메뉴 건너뛰기




Volumn 122, Issue 3-4, 2008, Pages 326-334

Molecular cloning and characterization of the alphaX subunit from CD11c/CD18 horse integrin

Author keywords

Antibody; CD11c; Dendritic cells; Horse; I domain; Integrin

Indexed keywords

AMINO ACID; CD18 ANTIGEN; COMPLEMENTARY DNA; GLYCOPROTEIN P 15095; INTEGRIN;

EID: 40849137667     PISSN: 01652427     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.vetimm.2007.12.004     Document Type: Article
Times cited : (6)

References (19)
  • 1
    • 0030310296 scopus 로고    scopus 로고
    • Fast protein fold recognition via sequence to structure alignment and contact capacity potentials
    • Alexandrov N.N., Nussinov R., and Zimmer R.M. Fast protein fold recognition via sequence to structure alignment and contact capacity potentials. Pac. Symp. Biocomput. (1996) 53-72
    • (1996) Pac. Symp. Biocomput. , pp. 53-72
    • Alexandrov, N.N.1    Nussinov, R.2    Zimmer, R.M.3
  • 2
    • 0032546352 scopus 로고    scopus 로고
    • Dendritic cells and the control of immunity
    • Banchereau J., and Steinman R.M. Dendritic cells and the control of immunity. Nature 392 (1998) 245-252
    • (1998) Nature , vol.392 , pp. 245-252
    • Banchereau, J.1    Steinman, R.M.2
  • 3
    • 0028265846 scopus 로고
    • The leukocyte integrin p150,95 (CD11c/CD18) as a receptor for iC3b. Activation by a heterologous beta subunit and localization of a ligand recognition site to the I domain
    • Bilsland C.A., Diamond M.S., and Springer T.A. The leukocyte integrin p150,95 (CD11c/CD18) as a receptor for iC3b. Activation by a heterologous beta subunit and localization of a ligand recognition site to the I domain. J. Immunol. 152 (1994) 4582-4589
    • (1994) J. Immunol. , vol.152 , pp. 4582-4589
    • Bilsland, C.A.1    Diamond, M.S.2    Springer, T.A.3
  • 4
    • 0036086751 scopus 로고    scopus 로고
    • Loops within the CD11c I domain critical for specific recognition of fibrinogen
    • Choi J., and Nham S.U. Loops within the CD11c I domain critical for specific recognition of fibrinogen. Biochem. Biophys. Res. Commun. 292 (2002) 756-760
    • (2002) Biochem. Biophys. Res. Commun. , vol.292 , pp. 756-760
    • Choi, J.1    Nham, S.U.2
  • 5
    • 0023661323 scopus 로고
    • cDNA cloning and complete primary structure of the alpha subunit of a leukocyte adhesion glycoprotein, p. 150, 95
    • Corbi A.L., Miller L.J., O'Connor K., Larson R.S., and Springer T.A. cDNA cloning and complete primary structure of the alpha subunit of a leukocyte adhesion glycoprotein, p. 150, 95. EMBO J. 6 (1987) 4023-4028
    • (1987) EMBO J. , vol.6 , pp. 4023-4028
    • Corbi, A.L.1    Miller, L.J.2    O'Connor, K.3    Larson, R.S.4    Springer, T.A.5
  • 6
    • 0035145187 scopus 로고    scopus 로고
    • Evolution of the integrin alpha and beta protein families
    • Hughes A.L. Evolution of the integrin alpha and beta protein families. J. Mol. Evol. 52 (2001) 63-72
    • (2001) J. Mol. Evol. , vol.52 , pp. 63-72
    • Hughes, A.L.1
  • 7
  • 8
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: bidirectional, allosteric signaling machines
    • Hynes R.O. Integrins: bidirectional, allosteric signaling machines. Cell 110 (2002) 673-687
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 9
    • 0034595501 scopus 로고    scopus 로고
    • Enhanced genome annotation using structural profiles in the program 3D-PSSM
    • Kelley L.A., MacCallum R.M., and Sternberg M.J. Enhanced genome annotation using structural profiles in the program 3D-PSSM. J. Mol. Biol. 299 (2000) 499-520
    • (2000) J. Mol. Biol. , vol.299 , pp. 499-520
    • Kelley, L.A.1    MacCallum, R.M.2    Sternberg, M.J.3
  • 10
    • 34247891506 scopus 로고    scopus 로고
    • Structural basis of integrin regulation and signaling
    • Luo B.H., Carman C.V., and Springer T.A. Structural basis of integrin regulation and signaling. Annu. Rev. Immunol. 25 (2007) 619-647
    • (2007) Annu. Rev. Immunol. , vol.25 , pp. 619-647
    • Luo, B.H.1    Carman, C.V.2    Springer, T.A.3
  • 11
    • 0023197884 scopus 로고
    • Biosynthesis and glycosylation of p150,95 and related leukocyte adhesion proteins
    • Miller L.J., and Springer T.A. Biosynthesis and glycosylation of p150,95 and related leukocyte adhesion proteins. J. Immunol. 139 (1987) 842-847
    • (1987) J. Immunol. , vol.139 , pp. 842-847
    • Miller, L.J.1    Springer, T.A.2
  • 12
    • 0033517847 scopus 로고    scopus 로고
    • Characteristics of fibrinogen binding to the domain of CD11c, an alpha subunit of p150,95
    • Nham S.U. Characteristics of fibrinogen binding to the domain of CD11c, an alpha subunit of p150,95. Biochem. Biophys. Res. Commun. 264 (1999) 630-634
    • (1999) Biochem. Biophys. Res. Commun. , vol.264 , pp. 630-634
    • Nham, S.U.1
  • 13
    • 0034923333 scopus 로고    scopus 로고
    • Modulating the immune response with dendritic cells and their growth factors
    • Pulendran B., Banchereau J., Maraskovsky E., and Maliszewski C. Modulating the immune response with dendritic cells and their growth factors. Trends Immunol. 22 (2001) 41-47
    • (2001) Trends Immunol. , vol.22 , pp. 41-47
    • Pulendran, B.1    Banchereau, J.2    Maraskovsky, E.3    Maliszewski, C.4
  • 15
    • 0025182959 scopus 로고
    • Adhesion receptors of the immune system
    • Springer T.A. Adhesion receptors of the immune system. Nature 346 (1990) 425-434
    • (1990) Nature , vol.346 , pp. 425-434
    • Springer, T.A.1
  • 16
    • 0036065586 scopus 로고    scopus 로고
    • CR3 (CD11b/CD18) and CR4 (CD11c/CD18) are involved in complement-independent antibody-mediated phagocytosis of Cryptococcus neoformans
    • Taborda C.P., and Casadevall A. CR3 (CD11b/CD18) and CR4 (CD11c/CD18) are involved in complement-independent antibody-mediated phagocytosis of Cryptococcus neoformans. Immunity 16 (2002) 791-802
    • (2002) Immunity , vol.16 , pp. 791-802
    • Taborda, C.P.1    Casadevall, A.2
  • 17
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., and Higgins D.G. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25 (1997) 4876-4882
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 19
    • 0041846758 scopus 로고    scopus 로고
    • Murine dendritic cell development: difficulties associated with subset analysis
    • Wilson H.L., and O'Neill H.C. Murine dendritic cell development: difficulties associated with subset analysis. Immunol. Cell Biol. 81 (2003) 239-246
    • (2003) Immunol. Cell Biol. , vol.81 , pp. 239-246
    • Wilson, H.L.1    O'Neill, H.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.