메뉴 건너뛰기




Volumn 16, Issue C, 1996, Pages 193-222

GPI-Anchored Proteins in Neural Cell Adhesion

Author keywords

[No Author keywords available]

Indexed keywords


EID: 77956742530     PISSN: 15692558     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1569-2558(08)60067-3     Document Type: Article
Times cited : (11)

References (134)
  • 1
    • 0024270874 scopus 로고
    • Characterization of a hydrophilic form of Thy-1 purified from human cerebrospinal fluid
    • Almqvist P., and Carlsson S.R. Characterization of a hydrophilic form of Thy-1 purified from human cerebrospinal fluid. J Biol Chem. 263 (1988) 12709-12715
    • (1988) J Biol Chem. , vol.263 , pp. 12709-12715
    • Almqvist, P.1    Carlsson, S.R.2
  • 2
    • 0027639941 scopus 로고
    • Plasmalemmal caveolae and GPI-anchored membrane proteins
    • Anderson R.G.W. Plasmalemmal caveolae and GPI-anchored membrane proteins. Curr. Opin. Cell Biol. 5 (1993) 647-652
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 647-652
    • Anderson, R.G.W.1
  • 3
    • 0026545612 scopus 로고
    • Potocytosisis: Sequestration and transport of small molecules by caveolae
    • Anderson R.G.W., Kamen B.A., Rothberg K.G., and Lacey S.W. Potocytosisis: Sequestration and transport of small molecules by caveolae. Science. 255 (1992) 410-411
    • (1992) Science. , vol.255 , pp. 410-411
    • Anderson, R.G.W.1    Kamen, B.A.2    Rothberg, K.G.3    Lacey, S.W.4
  • 5
    • 0028306477 scopus 로고
    • Molecular cloning and in situ localization of the human contactin gene (CNTN1) on chromosome 12q11-q12
    • Berglund E.O., and Ranscht B. Molecular cloning and in situ localization of the human contactin gene (CNTN1) on chromosome 12q11-q12. Genomics 21 (1994) 571-582
    • (1994) Genomics , vol.21 , pp. 571-582
    • Berglund, E.O.1    Ranscht, B.2
  • 6
    • 0020341179 scopus 로고
    • In vitro experiments on axon guidance demonstrating an anterior-posterior gradient on the tectum
    • Bonhoeffer F., and Huf J. In vitro experiments on axon guidance demonstrating an anterior-posterior gradient on the tectum. Embo J. 1 (1982) 427-431
    • (1982) Embo J. , vol.1 , pp. 427-431
    • Bonhoeffer, F.1    Huf, J.2
  • 7
    • 0025304678 scopus 로고
    • Scrapie and cellular prion proteins differ in their kinetics of synthesis and topology in cultured cells
    • Borchelt D.R., Scott M., Taraboulos A., Stahl N., and Prusiner S.B. Scrapie and cellular prion proteins differ in their kinetics of synthesis and topology in cultured cells. J Cell Biol. 110 (1990) 743-752
    • (1990) J Cell Biol. , vol.110 , pp. 743-752
    • Borchelt, D.R.1    Scott, M.2    Taraboulos, A.3    Stahl, N.4    Prusiner, S.B.5
  • 8
    • 0019887744 scopus 로고
    • Phase separation of integral membrane proteins in Triton X-14
    • Bordier C. Phase separation of integral membrane proteins in Triton X-14. J. Biol. Chem. 256 (1981) 1604-1607
    • (1981) J. Biol. Chem. , vol.256 , pp. 1604-1607
    • Bordier, C.1
  • 9
    • 77956775379 scopus 로고
    • Mechanism of membrane anchoring affects polarized expression of two proteins in MDCK cells
    • Brown D.A., Crise B., and Rose J.K. Mechanism of membrane anchoring affects polarized expression of two proteins in MDCK cells. Cell 62 (1989) 1499-1501
    • (1989) Cell , vol.62 , pp. 1499-1501
    • Brown, D.A.1    Crise, B.2    Rose, J.K.3
  • 10
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown D.A., and Rose J.K. Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 68 (1992) 533-544
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 11
    • 0027429723 scopus 로고
    • Axonal glycoproteins with immunoglobulin-and fibronectin type Ill-related domains in vertebrates: Structural features, binding activities, and signal transduction
    • Brümmendorf T., and Rathjen F.G. Axonal glycoproteins with immunoglobulin-and fibronectin type Ill-related domains in vertebrates: Structural features, binding activities, and signal transduction. J. Neurochem. 61 (1993) 1207-1219
    • (1993) J. Neurochem. , vol.61 , pp. 1207-1219
    • Brümmendorf, T.1    Rathjen, F.G.2
  • 12
    • 0024644865 scopus 로고
    • Neural celll recognition molecule F11: Homology with Fibronectin type III and immunoglobulin type C domains
    • Brümmendorf T., Wolff J.M., Frank R., and Rathjen F. Neural celll recognition molecule F11: Homology with Fibronectin type III and immunoglobulin type C domains. Neuron 2 (1989) 1351-1361
    • (1989) Neuron , vol.2 , pp. 1351-1361
    • Brümmendorf, T.1    Wolff, J.M.2    Frank, R.3    Rathjen, F.4
  • 13
    • 0028324598 scopus 로고
    • An endogenous glycosylphosphatidylinositol-specific phospholipase D releases basic fibroblast growth factor-heparan sulfate proteoglycan complexes from human bone marrow cultures
    • Brunner G., Metz C.N., Nguyen H., Gabrilove J., Patel S.R., Davitz M.A., Rifkin D.B., and Wilson E.L. An endogenous glycosylphosphatidylinositol-specific phospholipase D releases basic fibroblast growth factor-heparan sulfate proteoglycan complexes from human bone marrow cultures. Blood. (1994)
    • (1994) Blood.
    • Brunner, G.1    Metz, C.N.2    Nguyen, H.3    Gabrilove, J.4    Patel, S.R.5    Davitz, M.A.6    Rifkin, D.B.7    Wilson, E.L.8
  • 14
    • 0023784652 scopus 로고
    • Insulin-stimulated release of lipoprotein lipase by metabolism of its phosphatidylinositol anchor
    • Chan B.L., Lisanti M.P., Rodriguez B.E., and Saltiel A.R. Insulin-stimulated release of lipoprotein lipase by metabolism of its phosphatidylinositol anchor. Science 241 (1988) 1670-1672
    • (1988) Science , vol.241 , pp. 1670-1672
    • Chan, B.L.1    Lisanti, M.P.2    Rodriguez, B.E.3    Saltiel, A.R.4
  • 15
    • 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., and Springer T.A. Influence of receptor lateral mobility on adhesion strengthening between membranes containing LFA-3 and CD2. J Cell Biol. 115 (1991) 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
  • 16
    • 0026516708 scopus 로고
    • Disruption of pioneer growth cone guidance in vivo by removal of glycosyl-phosphatidylinositolanchored cell surface proteins
    • Chang W.S., Serikawa K., Allen K., and Bentley D. Disruption of pioneer growth cone guidance in vivo by removal of glycosyl-phosphatidylinositolanchored cell surface proteins. Devel. 114 (1992) 507-519
    • (1992) Devel. , vol.114 , pp. 507-519
    • Chang, W.S.1    Serikawa, K.2    Allen, K.3    Bentley, D.4
  • 17
    • 0025203675 scopus 로고
    • Glycolipid anchoring of plasma membrane proteins
    • Cross G.A.M. Glycolipid anchoring of plasma membrane proteins. Ann. Rev. Cell Biol. 6 (1990) 1-39
    • (1990) Ann. Rev. Cell Biol. , vol.6 , pp. 1-39
    • Cross, G.A.M.1
  • 18
    • 0023186308 scopus 로고
    • Neural cell adhesion molecule: Structure, immunoglobulin-like domains, cell surface modulation, and alternative splicing
    • Cunningham B.A., Hemperly J.J., Murray B.A., Prediger E.A., Brackenbury R., and Edelman G. Neural cell adhesion molecule: Structure, immunoglobulin-like domains, cell surface modulation, and alternative splicing. Science 236 (1987) 799-806
    • (1987) Science , vol.236 , pp. 799-806
    • Cunningham, B.A.1    Hemperly, J.J.2    Murray, B.A.3    Prediger, E.A.4    Brackenbury, R.5    Edelman, G.6
  • 20
    • 0023986284 scopus 로고
    • Spatial regulation of axonal glycoprotein expression on subsets of embryonic spinal neurons
    • Dodd J., Morton S.B., Karagogeos D., Yamamoto M., and Jessell T.M. Spatial regulation of axonal glycoprotein expression on subsets of embryonic spinal neurons. Neuron 1 (1988) 105-116
    • (1988) Neuron , vol.1 , pp. 105-116
    • Dodd, J.1    Morton, S.B.2    Karagogeos, D.3    Yamamoto, M.4    Jessell, T.M.5
  • 22
    • 0026017320 scopus 로고
    • Polarized sorting of glypiated proteins in hippocampal neurons
    • Dotti C.G., Parton R.G., and Simons K. Polarized sorting of glypiated proteins in hippocampal neurons. Nature 349 (1991) 158-161
    • (1991) Nature , vol.349 , pp. 158-161
    • Dotti, C.G.1    Parton, R.G.2    Simons, K.3
  • 23
    • 0025361892 scopus 로고
    • Polarized sorting of viral glycoproteins to the axon and dendrites of hippocampal neurons in Culture
    • Dotti C.G., and Simons K. Polarized sorting of viral glycoproteins to the axon and dendrites of hippocampal neurons in Culture. Cell 62 (1990) 63-72
    • (1990) Cell , vol.62 , pp. 63-72
    • Dotti, C.G.1    Simons, K.2
  • 24
    • 0027460655 scopus 로고
    • lyn are associated in large detergent-resistant complexes in rat basophilic leukemia cells
    • lyn are associated in large detergent-resistant complexes in rat basophilic leukemia cells. Proc. Natl. Acad. Sci. USA 90 (1993) 3611-3615
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3611-3615
    • Dráberová, L.1    Dráber, P.2
  • 25
    • 0026718214 scopus 로고
    • A soluble form of the F3 neuronal cell adhesion molecule promotes neurite outgrowth
    • Durbec P., Gennarini G., Goridis C., and Rougon G. A soluble form of the F3 neuronal cell adhesion molecule promotes neurite outgrowth. J Cell Biol. 117 (1992) 877-888
    • (1992) J Cell Biol. , vol.117 , pp. 877-888
    • Durbec, P.1    Gennarini, G.2    Goridis, C.3    Rougon, G.4
  • 26
    • 0025817934 scopus 로고
    • Cell adhesion molecules: Implications for a molecular histology
    • Edelman G.M., and Crossin K.L. Cell adhesion molecules: Implications for a molecular histology. Ann Rev Biochem. 60 (1991) 155-190
    • (1991) Ann Rev Biochem. , vol.60 , pp. 155-190
    • Edelman, G.M.1    Crossin, K.L.2
  • 27
    • 0026071833 scopus 로고
    • Differences between the lateral organization of conventional and inositol phospholipid-anchored membrane proteins: A further definition of micrometer scale membrane domains
    • Edidin M., and Stroynowski I. Differences between the lateral organization of conventional and inositol phospholipid-anchored membrane proteins: A further definition of micrometer scale membrane domains. J Cell-Biol. 112 (1991) 1143-1150
    • (1991) J Cell-Biol. , vol.112 , pp. 1143-1150
    • Edidin, M.1    Stroynowski, I.2
  • 28
    • 0025037965 scopus 로고
    • Genetic analysis of a Drosophila neural cell adhesion molecule: Interaction of fasciclin I and Abelson tyrosine kinase mutations
    • Elkins T., Zinn K., McAllister L., Hoffmann F.M., and Goodman C.S. Genetic analysis of a Drosophila neural cell adhesion molecule: Interaction of fasciclin I and Abelson tyrosine kinase mutations. Cell 60 (1990) 565-575
    • (1990) Cell , vol.60 , pp. 565-575
    • Elkins, T.1    Zinn, K.2    McAllister, L.3    Hoffmann, F.M.4    Goodman, C.S.5
  • 29
    • 0027294030 scopus 로고
    • The structure and biosynthesis of glycosyl phosphatidylinositol protein anchors
    • Englund P.T. The structure and biosynthesis of glycosyl phosphatidylinositol protein anchors. Annu. Rev. Biochem. 62 (1993) 121-138
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 121-138
    • Englund, P.T.1
  • 30
    • 0026579471 scopus 로고
    • F3/F11 cell surface molecule expression in the developing mouse cerebellum is polarized at synaptic sites and within granule cells
    • Faivre-Sarrailh C., Gennarini G., Goridis C., and Rougon G. F3/F11 cell surface molecule expression in the developing mouse cerebellum is polarized at synaptic sites and within granule cells. J. Neurosci. 12 (1992) 257-267
    • (1992) J. Neurosci. , vol.12 , pp. 257-267
    • Faivre-Sarrailh, C.1    Gennarini, G.2    Goridis, C.3    Rougon, G.4
  • 31
    • 0028273033 scopus 로고
    • TAG-1 can mediate homophilic binding, but neurite outgrowth on TAG-1 requires an L1-like molecule and b1 integrals
    • Felsenfeld D.P., Hynes M.A., Skoler K.M., Furley A.J., and Jessel T.M. TAG-1 can mediate homophilic binding, but neurite outgrowth on TAG-1 requires an L1-like molecule and b1 integrals. Neuron 12 (1994) 675-690
    • (1994) Neuron , vol.12 , pp. 675-690
    • Felsenfeld, D.P.1    Hynes, M.A.2    Skoler, K.M.3    Furley, A.J.4    Jessel, T.M.5
  • 32
    • 0026856908 scopus 로고
    • Glycosyl-phosphatidylinositol membrane anchors: The tale of a tail
    • Ferguson M.A.J. Glycosyl-phosphatidylinositol membrane anchors: The tale of a tail. Biochem. Soc. Trans. 20 (1992) 243-256
    • (1992) Biochem. Soc. Trans. , vol.20 , pp. 243-256
    • Ferguson, M.A.J.1
  • 33
    • 0001902665 scopus 로고
    • Glycolipid anchoring of cell surface proteins
    • Schlesinger M.J. (Ed), CRC Press, Boca Ratan, FL
    • Field M.C., and Menon A.K. Glycolipid anchoring of cell surface proteins. In: Schlesinger M.J. (Ed). Lipid Modifications of Proteins (1993), CRC Press, Boca Ratan, FL 84-134
    • (1993) Lipid Modifications of Proteins , pp. 84-134
    • Field, M.C.1    Menon, A.K.2
  • 34
    • 0025276826 scopus 로고
    • Identification of glycosylphosphatidylinositol-specific-phospholipase C in mouse brain membranes
    • Fouchier F., Baltz T., and Rougon G. Identification of glycosylphosphatidylinositol-specific-phospholipase C in mouse brain membranes. Biochem. J. 269 (1990) 321-327
    • (1990) Biochem. J. , vol.269 , pp. 321-327
    • Fouchier, F.1    Baltz, T.2    Rougon, G.3
  • 35
    • 0029943807 scopus 로고    scopus 로고
    • Eph receptor tryosine kinases and their ligands in neural development
    • Friedman G.C., and O'Leary D.D.M. Eph receptor tryosine kinases and their ligands in neural development. Curr. Opin. Neurobiol. 6 (1996) 127-133
    • (1996) Curr. Opin. Neurobiol. , vol.6 , pp. 127-133
    • Friedman, G.C.1    O'Leary, D.D.M.2
  • 36
    • 0025237057 scopus 로고
    • The axonal glycoprotein TAG-1 is an immunoglobulin superfamily member with neurite outgrowth-promoting activity
    • Furley A.J., Morton S.B., Manalo D., Karagogeos D., Dodd J., and Jessell T.M. The axonal glycoprotein TAG-1 is an immunoglobulin superfamily member with neurite outgrowth-promoting activity. Cell 61 (1990) 157-170
    • (1990) Cell , vol.61 , pp. 157-170
    • Furley, A.J.1    Morton, S.B.2    Manalo, D.3    Karagogeos, D.4    Dodd, J.5    Jessell, T.M.6
  • 37
    • 0024369647 scopus 로고
    • The mouse neuronal cell surface protein F3: A phosphatidylinositol-anchored member of the immunoglobulin superfamily related to chicken contactin
    • Gennarini G., Cibelli G., Rougon G., Mattei M.-G., and Goridis C. The mouse neuronal cell surface protein F3: A phosphatidylinositol-anchored member of the immunoglobulin superfamily related to chicken contactin. J. Cell Biol. 109 (1989) 775-778
    • (1989) J. Cell Biol. , vol.109 , pp. 775-778
    • Gennarini, G.1    Cibelli, G.2    Rougon, G.3    Mattei, M.-G.4    Goridis, C.5
  • 38
    • 0025809906 scopus 로고
    • Transfected F3/F11 neuronal cell surface protein mediates intercellular adhesion and promotes neurite outgrowth
    • Gennarini G., Durbec P., Boned A., Rougon G., and Goridis C. Transfected F3/F11 neuronal cell surface protein mediates intercellular adhesion and promotes neurite outgrowth. Neuron 6 (1991) 595-606
    • (1991) Neuron , vol.6 , pp. 595-606
    • Gennarini, G.1    Durbec, P.2    Boned, A.3    Rougon, G.4    Goridis, C.5
  • 39
    • 0028926204 scopus 로고
    • Glycolipid-anchored proteins in neuroblastoma cells form detergent-resistant complexes without caveolin
    • Gorodinsky A., and Harris D.A. Glycolipid-anchored proteins in neuroblastoma cells form detergent-resistant complexes without caveolin. J. Cell Biol. 129 (1995) 619-627
    • (1995) J. Cell Biol. , vol.129 , pp. 619-627
    • Gorodinsky, A.1    Harris, D.A.2
  • 41
    • 0024277922 scopus 로고
    • Growth cone guidance in insects: Fasciclin II is a member of the immunoglobulin superfamily
    • Harrelson A.L., and Goodman C.S. Growth cone guidance in insects: Fasciclin II is a member of the immunoglobulin superfamily. Science 242 (1988) 700-708
    • (1988) Science , vol.242 , pp. 700-708
    • Harrelson, A.L.1    Goodman, C.S.2
  • 42
    • 0022802628 scopus 로고
    • Phosphatidylinositol is involved in the membrane attachment of NCAM-120, the smallest component of the neural cell adhesion molecule
    • He H.T., Barbet J., Chaix J.C., and Goridis C. Phosphatidylinositol is involved in the membrane attachment of NCAM-120, the smallest component of the neural cell adhesion molecule. Embo J. 5 (1986) 2489-2494
    • (1986) Embo J. , vol.5 , pp. 2489-2494
    • He, H.T.1    Barbet, J.2    Chaix, J.C.3    Goridis, C.4
  • 43
    • 0023576304 scopus 로고
    • Biosynthesis, membrane association, and release of N-CAM-120, a phosphatidylinositol-linked form of the neural cell adhesion molecule
    • He H.T., Finne J., and Goridis C. Biosynthesis, membrane association, and release of N-CAM-120, a phosphatidylinositol-linked form of the neural cell adhesion molecule. J. Cell Biol. 105 (1987) 2489-2500
    • (1987) J. Cell Biol. , vol.105 , pp. 2489-2500
    • He, H.T.1    Finne, J.2    Goridis, C.3
  • 44
    • 0025282338 scopus 로고
    • A diverse set of developmentally regulated proteoglycans is expressed in the rat central nervous system
    • Herndon M.E., and Lander A.D. A diverse set of developmentally regulated proteoglycans is expressed in the rat central nervous system. Neuron 4 (1990) 949-961
    • (1990) Neuron , vol.4 , pp. 949-961
    • Herndon, M.E.1    Lander, A.D.2
  • 45
    • 0025700677 scopus 로고
    • Isolation and charcterization of a phosphatidylinositol-glyean-specific phospholipase D from bovine brain
    • Hoener M.C., Stieger S., and Brodeck U. Isolation and charcterization of a phosphatidylinositol-glyean-specific phospholipase D from bovine brain. Eur. J. Biochem. 190 (1990) 593-601
    • (1990) Eur. J. Biochem. , vol.190 , pp. 593-601
    • Hoener, M.C.1    Stieger, S.2    Brodeck, U.3
  • 46
    • 0021075678 scopus 로고
    • Kinetics of homophilic binding by E and A forms of the neural cell adhesion molecule
    • Hoffman S., and Edelman G.M. Kinetics of homophilic binding by E and A forms of the neural cell adhesion molecule. Proc. Natl. Acad. Sci. USA 80 (1983) 5762-5766
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 5762-5766
    • Hoffman, S.1    Edelman, G.M.2
  • 47
    • 0025106007 scopus 로고
    • Drosophila fasciclin I, a neural cell adhesion molecule, has a phosphatidylinositol lipid membrane anchor that is developmentally regulated
    • Hortsch M., and Goodman C.S. Drosophila fasciclin I, a neural cell adhesion molecule, has a phosphatidylinositol lipid membrane anchor that is developmentally regulated. J. Biol. Chem. 265 (1990) 15104-15109
    • (1990) J. Biol. Chem. , vol.265 , pp. 15104-15109
    • Hortsch, M.1    Goodman, C.S.2
  • 48
    • 0024380698 scopus 로고
    • T cell activation induces rapid tyrosine phosphorylation of a limited number of cellular substrates
    • Hsi E.D., Siegel J.N., Minami Y., Luong E.T., Klausner R.D., and Samelson L.E. T cell activation induces rapid tyrosine phosphorylation of a limited number of cellular substrates. J. Biol. Chem. 264 (1989) 10836-10842
    • (1989) J. Biol. Chem. , vol.264 , pp. 10836-10842
    • Hsi, E.D.1    Siegel, J.N.2    Minami, Y.3    Luong, E.T.4    Klausner, R.D.5    Samelson, L.E.6
  • 49
    • 0026038704 scopus 로고
    • Bacterial PIPLCs-unique properties and usefulness in studies on GPI anchors
    • Ikezawa H. Bacterial PIPLCs-unique properties and usefulness in studies on GPI anchors. Cell Biol. Int. Rep. 15 (1991) 1115-1131
    • (1991) Cell Biol. Int. Rep. , vol.15 , pp. 1115-1131
    • Ikezawa, H.1
  • 50
    • 0039309229 scopus 로고
    • The Thy-1 antigen exhibits rapid lateral diffusion in the plasma membrane of rodent lymphoid cells and fibroblasts
    • Ishihara A., Hou Y., and Jacobson K. The Thy-1 antigen exhibits rapid lateral diffusion in the plasma membrane of rodent lymphoid cells and fibroblasts. Proc. Natl. Acad. Sci. USA 84 (1987) 1290-1293
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 1290-1293
    • Ishihara, A.1    Hou, Y.2    Jacobson, K.3
  • 51
    • 0023257520 scopus 로고
    • Involvement of phosphatidylinositol and insulin in the coordinate regulation of proteoheparan sulfate metabolism and hepatocyte growth
    • Ishihara M., Fedarko N.S., and Conrad H.E. Involvement of phosphatidylinositol and insulin in the coordinate regulation of proteoheparan sulfate metabolism and hepatocyte growth. J. Biol. Chem. 262 (1987) 4708
    • (1987) J. Biol. Chem. , vol.262 , pp. 4708
    • Ishihara, M.1    Fedarko, N.S.2    Conrad, H.E.3
  • 52
    • 0023967787 scopus 로고
    • Adhesion molecules and the hierarchy of neural development
    • Jessel T.M. Adhesion molecules and the hierarchy of neural development. Neuron 1 (1988) 3-13
    • (1988) Neuron , vol.1 , pp. 3-13
    • Jessel, T.M.1
  • 53
    • 0027272323 scopus 로고
    • Lachesin: An immunoglobulin superfamily protein whose expression correlates with neurogenesis in grasshopper embryos
    • Karlstrom R.O., Wilder L.P., and Bastiani M.J. Lachesin: An immunoglobulin superfamily protein whose expression correlates with neurogenesis in grasshopper embryos. Development 118 (1993) 509-522
    • (1993) Development , vol.118 , pp. 509-522
    • Karlstrom, R.O.1    Wilder, L.P.2    Bastiani, M.J.3
  • 54
    • 0026440036 scopus 로고
    • Cloning of a major heparan sulfate proteoglycan from brain and identification as the rat form of glypican
    • Karthikeyan L., Maurel P., Rauch U., Margolis R.K., and Margolis R.U. Cloning of a major heparan sulfate proteoglycan from brain and identification as the rat form of glypican. Biochem. Biophys. Res. Commun. 188 (1992) 395-401
    • (1992) Biochem. Biophys. Res. Commun. , vol.188 , pp. 395-401
    • Karthikeyan, L.1    Maurel, P.2    Rauch, U.3    Margolis, R.K.4    Margolis, R.U.5
  • 55
    • 0026587547 scopus 로고
    • Endocytosis of glycophospholipid-anchored and transmembrane forms of CD4 by different endocytic pathways
    • Keller G.-A., Siegel M.W., and Caras I.W. Endocytosis of glycophospholipid-anchored and transmembrane forms of CD4 by different endocytic pathways. Embo J. 11 (1992) 863-874
    • (1992) Embo J. , vol.11 , pp. 863-874
    • Keller, G.-A.1    Siegel, M.W.2    Caras, I.W.3
  • 56
    • 0027498149 scopus 로고
    • Biosynthesis of glycosylphosphatidylinositol (GPI)-anchored membrane proteins in intact cells: Specific amino acid requirements adjacent to the site of cleavage and GPI attachment
    • Kodukula K., Gerber L.D., Amthauer R., Brink L., and Udenfriend S. Biosynthesis of glycosylphosphatidylinositol (GPI)-anchored membrane proteins in intact cells: Specific amino acid requirements adjacent to the site of cleavage and GPI attachment. J. Cell Biol. 120 (1993) 657-664
    • (1993) J. Cell Biol. , vol.120 , pp. 657-664
    • Kodukula, K.1    Gerber, L.D.2    Amthauer, R.3    Brink, L.4    Udenfriend, S.5
  • 57
    • 0025369197 scopus 로고
    • Drosophila chaoptin, a member of the leucinerich repeat family, is a photoreceptor cell-specific adhesion molecule
    • Krantz D.E., and Zipursky S.L. Drosophila chaoptin, a member of the leucinerich repeat family, is a photoreceptor cell-specific adhesion molecule. EMBO J. 9 (1990) 1969-19977
    • (1990) EMBO J. , vol.9 , pp. 1969-19977
    • Krantz, D.E.1    Zipursky, S.L.2
  • 58
    • 0022535524 scopus 로고
    • Thy-1 functions as a signal transduction molecule in T lymphocytes and transfected B lymphocytes
    • Kroczek R.A., Gunter K.C., Germain R.N., and Shevach E.M. Thy-1 functions as a signal transduction molecule in T lymphocytes and transfected B lymphocytes. Nature 322 (1986) 181-184
    • (1986) Nature , vol.322 , pp. 181-184
    • Kroczek, R.A.1    Gunter, K.C.2    Germain, R.N.3    Shevach, E.M.4
  • 59
    • 0025200349 scopus 로고
    • Identification and gene cloning of a new phosphatidylinositol-linked antigen expressed on mature lymphocytes. Down-regulation by lymphocyte activation
    • Kubota H., Okazaki H., Onuma M., Kano S., Hattori M., and Minato N. Identification and gene cloning of a new phosphatidylinositol-linked antigen expressed on mature lymphocytes. Down-regulation by lymphocyte activation. J Immunol. 145 (1990) 3924-3931
    • (1990) J Immunol. , vol.145 , pp. 3924-3931
    • Kubota, H.1    Okazaki, H.2    Onuma, M.3    Kano, S.4    Hattori, M.5    Minato, N.6
  • 60
    • 0024791964 scopus 로고
    • Location of a transiently expressed glycoprotein in developing cerebellum delineating its possible ontogenetic role
    • Kuchler S., Rougon G., Marschal P., Lehman S., Reeber A., Vincendon, and Zanetta J.-P. Location of a transiently expressed glycoprotein in developing cerebellum delineating its possible ontogenetic role. J. Neuroscience 33 (1989) 111-124
    • (1989) J. Neuroscience , vol.33 , pp. 111-124
    • Kuchler, S.1    Rougon, G.2    Marschal, P.3    Lehman, S.4    Reeber, A.5    Vincendon6    Zanetta, J.-P.7
  • 61
    • 0026319551 scopus 로고
    • Neurite outgrowth on immobilized Axonin-1 is mediated by a heterophilic interaction with L1 (G4
    • Kuhn T.B., Stoeckli E.T., Condrau M.A., Rathjen F.G., and Sonderegger P. Neurite outgrowth on immobilized Axonin-1 is mediated by a heterophilic interaction with L1 (G4. J. Cell Biol. 115 (1991) 1113-1126
    • (1991) J. Cell Biol. , vol.115 , pp. 1113-1126
    • Kuhn, T.B.1    Stoeckli, E.T.2    Condrau, M.A.3    Rathjen, F.G.4    Sonderegger, P.5
  • 62
    • 0030330635 scopus 로고    scopus 로고
    • The glypican family of heparan sulfate proteoglycans: Major cell-surface proteoglycans of the developing nervous system
    • R. U. Margolis & M. Grumet, Eds
    • Lander, A. D., Stipp, C. S., & Ivins, J. K. (1996). The glypican family of heparan sulfate proteoglycans: Major cell-surface proteoglycans of the developing nervous system. In: Proteoglycans in Neural Development (R. U. Margolis & M. Grumet, Eds.).
    • (1996) Proteoglycans in Neural Development
    • Lander, A.D.1    Stipp, C.S.2    Ivins, J.K.3
  • 64
    • 0024468669 scopus 로고
    • A glycophospholipid membrane anchor acts as an apical targeting signal in polarized epithelial cells
    • Lisanti M.P., Caras I.W., Davitz M.A., and Rodriguez-Boulan E. A glycophospholipid membrane anchor acts as an apical targeting signal in polarized epithelial cells. J. Cell Biol. 109 (1989) 2145-2156
    • (1989) J. Cell Biol. , vol.109 , pp. 2145-2156
    • Lisanti, M.P.1    Caras, I.W.2    Davitz, M.A.3    Rodriguez-Boulan, E.4
  • 65
    • 0024455829 scopus 로고
    • The distribution of glycosyl-phosphatidylinositol anchored proteins is differentially regulated by serum and insulin
    • Lisanti M.P., Darnell J.C., Chan B.L., Rodriguez-Boulan E., and Saltiel A.R. The distribution of glycosyl-phosphatidylinositol anchored proteins is differentially regulated by serum and insulin. Biochem. Biophys. Res. Commun. 164 (1989) 824-832
    • (1989) Biochem. Biophys. Res. Commun. , vol.164 , pp. 824-832
    • Lisanti, M.P.1    Darnell, J.C.2    Chan, B.L.3    Rodriguez-Boulan, E.4    Saltiel, A.R.5
  • 66
    • 0025055080 scopus 로고
    • Glycophospholipid membrane anchoring provides clues to the mechanism of protein sorting in polarized epithelial cells
    • Lisanti M.P., and Rodriguez-Boulan E. Glycophospholipid membrane anchoring provides clues to the mechanism of protein sorting in polarized epithelial cells. Trends Biochem. 15 (1990) 113-118
    • (1990) Trends Biochem. , vol.15 , pp. 113-118
    • Lisanti, M.P.1    Rodriguez-Boulan, E.2
  • 67
    • 0000441994 scopus 로고
    • Polarized apical distribution of glycosyl-phosphatidylinositolanchored proteins in a renal epithelial cell line
    • Lisanti M.P., Sargiacomo M., Graeve L., Saltiel A.R., and Rodriguez-Boulan E. Polarized apical distribution of glycosyl-phosphatidylinositolanchored proteins in a renal epithelial cell line. Proc. Natl. Acad. Sci. USA 85 (1988) 9557-9561
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 9557-9561
    • Lisanti, M.P.1    Sargiacomo, M.2    Graeve, L.3    Saltiel, A.R.4    Rodriguez-Boulan, E.5
  • 68
    • 0024316809 scopus 로고
    • The glycosyl-phosphatidylinositol anchor of membrane proteins
    • Low M. The glycosyl-phosphatidylinositol anchor of membrane proteins. Biochim. Biophys. Acta. 988 (1989) 427-454
    • (1989) Biochim. Biophys. Acta. , vol.988 , pp. 427-454
    • Low, M.1
  • 69
    • 0025998739 scopus 로고
    • Factors affecting the ability of glycosylphosphatidylinositol-specific phospholipase D to degrade the membrane anchors of cell surface proteins
    • Low M.G., and Huang K.S. Factors affecting the ability of glycosylphosphatidylinositol-specific phospholipase D to degrade the membrane anchors of cell surface proteins. Biochem J. (1991)
    • (1991) Biochem J.
    • Low, M.G.1    Huang, K.S.2
  • 70
    • 0027373701 scopus 로고
    • Collapsin: A protein in brain that induces the collapse and paralysis of neuronal growth cones
    • Luo Y., Raible D., and Raper J.A. Collapsin: A protein in brain that induces the collapse and paralysis of neuronal growth cones. Cell 75 (1993) 217-227
    • (1993) Cell , vol.75 , pp. 217-227
    • Luo, Y.1    Raible, D.2    Raper, J.A.3
  • 71
    • 0026554563 scopus 로고
    • Modulation of an NCAM-related adhesion molecule with long-term synaptic plasticity in Aplysia.
    • Mayford M., Varzilai A., Keller F., Schacher S., and Kandel E.R. Modulation of an NCAM-related adhesion molecule with long-term synaptic plasticity in Aplysia. Science 256 (1992) 638-644
    • (1992) Science , vol.256 , pp. 638-644
    • Mayford, M.1    Varzilai, A.2    Keller, F.3    Schacher, S.4    Kandel, E.R.5
  • 72
    • 0029044628 scopus 로고
    • Insolubility and redistribution of GPI-anchored proteins at the cell surface after detergent treatment
    • Mayor S., and Maxfield F.R. Insolubility and redistribution of GPI-anchored proteins at the cell surface after detergent treatment. Mol. Biol. Cell 6 (1995) 929-944
    • (1995) Mol. Biol. Cell , vol.6 , pp. 929-944
    • Mayor, S.1    Maxfield, F.R.2
  • 73
    • 0028000605 scopus 로고
    • Sequestration of GPI-anchored proteins in caveolae triggered by cross-Unking
    • Mayor S., Rothberg K.G., and Maxfield F.R. Sequestration of GPI-anchored proteins in caveolae triggered by cross-Unking. Science 264 (1994) 1948-1951
    • (1994) Science , vol.264 , pp. 1948-1951
    • Mayor, S.1    Rothberg, K.G.2    Maxfield, F.R.3
  • 75
    • 0026663815 scopus 로고
    • Immunolocalization of a glycosylphosphatidylinsitol-specific phosphilipase D (GPI-PLD) in mast cells found in normal tissue and neurofibromatosis lesions
    • Metz C.M., Thomas P., and Davitz M.A. Immunolocalization of a glycosylphosphatidylinsitol-specific phosphilipase D (GPI-PLD) in mast cells found in normal tissue and neurofibromatosis lesions. Amer. J. Path. 140 (1992) 1275-1281
    • (1992) Amer. J. Path. , vol.140 , pp. 1275-1281
    • Metz, C.M.1    Thomas, P.2    Davitz, M.A.3
  • 76
    • 0025990728 scopus 로고
    • Production of the glycosylphosphatidylinositol-specific phospholipase D by the islets of Langerhans
    • Metz C.N., Zhang Y.Y., Guo Y., Tsang T.C., Kochan J.P., Altszuler N., and Davitz M.A. Production of the glycosylphosphatidylinositol-specific phospholipase D by the islets of Langerhans. J. Biol Chem. 266 (1991) 17733-17736
    • (1991) J. Biol Chem. , vol.266 , pp. 17733-17736
    • Metz, C.N.1    Zhang, Y.Y.2    Guo, Y.3    Tsang, T.C.4    Kochan, J.P.5    Altszuler, N.6    Davitz, M.A.7
  • 77
    • 0025089896 scopus 로고
    • The oligodendrocyte-myelin glycoprotein belongs to a distinct family of proteins and contains the HNK-1 carbohydrate
    • Mikol D.D., Gulcher J.R., and Stefansson K. The oligodendrocyte-myelin glycoprotein belongs to a distinct family of proteins and contains the HNK-1 carbohydrate. J Cell Biol. 110 (1990) 471-479
    • (1990) J Cell Biol. , vol.110 , pp. 471-479
    • Mikol, D.D.1    Gulcher, J.R.2    Stefansson, K.3
  • 78
    • 0026597554 scopus 로고
    • Solubility and posttranslational regulation of GP130/F11-a neuronal GPI-linked cell adhesion molecule enriched in the neuronal membrane skeleton
    • Moss D.J., and White C.A. Solubility and posttranslational regulation of GP130/F11-a neuronal GPI-linked cell adhesion molecule enriched in the neuronal membrane skeleton. Eur. J. Cell Biol. 57 (1992) 59-65
    • (1992) Eur. J. Cell Biol. , vol.57 , pp. 59-65
    • Moss, D.J.1    White, C.A.2
  • 79
    • 0024755646 scopus 로고
    • Transmembrane control of cadherin-mediated cell adhesion: A 94 kDa protein functionally associated with a specific region of the cytoplasmic domain of E-cadherin
    • Nagafuchi A., and Takeichi M. Transmembrane control of cadherin-mediated cell adhesion: A 94 kDa protein functionally associated with a specific region of the cytoplasmic domain of E-cadherin. Cell Regulation 1 (1989) 37-44
    • (1989) Cell Regulation , vol.1 , pp. 37-44
    • Nagafuchi, A.1    Takeichi, M.2
  • 80
    • 0023430368 scopus 로고
    • High lateral mobility of endogenous and transfected alkaline phosphatase: A phosphatidylinositolanchored membrane protein
    • Noda M., Yoon K., Rodan G.A., and Koppel D.E. High lateral mobility of endogenous and transfected alkaline phosphatase: A phosphatidylinositolanchored membrane protein. J. Cell Biol. 105 (1987) 1671-1677
    • (1987) J. Cell Biol. , vol.105 , pp. 1671-1677
    • Noda, M.1    Yoon, K.2    Rodan, G.A.3    Koppel, D.E.4
  • 81
    • 0028805468 scopus 로고
    • The F3 neuronal glycosylphosphatidylinositol-linked molecule is localized to glycolipid-enriched membrane subdomains and interacts with L1 and fyn kinase in cerebellum
    • Olive S., Dubois C., Schachner M., and Rougon G. The F3 neuronal glycosylphosphatidylinositol-linked molecule is localized to glycolipid-enriched membrane subdomains and interacts with L1 and fyn kinase in cerebellum. J. Neurochem. 65 (1995) 2307-2317
    • (1995) J. Neurochem. , vol.65 , pp. 2307-2317
    • Olive, S.1    Dubois, C.2    Schachner, M.3    Rougon, G.4
  • 82
    • 0024451982 scopus 로고
    • The cytoplasmic domain of the cell adhesion molecule uvomorulin associates with three independent proteins structurally related in different species
    • Ozawa M., Baribault H., and Kemler R. The cytoplasmic domain of the cell adhesion molecule uvomorulin associates with three independent proteins structurally related in different species. EMBO J. 8 (1989) 1711-1717
    • (1989) EMBO J. , vol.8 , pp. 1711-1717
    • Ozawa, M.1    Baribault, H.2    Kemler, R.3
  • 83
    • 0029147426 scopus 로고
    • Digging into caveolae
    • Parton R.G., and Simons K. Digging into caveolae. Science 269 (1995) 1398-1399
    • (1995) Science , vol.269 , pp. 1398-1399
    • Parton, R.G.1    Simons, K.2
  • 85
    • 0027526588 scopus 로고
    • The F3/F11 cell adhesion molecule mediates the repulsion of neurons by the extracellular matrix glycoprotein J1-160/180
    • Pesheva P., Gennarini G., Goridis C., and Schachner M. The F3/F11 cell adhesion molecule mediates the repulsion of neurons by the extracellular matrix glycoprotein J1-160/180. Neuron 10 (1993) 69-82
    • (1993) Neuron , vol.10 , pp. 69-82
    • Pesheva, P.1    Gennarini, G.2    Goridis, C.3    Schachner, M.4
  • 87
    • 0029082199 scopus 로고
    • The limbic system-associated membrane protein is an Ig superfamily member that mediates selective neuronal growth and axon targeting
    • Pimenta A.F., Zhukareva V., Barbe M.F., Reinoso B.S., Grimley C., Henzel W., Fischer I., and Levitt P. The limbic system-associated membrane protein is an Ig superfamily member that mediates selective neuronal growth and axon targeting. Neuron 15 (1995) 287-297
    • (1995) Neuron , vol.15 , pp. 287-297
    • Pimenta, A.F.1    Zhukareva, V.2    Barbe, M.F.3    Reinoso, B.S.4    Grimley, C.5    Henzel, W.6    Fischer, I.7    Levitt, P.8
  • 88
    • 0025874210 scopus 로고
    • Targeting of transmembrane and GPI-anchored forms of N-CAM to opposite domains of a polarized epithelial cell
    • Powell S.K., Cunningham B.A., Edelman G.M., and Rodriguez B.E. Targeting of transmembrane and GPI-anchored forms of N-CAM to opposite domains of a polarized epithelial cell. Nature 353 (1991) 76-77
    • (1991) Nature , vol.353 , pp. 76-77
    • Powell, S.K.1    Cunningham, B.A.2    Edelman, G.M.3    Rodriguez, B.E.4
  • 89
    • 0025157628 scopus 로고
    • Role of phosphatidylinositol-anchored proteins in T cell activation
    • Presky D.H., Low M.G., and Shevach E.M. Role of phosphatidylinositol-anchored proteins in T cell activation. J. Immunol. 144 (1990) 860-868
    • (1990) J. Immunol. , vol.144 , pp. 860-868
    • Presky, D.H.1    Low, M.G.2    Shevach, E.M.3
  • 90
    • 0028847151 scopus 로고
    • Neuronal polarity: Giving neurons heads and tails
    • Prochiantz A. Neuronal polarity: Giving neurons heads and tails. Neuron 15 (1995) 743-746
    • (1995) Neuron , vol.15 , pp. 743-746
    • Prochiantz, A.1
  • 91
    • 0026052670 scopus 로고
    • T-cadherin, a novel cadherin cell adhesion molecule in the nervous system lacks the conserved cytoplasmic region
    • Ranscht B., and Dours-Zimmerman M.T. T-cadherin, a novel cadherin cell adhesion molecule in the nervous system lacks the conserved cytoplasmic region. Neuron 7 (1991) 391-402
    • (1991) Neuron , vol.7 , pp. 391-402
    • Ranscht, B.1    Dours-Zimmerman, M.T.2
  • 92
    • 0026020097 scopus 로고
    • Extracellular matrix molecules and their receptors: functions in neural development
    • Reichardt L.F., and Tomaselli K.J. Extracellular matrix molecules and their receptors: functions in neural development. Annu. Rev. Neurosci. 14 (1991) 531-570
    • (1991) Annu. Rev. Neurosci. , vol.14 , pp. 531-570
    • Reichardt, L.F.1    Tomaselli, K.J.2
  • 93
    • 0025360479 scopus 로고
    • Growth factor-induced release of a glycosyl-phosphatidylinositol (GPI)-linked protein from the HEp-2 human carcinoma cell line
    • Roberts J.M., Kenton P., and Johnson P.M. Growth factor-induced release of a glycosyl-phosphatidylinositol (GPI)-linked protein from the HEp-2 human carcinoma cell line. Febs Lett. 267 (1990) 213-216
    • (1990) Febs Lett. , vol.267 , pp. 213-216
    • Roberts, J.M.1    Kenton, P.2    Johnson, P.M.3
  • 94
    • 0026013817 scopus 로고
    • Phosphatidylinositol membrane anchors and T-cell activation
    • Robinson P.J. Phosphatidylinositol membrane anchors and T-cell activation. Immunol. Today 12 (1991) 35-41
    • (1991) Immunol. Today , vol.12 , pp. 35-41
    • Robinson, P.J.1
  • 95
    • 0026563684 scopus 로고
    • Expression of unique sets of GP1-linked proteins by different primary neurons in vitro.
    • Rosen C.L., Lisanti M.P., and Salzer J.L. Expression of unique sets of GP1-linked proteins by different primary neurons in vitro. J. Cell Biol. 117 (1992) 617-627
    • (1992) J. Cell Biol. , vol.117 , pp. 617-627
    • Rosen, C.L.1    Lisanti, M.P.2    Salzer, J.L.3
  • 96
    • 0025264867 scopus 로고
    • Phosphatidylinositol-linked proteins and paroxysmal nocturnal hemoglobinuria
    • Rosse W. Phosphatidylinositol-linked proteins and paroxysmal nocturnal hemoglobinuria. Blood 75 (1990) 1595-1601
    • (1990) Blood , vol.75 , pp. 1595-1601
    • Rosse, W.1
  • 97
    • 0027299164 scopus 로고
    • T-cadherin 2: Molecular characterization, function in cell adhesion, and coexpression with T-cadherin and N-cadherin
    • Sacristán M.P., Vestal D.J., Dours-Zimmerman M.T., and Ranscht B. T-cadherin 2: Molecular characterization, function in cell adhesion, and coexpression with T-cadherin and N-cadherin. J. Neurosci. Res. 34 (1993) 664-680
    • (1993) J. Neurosci. Res. , vol.34 , pp. 664-680
    • Sacristán, M.P.1    Vestal, D.J.2    Dours-Zimmerman, M.T.3    Ranscht, B.4
  • 98
    • 0025847074 scopus 로고
    • Primary structure and functional activity of a phosphatidylinositol-glycan-specific phospholipase D
    • Scallon B.J., Fung W.-J.C., Tsang T.C., Li S., Kado-Fong H., Juang K.-S., and Kochan J.P. Primary structure and functional activity of a phosphatidylinositol-glycan-specific phospholipase D. Science 252 (1991) 446-448
    • (1991) Science , vol.252 , pp. 446-448
    • Scallon, B.J.1    Fung, W.-J.C.2    Tsang, T.C.3    Li, S.4    Kado-Fong, H.5    Juang, K.-S.6    Kochan, J.P.7
  • 99
    • 0029082412 scopus 로고
    • Separation of caveolae from associated microdomains of GPI-anchored proteins
    • Schnitzer J.E., Mclntosh D.P., Dvorak A.M., Liu J., and Oh P. Separation of caveolae from associated microdomains of GPI-anchored proteins. Science 269 (1995) 1435-1439
    • (1995) Science , vol.269 , pp. 1435-1439
    • Schnitzer, J.E.1    Mclntosh, D.P.2    Dvorak, A.M.3    Liu, J.4    Oh, P.5
  • 100
    • 0024378415 scopus 로고
    • Molecular characterization of a new immunoglobulin superfamily protein with potential roles in opioid binding and cell contact
    • Schofield P.R., McFarland K.C., Hayflick J.S., Wilcox J.N., Cho T.M., Roy S., Lee N.M., Loh H.H., and Seeburg P.H. Molecular characterization of a new immunoglobulin superfamily protein with potential roles in opioid binding and cell contact. EMBO J. 8 (1989) 489-495
    • (1989) EMBO J. , vol.8 , pp. 489-495
    • Schofield, P.R.1    McFarland, K.C.2    Hayflick, J.S.3    Wilcox, J.N.4    Cho, T.M.5    Roy, S.6    Lee, N.M.7    Loh, H.H.8    Seeburg, P.H.9
  • 101
    • 0026008414 scopus 로고
    • Molecular cloning of gp42, a cell-surface molecule that is selectively induced on rat natural killer cells by interleukin 2: Glycolipid membrane anchoring and capacity for transmembrane signaling
    • Seaman W.E., Niemi E.C., Stark M.R., Goldfine R.D., Pollock A.S., and Imboden J.B. Molecular cloning of gp42, a cell-surface molecule that is selectively induced on rat natural killer cells by interleukin 2: Glycolipid membrane anchoring and capacity for transmembrane signaling. J Exp. Med. 173 (1991) 251-260
    • (1991) J Exp. Med. , vol.173 , pp. 251-260
    • Seaman, W.E.1    Niemi, E.C.2    Stark, M.R.3    Goldfine, R.D.4    Pollock, A.S.5    Imboden, J.B.6
  • 102
    • 0030062592 scopus 로고    scopus 로고
    • REGA-1 is a GPl-linked member of the immunoglobulin superfamily present on restricted regions of sheath cell processes in grasshopper
    • Seaver E.C., Carpenter E.M., and Bastiani M.J. REGA-1 is a GPl-linked member of the immunoglobulin superfamily present on restricted regions of sheath cell processes in grasshopper. Development 122 (1996) 567-578
    • (1996) Development , vol.122 , pp. 567-578
    • Seaver, E.C.1    Carpenter, E.M.2    Bastiani, M.J.3
  • 103
    • 0024291344 scopus 로고
    • Characterization of amalgam: A member of the immunoglobulin gene superfamily from Drosphila.
    • Seeger M.A., Haffley L., and Kaufman T.C. Characterization of amalgam: A member of the immunoglobulin gene superfamily from Drosphila. Cell 55 (1988) 589-600
    • (1988) Cell , vol.55 , pp. 589-600
    • Seeger, M.A.1    Haffley, L.2    Kaufman, T.C.3
  • 104
    • 24444453578 scopus 로고
    • Immunolocalization of glycosyl phosphatidylinositol-specific phospholipase D (GPI-PLD) in mammalian tissues
    • Sesko A.M., and Low M.G. Immunolocalization of glycosyl phosphatidylinositol-specific phospholipase D (GPI-PLD) in mammalian tissues. FASEB J. 5 (1991) A839
    • (1991) FASEB J. , vol.5
    • Sesko, A.M.1    Low, M.G.2
  • 105
    • 0025341760 scopus 로고
    • Polarized sorting in epithelia
    • Simons K., and Wandinger-Ness A. Polarized sorting in epithelia. Cell 62 (1990) 207-210
    • (1990) Cell , vol.62 , pp. 207-210
    • Simons, K.1    Wandinger-Ness, A.2
  • 106
    • 0029865781 scopus 로고    scopus 로고
    • CEPU-1, a novel immunoglobulin superfamily molecule, is expressed by developing cerebellar Purkinje cells
    • Spaltmann F., and Brümmendorf T. CEPU-1, a novel immunoglobulin superfamily molecule, is expressed by developing cerebellar Purkinje cells. J. Neurosci. 16 (1996) 1770-1779
    • (1996) J. Neurosci. , vol.16 , pp. 1770-1779
    • Spaltmann, F.1    Brümmendorf, T.2
  • 108
    • 0025746722 scopus 로고
    • Prions and prion proteins
    • Stahl N., and Prusiner S.B. Prions and prion proteins. FASEB J. 5 (1991) 2799-2807
    • (1991) FASEB J. , vol.5 , pp. 2799-2807
    • Stahl, N.1    Prusiner, S.B.2
  • 109
    • 0026352248 scopus 로고
    • GPI-anchored cell-surface molecules complexed to protein tyrosine kinases
    • Stefanová I., Horeksí V., Ansotegui J., Knapp W., and Stockinger H. GPI-anchored cell-surface molecules complexed to protein tyrosine kinases. Science 254 (1991) 1016-1019
    • (1991) Science , vol.254 , pp. 1016-1019
    • Stefanová, I.1    Horeksí, V.2    Ansotegui, J.3    Knapp, W.4    Stockinger, H.5
  • 110
    • 0028118405 scopus 로고
    • Cerebroglycan: An integral membrane heparan sulfate proteoglycan that is unique to the developing nervous system and expressed specifically during neuronal differentiation
    • Stipp C.S., Litwack E.D., and Lander A.D. Cerebroglycan: An integral membrane heparan sulfate proteoglycan that is unique to the developing nervous system and expressed specifically during neuronal differentiation. J. Cell Biol. 124 (1994) 149-160
    • (1994) J. Cell Biol. , vol.124 , pp. 149-160
    • Stipp, C.S.1    Litwack, E.D.2    Lander, A.D.3
  • 111
    • 0025974195 scopus 로고
    • The axonally secreted protein axonin-1 is a potent substratum for neurite growth
    • Stoeckli E.T., Kuhn T.B., Duc C.O., Ruegg M.A., and Sonderegger P. The axonally secreted protein axonin-1 is a potent substratum for neurite growth. J. Cell Biol. 112 (1991) 449-455
    • (1991) J. Cell Biol. , vol.112 , pp. 449-455
    • Stoeckli, E.T.1    Kuhn, T.B.2    Duc, C.O.3    Ruegg, M.A.4    Sonderegger, P.5
  • 113
    • 0028905174 scopus 로고
    • Molecular cloning of neurotrimin defines a new subfamily of differentially expressed neural cell adhesion molecules
    • Struyk A.F., Canoll P., Wolfgang M., Rosen C.L., D'Eustachio P., and Salzer J.L. Molecular cloning of neurotrimin defines a new subfamily of differentially expressed neural cell adhesion molecules. J. Neurosci. 15 (1995) 2141-2156
    • (1995) J. Neurosci. , vol.15 , pp. 2141-2156
    • Struyk, A.F.1    Canoll, P.2    Wolfgang, M.3    Rosen, C.L.4    D'Eustachio, P.5    Salzer, J.L.6
  • 114
    • 0026090037 scopus 로고
    • The glycosyl phosphatidylinositol anchor is critical for Ly-6A/ E-mediated T cell activation
    • Su G., Waneck G.L., Flavell R.A., and Bothwell A.L. The glycosyl phosphatidylinositol anchor is critical for Ly-6A/ E-mediated T cell activation. J Cell Biol. 112 (1991) 377-384
    • (1991) J Cell Biol. , vol.112 , pp. 377-384
    • Su, G.1    Waneck, G.L.2    Flavell, R.A.3    Bothwell, A.L.4
  • 116
    • 0027310539 scopus 로고
    • Deficiency of the GPI anchor caused by a somatic mutation of the PIG-A gene in paroxysmal nocturnal hemoglobinuria
    • Takeda J., Miyata T., Kawagoe K., Iida Y., Endo Y., Fujita T., Takahashi M., Kitani T., and Kinoshita T. Deficiency of the GPI anchor caused by a somatic mutation of the PIG-A gene in paroxysmal nocturnal hemoglobinuria. Cell 73 (1993) 703-711
    • (1993) Cell , vol.73 , pp. 703-711
    • Takeda, J.1    Miyata, T.2    Kawagoe, K.3    Iida, Y.4    Endo, Y.5    Fujita, T.6    Takahashi, M.7    Kitani, T.8    Kinoshita, T.9
  • 117
    • 0026494835 scopus 로고
    • How to make a glycoinositol phospholipid anchor
    • Tartakoff A.M., and Singh N. How to make a glycoinositol phospholipid anchor. Trends Biochem. Sci. 17 (1992) 470-473
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 470-473
    • Tartakoff, A.M.1    Singh, N.2
  • 118
  • 119
    • 0025239824 scopus 로고
    • Detection of a phosphatidylinositol-specific Phospholipase C at the surface of Swiss 3T3 cells and its potential role in the regulation of cell growth
    • Ting A.E., and Pagano R.E. Detection of a phosphatidylinositol-specific Phospholipase C at the surface of Swiss 3T3 cells and its potential role in the regulation of cell growth. J. Biol. Chem. 265 (1990) 5337-5340
    • (1990) J. Biol. Chem. , vol.265 , pp. 5337-5340
    • Ting, A.E.1    Pagano, R.E.2
  • 121
    • 0025058952 scopus 로고
    • Molecular forms of acetylcholinesterase in two sublines of human erythroleukemia K562 cells: Sensitivity or resistance to phosphatidylinositol-specific phospholipase C and biosynthesis
    • Toutant J.-P., Richards M.K., Krall J.A., and Rosenberry T.L. Molecular forms of acetylcholinesterase in two sublines of human erythroleukemia K562 cells: Sensitivity or resistance to phosphatidylinositol-specific phospholipase C and biosynthesis. Eur. J. Biochem. 187 (1990) 31-38
    • (1990) Eur. J. Biochem. , vol.187 , pp. 31-38
    • Toutant, J.-P.1    Richards, M.K.2    Krall, J.A.3    Rosenberry, T.L.4
  • 123
    • 0022346423 scopus 로고
    • A glycophosphilipid tail at the carboxy terminus of the Thy-1 glycoprotein of neurons and thymocytes
    • Tse A.G., Barclay A.N., Watts A., and Williams A.F. A glycophosphilipid tail at the carboxy terminus of the Thy-1 glycoprotein of neurons and thymocytes. Science 230 (1985) 1003-1008
    • (1985) Science , vol.230 , pp. 1003-1008
    • Tse, A.G.1    Barclay, A.N.2    Watts, A.3    Williams, A.F.4
  • 124
    • 0026646522 scopus 로고
    • Glycosyl phosphatidylinositol-anchored T-cadherin mediates calcium dependent, homophilic cell adhesion
    • Vestal D.J., and Ranscht B. Glycosyl phosphatidylinositol-anchored T-cadherin mediates calcium dependent, homophilic cell adhesion. J. Cell Biol. 119 (1992) 451-461
    • (1992) J. Cell Biol. , vol.119 , pp. 451-461
    • Vestal, D.J.1    Ranscht, B.2
  • 125
    • 0025062283 scopus 로고
    • Structural basis for variations in the sensitivity of human decay accelerating factor to phosphatidylinositol-specific phosphilipase C cleavage
    • [Published erratum appears in J. Immunol. (1990, May 15), 144(10), 4072.]
    • Walter E.I., Roberts W.L., Rosenberry T.L., Ratnoff W.D., and Medof M.E. Structural basis for variations in the sensitivity of human decay accelerating factor to phosphatidylinositol-specific phosphilipase C cleavage. J Immunol. 144 (1990) 1030-1036 [Published erratum appears in J. Immunol. (1990, May 15), 144(10), 4072.]
    • (1990) J Immunol. , vol.144 , pp. 1030-1036
    • Walter, E.I.1    Roberts, W.L.2    Rosenberry, T.L.3    Ratnoff, W.D.4    Medof, M.E.5
  • 127
    • 0020318329 scopus 로고
    • Neuronal Thy-1 glycoprotein: Homology with immunoglobulin
    • Williams A.F., and Gagnon J. Neuronal Thy-1 glycoprotein: Homology with immunoglobulin. Science 216 (1982) 696-703
    • (1982) Science , vol.216 , pp. 696-703
    • Williams, A.F.1    Gagnon, J.2
  • 128
    • 0025752428 scopus 로고
    • The surface glycoprotein Thy-1 is excluded from growing axons during development: A study of the expression of Thy-1 during axogenesis in hippocampus and hindbrain
    • Xue G.P., Rivero B.P., and Morris R.J. The surface glycoprotein Thy-1 is excluded from growing axons during development: A study of the expression of Thy-1 during axogenesis in hippocampus and hindbrain. Development 112 (1991) 161-176
    • (1991) Development , vol.112 , pp. 161-176
    • Xue, G.P.1    Rivero, B.P.2    Morris, R.J.3
  • 129
    • 0029093081 scopus 로고
    • Overlapping and differential expression of BIG-2, BIG-1, TAG-1, and F3: Four members of an axon-associated cell adhesion molecule subgroup of the immunoglobulin superfamily
    • Yoshihara Y., Kawasaki M., Tamada A., Nagata S., Kagamiyama H., and Mori K. Overlapping and differential expression of BIG-2, BIG-1, TAG-1, and F3: Four members of an axon-associated cell adhesion molecule subgroup of the immunoglobulin superfamily. J. Neurobiol. 28 (1995) 51-69
    • (1995) J. Neurobiol. , vol.28 , pp. 51-69
    • Yoshihara, Y.1    Kawasaki, M.2    Tamada, A.3    Nagata, S.4    Kagamiyama, H.5    Mori, K.6
  • 130
    • 0028145042 scopus 로고
    • BIG-1: A new TAG-l/F3-related member of the immunoglobulin superfamily with neurite outgrowth-promoting activity
    • Yoshihara Y., Kawasaki M., Tani A., Tamada A., Nagata S., Kagamiyama H., and Mori K. BIG-1: A new TAG-l/F3-related member of the immunoglobulin superfamily with neurite outgrowth-promoting activity. Neuron 13 (1994) 415-426
    • (1994) Neuron , vol.13 , pp. 415-426
    • Yoshihara, Y.1    Kawasaki, M.2    Tani, A.3    Tamada, A.4    Nagata, S.5    Kagamiyama, H.6    Mori, K.7
  • 131
    • 0026076574 scopus 로고
    • Lateral diffusion of membrane-spanning and glycosylphosphati-dylinositol-linked proteins: Toward establishing rules governing the lateral mobility of membrane proteins
    • Zhang F., Crise B., Su B., Hou Y., Rose J.K., Bothwell A., and Jacobson K. Lateral diffusion of membrane-spanning and glycosylphosphati-dylinositol-linked proteins: Toward establishing rules governing the lateral mobility of membrane proteins. J. Cell Biol. 15 (1991) 75-84
    • (1991) J. Cell Biol. , vol.15 , pp. 75-84
    • Zhang, F.1    Crise, B.2    Su, B.3    Hou, Y.4    Rose, J.K.5    Bothwell, A.6    Jacobson, K.7
  • 132
    • 0024292597 scopus 로고
    • Sequence analysis of neuronal expression of Fasciclin I in grasshopper and Drosphila.
    • Zinn K., McAllister L., and Goodman C.S. Sequence analysis of neuronal expression of Fasciclin I in grasshopper and Drosphila. Cell 53 (1988) 577-587
    • (1988) Cell , vol.53 , pp. 577-587
    • Zinn, K.1    McAllister, L.2    Goodman, C.S.3
  • 133
    • 0029165973 scopus 로고
    • The glypiated neuronal cell adhesion molecule contactin/F11 complexes with src-family protein tyrosine kinase Fyn
    • Zisch A.H., D'Alessandri L., Amrein K., Ranscht B., Winterhalter K.H., and Vaughan L. The glypiated neuronal cell adhesion molecule contactin/F11 complexes with src-family protein tyrosine kinase Fyn. Mol. Cell Neurosci. 6 (1995) 263-279
    • (1995) Mol. Cell Neurosci. , vol.6 , pp. 263-279
    • Zisch, A.H.1    D'Alessandri, L.2    Amrein, K.3    Ranscht, B.4    Winterhalter, K.H.5    Vaughan, L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.