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Volumn 187, Issue 4, 2009, Pages 553-567

The CEACAM1 N-terminal Ig domain mediates cis- and trans-binding and is essential for allosteric rearrangements of CEACAM1 microclusters

Author keywords

[No Author keywords available]

Indexed keywords

CARCINOEMBRYONIC ANTIGEN RELATED CELL ADHESION MOLECULE 1; IMMUNOGLOBULIN; CD66 ANTIGENS; CELL ADHESION MOLECULE; FC RECEPTOR; LEUKOCYTE ANTIGEN; PEPTIDE FRAGMENT;

EID: 73349119132     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.200904149     Document Type: Article
Times cited : (45)

References (47)
  • 1
    • 0022760449 scopus 로고
    • Cell surface glycoproteins of hepatocytes and hepatoma cells identified by monoclonal antibodies
    • Becker, A., R. Neumeier, C. Heidrich, N. Loch, S. Hartel, and W. Reutter. 1986. Cell surface glycoproteins of hepatocytes and hepatoma cells identified by monoclonal antibodies. Biol. Chem. Hoppe Seyler. 367:681-688.
    • (1986) Biol. Chem. Hoppe Seyler , vol.367 , pp. 681-688
    • Becker, A.1    Neumeier, R.2    Heidrich, C.3    Loch, N.4    Hartel, S.5    Reutter, W.6
  • 2
    • 0030596495 scopus 로고    scopus 로고
    • Extended glycoprotein structure of the seven domains in human carcinoembryonic antigen by X-ray and neutron solution scattering and an automated curve fitting procedure: Implications for cellular adhesion
    • doi:10.1006/jmbi.1996.0353
    • Boehm, M.K., M.O. Mayans, J.D. Thornton, R.H. Begent, P.A. Keep, and S.J. Perkins. 1996. Extended glycoprotein structure of the seven domains in human carcinoembryonic antigen by X-ray and neutron solution scattering and an automated curve fitting procedure: implications for cellular adhesion. J. Mol. Biol. 259:718-736. doi:10.1006/jmbi.1996.0353
    • (1996) J. Mol. Biol , vol.259 , pp. 718-736
    • Boehm, M.K.1    Mayans, M.O.2    Thornton, J.D.3    Begent, R.H.4    Keep, P.A.5    Perkins, S.J.6
  • 3
    • 0037123593 scopus 로고    scopus 로고
    • C-cadherin ectodomain structure and implications for cell adhesion mechanisms
    • doi:10.1126/ science.1071559
    • Boggon, T.J., J. Murray, S. Chappuis-Flament, E. Wong, B.M. Gumbiner, and L. Shapiro. 2002. C-cadherin ectodomain structure and implications for cell adhesion mechanisms. Science. 296:1308-1313. doi:10.1126/ science.1071559
    • (2002) Science , vol.296 , pp. 1308-1313
    • Boggon, T.J.1    Murray, J.2    Chappuis-Flament, S.3    Wong, E.4    Gumbiner, B.M.5    Shapiro, L.6
  • 5
    • 0027325147 scopus 로고
    • Different isoforms and stock-specific variants of the cell adhesion molecule C-CAM (cell-CAM 105) in rat liver
    • doi:10.1111/ j.1432-1033.1993.tb17860.x
    • Edlund, M., H. Gaardsvoll, E. Bock, and B. Öbrink. 1993. Different isoforms and stock-specific variants of the cell adhesion molecule C-CAM (cell-CAM 105) in rat liver. Eur. J. Biochem. 213:1109-1116. doi:10.1111/ j.1432-1033.1993.tb17860.x
    • (1993) Eur. J. Biochem , vol.213 , pp. 1109-1116
    • Edlund, M.1    Gaardsvoll, H.2    Bock, E.3    Öbrink, B.4
  • 6
    • 0016721052 scopus 로고
    • Rotational allomerism and divergent evolution of domains in immunoglobulin light chains
    • doi:10.1021/ bi00689a005
    • Edmundson, A.B., K.R. Ely, E.E. Abola, M. Schiffer, and N. Panagiotopoulos. 1975. Rotational allomerism and divergent evolution of domains in immunoglobulin light chains. Biochemistry. 14:3953-3961. doi:10.1021/ bi00689a005
    • (1975) Biochemistry , vol.14 , pp. 3953-3961
    • Edmundson, A.B.1    Ely, K.R.2    Abola, E.E.3    Schiffer, M.4    Panagiotopoulos, N.5
  • 7
    • 41849101999 scopus 로고    scopus 로고
    • Electron tomography: A short overview with an emphasis on the absorption potential model for the forward problem
    • doi.org/10.1088/0266-5611/24/1/ 013001
    • Fanelli, D., and O. Öktem. 2008. Electron tomography: a short overview with an emphasis on the absorption potential model for the forward problem. Inverse Problems. 24:1-51. doi.org/10.1088/0266-5611/24/1/ 013001.
    • (2008) Inverse Problems , vol.24 , pp. 1-51
    • Fanelli, D.1    Öktem, O.2
  • 8
    • 33748352337 scopus 로고    scopus 로고
    • Structure of the N-terminal domain of human CEACAM1: Binding target of the opacity proteins during invasion of Neisseria meningitidis and N. gonorrhoeae
    • doi:10.1107/ S0907444906020737
    • Fedarovich, A., J. Tomberg, R.A. Nicholas, and C. Davies. 2006. Structure of the N-terminal domain of human CEACAM1: binding target of the opacity proteins during invasion of Neisseria meningitidis and N. gonorrhoeae. Acta Crystallogr. D Biol. Crystallogr. 62:971-979. doi:10.1107/ S0907444906020737
    • (2006) Acta Crystallogr. D Biol. Crystallogr , vol.62 , pp. 971-979
    • Fedarovich, A.1    Tomberg, J.2    Nicholas, R.A.3    Davies, C.4
  • 9
    • 0010564906 scopus 로고
    • Interaction between proteins localized in membranes
    • doi:10.1073/pnas.83.17.6258
    • Grasberger, B., A.P. Minton, C. DeLisi, and H. Metzger. 1986. Interaction between proteins localized in membranes. Proc. Natl. Acad. Sci. USA. 83:6258-6262. doi:10.1073/pnas.83.17.6258.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 6258-6262
    • Grasberger, B.1    Minton, A.P.2    DeLisi, C.3    Metzger, H.4
  • 10
    • 33745684548 scopus 로고    scopus 로고
    • CEACAM1: Contact-dependent control of immunity
    • doi:10.1038/nri1864
    • Gray-Owen, S.D., and R.S. Blumberg. 2006. CEACAM1: contact-dependent control of immunity. Nat. Rev. Immunol. 6:433-446. doi:10.1038/nri1864
    • (2006) Nat. Rev. Immunol , vol.6 , pp. 433-446
    • Gray-Owen, S.D.1    Blumberg, R.S.2
  • 11
    • 67349284040 scopus 로고    scopus 로고
    • Role of Ceacam1 in VEGF induced vasculogenesis of murine embryonic stem cell-derived embryoid bodies in 3D culture
    • doi:10.1016/ j.yexcr.2009.02.026
    • Gu, A., W. Tsark, K.V. Holmes, and J.E. Shively. 2009. Role of Ceacam1 in VEGF induced vasculogenesis of murine embryonic stem cell-derived embryoid bodies in 3D culture. Exp. Cell Res. 315:1668-1682. doi:10.1016/ j.yexcr.2009.02.026
    • (2009) Exp. Cell Res , vol.315 , pp. 1668-1682
    • Gu, A.1    Tsark, W.2    Holmes, K.V.3    Shively, J.E.4
  • 13
    • 0042681786 scopus 로고    scopus 로고
    • Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins
    • doi:10.1126/science.1084174
    • Kim, M., C.V. Carman, and T.A. Springer. 2003. Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins. Science. 301:1720-1725. doi:10.1126/science.1084174
    • (2003) Science , vol.301 , pp. 1720-1725
    • Kim, M.1    Carman, C.V.2    Springer, T.A.3
  • 14
    • 0037457986 scopus 로고    scopus 로고
    • CEACAM1-4S, a cell-cell adhesion molecule, mediates apoptosis and reverts mammary carcinoma cells to a normal morphogenic phenotype in a 3D culture
    • doi:10.1073/pnas.232711199
    • Kirshner, J., C.J. Chen, P. Liu, J. Huang, and J.E. Shively. 2003. CEACAM1-4S, a cell-cell adhesion molecule, mediates apoptosis and reverts mammary carcinoma cells to a normal morphogenic phenotype in a 3D culture. Proc. Natl. Acad. Sci. USA. 100:521-526. doi:10.1073/pnas.232711199
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 521-526
    • Kirshner, J.1    Chen, C.J.2    Liu, P.3    Huang, J.4    Shively, J.E.5
  • 15
    • 30544432615 scopus 로고    scopus 로고
    • CEACAM1 functionally interacts with filamin A and exerts a dual role in the regulation of cell migration
    • doi:10.1242/jcs.02660
    • Klaile, E., M.M. Müller, C. Kannicht, B.B. Singer, and L. Lucka. 2005. CEACAM1 functionally interacts with filamin A and exerts a dual role in the regulation of cell migration. J. Cell Sci. 118:5513-5524. doi:10.1242/jcs.02660
    • (2005) J. Cell Sci , vol.118 , pp. 5513-5524
    • Klaile, E.1    Müller, M.M.2    Kannicht, C.3    Singer, B.B.4    Lucka, L.5
  • 17
    • 17944374159 scopus 로고    scopus 로고
    • X-ray structure of junctional adhesion molecule: Structural basis for homophilic adhesion via a novel dimerization motif
    • doi:10.1093/emboj/20.16. 4391
    • Kostrewa, D., M. Brockhaus, A. D'Arcy, G.E. Dale, P. Nelboeck, G. Schmid, F. Mueller, G. Bazzoni, E. Dejana, T. Bartfai, et al. 2001. X-ray structure of junctional adhesion molecule: structural basis for homophilic adhesion via a novel dimerization motif. EMBO J. 20:4391-4398. doi:10.1093/emboj/20.16. 4391
    • (2001) EMBO J , vol.20 , pp. 4391-4398
    • Kostrewa, D.1    Brockhaus, M.2    D'Arcy, A.3    Dale, G.E.4    Nelboeck, P.5    Schmid, G.6    Mueller, F.7    Bazzoni, G.8    Dejana, E.9    Bartfai, T.10
  • 18
    • 50049091567 scopus 로고    scopus 로고
    • Intestinal tumor progression is promoted by decreased apoptosis and dysregulated Wnt signaling in Ceacam1-/- mice
    • Leung, N., C. Turbide, B. Balachandra, V. Marcus, and N. Beauchemin. 2008. Intestinal tumor progression is promoted by decreased apoptosis and dysregulated Wnt signaling in Ceacam1-/- mice. Oncogene. 27:4943-4953.
    • (2008) Oncogene , vol.27 , pp. 4943-4953
    • Leung, N.1    Turbide, C.2    Balachandra, B.3    Marcus, V.4    Beauchemin, N.5
  • 19
    • 0030601790 scopus 로고    scopus 로고
    • Ligandinduced conformational change within the CD2 ectodomain accompanies receptor clustering: Implication for molecular lattice formation
    • doi:10.1006/jmbi.1996.0570
    • Li, J., A. Smolyar, R. Sunder-Plassmann, and E.L. Reinherz. 1996. Ligandinduced conformational change within the CD2 ectodomain accompanies receptor clustering: implication for molecular lattice formation. J. Mol. Biol. 263:209-226. doi:10.1006/jmbi.1996.0570
    • (1996) J. Mol. Biol , vol.263 , pp. 209-226
    • Li, J.1    Smolyar, A.2    Sunder-Plassmann, R.3    Reinherz, E.L.4
  • 20
    • 34748840451 scopus 로고    scopus 로고
    • The crystal structure of the ligand-binding module of human TAG-1 suggests a new mode of homophilic interaction
    • doi:10.1110/ ps.072802707
    • Mörtl, M., P. Sonderegger, K. Diederichs, and W. Welte. 2007. The crystal structure of the ligand-binding module of human TAG-1 suggests a new mode of homophilic interaction. Protein Sci. 16:2174-2183. doi:10.1110/ ps.072802707
    • (2007) Protein Sci , vol.16 , pp. 2174-2183
    • Mörtl, M.1    Sonderegger, P.2    Diederichs, K.3    Welte, W.4
  • 21
    • 18544390544 scopus 로고    scopus 로고
    • Transmembrane CEACAM1 affects integrin-dependent signaling and regulates extracellular matrix protein-specific morphology and migration of endothelial cells
    • doi:10.1182/blood-2004-09-3618
    • Müller, M.M., B.B. Singer, E. Klaile, B. Öbrink, and L. Lucka. 2005. Transmembrane CEACAM1 affects integrin-dependent signaling and regulates extracellular matrix protein-specific morphology and migration of endothelial cells. Blood. 105:3925-3934. doi:10.1182/blood-2004-09-3618
    • (2005) Blood , vol.105 , pp. 3925-3934
    • Müller, M.M.1    Singer, B.B.2    Klaile, E.3    Öbrink, B.4    Lucka, L.5
  • 22
    • 73349083092 scopus 로고    scopus 로고
    • Homophilic adhesion and CEACAM1-S regulate dimerization of CEACAM1-L and recruitment of SHP-2 and c-Src
    • Müller, M.M., E. Klaile, O. Vorontsova, B.B. Singer, and B. Öbrink. 2009. Homophilic adhesion and CEACAM1-S regulate dimerization of CEACAM1-L and recruitment of SHP-2 and c-Src. J. Cell Biol. 187:569-581.
    • (2009) J. Cell Biol , vol.187 , pp. 569-581
    • Müller, M.M.1    Klaile, E.2    Vorontsova, O.3    Singer, B.B.4    Öbrink, B.5
  • 24
    • 0030890210 scopus 로고    scopus 로고
    • Kinetic analysis of a protein antigen-antibody interaction limited by mass transport on an optical biosensor
    • doi:10.1016/ S0301-4622(96)02230-2
    • Myszka, D.G., T.A. Morton, M.L. Doyle, and I.M. Chaiken. 1997. Kinetic analysis of a protein antigen-antibody interaction limited by mass transport on an optical biosensor. Biophys. Chem. 64:127-137. doi:10.1016/ S0301-4622(96)02230-2
    • (1997) Biophys. Chem , vol.64 , pp. 127-137
    • Myszka, D.G.1    Morton, T.A.2    Doyle, M.L.3    Chaiken, I.M.4
  • 25
    • 0023901114 scopus 로고
    • Immunohistochemical localization of cellCAM 105 in rat tissues: Appearance in epithelia, platelets, and granulocytes
    • Odin, P., M. Asplund, C. Busch, and B. Öbrink. 1988. Immunohistochemical localization of cellCAM 105 in rat tissues: appearance in epithelia, platelets, and granulocytes. J. Histochem. Cytochem. 36:729-739.
    • (1988) J. Histochem. Cytochem , vol.36 , pp. 729-739
    • Odin, P.1    Asplund, M.2    Busch, C.3    Öbrink, B.4
  • 27
    • 41449095679 scopus 로고    scopus 로고
    • A componentwise iterated relative entropy regularization method with updated prior and regularization parameter
    • doi:10.1088/0266-5611/ 23/5/018
    • Rullgård, H., O. Öktem, and U. Skoglund. 2007. A componentwise iterated relative entropy regularization method with updated prior and regularization parameter. Inverse Probl. 23:2121-2139. doi:10.1088/0266-5611/ 23/5/018
    • (2007) Inverse Probl , vol.23 , pp. 2121-2139
    • Rullgård, H.1    Öktem, O.2    Skoglund, U.3
  • 28
    • 1542393385 scopus 로고    scopus 로고
    • Structure and flexibility of individual immunoglobulin G molecules in solution
    • doi:10.1016/j.str.2004.02. 011
    • Sandin, S., L.G. Öfverstedt, A.C. Wikström, O. Wrange, and U. Skoglund. 2004. Structure and flexibility of individual immunoglobulin G molecules in solution. Structure. 12:409-415. doi:10.1016/j.str.2004.02. 011
    • (2004) Structure , vol.12 , pp. 409-415
    • Sandin, S.1    Öfverstedt, L.G.2    Wikström, A.C.3    Wrange, O.4    Skoglund, U.5
  • 29
    • 20444429449 scopus 로고    scopus 로고
    • Control of density-dependent, cell state-specific signal transduction by the cell adhesion molecule CEACAM1, and its influence on cell cycle regulation
    • doi:10.1016/j.yexcr .2005.03.030
    • Scheffrahn, I., B.B. Singer, K. Sigmundsson, L. Lucka, and B. Öbrink. 2005. Control of density-dependent, cell state-specific signal transduction by the cell adhesion molecule CEACAM1, and its influence on cell cycle regulation. Exp. Cell Res. 307:427-435. doi:10.1016/j.yexcr .2005.03.030
    • (2005) Exp. Cell Res , vol.307 , pp. 427-435
    • Scheffrahn, I.1    Singer, B.B.2    Sigmundsson, K.3    Lucka, L.4    Öbrink, B.5
  • 30
    • 0037008090 scopus 로고    scopus 로고
    • Determination of active concentrations and association and dissociation rate constants of interacting biomolecules: An analytical solution to the theory for kinetic and mass transport limitations in biosensor technology and its experimental verification
    • doi:10.1021
    • Sigmundsson, K., G. Másson, R. Rice, N. Beauchemin, and B. Öbrink. 2002. Determination of active concentrations and association and dissociation rate constants of interacting biomolecules: an analytical solution to the theory for kinetic and mass transport limitations in biosensor technology and its experimental verification. Biochemistry. 41:8263-8276. doi:10.1021/
    • (2002) Biochemistry , vol.41 , pp. 8263-8276
    • Sigmundsson, K.1    Másson, G.2    Rice, R.3    Beauchemin, N.4    Öbrink, B.5
  • 31
    • 76149115955 scopus 로고    scopus 로고
    • Singer, B.B., and L. Lucka. 2005. CEACAM1. UCSD Nature Molecule Pages. http://www.signaling-gateway.org/molecule/query?afcsid=A003597. doi:10.1038/mp.a003597.01.
    • Singer, B.B., and L. Lucka. 2005. CEACAM1. UCSD Nature Molecule Pages. http://www.signaling-gateway.org/molecule/query?afcsid=A003597. doi:10.1038/mp.a003597.01.
  • 32
    • 0034163462 scopus 로고    scopus 로고
    • The tumor growth-inhibiting cell adhesion molecule CEACAM1 (C-CAM) is differently expressed in proliferating and quiescent epithelial cells and regulates cell proliferation
    • Singer, B.B., I. Scheffrahn, and B. Öbrink. 2000. The tumor growth-inhibiting cell adhesion molecule CEACAM1 (C-CAM) is differently expressed in proliferating and quiescent epithelial cells and regulates cell proliferation. Cancer Res. 60:1236-1244.
    • (2000) Cancer Res , vol.60 , pp. 1236-1244
    • Singer, B.B.1    Scheffrahn, I.2    Öbrink, B.3
  • 33
    • 0037093981 scopus 로고    scopus 로고
    • Carcinoembryonic antigen-related cell adhesion molecule 1 expression and signaling in human, mouse, and rat leukocytes: Evidence for replacement of the short cytoplasmic domain isoform by glycosylphosphatidylinositol-linked proteins in human leukocytes
    • Singer, B.B., I. Scheffrahn, R. Heymann, K. Sigmundsson, R. Kammerer, and B. Öbrink. 2002. Carcinoembryonic antigen-related cell adhesion molecule 1 expression and signaling in human, mouse, and rat leukocytes: evidence for replacement of the short cytoplasmic domain isoform by glycosylphosphatidylinositol-linked proteins in human leukocytes. J. Immunol. 168:5139-5146.
    • (2002) J. Immunol , vol.168 , pp. 5139-5146
    • Singer, B.B.1    Scheffrahn, I.2    Heymann, R.3    Sigmundsson, K.4    Kammerer, R.5    Öbrink, B.6
  • 34
    • 20844441677 scopus 로고    scopus 로고
    • CEACAM1 (CD66a) mediates delay of spontaneous and Fas ligand-induced apoptosis in granulocytes
    • doi:10.1002/eji.200425691
    • Singer, B.B., E. Klaile, I. Scheffrahn, M.M. Müller, R. Kammerer, W. Reutter, B. Öbrink, and L. Lucka. 2005. CEACAM1 (CD66a) mediates delay of spontaneous and Fas ligand-induced apoptosis in granulocytes. Eur. J. Immunol. 35:1949-1959. doi:10.1002/eji.200425691
    • (2005) Eur. J. Immunol , vol.35 , pp. 1949-1959
    • Singer, B.B.1    Klaile, E.2    Scheffrahn, I.3    Müller, M.M.4    Kammerer, R.5    Reutter, W.6    Öbrink, B.7    Lucka, L.8
  • 35
    • 0030295008 scopus 로고    scopus 로고
    • Maximumentropy three-dimensional reconstruction with deconvolution of the contrast transfer function: A test application with adenovirus
    • doi:10.1006/jsbi.1996.0081
    • Skoglund, U., L.G. Öfverstedt, R.M. Burnett, and G. Bricogne. 1996. Maximumentropy three-dimensional reconstruction with deconvolution of the contrast transfer function: a test application with adenovirus. J. Struct. Biol. 117:173-188. doi:10.1006/jsbi.1996.0081
    • (1996) J. Struct. Biol , vol.117 , pp. 173-188
    • Skoglund, U.1    Öfverstedt, L.G.2    Burnett, R.M.3    Bricogne, G.4
  • 37
    • 58549108194 scopus 로고    scopus 로고
    • Structural basis for selectin mechanochemistry
    • doi:10.1073/pnas.0810784105
    • Springer, T.A. 2009. Structural basis for selectin mechanochemistry. Proc. Natl. Acad. Sci. USA. 106:91-96. doi:10.1073/pnas.0810784105.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 91-96
    • Springer, T.A.1
  • 38
    • 0026153423 scopus 로고
    • Quantitative determination of surface concentration of protein with surface plasmon resonance using radiolabeled proteins
    • doi:10.1016/0021-9797(91)90284-F
    • Stenberg, E., B. Persson, H. Ross, and C. Urbaniczky. 1991. Quantitative determination of surface concentration of protein with surface plasmon resonance using radiolabeled proteins. J. Colloid Interface Sci. 143:513-526. doi:10.1016/0021-9797(91)90284-F
    • (1991) J. Colloid Interface Sci , vol.143 , pp. 513-526
    • Stenberg, E.1    Persson, B.2    Ross, H.3    Urbaniczky, C.4
  • 39
    • 0141625303 scopus 로고    scopus 로고
    • Structure of integrin alpha5beta1 in complex with fibronectin
    • doi:10.1093/emboj/cdg445
    • Takagi, J., K. Strokovich, T.A. Springer, and T. Walz. 2003. Structure of integrin alpha5beta1 in complex with fibronectin. EMBO J. 22:4607-4615. doi:10.1093/emboj/cdg445
    • (2003) EMBO J , vol.22 , pp. 4607-4615
    • Takagi, J.1    Strokovich, K.2    Springer, T.A.3    Walz, T.4
  • 41
    • 0027576716 scopus 로고
    • Morphological grayscale reconstruction in image analysis: Applications and efficient algorithms
    • doi:10.1109/83.217222
    • Vincent, L. 1993. Morphological grayscale reconstruction in image analysis: applications and efficient algorithms. IEEE Trans. Image Process. 2:176-201. doi:10.1109/83.217222
    • (1993) IEEE Trans. Image Process , vol.2 , pp. 176-201
    • Vincent, L.1
  • 42
    • 58549112954 scopus 로고    scopus 로고
    • Transmission of allostery through the lectin domain in selectin-mediated cell adhesion
    • doi:10.1073/pnas.0810620105
    • Waldron, T.T., and T.A. Springer. 2009. Transmission of allostery through the lectin domain in selectin-mediated cell adhesion. Proc. Natl. Acad. Sci. USA. 106:85-90. doi:10.1073/pnas.0810620105
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 85-90
    • Waldron, T.T.1    Springer, T.A.2
  • 43
    • 0035469860 scopus 로고    scopus 로고
    • Homophilic adhesion of human CEACAM1 involves N-terminal domain interactions: Structural analysis of the binding site
    • doi:10.1182/ blood.V98.5.1469
    • Watt, S.M., A.M. Teixeira, G.Q. Zhou, R. Doyonnas, Y. Zhang, F. Grunert, R.S. Blumberg, M. Kuroki, K.M. Skubitz, and P.A. Bates. 2001. Homophilic adhesion of human CEACAM1 involves N-terminal domain interactions: structural analysis of the binding site. Blood. 98:1469-1479. doi:10.1182/ blood.V98.5.1469
    • (2001) Blood , vol.98 , pp. 1469-1479
    • Watt, S.M.1    Teixeira, A.M.2    Zhou, G.Q.3    Doyonnas, R.4    Zhang, Y.5    Grunert, F.6    Blumberg, R.S.7    Kuroki, M.8    Skubitz, K.M.9    Bates, P.A.10
  • 44
    • 0030587461 scopus 로고    scopus 로고
    • Homophilic intercellular adhesion mediated by C-CAM is due to a domain 1-domain 1 reciprocal binding
    • doi:10.1006/excr.1996. 0285
    • Wikström, K., G. Kjellström, and B. Öbrink. 1996. Homophilic intercellular adhesion mediated by C-CAM is due to a domain 1-domain 1 reciprocal binding. Exp. Cell Res. 227:360-366. doi:10.1006/excr.1996. 0285
    • (1996) Exp. Cell Res , vol.227 , pp. 360-366
    • Wikström, K.1    Kjellström, G.2    Öbrink, B.3
  • 45
    • 8544259562 scopus 로고    scopus 로고
    • Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics
    • doi:10.1038/nature02976
    • Xiao, T., J. Takagi, B.S. Coller, J.H. Wang, and T.A. Springer. 2004. Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics. Nature. 432:59-67. doi:10.1038/nature02976
    • (2004) Nature , vol.432 , pp. 59-67
    • Xiao, T.1    Takagi, J.2    Coller, B.S.3    Wang, J.H.4    Springer, T.A.5
  • 47
    • 36849003589 scopus 로고    scopus 로고
    • Role of CEACAM1 isoforms in an in vivo model of mammary morphogenesis: Mutational analysis of the cytoplasmic domain of CEACAM1 -4S reveals key residues involved in lumen formation
    • doi:10.1038/sj.onc.1210577
    • Yokoyama, S., C.J. Chen, T. Nguyen, and J.E. Shively. 2007. Role of CEACAM1 isoforms in an in vivo model of mammary morphogenesis: mutational analysis of the cytoplasmic domain of CEACAM1 -4S reveals key residues involved in lumen formation. Oncogene. 26:7637-7646. doi:10.1038/sj.onc.1210577
    • (2007) Oncogene , vol.26 , pp. 7637-7646
    • Yokoyama, S.1    Chen, C.J.2    Nguyen, T.3    Shively, J.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.