scopus 로고
    • Spontaneous skin ulceration and defective T cell function in CD18 null mice
    • Scharffetter-Kochanek, K., et al. 1998. Spontaneous skin ulceration and defective T cell function in CD18 null mice. J. Exp. Med. 188:119-131.
    • (1998) J. Exp. Med. , vol.188 , pp. 119-131
    • Scharffetter-Kochanek, K.1
  • 46
    • 0033968448 scopus 로고    scopus 로고
    • Decreased neointimal formation in Mac-1(-/-) mice reveals a role for inflammation in vascular repair after angioplasty
    • Simon, D.I., et al. 2000. Decreased neointimal formation in Mac-1(-/-) mice reveals a role for inflammation in vascular repair after angioplasty. J. Clin. Invest. 105:293-300.
    • (2000) J. Clin. Invest. , vol.105 , pp. 293-300
    • Simon, D.I.1
  • 47
    • 0029947679 scopus 로고    scopus 로고
    • Neutrophil rolling, arrest, and transmigration across activated, surface-adherent platelets via sequential action of P-selectin and the β2-integrin CD11b/CD18
    • Diacovo, T.G., Roth, S.J., Buccola, J.M., Bainton, D.F., and Springer, T.A. 1996. Neutrophil rolling, arrest, and transmigration across activated, surface-adherent platelets via sequential action of P-selectin and the β2-integrin CD11b/CD18. Blood. 88:146-157.
    • (1996) Blood , vol.88 , pp. 146-157
    • Diacovo, T.G.1    Roth, S.J.2    Buccola, J.M.3    Bainton, D.F.4    Springer, T.A.5
  • 48
    • 0035657925 scopus 로고    scopus 로고
    • Evasion of human innate and acquired immunity by a bacterial homolog of CD11b that inhibits opsonophagocytosis
    • Lei, B., et al. 2001. Evasion of human innate and acquired immunity by a bacterial homolog of CD11b that inhibits opsonophagocytosis. Nat. Med. 7:1298-1305.
    • (2001) Nat. Med. , vol.7 , pp. 1298-1305
    • Lei, B.1
  • 49
    • 0028834487 scopus 로고
    • Role of Staphylacoccus aureus coagulase and clumping factor in pathogenesis of experimental endocarditis
    • Moreillon, P., et al. 1995. Role of Staphylacoccus aureus coagulase and clumping factor in pathogenesis of experimental endocarditis. Infect. Immun. 63:4738-4743.
    • (1995) Infect. Immun. , vol.63 , pp. 4738-4743
    • Moreillon, P.1
  • 50
    • 0030758696 scopus 로고    scopus 로고
    • Characterization of the interaction between the Staphylococcus aureus clumping factor (ClfA) and fibrinogen
    • McDevitt, D., et al. 1997. Characterization of the interaction between the Staphylococcus aureus clumping factor (ClfA) and fibrinogen. Eur. J. Biochem. 247:416-424.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 416-424
    • McDevitt, D.1
  • 51
    • 0036957150 scopus 로고    scopus 로고
    • Protein C pathway in sepsis
    • Esmon, C.T. 2002. Protein C pathway in sepsis. Ann. Med. 34:598-605.
    • (2002) Ann. Med. , vol.34 , pp. 598-605
    • Esmon, C.T.1
  • 52
    • 2642616219 scopus 로고    scopus 로고
    • Exacerbation of antigen-induced arthritis in urokinase-deficient mice
    • Busso, N., et al. 1998. Exacerbation of antigen-induced arthritis in urokinase-deficient mice. J. Clin. Invest. 102:41-50.
    • (1998) J. Clin. Invest. , vol.102 , pp. 41-50
    • Busso, N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.